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