E2RU97 14-3-3 GL50803_006430 184922 None SL-0178 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}. UNIPROT E2RU97 PDB 4F7R PDB 4ZQ0 PDB 5BY9 Pfam PF00244 PROSITE PS00796 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}. GO:0005930 GO:0005737 GO:0005856 GO:0005783 GO:0031514 GO:0005635 GO:0005634 GO:0005819 GO:0003779 GO:0042802 GO:0019900 GO:0051219 GO:0050815 GO:0042803 GO:0030036 GO:1990051 GO:0030010 GO:0000165 GO:0051495 GO:0051289 GO:0070207 GO:0008104 GO:0097298 GO:0007165 Unknown UniProt Sequence Analysis MAEAFTREDYVFMAQLNENAERYDEMVETMRKISGMEGELSDKERNLLSVAYKNVIGPRRAAWRIVSSIEAKEKGRQKPNAKRIEQIRVYRQKIEKELSDICNDILKLLQEQFVPRSTNADAKVFYYKMQGDYYRYLAEYSSGEDKEKIAGSALNAYNSAFEISQQLPPTHPIRLGLALNFSVFYYEILASPDRACELARKAFDAAITDLDKLTEESYKDSTLIMQLLRDNLNLWVTDSAGDDNAEEK 248 F1P963 Oxidized NUDT1 9615 None SL-0178 SL-0182 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}. UNIPROT F1P963 PDB 5MZF Pfam PF00293 PROSITE PS51462 PROSITE PS00893 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}. GO:0001669 GO:0005737 GO:0005829 GO:0005759 GO:0031965 GO:0106377 GO:0106378 GO:0035539 GO:0008413 GO:0047693 GO:0008828 GO:0016818 GO:0046872 GO:0030515 GO:0042262 GO:0006152 Unknown UniProt Sequence Analysis MGTSRLYTLVLVLQPERVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELREESGLTVDTLHKVGQIMFEFVGEPELMDVHIFCTDSVQGTPVESDEMRPQWFQLDQIPFTDMWPDDSYWFPLLLQKKKFHGYFRFQGPNTILDYTLREVDKL 156 P53368 Oxidized Nudt1 10090 None SL-0178 SL-0182 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}. UNIPROT P53368 UNIPROT P97795 UNIPROT Q542J4 UNIPROT Q8VDG0 PDB 5MZE PDB 5MZG PDB 6EHH Pfam PF00293 PROSITE PS51462 PROSITE PS00893 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}. GO:0001669 GO:0005737 GO:0005829 GO:0005615 GO:0005759 GO:0005739 GO:0031965 GO:0005634 GO:0005886 GO:0106377 GO:0106378 GO:0035539 GO:0008413 GO:0047693 GO:0008828 GO:0016818 GO:0046872 GO:0030515 GO:0007568 GO:0042262 GO:0008584 GO:0006152 GO:0046686 Unknown UniProt Sequence Analysis MSTSRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELLEESGLSVDTLHKVGHISFEFVGSPELMDVHIFSADHVHGTPTESEEMRPQWFQLDQIPFADLWPDDSYWFPLLLQKKKFCGHFKFQDQDTILSYSLREVDSF 156 P53369 Oxidized Nudt1 10116 None SL-0178 SL-0182 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}. UNIPROT P53369 Pfam PF00293 PROSITE PS51462 PROSITE PS00893 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}. GO:0001669 GO:0005737 GO:0005829 GO:0005615 GO:0005759 GO:0005739 GO:0031965 GO:0005634 GO:0005886 GO:0106377 GO:0106378 GO:0035539 GO:0008413 GO:0047693 GO:0008828 GO:0016818 GO:0046872 GO:0030515 GO:0007568 GO:0042262 GO:0008584 GO:0006152 GO:0046686 Unknown UniProt Sequence Analysis MSTSRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELLEESGLRVDTLHKVGHISFEFVGSPELMDVHIFSTDHVHGTPTESEEMRPQWFQLDQIPFADMWPDDSYWFPLLLQKKKFCGHFKFHGQDTILSYSLREVDEF 156 Q8GWR1 Aladin AAAS 3702 None SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT Q8GWR1 UNIPROT Q9LER8 Pfam PF00400 Q9LXJ0 EBI-4496544 0.37 Q9SJH7 EBI-4496552 0.37 Q8GWK2 EBI-25521640 0.56 GO:0005783 GO:0005635 GO:0005643 GO:0051028 GO:0006913 GO:0015031 Unknown UniProt Sequence Analysis MASFPHPGSVTVCEINRDLITAQNLSDERAQETYGKVLGMVFSPVSFDSTPSSLQENEGQENGDKASGESKGLVATLQMKVADSLKQILQPTDVTLLSEIDLQGVSWHQGKHIIAFISGANQVTIRDYEDKDEKEPCILTSDSQRNVKALEWRPNGGKSLSIACRGGICIWAASYPGNMALVRSGGSALRGSLSRGSGTRWILVDFLRCQNDEQISALSWSPCGRYLASASYDSSSFTIWDVSQGAGTPIRRGLGGISMLKWSPTGDYFFAARFDGTFCLWETNTWTSEPWSLSSGSGSVTGAIWDPEGRFILISFSKSSTLGSVHFSSKPPSLDAHLLPVELPEIASLTGCEGIEKIAWDASGERLAVSYKGGDENYKGLIAIYDTRRTPIVSASLVGFIRGPGENPKALSFSFHDKFKQGPLLSVCWSTGFCCTYPLIFRSHVLP 447 Q9W351 Aladin Aladin 7227 None SL-0178 SL-0185 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}. UNIPROT Q9W351 Pfam PF00400 Involved in mitotic spindle assembly. {ECO:0000269|PubMed:26246606}. Q8SXP8 EBI-201616 0.00 Q95TJ9 EBI-468503 0.00 O97143 EBI-468506 0.00 P50445 EBI-468509 0.00 Q9VTU3 EBI-468512 0.00 Q9VEH1 EBI-468515 0.00 Q95TP4 EBI-470843 0.00 P34082 EBI-9928090 0.35 GO:0005737 GO:0012505 GO:0072686 GO:0005643 GO:0000922 GO:0001578 GO:0090307 GO:0051028 GO:0006913 GO:1902365 GO:0015031 Unknown UniProt Sequence Analysis MAALSNLKQCPPFSTLPDLALRHNHIPELERYPQINLNSELLANPAGQRYYGGQSFVSVNEGVLKRIARSFFNGGFWKTLEEARSPETREQAPLIAQAGDLIAQFLGLATGLRILPHTQQLSAERIAQFVETRDWLNSDVRYLAWNQHFFCLAVAGVDDVVRIYTKSSSATTATVLKSPSQTQITCMAWRPLCASEIVIGCRQGLCFWEVDSTLHLGRTNAPSEIFKYPNNLPITSMQWNKDGTQLATASIGDRSIIIWQPDTGMMQPLKRLGPPGSLLKWSPDNDWLFAATVDRVFRVWNCHQQWTTERWVCGPGGYVQTACWSPCGRFLLFVSSAEPILYRLQFVQQSLLSSSADEKEILPIADLNACSIDANRTLVGGPAQQLAWDPHGNYLVVTFKATNCIAVFRTFIQKFDLQISAAYYLSGETAAEHPSFICFQPLYEDNDRSVLTIAWSSGRIQYYAFD 466 Q9NRG9 Aladin AAAS 9606 None SL-0178 SL-0185 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}. UNIPROT Q9NRG9 UNIPROT Q5JB47 UNIPROT Q9NWI6 UNIPROT Q9UG19 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 OMIM 231550 OMIM 605378 DisGeNET 8086 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}. 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. A0A142I5B9 EBI-20626314 0.35 O95476 EBI-27115722 0.27 P01112 EBI-27045317 0.27 P0DTD1 EBI-27030072 0.35 P49790 EBI-11076796 0.35 P57740 EBI-11160436 0.35 P63279 EBI-11105225 0.35 Q14974 EBI-11115566 0.35 Q6PFD9 EBI-10994876 0.35 Q8BH74 EBI-10997196 0.35 Q8WUM0 EBI-11888192 0.37 Q96EE3 EBI-11086798 0.35 Q9ERU9 EBI-10999306 0.35 Q04864 EBI-3912907 0.37 Q9Y266 EBI-9484795 0.40 Q8IVD9 EBI-9484780 0.40 Q16659 EBI-12502733 0.35 Q8VE37 EBI-11043815 0.35 P63280 EBI-11044140 0.35 Q6NUS6 EBI-11368748 0.27 Q96GX1 EBI-11375285 0.27 Q6P5F9 EBI-11603310 0.35 Q8IWL3 EBI-13943458 0.35 P27824 EBI-16788621 0.27 Q9H1C4 EBI-21266770 0.35 P0DOF2 EBI-25603126 0.35 Q2TAZ0 EBI-26443127 0.35 P01116 EBI-27041844 0.27 P01111 EBI-27042293 0.27 Q8NCK7 EBI-27103180 0.35 Q13283 EBI-28955349 0.35 Q9UN86 EBI-28955513 0.35 Q9UM73 EBI-32719830 0.27 P29322 EBI-32721175 0.27 P08069 EBI-32722947 0.27 P06213 EBI-32723092 0.27 O15146 EBI-32724025 0.27 Q16288 EBI-32724526 0.27 GO:0005813 GO:0005829 GO:0016020 GO:0072686 GO:0005635 GO:0031965 GO:0005643 GO:0005654 GO:0005634 GO:0000922 GO:0009566 GO:0007612 GO:0001578 GO:0090307 GO:0051028 GO:0006913 GO:0015031 GO:0046822 Unknown UniProt Sequence Analysis MCSLGLFPPPPPRGQVTLYEHNNELVTGSSYESPPPDFRGQWINLPVLQLTKDPLKTPGRLDHGTRTAFIHHREQVWKRCINIWRDVGLFGVLNEIANSEEEVFEWVKTASGWALALCRWASSLHGSLFPHLSLRSEDLIAEFAQVTNWSSCCLRVFAWHPHTNKFAVALLDDSVRVYNASSTIVPSLKHRLQRNVASLAWKPLSASVLAVACQSCILIWTLDPTSLSTRPSSGCAQVLSHPGHTPVTSLAWAPSGGRLLSASPVDAAIRVWDVSTETCVPLPWFRGGGVTNLLWSPDGSKILATTPSAVFRVWEAQMWTCERWPTLSGRCQTGCWSPDGSRLLFTVLGEPLIYSLSFPERCGEGKGCVGGAKSATIVADLSETTIQTPDGEERLGGEAHSMVWDPSGERLAVLMKGKPRVQDGKPVILLFRTRNSPVFELLPCGIIQGEPGAQPQLITFHPSFNKGALLSVGWSTGRIAHIPLYFVNAQFPRFSPVLGRAQEPPAGGGGSIHDLPLFTETSPTSAPWDPLPGPPPVLPHSPHSHL 546 P58742 Aladin Aaas 10090 None SL-0178 SL-0185 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}. UNIPROT P58742 UNIPROT Q544M6 Pfam PF00400 PROSITE PS00678 PROSITE PS50294 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}. P45561 EBI-22091982 0.35 GO:0005813 GO:0005829 GO:0072686 GO:0005635 GO:0031965 GO:0005643 GO:0005654 GO:0000922 GO:0009566 GO:0007612 GO:0001578 GO:0090307 GO:0051028 GO:0006913 GO:0015031 Unknown UniProt Sequence Analysis MCSLGLFPPPPPRGQVTLYEHNNELVTGNSYESPPPDFRGQWINLPVLHLTKDPLKAPGRLDHGTRTAFIHHREQVWKRCINVWHDVGLFGVLNEIANSEEEVFEWVKTACSWALALCGRASSLHGSLFPHLSLRSEDLIAEFAQVTNWSSCCLRVFAWHPHTNKFAVALLDDSIRVYNANSTIVPSLKHRLQRNVAALAWKPLSASVLAVACQSCILIWTLDPTSLSTRPSSGCAQVLSHPGHTPVTSLAWAPNGGWLLSASPVDAVILVWDVSTETCVPLPWFRGGGVTNLLWSPDGSKVLATTPSAVFRVWEAQMWTCEAWPTLSGRCQTGCWSPDGNRLLFTVLGEALIYSLSFPERCGTGKGHVGGAKSATIVADLSETTIQTPDGEERLGGEAHSMVWDPSGERLAVLMKGNPQVQDGNPVILLFRTRNSPVFELLPCGIIQGEPGAQAQLITFHPSFNKGALLSVCWSTGRITHIPLYFVNAQFPRFSPVLGRAQEPPAGGGGSIHEVPLFTETSPTSAPWDPLPGQSSAQPHSPHSHL 546 Q39134 Amino AAP3 3702 None SL-0178 SL-0182 Cell membrane {ECO:0000269|PubMed:15361541}. Nucleus membrane {ECO:0000269|PubMed:15361541}. Endomembrane system {ECO:0000269|PubMed:15361541}. Note=Not found in vacuole membrane. UNIPROT Q39134 UNIPROT Q8LE75 Pfam PF01490 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}. F4JN35 EBI-4491128 0.37 Q94F58 EBI-4491136 0.37 Q39222 EBI-17000145 0.37 Q84N34 EBI-17000085 0.37 Q8LAA6 EBI-17000073 0.37 Q9SHI7 EBI-17000820 0.37 Q9LSP7 EBI-17000808 0.37 Q9FN48 EBI-17001567 0.37 Q9FNH6 EBI-17001531 0.37 P57752 EBI-17001519 0.37 F4I1Z0 EBI-17002230 0.37 Q9LPN5 EBI-17002206 0.37 Q9C7D7 EBI-17002194 0.37 Q8GW19 EBI-17001990 0.37 O04265 EBI-17002290 0.37 O64852 EBI-17002266 0.37 Q8RY98 EBI-17002869 0.37 Q94F23 EBI-17002821 0.37 Q9FJB4 EBI-17002761 0.37 Q93Z82 EBI-17002749 0.37 Q9LHA6 EBI-17002737 0.37 Q1JPM5 EBI-17002353 0.37 Q8L8T2 EBI-17002677 0.37 Q9LVU1 EBI-17002629 0.37 Q8L9S0 EBI-17002605 0.37 C0LGW2 EBI-17002581 0.37 Q9SVG8 EBI-17002557 0.37 Q9LMN8 EBI-17002545 0.37 Q9AST5 EBI-17002497 0.37 Q8H129 EBI-17002485 0.37 Q944J0 EBI-17002449 0.37 Q9C835 EBI-17002401 0.37 GO:0016021 GO:0016020 GO:0031965 GO:0005886 GO:0015171 GO:0015174 GO:0015293 GO:0003333 GO:0015802 GO:0006952 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVQNHQTVLAVDMPQTGGSKYLDDDGKNKRTGSVWTASAHIITAVIGSGVLSLAWATAQLGWLAGPVVMLLFSAVTYFTSSLLAACYRSGDPISGKRNYTYMDAVRSNLGGVKVTLCGIVQYLNIFGVAIGYTIASAISMMAIKRSNCFHKSGGKDPCHMNSNPYMIAFGLVQILFSQIPDFDQLWWLSILAAVMSFTYSSAGLALGIAQVVVNGKVKGSLTGISIGAVTETQKIWRTFQALGDIAFAYSYSIILIEIQDTVKSPPSEEKTMKKATLVSVSVTTMFYMLCGCMGYAAFGDLSPGNLLTGFGFYNPYWLLDIANAAIVIHLIGAYQVYCQPLFAFIEKQASIQFPDSEFIAKDIKIPIPGFKPLRLNVFRLIWRTVFVIITTVISMLLPFFNDVVGLLGALGFWPLTVYFPVEMYIAQKKIPRWSTRWVCLQVFSLGCLVVSIAAAAGSIAGVLLDLKSYKPFRSEY 476 Q8NE71 ATP-binding ABCF1 9606 None SL-0178 [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19570978}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19570978}. Nucleus envelope {ECO:0000269|PubMed:19570978}. UNIPROT Q8NE71 UNIPROT A2BF75 UNIPROT O14897 UNIPROT Q69YP6 PDB 5ZXD Pfam PF00005 PROSITE PS00211 PROSITE PS50893 OMIM 603429 DisGeNET 23 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}. Q13352 EBI-734862 0.00 Q96BK5 EBI-1069655 0.00 Q9NX58 EBI-1069968 0.00 Q9Y478 EBI-1078286 0.00 Q13573 EBI-7950968 0.35 Q99459 EBI-7954144 0.35 P51858 EBI-4409719 0.35 P02751 EBI-6285956 0.35 Q96SB4 EBI-6660614 0.44 Q92905 EBI-21325777 0.35 Q13617 EBI-21327106 0.35 O75807 EBI-9976880 0.35 Q16666 EBI-9995438 0.35 Q96FW1 EBI-10770028 0.35 P05412 EBI-11324725 0.35 A5YKK6 EBI-11005861 0.35 P35550 EBI-11044604 0.35 Q17RP2 EBI-11051402 0.35 Q99PL5 EBI-11066888 0.35 O00567 EBI-11069711 0.35 O75530 EBI-11070890 0.35 Q15006 EBI-11130215 0.35 Q6P5F9 EBI-11603310 0.35 Q68CZ1 EBI-12452141 0.35 O60341 EBI-16191678 0.35 Q14684 EBI-16686997 0.35 Q96JN8 EBI-16813376 0.35 P10636 EBI-20798291 0.35 Q6UW60 EBI-20905064 0.40 P05204 EBI-20907640 0.40 Q93079 EBI-20926618 0.40 P0C0S5 EBI-20926610 0.40 Q16695 EBI-20926626 0.40 Q5TID7 EBI-20928496 0.40 P14404 EBI-21026252 0.35 O96013 EBI-26962273 0.35 Q5S007 EBI-21360986 0.35 P03372 EBI-21301141 0.35 P17813 EBI-22197411 0.44 P16333 EBI-25385626 0.35 Q9UER7 EBI-25477958 0.35 P0DTC2 EBI-26495778 0.40 P0DTC9 EBI-26994159 0.35 P35226 EBI-27109494 0.35 Q8N488 EBI-27111302 0.35 P57078 EBI-28938584 0.35 GO:0005737 GO:0005829 GO:0016020 GO:0005635 GO:0005654 GO:0042788 GO:0005524 GO:0043022 GO:0003723 GO:0008494 GO:0008135 GO:0006954 GO:0045727 GO:0006412 GO:0006413 Unknown UniProt Sequence Analysis MPKAPKQQPPEPEWIGDGESTSPSDKVVKKGKKDKKIKKTFFEELAVEDKQAGEEEKVLKEKEQQQQQQQQQQKKKRDTRKGRRKKDVDDDGEEKELMERLKKLSVPTSDEEDEVPAPKPRGGKKTKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNRINKAVSEEQQPALKGKKGKEEKSKGKAKPQNKFAALDNEEEDKEEEIIKEKEPPKQGKEKAKKAEQGSEEEGEGEEEEEEGGESKADDPYAHLSKKEKKKLKKQMEYERQVASLKAANAAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQGDDTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEAPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFEDYKREVLEALGEVMVSRPRE 845 Q6P542 ATP-binding Abcf1 10090 None SL-0178 Cytoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NE71}. UNIPROT Q6P542 UNIPROT Q6NV71 Pfam PF00005 Pfam PF12848 PROSITE PS00211 PROSITE PS50893 Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity). {ECO:0000250}. P47713 EBI-6909752 0.35 Q9D2E2 EBI-6909752 0.35 Q921K2 EBI-6909752 0.35 Q8BIQ5 EBI-6909752 0.35 P14869 EBI-6909752 0.35 Q80ZH7 EBI-6909752 0.35 P34022 EBI-6909752 0.35 Q8BX17 EBI-6909752 0.35 Q8BG79 EBI-6909752 0.35 Q3UHD6 EBI-6909752 0.35 Q3TZX8 EBI-6909752 0.35 Q9EQU5 EBI-6909752 0.51 Q6P9Q4 EBI-6909752 0.35 Q9DCN2 EBI-6909752 0.35 O35309 EBI-6909752 0.35 Q3URQ0 EBI-6909752 0.35 Q3UL36 EBI-6909752 0.35 Q9JLI8 EBI-6909752 0.35 Q9D8C4 EBI-6909752 0.35 Q04690 EBI-6909752 0.35 A2BE28 EBI-6909752 0.35 P62918 EBI-6909752 0.35 P14148 EBI-6909752 0.35 P47911 EBI-6909752 0.35 O35381 EBI-6909752 0.35 P06151 EBI-6909752 0.35 P15092 EBI-6909752 0.46 Q99MD9 EBI-6909752 0.35 P36371 EBI-6909752 0.35 P30681 EBI-6909752 0.46 Q9QZ85 EBI-6909752 0.35 Q3UX10 EBI-6909752 0.35 Q7TPD0 EBI-6909752 0.35 D3Z7P3 EBI-6909752 0.35 Q9ESU7 EBI-6909752 0.35 B1ARD6 EBI-6909752 0.35 Q8CD98 EBI-6909752 0.35 Q9D2Y4 EBI-6909752 0.35 O35613 EBI-6909752 0.35 Q62036 EBI-6909752 0.35 Q9Z2X8 EBI-6909752 0.35 O08749 EBI-6909752 0.35 Q61735 EBI-6909752 0.35 Q8CCF0 EBI-6909752 0.35 Q99K01 EBI-6909752 0.35 Q9R099 EBI-6909752 0.35 Q9Z0E6 EBI-6909752 0.35 Q8BQ30 EBI-6909752 0.35 P70227 EBI-6909752 0.35 Q3UPN1 EBI-6909752 0.35 Q62293 EBI-6909752 0.35 P05064 EBI-6909752 0.35 Q9Z1M2 EBI-6909752 0.35 P60122 EBI-26898362 0.35 GO:0005737 GO:0005829 GO:0005635 GO:0005654 GO:0042788 GO:0005840 GO:0005524 GO:0043022 GO:0008494 GO:0045727 GO:0006413 Unknown UniProt Sequence Analysis MPKGPKQQPPEPEWIGDGEGTSPADKVVKKGKKDKKTKKTFFEELAVEDKQAGEEEKLQKEKEQQQQQQQQKKKRDTRKGRRKKDVDDDSDERVLMERLKQLSVPASDEEDEVPAPIPRGRKKAKGGNVFEALIQDDSEEEEEEEENRVLKPAKPEKNRINKAVAEEPPGLRSKKGKEEKSKGKAKSKPAAADSEGEEEEEDTAKEKEPPQQGKDRDKKEAEQGSGEEKEEKEGDLKANDPYANLSKKEKKKLKKQMDYERQVESLKAANAAENDFSVSQAEVSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLRLLEEERRLQGQLEQGDDTAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEVLTRKQQKCRRKNQDEESQEPPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQLHMEETPTEYLQRSFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKGAVIVVSHDARLITETNCQLWVVEEQGVSQIDGDFDDYKREVLEALGEVMVNRPRD 837 Q7YR37 ATP-binding ABCF1 9598 None SL-0178 Cytoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NE71}. UNIPROT Q7YR37 UNIPROT Q1XI20 Pfam PF00005 PROSITE PS00211 PROSITE PS50893 Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity). {ECO:0000250}. GO:0005737 GO:0005635 GO:0005654 GO:0042788 GO:0005524 GO:0043022 GO:0008494 GO:0045727 GO:0006413 Unknown UniProt Sequence Analysis MPKAPKQQPPEPEWIGDGESTSPSDKVVKKGKKDKKIKKTFFEELAVEDKQAGEEEKVLKEKEQQQQQQQVQQKKKRDTRKGRRKKDVDDDGEEKELMERLKKLSVPASDEEDEVPAPKPRGGKKTKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNRINKAVSEEQQPALKGKKGKEEKSKGKAKPQNKFAALDNEEEDKEEEIIKEKEPPKQGKEKAKKAEQMEYERQVASLKAANAAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVASRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQGDDTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEAPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFEDYKREVLEALGEVMVSRPRE 807 Q767L0 ATP-binding ABCF1 9823 None SL-0178 Cytoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NE71}. UNIPROT Q767L0 Pfam PF00005 PROSITE PS00211 PROSITE PS50893 Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity). {ECO:0000250}. GO:0005737 GO:0005635 GO:0005654 GO:0042788 GO:0005524 GO:0043022 GO:0008494 GO:0045727 GO:0006413 Unknown UniProt Sequence Analysis MPKGPKQQPPEPEWIGDGESTSPTDKVVKKGKKDKKTKKTFFEELAVEDRQAGEEEKVLKEKEQQQQHQQQQQKKKRDTRKGRRKKDVDDDDGEEKELMERLKKLSVPASDEEEEAPAPVPRGGKKNKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNRINKAVSQEQQPGPKGRKGKEEKSKGKAKPQNKFAALDDEEEQDEEEIKEKEPPKQGKEKAKKAEQMEYERQVASLKAANAAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQGDDTAADRLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEAPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTRGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFDDYKREVLEALGEVMVSRPRE 807 Q6MG08 ATP-binding Abcf1 10116 None SL-0178 Cytoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NE71}. UNIPROT Q6MG08 UNIPROT Q9ERQ2 Pfam PF00005 Pfam PF12848 PROSITE PS00211 PROSITE PS50893 Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:10931828}. P11362 EBI-22243924 0.35 P08069 EBI-22245613 0.35 O75096 EBI-22258804 0.35 GO:0005737 GO:0005635 GO:0005654 GO:0042788 GO:0005840 GO:0005524 GO:0043022 GO:0008494 GO:0045727 GO:0006412 GO:0006413 Unknown UniProt Sequence Analysis MPKGPKQQPPEPEWIGDGEGTSPADKVVKKGKKDKKTKKTFFEELAVEDKQAGEEEKLQKEKEQQQQQQQQKKKRDTRKGRRKKDVDDDDDGDERVLMERLKQLSVPASDEEDEVPVPVPRGRKKAKGGNVFEALIQDESEEEKEEEEEKPVLKPAKPEKNRINKAVAEEPPGLRNKKGKEEKSKGKAKNKPSATDSEGEDDEDMTKEKEPPRPGKDKDKKGAEQGSEEEKEEKEGEVKANDPYAHLSKKEKKKLKKQMDYERQVESLKAANAAENDFSVSQAEVSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLRLLEEEKRLQGQLEQGDDTAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEVLTRKQQKCRRKNQDEESQDPPELLKRPREYTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQLHMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFDDYKREVLEALGEVMVNRPRD 839 P00519 Tyrosine-protein ABL1 9606 None SL-0178 SL-0182 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. UNIPROT P00519 UNIPROT A3KFJ3 UNIPROT Q13869 UNIPROT Q13870 UNIPROT Q16133 UNIPROT Q17R61 UNIPROT Q45F09 PDB 1AB2 PDB 1AWO PDB 1BBZ PDB 1JU5 PDB 1OPL PDB 1ZZP PDB 2ABL PDB 2E2B PDB 2F4J PDB 2FO0 PDB 2G1T PDB 2G2F PDB 2G2H PDB 2G2I PDB 2GQG PDB 2HIW PDB 2HYY PDB 2HZ0 PDB 2HZ4 PDB 2HZI PDB 2O88 PDB 2V7A PDB 3CS9 PDB 3EG0 PDB 3EG1 PDB 3EG2 PDB 3EG3 PDB 3EGU PDB 3K2M PDB 3PYY PDB 3QRI PDB 3QRJ PDB 3QRK PDB 3T04 PDB 3UE4 PDB 3UYO PDB 4J9B PDB 4J9C PDB 4J9D PDB 4J9E PDB 4J9F PDB 4J9G PDB 4J9H PDB 4J9I PDB 4JJB PDB 4JJC PDB 4JJD PDB 4TWP PDB 4WA9 PDB 4XEY PDB 4YC8 PDB 4ZOG PDB 5DC0 PDB 5DC4 PDB 5DC9 PDB 5HU9 PDB 5MO4 PDB 5NP2 PDB 5OAZ PDB 6AMV PDB 6AMW PDB 6BL8 PDB 6NPE PDB 6NPU PDB 6NPV PDB 6XR6 PDB 6XR7 PDB 6XRG PDB 7CC2 PDB 7DT2 Pfam PF08919 Pfam PF07714 Pfam PF00017 Pfam PF00018 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 PROSITE PS50001 PROSITE PS50002 OMIM 189980 OMIM 608232 OMIM 617602 DisGeNET 25 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}. 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. Q92558 EBI-7380789 0.57 P08631 EBI-7296396 0.40 P05067 EBI-7810061 0.35 Q9XSK8 EBI-7047340 0.31 Q8CBW3 EBI-375573 0.40 Q8IZP0 EBI-375643 0.90 P22681 EBI-7392045 0.31 P62258 EBI-593829 0.53 P31946 EBI-593829 0.53 P63104 EBI-593829 0.62 P31947 EBI-593829 0.50 P61981 EBI-593829 0.74 Q04917 EBI-593829 0.64 Q9BX66 EBI-624110 0.52 Q15303 EBI-7872165 0.44 P04626 EBI-7881352 0.44 P00533 EBI-7887814 0.69 P21860 EBI-7896542 0.44 Q05655 EBI-8488876 0.40 Q07817 EBI-8488890 0.40 P78524 EBI-962642 0.40 Q09472 EBI-8504608 0.27 O60504 EBI-8565293 0.54 P15941 EBI-8597680 0.66 Q13315 EBI-1005980 0.70 P54274 EBI-1005991 0.40 Q13671 EBI-1102754 0.61 O15350 EBI-7807114 0.40 Q9NYB9 EBI-7088267 0.52 Q63767 EBI-1176858 0.44 P12931 EBI-7286298 0.59 P35222 EBI-7286271 0.54 O43900 EBI-1957060 0.40 Q9HCM9 EBI-1957076 0.40 Q9Y697 EBI-1957120 0.40 Q92918 EBI-1957132 0.57 P78345 EBI-1957144 0.40 Q8NFP9 EBI-1957156 0.40 O43390 EBI-1957168 0.40 O00254 EBI-1957180 0.40 Q9Y5Y3 EBI-1957192 0.40 Q9UL51 EBI-1957204 0.40 P78357 EBI-1957216 0.40 Q96NS5 EBI-1957228 0.40 Q07890 EBI-1957240 0.40 O94856 EBI-1957252 0.40 Q9NZV5 EBI-1957264 0.40 P49450 EBI-1957276 0.40 Q92874 EBI-1957288 0.40 Q7Z408 EBI-1957319 0.40 P98161 EBI-1957300 0.40 P43699 EBI-1957331 0.40 P50570 EBI-1957343 0.40 Q96GP6 EBI-1957367 0.40 Q14315 EBI-1957355 0.40 P31273 EBI-1957391 0.40 Q92664 EBI-1957379 0.40 Q9UJV9 EBI-1957403 0.40 O43493 EBI-1957415 0.40 Q15427 EBI-1957427 0.40 Q12979 EBI-1957439 0.40 Q13023 EBI-1957451 0.40 P15586 EBI-1957463 0.40 P23760 EBI-1957487 0.40 Q9UIF9 EBI-1957475 0.40 Q9UM47 EBI-1957499 0.40 Q13415 EBI-1957511 0.40 P06865 EBI-1957523 0.40 Q9H2X0 EBI-1957535 0.40 P51587 EBI-1957563 0.40 Q9UMN6 EBI-1957551 0.40 Q12947 EBI-1957575 0.40 Q9BYB0 EBI-1957587 0.40 Q9UBS5 EBI-1957599 0.40 Q8IZD9 EBI-1957611 0.40 P28340 EBI-1957623 0.40 Q9NYQ7 EBI-1957635 0.40 P78329 EBI-1957659 0.40 O43708 EBI-1957647 0.40 Q9H5I1 EBI-1957671 0.40 P46013 EBI-1957683 0.40 O76039 EBI-1957707 0.40 Q14008 EBI-1957719 0.40 Q13087 EBI-1957755 0.40 O14513 EBI-1957743 0.40 O95886 EBI-1957767 0.40 Q9Y5X2 EBI-1957793 0.40 P42566 EBI-1957805 0.40 Q96RL7 EBI-1957817 0.40 Q9UMY4 EBI-1957829 0.40 Q9C0E4 EBI-1957853 0.40 Q15036 EBI-1957841 0.40 P34820 EBI-1957877 0.40 P30260 EBI-1957865 0.40 O75751 EBI-1957889 0.40 Q86UR5 EBI-1957906 0.40 Q9NZQ3 EBI-1957930 0.40 P26992 EBI-1957918 0.40 P50851 EBI-1957942 0.40 O76081 EBI-1957956 0.40 Q92988 EBI-1957968 0.40 Q96PC5 EBI-1957980 0.40 Q9BQ89 EBI-1958016 0.40 P20810 EBI-1957992 0.40 Q9H1R2 EBI-1958004 0.40 P02765 EBI-1958028 0.40 Q9Y3S1 EBI-1958040 0.40 Q13905 EBI-1958052 0.66 Q9UQ16 EBI-1958064 0.40 Q9Y5K6 EBI-1958076 0.40 O15255 EBI-1958088 0.40 Q8TB24 EBI-1958100 0.40 O95157 EBI-1958112 0.40 O43281 EBI-1958124 0.40 O15085 EBI-1958148 0.40 P08047 EBI-1958160 0.40 P98164 EBI-1958172 0.40 Q86SG6 EBI-1958184 0.40 Q9H0X9 EBI-1958196 0.40 Q9NQC3 EBI-1958208 0.40 O60244 EBI-1958225 0.40 Q9UK85 EBI-1958237 0.40 Q9BXM0 EBI-1958249 0.40 O43918 EBI-1958261 0.40 Q96AC6 EBI-1958273 0.40 Q9HCQ7 EBI-1958285 0.40 O15056 EBI-1958297 0.40 P32239 EBI-1958309 0.40 Q15027 EBI-1958333 0.40 O14490 EBI-1958369 0.40 Q8WX92 EBI-1958345 0.40 Q9NUR3 EBI-1958357 0.40 P13671 EBI-1958381 0.40 P42167 EBI-1958393 0.40 Q99572 EBI-1958405 0.40 O15117 EBI-1958417 0.40 Q14767 EBI-1958429 0.40 Q9NQ76 EBI-1958441 0.40 Q9Y2J2 EBI-1958453 0.40 O60493 EBI-1958465 0.40 Q9UHL9 EBI-1958477 0.40 Q05193 EBI-1958489 0.40 Q9ULH1 EBI-1958501 0.40 Q9UN86 EBI-1958513 0.40 P49916 EBI-1958525 0.40 Q9P1A6 EBI-1958537 0.40 Q9Y2H0 EBI-1958551 0.40 Q9BZM3 EBI-1958563 0.40 Q9UJT2 EBI-1958575 0.40 P12018 EBI-1958587 0.40 Q9ULD4 EBI-1958599 0.40 Q9Y3Q4 EBI-1958635 0.40 Q9NRJ4 EBI-1958611 0.40 O60721 EBI-1958623 0.40 O75326 EBI-1958647 0.40 Q08209 EBI-1958680 0.40 Q14999 EBI-1958704 0.40 Q9BWW9 EBI-1958716 0.40 Q8TAS1 EBI-1958728 0.40 P21333 EBI-1958740 0.40 P29074 EBI-1958764 0.40 Q9UN72 EBI-1958776 0.40 P52803 EBI-1958788 0.40 P20774 EBI-1958800 0.40 Q99259 EBI-1958816 0.40 P46108 EBI-1959666 0.67 P06241 EBI-1961835 0.40 P62993 EBI-1963179 0.40 P16333 EBI-1967005 0.40 P27986 EBI-1969653 0.40 P19174 EBI-1970973 0.40 P18031 EBI-8174353 0.44 Q06609 EBI-6995587 0.40 Q15464 EBI-7100971 0.52 O43196 EBI-7989580 0.82 O15457 EBI-7989665 0.37 P46109 EBI-8046579 0.67 Q06830 EBI-7319754 0.37 P38398 EBI-7319796 0.37 Q9Y3L3 EBI-7319868 0.40 P70218 EBI-8670837 0.37 Q13444 EBI-8061278 0.40 Q71SY5 EBI-8595983 0.44 O35158 EBI-7016759 0.58 Q4KMG0 EBI-7016887 0.52 P05107 EBI-8576224 0.52 Q9Y4G6 EBI-8576260 0.60 P15498 EBI-8576308 0.60 P04370 EBI-7727798 0.40 Q7Z434 EBI-7599276 0.59 P11387 EBI-7328831 0.60 P35326 EBI-7743121 0.44 Q9QUM7 EBI-7004732 0.37 P55194 EBI-7094170 0.44 Q64010 EBI-2642542 0.35 P97465 EBI-2642676 0.35 Q38SD2 EBI-2906661 0.59 Q04929 EBI-5278171 0.44 O95758 EBI-7850130 0.35 P78362 EBI-6657338 0.44 P08238 EBI-6423900 0.40 Q99497 EBI-8544196 0.44 P37840 EBI-27101585 0.60 O55042 EBI-9212687 0.27 P10275 EBI-9451938 0.44 P10721 EBI-9467046 0.44 P14618 EBI-9354876 0.44 Q5S007 EBI-9659734 0.44 Q15637 EBI-11299755 0.00 P53999 EBI-10101341 0.35 P26641 EBI-10101341 0.35 Q9Y295 EBI-10101341 0.35 Q01844 EBI-10101341 0.35 P63220 EBI-10101341 0.35 Q12906 EBI-10101341 0.35 P52272 EBI-10101341 0.35 P35637 EBI-10101341 0.35 Q9BY44 EBI-10101341 0.35 P27348 EBI-10101341 0.35 P05386 EBI-10101341 0.35 P61604 EBI-10101341 0.35 P17844 EBI-10101379 0.35 P12956 EBI-10101379 0.35 Q96AG4 EBI-10101379 0.35 Q07065 EBI-10101379 0.35 Q6VGS8 EBI-11733617 0.35 Q8BTZ4 EBI-11003821 0.35 Q8BL66 EBI-11027295 0.35 Q1H9T6 EBI-11104278 0.35 Q15323 EBI-24307132 0.56 P48165 EBI-24796696 0.56 Q03135 EBI-15875070 0.44 P42229 EBI-15965981 0.44 P53355 EBI-20588441 0.44 P36888 EBI-20639282 0.44 Q03468 EBI-21017040 0.66 O14672 EBI-21223666 0.54 Q9BY11 EBI-21376479 0.00 P51692 EBI-25432371 0.56 P60006 EBI-27039580 0.37 O14641 EBI-27039584 0.37 Q9H4M7 EBI-27039588 0.37 Q8IYX8 EBI-27039592 0.37 Q8TAP6 EBI-27039596 0.37 O14595 EBI-27039600 0.37 O94818 EBI-27039604 0.37 P46531 EBI-27039608 0.37 P56279 EBI-27039612 0.37 Q96GJ1 EBI-27039616 0.37 P42684 EBI-27039620 0.37 Q13619 EBI-30863570 0.35 Q13620 EBI-30863806 0.35 Q06418 EBI-32719716 0.35 GO:0015629 GO:0005737 GO:0005829 GO:0030425 GO:0005783 GO:0030426 GO:0005739 GO:0043025 GO:0016604 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0098794 GO:0032991 GO:0001726 GO:0051015 GO:0003785 GO:0005524 GO:0000405 GO:0070097 GO:0003677 GO:0046875 GO:0000400 GO:0016301 GO:0000287 GO:0030145 GO:0051019 GO:0038191 GO:0004515 GO:0004715 GO:0001784 GO:0070064 GO:0008022 GO:0004672 GO:0005080 GO:0043621 GO:0004713 GO:1990837 GO:0042169 GO:0017124 GO:0019905 GO:0003713 GO:0030036 GO:0030041 GO:0050798 GO:1990051 GO:0046632 GO:0008306 GO:0006914 GO:0002322 GO:0050853 GO:0001922 GO:0060020 GO:0030509 GO:0060038 GO:0098609 GO:0006974 GO:1903351 GO:0070301 GO:0071222 GO:0034599 GO:0071560 GO:0090398 GO:0021587 GO:1904157 GO:0071103 GO:0006975 GO:0006897 GO:0043542 GO:0007173 GO:0070371 GO:0051649 GO:0038096 GO:0007249 GO:0007229 GO:0008630 GO:0030035 GO:0006298 GO:0051882 GO:0000278 GO:0051450 GO:0030514 GO:0022408 GO:2000773 GO:2000352 GO:0070373 GO:0043124 GO:1900272 GO:0045930 GO:1900275 GO:0071901 GO:0051444 GO:0001843 GO:0060563 GO:0050885 GO:0070997 GO:0030182 GO:0038189 GO:0038083 GO:0018108 GO:0035791 GO:1903210 GO:2000251 GO:1904531 GO:0043065 GO:1905555 GO:0090050 GO:0007204 GO:1900006 GO:0010595 GO:0070374 GO:1903905 GO:1903055 GO:0048146 GO:0051894 GO:1901300 GO:0043123 GO:0032729 GO:0032743 GO:1904528 GO:0045931 GO:0043525 GO:0033690 GO:0051353 GO:0050731 GO:0001934 GO:0051281 GO:0051496 GO:1900026 GO:2000406 GO:0045944 GO:0045907 GO:2000096 GO:0009791 GO:0046777 GO:1904518 GO:0036211 GO:0006468 GO:0032956 GO:2000249 GO:0042981 GO:0010506 GO:0030516 GO:0032489 GO:0030155 GO:0051726 GO:2000145 GO:0006355 GO:0030100 GO:1902036 GO:0031113 GO:1905244 GO:2001020 GO:0045580 GO:0034976 GO:0071871 GO:0006979 GO:0009410 GO:0042770 GO:0048536 GO:0034446 GO:0050852 GO:0048538 GO:0002333 Lipid-Anchored UniProt Sequence Analysis MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR 1130 Q07912 Activated TNK2 9606 None SL-0198 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}. UNIPROT Q07912 UNIPROT Q6ZMQ0 UNIPROT Q8N6U7 UNIPROT Q96H59 PDB 1CF4 PDB 1U46 PDB 1U4D PDB 1U54 PDB 3EQP PDB 3EQR PDB 4EWH PDB 4HZR PDB 4HZS PDB 4ID7 PDB 5ZXB PDB 6VQM PDB 7KP6 Pfam PF09027 Pfam PF11555 Pfam PF07714 Pfam PF14604 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 PROSITE PS50002 OMIM 606994 DisGeNET 10188 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}. O14976 EBI-11150908 0.35 O43426 EBI-7809036 0.27 P00533 EBI-702075 0.35 P60953 EBI-603486 0.59 Q9Y5X1 EBI-7808593 0.54 P62993 EBI-7808665 0.66 P16333 EBI-7808721 0.59 Q00610 EBI-7808962 0.79 P51690 EBI-736241 0.00 Q969R8 EBI-736244 0.00 Q8N431 EBI-736247 0.00 Q02543 EBI-736250 0.00 Q53EL9 EBI-736253 0.00 Q13243 EBI-736256 0.00 Q9UEU0 EBI-736259 0.00 P08575 EBI-2257200 0.00 Q12913 EBI-2265049 0.00 Q05209 EBI-2266438 0.00 P56945 EBI-7040520 0.52 P46108 EBI-7040708 0.40 Q07912 EBI-8071904 0.59 Q13177 EBI-8143865 0.44 Q8IUQ4 EBI-3934992 0.37 P08238 EBI-6424981 0.56 Q8WXH5 EBI-10692509 0.49 Q96JZ2 EBI-10697958 0.37 O60880 EBI-10187478 0.56 P07902 EBI-10195306 0.56 P29972 EBI-10205037 0.56 Q7Z3S9 EBI-10224749 0.56 Q9HC98 EBI-10310684 0.56 G3X972 EBI-11079358 0.35 Q9NYZ3 EBI-11081743 0.35 O95817 EBI-11135110 0.35 Q9BQC3 EBI-24322875 0.56 A8MQ03 EBI-24423586 0.56 O14796 EBI-24542932 0.56 Q92569 EBI-24656100 0.56 O43639 EBI-21521290 0.35 Q58FF7 EBI-21831391 0.35 Q16543 EBI-21831391 0.35 P05161 EBI-21831391 0.35 P10275 EBI-15636365 0.40 P16749 EBI-15832981 0.41 Q01968 EBI-16412116 0.35 P85968 EBI-22241111 0.35 B2RZ33 EBI-22241111 0.35 D4A3M8 EBI-22241111 0.35 P97573 EBI-22241127 0.35 O35244 EBI-22241127 0.35 Q6UY14 EBI-22141818 0.37 Q7Z7F7 EBI-25377008 0.35 P07900 EBI-25377008 0.35 P10809 EBI-25377008 0.35 P17987 EBI-25377008 0.35 P40227 EBI-25377008 0.35 P48643 EBI-25377008 0.35 P50991 EBI-25377008 0.35 P78371 EBI-25377008 0.35 P05141 EBI-25388582 0.35 P49368 EBI-25388582 0.35 P49411 EBI-25388582 0.35 P50990 EBI-25388582 0.35 Q58FF8 EBI-25388582 0.35 O43264 EBI-28939183 0.35 Q9Y262 EBI-28939183 0.35 Q9BZD4 EBI-28939183 0.35 Q2NL82 EBI-28939183 0.35 Q13330 EBI-28939183 0.35 P56134 EBI-28939183 0.35 P25205 EBI-28939183 0.35 O15075 EBI-28939183 0.35 P46937 EBI-30846635 0.44 P07947 EBI-30849214 0.44 GO:0005912 GO:0005905 GO:0030136 GO:0097268 GO:0005737 GO:0030659 GO:0005829 GO:0005768 GO:0031234 GO:0070436 GO:0043231 GO:0016020 GO:0005634 GO:0048471 GO:0005886 GO:0005524 GO:0005154 GO:0005095 GO:0042802 GO:0046872 GO:0004715 GO:0106310 GO:0004674 GO:0004712 GO:0004713 GO:0005102 GO:0031625 GO:0050699 GO:0030154 GO:0007166 GO:0006897 GO:0045087 GO:0016310 GO:0050731 GO:2000369 GO:0007264 GO:0007169 Peripheral UniProt Sequence Analysis MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNVTRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKALCKRKSWMSKVFSGKRLEAEFPPHHSQSTFRKTSPAPGGPAGEGPLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPDRIDELYLGNPMDPPDLLSVELSTSRPPQHLGGVKKPTYDPVSEDQDPLSSDFKRLGLRKPGLPRGLWLAKPSARVPGTKASRGSGAEVTLIDFGEEPVVPALRPCAPSLAQLAMDACSLLDETPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEICSINSTLVGAGVPAGPSQGQTNYAFVPEQARPPPPLEDNLFLPPQGGGKPPSSAQTAEIFQALQQECMRQLQAPAGSPAPSPSPGGDDKPQVPPRVPIPPRPTRPHVQLSPAPPGEEETSQWPGPASPPRVPPREPLSPQGSRTPSPLVPPGSSPLPPRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGKKVSSTHYYLLPERPSYLERYQRFLREAQSPEEPTPLPVPLLLPPPSTPAPAAPTATVRPMPQAALDPKANFSTNNSNPGARPPPPRATARLPQRGCPGDGPEAGRPADKIQMAMVHGVTTEECQAALQCHGWSVQRAAQYLKVEQLFGLGLRPRGECHKVLEMFDWNLEQAGCHLLGSWGPAHHKR 1038 A5D7D1 Alpha-actinin-4 ACTN4 9913 None SL-0198 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}. UNIPROT A5D7D1 Pfam PF00307 Pfam PF08726 Pfam PF00435 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS00018 PROSITE PS50222 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}. A6QLL8 EBI-1220272 0.35 P20909 EBI-5281033 0.35 GO:0070161 GO:0005737 GO:0005856 GO:0005634 GO:0048471 GO:1990904 GO:0003779 GO:0005509 GO:0030374 GO:0035357 GO:0015031 GO:0048384 Unknown UniProt Sequence Analysis MVDYHAANQSYQYGPSSGSNGAGGGGTMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANIVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL 911 Q90734 Alpha-actinin-4 ACTN4 9031 None SL-0198 Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. UNIPROT Q90734 Pfam PF00307 Pfam PF08726 Pfam PF00435 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS50222 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}. GO:0070161 GO:0030054 GO:0042995 GO:0030864 GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0001725 GO:0030018 GO:0051015 GO:0005509 GO:0030374 GO:0030036 GO:0055001 GO:0035357 GO:0015031 GO:1903506 GO:0048384 Unknown UniProt Sequence Analysis MVDYHSAGQPYPYGGNGPGPNGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVNVVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRSPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINTGWQHLEQAEKGYEEWLLNEIRRLEPLDHLAEKFRQKASIHEAWTEGKEAMLKQKDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDVLGSLTHSRREALEKTEKQLETIDELHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLIAAHDQFKATLPDADREREAILGIQREAQRIADLHSIKLSGNNPYTSVTPQVINSKWERVQQLVPTRDRALQDEQSRQQCNERLRRQFAGQANIVGPWMQTKMEEIGRISIEMHGTLEDQLQHLKHYEQSIVDYKPNLELLEHEHQLVEEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHCGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSLVDPNGSGSVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNYITAEELRRELPPEQAEYCIARMAPYRGPDAAPGALDYKSFSTALYGESDL 904 O43707 Alpha-actinin-4 ACTN4 9606 None SL-0198 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}. UNIPROT O43707 UNIPROT A4K467 UNIPROT D6PXK4 UNIPROT O76048 PDB 1WLX PDB 1YDI PDB 2R0O PDB 6O31 PDB 6OA6 Pfam PF00307 Pfam PF08726 Pfam PF00435 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS00018 PROSITE PS50222 OMIM 603278 OMIM 604638 DisGeNET 81 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}. 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. P62993 EBI-350217 0.35 Q99759 EBI-362163 0.00 Q9Y572 EBI-363781 0.00 Q9NPC6 EBI-756484 0.93 Q9NP98 EBI-759703 0.37 O00151 EBI-760309 0.67 P12830 EBI-727492 0.50 P38432 EBI-952558 0.00 Q9NZJ4 EBI-953488 0.00 P63104 EBI-7197640 0.40 Q07157 EBI-1103214 0.60 P35222 EBI-1537638 0.68 P42771 EBI-1641665 0.35 Q69139 EBI-2623676 0.37 Q8TDR0 EBI-2650416 0.35 P29474 EBI-3385333 0.37 P42224 EBI-3451685 0.00 O15265 EBI-3866243 0.37 Q9NUX5 EBI-3925821 0.37 P52292 EBI-3944055 0.37 Q13164 EBI-3944105 0.37 P42677 EBI-3944125 0.37 P10599 EBI-3944155 0.44 Q8WZ42 EBI-5665670 0.00 Q3UQN2 EBI-6097080 0.35 P19320 EBI-6191076 0.53 P02751 EBI-6285956 0.35 P04792 EBI-6870912 0.37 P46940 EBI-6897999 0.60 Q5L4H4 EBI-9512219 0.59 P03466 EBI-9512541 0.40 C3W6D7 EBI-9513951 0.40 Q91U50 EBI-9514006 0.40 Q6DPG0 EBI-9513984 0.40 B2BU63 EBI-9513930 0.40 C9S3S8 EBI-9513909 0.40 Q8JR21 EBI-9514040 0.27 Q38SD2 EBI-9656528 0.35 O41957 EBI-9640710 0.37 Q92754 EBI-9680045 0.37 P05549 EBI-9679922 0.37 P00533 EBI-9689686 0.55 P67809 EBI-9985228 0.35 A8K571 EBI-10174341 0.56 B2R8Y4 EBI-10175592 0.56 P03372 EBI-9996267 0.35 Q92731 EBI-9996422 0.35 Q9UH99 EBI-10761374 0.35 P35579 EBI-11004631 0.35 Q9NQW6 EBI-11009421 0.35 Q9CQ49 EBI-11022137 0.35 Q60634 EBI-11025478 0.35 Q92614 EBI-11030093 0.35 O00159 EBI-11030803 0.35 Q96H55 EBI-11031416 0.35 P21333 EBI-11038784 0.35 P60710 EBI-11045267 0.35 Q80X90 EBI-11053320 0.35 Q9ERG0 EBI-11054044 0.35 Q9UHB6 EBI-11058729 0.35 Q9D6P8 EBI-11062262 0.35 Q9JHJ0 EBI-11063313 0.35 P58771 EBI-11063826 0.35 Q9WUM4 EBI-11065690 0.35 Q9P2K5 EBI-11077096 0.35 Q16643 EBI-11080402 0.35 O75182 EBI-11085017 0.35 Q8N3V7 EBI-11086992 0.35 Q15691 EBI-11091481 0.35 Q8VDD5 EBI-11092730 0.35 Q9WTI7 EBI-11093786 0.35 Q61879 EBI-11099615 0.35 Q9NQX4 EBI-11100755 0.35 Q9NR12 EBI-11105742 0.53 P47755 EBI-11117728 0.35 P62140 EBI-11142496 0.35 Q15599 EBI-12452194 0.51 Q14160 EBI-11794686 0.40 Q9NWQ9 EBI-24303215 0.56 Q8IY33 EBI-24365113 0.56 Q08043 EBI-24497993 0.56 Q8TBB1 EBI-24475492 0.56 O94875 EBI-12689671 0.60 O60294 EBI-12697987 0.56 P50222 EBI-12702268 0.56 O15297 EBI-14024588 0.35 Q6IQ23 EBI-16398399 0.35 P10276 EBI-15971728 0.52 P37231 EBI-15971696 0.40 O43707 EBI-15971763 0.40 P09622 EBI-20304669 0.35 O00429 EBI-20305770 0.35 P08559 EBI-20306509 0.35 P00441 EBI-20307497 0.35 P69968 EBI-20817323 0.37 Q8D0P1 EBI-20818271 0.37 P46013 EBI-20562326 0.35 P35408 EBI-20811214 0.37 P51957 EBI-20721387 0.35 A2A935 EBI-21024514 0.35 P14404 EBI-21026252 0.35 P61981 EBI-26966879 0.35 Q5S007 EBI-21360986 0.35 P04156 EBI-21014477 0.35 P13569 EBI-25416349 0.35 P12931 EBI-25384369 0.35 Q8N5H7 EBI-25387159 0.35 P0DOF2 EBI-25603126 0.35 Q9H3R0 EBI-25479978 0.35 P83105 EBI-25745135 0.35 Q13363 EBI-27044482 0.35 Q99592 EBI-27093179 0.35 P53355 EBI-28938354 0.35 Q05513 EBI-28938998 0.35 Q86V86 EBI-28942203 0.35 Q8TEA7 EBI-28943849 0.35 Q8TF76 EBI-28943924 0.35 Q9Y2U5 EBI-28947216 0.35 Q8WYL5 EBI-27116808 0.27 GO:0015629 GO:0030054 GO:0042995 GO:0030864 GO:0005737 GO:0005829 GO:0070062 GO:0005576 GO:0005615 GO:0005925 GO:0043005 GO:0016604 GO:0005634 GO:0048471 GO:0005886 GO:0031093 GO:0032991 GO:0031143 GO:1990904 GO:0001725 GO:0030018 GO:0003779 GO:0051015 GO:0005509 GO:0031490 GO:0005178 GO:0016922 GO:0030374 GO:0042974 GO:0001882 GO:0042803 GO:0047485 GO:0003723 GO:0000977 GO:0003713 GO:0044325 GO:0030036 GO:0055001 GO:1900025 GO:0035357 GO:0030335 GO:1901224 GO:0032417 GO:0015031 GO:0042981 GO:1903506 GO:0001666 GO:0048384 GO:0033209 GO:0030050 Unknown UniProt Sequence Analysis MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL 911 P57780 Alpha-actinin-4 Actn4 10090 None SL-0198 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}. UNIPROT P57780 Pfam PF00307 Pfam PF08726 Pfam PF00435 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS00018 PROSITE PS50222 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}. P39447 EBI-1103365 0.54 O08601 EBI-1183624 0.40 P09103 EBI-1183624 0.40 Q62468 EBI-1183624 0.40 Q3TN34 EBI-1779866 0.64 P51153 EBI-1780138 0.35 Q62108 EBI-2307988 0.35 O35400 EBI-8174161 0.35 Q8BP00 EBI-4282064 0.35 Q3UHD9 EBI-16750831 0.35 O08749 EBI-20313604 0.35 Q8K1M6 EBI-20313833 0.35 P35486 EBI-20313969 0.35 P08228 EBI-20314123 0.35 P51637 EBI-20565496 0.35 P97493 EBI-26500418 0.35 Q4ACU6 EBI-26573447 0.35 A0A0F6B063 EBI-27034862 0.35 Q8K4E0 EBI-27076664 0.51 Q9QWI6 EBI-27100778 0.35 GO:0015629 GO:0030054 GO:0042995 GO:0005911 GO:0030864 GO:0030863 GO:0005737 GO:0005829 GO:0005925 GO:0043005 GO:0016604 GO:0005634 GO:0048471 GO:0005886 GO:0032991 GO:0031143 GO:1990904 GO:0001725 GO:0030018 GO:0051015 GO:0005509 GO:0031490 GO:0016922 GO:0030374 GO:0042974 GO:0001882 GO:0042803 GO:0047485 GO:0044877 GO:0000977 GO:0005200 GO:0003713 GO:0044325 GO:0030036 GO:0051017 GO:0070830 GO:0032835 GO:0055001 GO:1900025 GO:0035357 GO:0090521 GO:0030335 GO:1901224 GO:0048549 GO:1902396 GO:0015031 GO:0042981 GO:1903506 GO:0048384 GO:0033209 GO:0030050 Unknown UniProt Sequence Analysis MVDYHAANQAYQYGPNSGGGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKQRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANMVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPSLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAAPGALDYKSFSTALYGESDL 912 Q5RCS6 Alpha-actinin-4 ACTN4 9601 None SL-0198 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}. UNIPROT Q5RCS6 Pfam PF00307 Pfam PF08726 Pfam PF00435 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS00018 PROSITE PS50222 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}. GO:0070161 GO:0005737 GO:0005856 GO:0005634 GO:0048471 GO:1990904 GO:0003779 GO:0005509 GO:0030374 GO:0035357 GO:0015031 GO:0048384 Unknown UniProt Sequence Analysis MVDYHAASQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICRVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL 911 Q9QXQ0 Alpha-actinin-4 Actn4 10116 None SL-0198 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}. UNIPROT Q9QXQ0 UNIPROT Q6P786 Pfam PF00307 Pfam PF08726 Pfam PF00435 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS00018 PROSITE PS50222 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}. P19357 EBI-921030 0.54 P21708 EBI-7617257 0.35 P54645 EBI-16399805 0.35 P80386 EBI-16400563 0.35 GO:0015629 GO:0030054 GO:0042995 GO:0005911 GO:0030864 GO:0030863 GO:0005737 GO:0005829 GO:0005925 GO:0043005 GO:0016604 GO:0005634 GO:0048471 GO:0005886 GO:0032991 GO:0031143 GO:1990904 GO:0001725 GO:0030018 GO:0051015 GO:0005509 GO:0031490 GO:0016922 GO:0030374 GO:0042974 GO:0001882 GO:0042803 GO:0047485 GO:0044877 GO:0000977 GO:0003713 GO:0044325 GO:0030036 GO:0051017 GO:0070830 GO:0055001 GO:1900025 GO:0035357 GO:0030335 GO:1901224 GO:0048549 GO:1902396 GO:0015031 GO:0042981 GO:1903506 GO:0001666 GO:0048384 GO:0033209 GO:0030050 Unknown UniProt Sequence Analysis MVDYHAANQAYQYGPSSGGNGTGGGGGMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTSVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANMVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHLRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAAPGALDYKSFSTALYGESDL 911 O76329 Interaptin abpD 44689 None SL-0178 SL-0182 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. UNIPROT O76329 UNIPROT Q54KE8 Pfam PF00307 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 May function as linker between cellular membranes and the actin cytoskeleton. Required for normal development of fruiting bodies. {ECO:0000269|PubMed:10704840}. Q54CH1 EBI-922911 0.40 Q55FK4 EBI-922911 0.40 Q55CS9 EBI-922911 0.40 Q23858 EBI-922911 0.40 P34122 EBI-922911 0.40 P25870 EBI-922911 0.40 P34121 EBI-922911 0.40 Q54HL0 EBI-922911 0.40 Q54KG1 EBI-922911 0.40 Q54T81 EBI-922911 0.40 Q54NB6 EBI-922911 0.40 P46800 EBI-922911 0.40 Q552M5 EBI-922911 0.40 Q557E0 EBI-922911 0.40 P54651 EBI-922911 0.40 Q55GF9 EBI-922911 0.40 Q6RZZ9 EBI-922911 0.40 Q54BF6 EBI-922911 0.40 P34118 EBI-922911 0.40 Q86HW7 EBI-922911 0.40 Q869Y7 EBI-922911 0.40 Q23921 EBI-922911 0.40 Q54JM5 EBI-922911 0.40 Q54BH4 EBI-922911 0.40 Q54BP1 EBI-922911 0.40 Q54DL5 EBI-922911 0.40 Q54FU0 EBI-922911 0.40 Q54G01 EBI-922911 0.40 Q54G31 EBI-922911 0.40 Q54GS4 EBI-922911 0.40 Q54GY1 EBI-922911 0.40 Q54H23 EBI-922911 0.40 Q54I73 EBI-922911 0.40 Q54NB4 EBI-922911 0.40 Q54R55 EBI-922911 0.40 Q54RZ4 EBI-922911 0.40 Q54SP3 EBI-922911 0.40 Q54TQ6 EBI-922911 0.40 Q54U97 EBI-922911 0.40 Q54U98 EBI-922911 0.40 Q54VJ7 EBI-922911 0.40 Q54VQ1 EBI-922911 0.40 Q54W02 EBI-922911 0.40 Q54XP9 EBI-922911 0.40 Q556V8 EBI-922911 0.40 Q55CE3 EBI-922911 0.40 Q55CZ0 EBI-922911 0.40 Q55DZ5 EBI-922911 0.40 Q55F82 EBI-922911 0.40 Q55F84 EBI-922911 0.40 Q55GC0 EBI-922911 0.40 Q55GC5 EBI-922911 0.40 Q75JY8 EBI-922911 0.40 P33519 EBI-922911 0.40 Q86K01 EBI-922911 0.40 Q559R0 EBI-922911 0.40 P52285 EBI-922911 0.40 Q95ZG4 EBI-922911 0.40 P32255 EBI-922911 0.40 P32256 EBI-922911 0.40 Q55AR3 EBI-922911 0.40 Q54TH8 EBI-922911 0.40 Q54LP7 EBI-922911 0.40 Q54WN5 EBI-922911 0.40 Q55EX9 EBI-922911 0.40 GO:0005789 GO:0032580 GO:0016021 GO:0005815 GO:0005635 GO:0031965 GO:0042175 GO:0003779 GO:0098609 GO:0030587 GO:0009847 Transmembrane UniProt Sequence Analysis MEHSTPLNEEIVHKKNDENWVIAQKKVFTNWCNIFLNQRSQKIEDLETDLYDGILLGSLLEILSGKNVILSKCKQLKTRLHYINNLNFSLKFIGDEGLRLVGVASEDITDGNLKLILGLVWTLILRYQIQSMQNSKSSQQNLHSSTKPSELMLNWVKSQISDYGHHIKDLTTSFQNGLLFCALVHKLVPEKLDYKSLSESDSLGNLTLAFEVANKELGIPSILDPHDIITTPDELSILTYISLFPKVYQQTLEPLNNNNNISPSLSSSSSSLLNTPNKRNSIQLSKSTSFEQQNQQQQQQNLLSPNSYRNSISFSKSPSFEGSQSTGSSRSISPISSPIKNSTTGNSNLSKSTSFEKIEASNTTNNNTIIIAEESRVIEKIVEKIIEVEKIVEVEKIVEVEKIVEVEKIVEVEKIVKVDDIEKLTNLQDQLTEQQQQYQEKSLKLVNLELELQEKSNQLVDKSNQLSTMQATNSELMEKIGGLMNDLTDIPTQDIKEKDEIIANLKIESEKNLKCFQDDFNALQSRYSLTIEQTSQLQDRIKQLINELQERDDKFIEFTNSSNQSLADNQRVIDQLTNEKQSITLQLQDQQDIKEKEFQFEKQQLLSQIDSITTNIQEYQDKFNNLQQEFNTQQTLNQQETHRLTQQLYQINTDYNEKQTQLQSEIKDNQTINEQLNKQLSEKDKEIEKLSNQQEQQQDEKINNLLLEIKEKDCLIERINQQLLENIDLNSKYQQLLLEFENFKLNSSKEKENQLNELQSKQDERFNQLNDEKLEKEKQLQSIEDEFNQYKQQQLSSNSNIDQQLQSTIIELSELKEQKELNDSKLIEKEKQLQQLQQEFDQLNEKNQKDHQDQLELLEKQLKQLQQEYDQLNETNQSIENQLNQQNLINKENLNEKEQELLKLQNQLNQQIEKIQFDQQEFSKQNSINIELVNEKNEKLIQLQQDYDQLKQQNRSNDEKDENDLIEKENQLKSIQNELNQLIEKNESDHKEQQLKQQSIENDLIEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLIEKNQFDQKEQQLKQQSIENDLFEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLIEKNESDQKEQQLKQQSIENDLIEKENQIQQLQLQLNEQRQLQSEVSIDNDKILELEKQLKQCQSDLLKLNDEKQQQDKQLQDKQIEFDQLQLTFNQFKNDKDSQFIQLQDDQKQQLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQFENQEKEKQLSEKDEKLQSIQQNLNQLNDENQEKVKQFSEKDEKLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQQDLNQLNDDQIKKNEKLKEKEEQLLKLQQDFNDQQSQQLKQLEEKLSEKENQLQQLKQENEINQLNQQQQSNEIIQQLKDQLLKQQQQEQQENNNEKEIERLIQEIEQLKQQQEIDQSELSNKEIKIQTTQQEFDQLSHNRSKDQLHLQQLQQELDQLKQSFDDQDHQFKKVIDERYNLQLQLEQSTLSNNQLDQLLKEKLKPLELDSNEKQKTIDDLLSNISNLQISLQNDKDLISERNNSIKTLESRITQQLSLLDEKDNLIKDLQQQKQQQQQPPTASSSPSSSPSLLSSTPTPKPQRPNQIEIDRLVNEIVNRNQDLIRKNKTKFYKLENGDYIVNSIIYRLSLDDDNDSDLIAQEYENGNSTTFEKSLRIFPSKNTRPIFDWRALFFIGAAVLAISTLFSSSRPIKYEKPT 1738 P18130 Alpha-1A ADRA1A 9913 None SL-0178 SL-0182 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}. UNIPROT P18130 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0005901 GO:0005737 GO:0005887 GO:0031965 GO:0005634 GO:0005886 GO:0004937 GO:0004930 GO:0046982 GO:0071880 GO:0007267 GO:0007200 GO:0007204 GO:0001996 GO:0043410 GO:0045907 GO:0055117 Transmembrane UniProt By Similarity {ECO:0000250} MVFLSGNASDSSNCTHPPPPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNVWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQKRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYVPLTIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAQVGGSGVTSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFRPSETVFKIAFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLRRKQSSKHTLGYTLHAPSHVLEGQHKDLVRIPVGSAETFYKISKTDGVCEWKIFSSLPRGSARMAVARDPSACTTARVRSKSFLQVCCCLGPSTPSHGENHQIPTIKIHTISLSENGEEV 466 O77621 Alpha-1A ADRA1A 9615 None SL-0178 SL-0182 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}. UNIPROT O77621 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0005901 GO:0005737 GO:0005887 GO:0031965 GO:0005634 GO:0005886 GO:0004937 GO:0004930 GO:0046982 GO:0071880 GO:0007267 GO:0007200 GO:0007204 GO:0001996 GO:0043410 GO:0045907 GO:0055117 Transmembrane UniProt By Similarity {ECO:0000250} MVFLSGNASDSSNCTHPPAPVNISKAILLGVILGGLIIFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQKRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQITEEPGYVLFSALGSFYVPLTIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPVGGTGVSSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIG 295 Q9WU25 Alpha-1A ADRA1A 10141 None SL-0178 SL-0182 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}. UNIPROT Q9WU25 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0005901 GO:0005737 GO:0016021 GO:0031965 GO:0005634 GO:0005886 GO:0004937 GO:0046982 GO:0043410 GO:0055117 GO:0019229 Transmembrane UniProt By Similarity {ECO:0000250} MVFLSGNASDSSNCTQPPAPVNIPKAILLGVILGVLILFGVPGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIMSLCIISIDRYIGVSYPLRYPTIVTQRRGLRALLCLWALSLVISIGPLFGWRQPAPQDETICQINEDPSYVLFSALGSFYVPLAIILVMYCRVYVVAKRESRGLTSGLKTDKSDSEQVTLRIHRKNAPLGGSGVASSKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLKIQCLRRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYKISKTDGVCEWKFFSSMPRGSARITVPKDQSACTTARVRSKSFLQVCCCVGPSTPNPGENHQVPTIKIHTISLSENGEEV 466 P35348 Alpha-1A ADRA1A 9606 None SL-0178 SL-0182 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. UNIPROT P35348 UNIPROT A8K0I3 UNIPROT B0ZBD1 UNIPROT B0ZBD2 UNIPROT B0ZBD4 UNIPROT B0ZBD5 UNIPROT B0ZBD6 UNIPROT B0ZBD8 UNIPROT B0ZBD9 UNIPROT O60451 UNIPROT Q13675 UNIPROT Q13729 UNIPROT Q4VBM7 UNIPROT Q6RUJ4 UNIPROT Q6RUJ5 UNIPROT Q6RUJ7 UNIPROT Q6RUJ8 UNIPROT Q6RUJ9 UNIPROT Q96RE8 UNIPROT Q9UD63 UNIPROT Q9UD67 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 OMIM 104221 DisGeNET 148 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}. P13497 EBI-489882 0.00 Q12979 EBI-489946 0.00 Q14315 EBI-489983 0.00 P29066 EBI-15953886 0.40 O75787 EBI-20801320 0.37 P60033 EBI-20801330 0.37 Q8WY98 EBI-20801340 0.37 Q9Y247 EBI-20801360 0.37 Q96D05 EBI-20801350 0.37 Q9NZC3 EBI-20801390 0.37 O15354 EBI-20801380 0.37 Q8IWK6 EBI-20801370 0.37 Q9HCP6 EBI-20801400 0.37 Q53GT1 EBI-20801411 0.37 Q8IYS2 EBI-20801421 0.37 Q96BZ9 EBI-20801471 0.37 Q96N66 EBI-20801431 0.37 Q9HCE9 EBI-20801481 0.37 Q8NHX9 EBI-20801491 0.37 Q16585 EBI-20801451 0.37 Q07699 EBI-20801461 0.37 Q96CW9 EBI-20801441 0.37 Q16880 EBI-20801511 0.37 Q5T4S7 EBI-20801501 0.37 Q13636 EBI-20902904 0.40 P08670 EBI-20929296 0.40 Q00610 EBI-21283112 0.46 P09496 EBI-21283119 0.46 P09497 EBI-21283123 0.46 P25106 EBI-21283763 0.42 P61073 EBI-21283881 0.61 Q96HD1 EBI-21288883 0.37 P35348 EBI-21282711 0.40 P35368 EBI-21282743 0.40 GO:0005901 GO:0005737 GO:0005829 GO:0098691 GO:0098982 GO:0098978 GO:0005887 GO:0099055 GO:0099056 GO:0043231 GO:0031965 GO:0005654 GO:0005634 GO:0005886 GO:0030315 GO:0030018 GO:0004937 GO:0004930 GO:0046982 GO:0007202 GO:0071880 GO:0007512 GO:0007568 GO:0006915 GO:0060402 GO:0061049 GO:0007267 GO:0007186 GO:0035556 GO:0000165 GO:0060073 GO:0010259 GO:0010507 GO:0008285 GO:0001985 GO:0035024 GO:0150099 GO:0001994 GO:0007200 GO:0097195 GO:0045760 GO:0060452 GO:0010613 GO:0007204 GO:0070374 GO:0001996 GO:0043410 GO:1903997 GO:0090037 GO:0045987 GO:0032230 GO:0003084 GO:0001997 GO:0045907 GO:2000300 GO:0009725 GO:0009410 GO:0007165 GO:0006939 Transmembrane UniProt By Similarity {ECO:0000250} MVFLSGNASDSSNCTQPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV 466 P97718 Alpha-1A Adra1a 10090 None SL-0178 SL-0182 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}. UNIPROT P97718 UNIPROT O54913 UNIPROT Q8BV77 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. P70658 EBI-21294249 0.27 GO:0005901 GO:0005737 GO:0005829 GO:0098691 GO:0098982 GO:0098978 GO:0005887 GO:0099055 GO:0099056 GO:0043231 GO:0016020 GO:0031965 GO:0005654 GO:0005634 GO:0005886 GO:0030315 GO:0030018 GO:0004937 GO:0004930 GO:0046982 GO:0007202 GO:0071880 GO:0007512 GO:0007568 GO:0060402 GO:0061049 GO:0007267 GO:0000165 GO:0060073 GO:0010259 GO:0010507 GO:0001985 GO:0035024 GO:0150099 GO:0001994 GO:0035265 GO:0007200 GO:0097195 GO:0045760 GO:0060452 GO:0010613 GO:0007204 GO:0070374 GO:0010460 GO:0001996 GO:0043410 GO:1903997 GO:0090037 GO:0045987 GO:0032230 GO:0003084 GO:0001997 GO:0045907 GO:0008217 GO:2000300 GO:0009725 GO:0009410 Transmembrane UniProt By Similarity {ECO:0000250} MVLLSENASEGSNCTHPPAQVNISKAILLGVILGGLIIFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGVRALLCVWALSLVISIGPLFGWRQQAPEDETICQINEEPGYVLFSALGSFYVPLTIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNVPAEGSGVSSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPNFKPPETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLRRRQSSKHALGYTLHPPSQAVEGQHRGMVRIPVGSGETFYKISKTDGVREWKFFSSMPQGSARITMPKDQSACTTARVRSKSFLQVCCCVGSSTPRPEENHQVPTIKIHTISLGENGEEV 466 O02824 Alpha-1A ADRA1A 9986 None SL-0178 SL-0182 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}. UNIPROT O02824 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0005901 GO:0005737 GO:0005829 GO:0016021 GO:0031965 GO:0005654 GO:0005634 GO:0005886 GO:0004937 GO:0046982 GO:0007512 GO:0061049 GO:0000165 GO:0010259 GO:0010507 GO:0001985 GO:0150099 GO:0001994 GO:0007200 GO:0097195 GO:0010613 GO:0001996 GO:0043410 GO:1903997 GO:0045987 GO:0001997 GO:0055117 GO:0019229 Transmembrane UniProt By Similarity {ECO:0000250} MVFLSGNASDSSNCTHPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIISLCVISIDRYIGVSYPLRYPTIVTQRRGLRALLCVWAFSLVISVGPLFGWRQPAPDDETICQINEEPGYVLFSALGSFYVPLTIILAMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGVASAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPPETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLKIQCLRRKQSSKHALGYTLHAPSQALEGQHKDMVRIPVGSGETFYKISKTDGVCEWKFFSSMPRGSARITVPKDQSACTTARVRSKSFLQVCCCVGPSTPNPGENHQVPTIKIHTISLSENGEEV 466 P43140 Alpha-1A Adra1a 10116 None SL-0178 SL-0182 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}. UNIPROT P43140 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. O08565 EBI-21284814 0.27 GO:0005901 GO:0005737 GO:0005829 GO:0098691 GO:0098982 GO:0098978 GO:0005887 GO:0099055 GO:0099056 GO:0016020 GO:0031965 GO:0005654 GO:0005634 GO:0005886 GO:0030315 GO:0030018 GO:0004937 GO:0004930 GO:0046982 GO:0007202 GO:0071880 GO:0071875 GO:0007512 GO:0007568 GO:0060402 GO:0061049 GO:0007267 GO:0000165 GO:0060073 GO:0010259 GO:0010507 GO:0001985 GO:0035024 GO:0150099 GO:0001994 GO:0035265 GO:0007200 GO:0097195 GO:0045760 GO:0060452 GO:0010613 GO:0007204 GO:0070374 GO:0010460 GO:0001996 GO:0043410 GO:1903997 GO:0090037 GO:0045987 GO:0032230 GO:0003084 GO:0001997 GO:0045907 GO:0008217 GO:2000300 GO:0009725 GO:0009410 Transmembrane UniProt By Similarity {ECO:0000250} MVLLSENASEGSNCTHPPAPVNISKAILLGVILGGLIIFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGVRALLCVWVLSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYVPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNVPAEGGGVSSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLRRRQSSKHALGYTLHPPSQALEGQHRDMVRIPVGSGETFYKISKTDGVCEWKFFSSMPQGSARITVPKDQSACTTARVRSKSFLQVCCCVGSSAPRPEENHQVPTIKIHTISLGENGEEV 466 P11615 Alpha-1B ADRA1B 9615 None SL-0178 SL-0182 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}. UNIPROT P11615 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0005901 GO:0005737 GO:0005887 GO:0031965 GO:0005634 GO:0005886 GO:0004937 GO:0004930 GO:0046982 GO:0071880 GO:0007267 GO:0007200 GO:0007204 GO:0001996 GO:0043410 GO:0045907 GO:0055117 Transmembrane UniProt By Similarity {ECO:0000250} VLPFSAALEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLGVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFVRILGCQCRGRRRRRRRRRLGGCAYTYRPWTRGGSLERSQSRKDSLDDSGSCLSGSQRTLPSASPSPGYLGRAAPPPVELCAVPEWKAPGALLSLPAPQPPGRRGRRDSGPLFTFRLLAERGSPAAGDGACRPAPDAANGQPGFKTNMPLAPGQF 417 P35368 Alpha-1B ADRA1B 9606 None SL-0178 SL-0182 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. UNIPROT P35368 UNIPROT B0LPE1 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 OMIM 104220 DisGeNET 147 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}. P35348 EBI-21282743 0.40 Q14315 EBI-490031 0.00 P02768 EBI-1220884 0.35 P01857 EBI-1222317 0.35 Q96SB3 EBI-7385236 0.40 P21917 EBI-15989057 0.47 P25106 EBI-21283831 0.42 P61073 EBI-21284190 0.61 P35368 EBI-21282722 0.40 P25100 EBI-21282754 0.40 GO:0005901 GO:0005737 GO:0005887 GO:0031965 GO:0005634 GO:0005886 GO:0004937 GO:0004930 GO:0046982 GO:0071880 GO:0007188 GO:0007267 GO:0007186 GO:0035556 GO:0150099 GO:0007200 GO:0007204 GO:0001996 GO:0043410 GO:0045907 GO:0055117 Transmembrane UniProt By Similarity {ECO:0000250} MNPDLDTGHNTSAPAHWGELKNANFTGPNQTSSNSTLPQLDITRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAMADLLLSFTVLPFSAALEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFVRILGCQCRGRGRRRRRRRRRLGGCAYTYRPWTRGGSLERSQSRKDSLDDSGSCLSGSQRTLPSASPSPGYLGRGAPPPVELCAFPEWKAPGALLSLPAPEPPGRRGRHDSGPLFTFKLLTEPESPGTDGGASNGGCEAAADVANGQPGFKSNMPLAPGQF 520 P18841 Alpha-1B ADRA1B 10036 None SL-0178 SL-0182 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}. UNIPROT P18841 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. O35796 EBI-6391260 0.54 GO:0005901 GO:0005737 GO:0016021 GO:0031965 GO:0005634 GO:0005886 GO:0004937 GO:0046982 GO:0043410 GO:0055117 GO:0019229 Transmembrane UniProt By Similarity {ECO:0000250} MNPDLDTGHNTSAPAQWGELKDANFTGPNQTSSNSTLPQLDVTRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAIADLLLSFTVLPFSATLEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFMRILGCQCRSGRRRRRRRRLGACAYTYRPWTRGGSLERSQSRKDSLDDSGSCMSGSQRTLPSASPSPGYLGRGAQPPLELCAYPEWKSGALLSLPEPPGRRGRLDSGPLFTFKLLGEPESPGTEGDASNGGCDATTDLANGQPGFKSNMPLAPGHF 515 P97717 Alpha-1B Adra1b 10090 None SL-0178 SL-0182 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}. UNIPROT P97717 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. P70658 EBI-21294339 0.27 GO:0005901 GO:0005737 GO:0016021 GO:0005887 GO:0014704 GO:0016020 GO:0031965 GO:0005634 GO:0005886 GO:0030315 GO:0004937 GO:0004930 GO:0046982 GO:0071880 GO:0007512 GO:0048148 GO:0001974 GO:0061049 GO:0007267 GO:0042593 GO:0005980 GO:0007626 GO:0010259 GO:0045818 GO:0035024 GO:0150099 GO:0035265 GO:0007200 GO:0007204 GO:0045819 GO:0001996 GO:0043410 GO:0001997 GO:0045907 GO:0008217 GO:0055117 GO:0001975 GO:0009725 GO:0043278 GO:0048545 GO:0001987 GO:0008542 Transmembrane UniProt By Similarity {ECO:0000250} MNPDLDTGHNTSAPAHWGELKDANFTGPNQTSSNSTLPQLDVTRAISVGCLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAIADLLLSFTDLPFSATLEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFMRILGCQCRGGRRRRRRRRLGACAYTYRPWTRGGSLERSQSRKDSLDDSGSCMSGSQRTLPSASPSPGYLGRGTQPPVELCAFPEWKPGALLSLPEPPGRRGRLDSGPLFTFKLLGEPESPGTEGDASNGGCDTTTDLANGQPGFKSNMPLAPGHF 514 P15823 Alpha-1B Adra1b 10116 None SL-0178 SL-0182 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}. UNIPROT P15823 UNIPROT Q63215 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. P30729 EBI-15989124 0.47 GO:0005901 GO:0005737 GO:0016021 GO:0005887 GO:0014704 GO:0016020 GO:0031965 GO:0005634 GO:0030315 GO:0004937 GO:0004930 GO:0046982 GO:0071880 GO:0071875 GO:0007512 GO:0048148 GO:0001974 GO:0061049 GO:0007267 GO:0042593 GO:0005980 GO:0007626 GO:0010259 GO:0045818 GO:0035024 GO:0150099 GO:0035265 GO:0007200 GO:0007204 GO:0045819 GO:0001996 GO:0043410 GO:0001997 GO:0045907 GO:0008217 GO:0055117 GO:0001975 GO:0043627 GO:0009725 GO:0043278 GO:0048545 GO:0009410 GO:0001987 GO:0008542 Transmembrane UniProt By Similarity {ECO:0000250} MNPDLDTGHNTSAPAHWGELKDDNFTGPNQTSSNSTLPQLDVTRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAIADLLLSFTVLPFSATLEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFMRILGCQCRGGRRRRRRRRLGACAYTYRPWTRGGSLERSQSRKDSLDDSGSCMSGTQRTLPSASPSPGYLGRGTQPPVELCAFPEWKPGALLSLPEPPGRRGRLDSGPLFTFKLLGDPESPGTEGDTSNGGCDTTTDLANGQPGFKSNMPLAPGHF 515 Q96PN6 Adenylate ADCY10 9606 None SL-0198 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}. UNIPROT Q96PN6 UNIPROT B4DZF0 UNIPROT F5GWS5 UNIPROT O95558 UNIPROT Q5R329 UNIPROT Q5R330 UNIPROT Q8WXV4 UNIPROT Q9NNX0 PDB 4CLF PDB 4CLK PDB 4CLL PDB 4CLP PDB 4CLS PDB 4CLT PDB 4CLU PDB 4CLW PDB 4CLY PDB 4CLZ PDB 4CM0 PDB 4CM2 PDB 4OYA PDB 4OYB PDB 4OYI PDB 4OYM PDB 4OYO PDB 4OYP PDB 4OYW PDB 4OYX PDB 4OYZ PDB 4OZ2 PDB 4OZ3 PDB 4UST PDB 4USU PDB 4USV PDB 4USW PDB 5D0R PDB 5IV3 PDB 5IV4 PDB 7OVD Pfam PF00211 PROSITE PS50125 OMIM 143870 OMIM 605205 DisGeNET 55811 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}. 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. P12270 EBI-20930080 0.40 GO:0016324 GO:0045178 GO:0005929 GO:0005737 GO:0005856 GO:0005829 GO:0030425 GO:0005576 GO:0030426 GO:0005739 GO:0043025 GO:0005634 GO:0048471 GO:0004016 GO:0005524 GO:0051117 GO:0071890 GO:0000287 GO:0030145 GO:0006171 GO:0071241 GO:0003351 GO:0035556 GO:0043065 GO:0007283 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:15659711} MNTPKEEFQDWPIVRIAAHLPDLIVYGHFSPERPFMDYFDGVLMFVDISGFTAMTEKFSSAMYMDRGAEQLVEILNYHISAIVEKVLIFGGDILKFAGDALLALWRVERKQLKNIITVVIKCSLEIHGLFETQEWEEGLDIRVKIGLAAGHISMLVFGDETHSHFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIESVPDQRAVKVNFLKPPPNFNFDEFFTKCTTFMHYYPSGEHKNLLRLACTLKPDPELEMSLQKYVMESILKQIDNKQLQGYLSELRPVTIVFVNLMFEDQDKAEEIGPAIQDAYMHITSVLKIFQGQINKVFMFDKGCSFLCVFGFPGEKVPDELTHALECAMDIFDFCSQVHKIQTVSIGVASGIVFCGIVGHTVRHEYTVIGQKVNLAARMMMYYPGIVTCDSVTYNGSNLPAYFFKELPKKVMKGVADSGPLYQYWGRTEKVMFGMACLICNRKEDYPLLGRNKEINYFMYTMKKFLISNSSQVLMYEGLPGYGKSQILMKIEYLAQGKNHRIIAISLNKISFHQTFYTIQMFMANVLGLDTCKHYKERQTNLRNKVMTLLDEKFYCLLNDIFHVQFPISREISRMSTLKKQKQLEILFMKILKLIVKEERIIFIIDEAQFVDSTSWRFMEKLIRTLPIFIIMSLCPFVNIPCAAARAVIKNRNTTYIVIGAVQPNDISNKICLDLNVSCISKELDSYLGEGSCGIPFYCEELLKNLEHHEVLVFQQTESEEKTNRTWNNLFKYSIKLTEKLNMVTLHSDKESEEVCHLTSGVRLKNLSPPTSLKEISLIQLDSMRLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKTLATLVESNIFYCFRNGKELQKALKQNDPSFEVHYRSLSLKPSEGMDHGEEEQLRELENEVIECHRIRFCNPMMQKTAYELWLKDQRKAMHLKCARFLEEDAHRCDHCRGRDFIPYHHFTVNIRLNALDMDAIKKMAMSHGFKTEEKLILSNSEIPETSAFFPENRSPEEIREKILNFFDHVLTKMKTSDEDIIPLESCQCEEILEIVILPLAHHFLALGENDKALYYFLEIASAYLIFCDNYMAYMYLNEGQKLLKTLKKDKSWSQTFESATFYSLKGEVCFNMGQIVLAKKMLRKALKLLNRIFPYNLISLFLHIHVEKNRHFHYVNRQAQESPPPGKKRLAQLYRQTVCLSLLWRIYSYSYLFHCKYYAHLAVMMQMNTALETQNCFQIIKAYLDYSLYHHLAGYKGVWFKYEVMAMEHIFNLPLKGEGIEIVAYVAETLVFNKLIMGHLDLAIELGSRALQMWALLQNPNRHYQSLCRLSRCLLLNSRYPQLIQVLGRLWELSVTQEHIFSKAFFYFVCLDILLYSGFVYRTFEECLEFIHQYENNRILKFHSGLLLGLYSSVAIWYARLQEWDNFYKFSNRAKNLLPRRTMTLTYYDGISRYMEGQVLHLQKQIKEQSENAQASGEELLKNLENLVAQNTTGPVFCPRLYHLMAYVCILMGDGQKCGLFLNTALRLSETQGNILEKCWLNMNKESWYSTSELKEDQWLQTILSLPSWEKIVAGRVNIQDLQKNKFLMRANTVDNHF 1610 Q8C0T9 Adenylate Adcy10 10090 None SL-0198 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}. UNIPROT Q8C0T9 UNIPROT B2RRJ9 UNIPROT Q3V0F8 Pfam PF00211 PROSITE PS50125 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}. Q6UJY2 EBI-15639120 0.52 GO:0045177 GO:0016324 GO:0030424 GO:0045178 GO:0005737 GO:0005829 GO:0030425 GO:0005576 GO:0030426 GO:0016020 GO:0015630 GO:0005739 GO:0031514 GO:0043025 GO:0005634 GO:0048471 GO:0004016 GO:0005524 GO:0051117 GO:0071890 GO:0000287 GO:0030145 GO:0006171 GO:0071241 GO:0003351 GO:0035556 GO:0043065 GO:0007283 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q96PN6} MSARRQELQDRAIVKIAAHLPDLIVYGDFSPERPSVKCFDGVLMFVDISGFTAMTEKFSTAMYMDRGAEQLVEILNYYISAIVEKVLIFGGDILKFAGDALLALWKVERKQLKNIITVVIKCSLEIHGLFEAKEAEEGLDIRVKIGLAAGHITMLVFGDETRNYFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIERIPDQRAVKVSFLKPPPTFNFDEFFTKCMGFMDYYPSGDHKNFLRLACMLESDPELELSLQKYVMEIILKQIDDKQLRGYLSELRPVTIVFVNLMFKEQDKVEVIGSAIQAACVHITSVLKVFRGQINKVFMFDKGCSFLCVFGFPGEKAPDEITHALESAVDIFDFCSQVHKIRTVSIGVASGIVFCGIVGHTVRHEYTVIGQKVNIAARMMMYYPGIVSCDSVTYDGSNLPAYFFKELPKKVMKGVADPGPVYQCLGLNEKVMFGMAYLICNRYEGYPLLGRVREIDYFMSTMKDFLMTNCSRVLMYEGLPGYGKSQVLMEIEYLASQHENHRAVAIALTKISFHQNFYTIQILMANVLGLDTCKHYKERQTNLQNRVKTLLDEKFHCLLNDIFHVQFPVSREMSRMSKIRKQKQLEALFMKILAQTVREERIIFIIDEAQFVDGTSWAFIEKLIRSMPIFIVMSLAPFSEVPCAAANAIMKNRNTTYITLGTMQPQEIRDKVCVDLSVSSIPRELDSYLVEGSCGIPYYCEELLKNLDHHRVLLFQQAETEQKTNVTWNNMFKHSVRPTDDMQLFTSISEGQKEVCYLVSGVRLNNLSPPASLKEISLVQLDSMSLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKALATLVESNVFNCFRSSKDLQLALKQNVPTFEVHYRSLALKLKEGLTYGEEEELREMEGEVVECRILRFCRPIMQKTAYELWLKDQKKVLHLKCARFLEESAHRCNHCRNVDFIPYHHFIVDIRLNTLDMDTVKRMVTSQGFKIDEEEAIFSKSELPRKYKFPENLSITEIREKILHFFDNVILKMKSSPNDIIPLESCQCKELLQIVILPLAQHFVALEENNKALYYFLELASAYLILGDNYNAYMYLGEGERLLKSLTNEDSWSQTFEYATFYSLKAEVCFNMGQMVLAKKMLRKALKLLNRMFPCNLLTLTFQMHVEKNRLSHFMNQHTQEGSVPGKKLAQLYLQASCFSLLWRIYSLNFFFHYKYYGHLAAMMEMNTSLETQNDFQIIKAYLDFSLYHHLAGYQGVWFKYEILVMEQLLNLPLKGEAIEIMAYTADTLGHIKFLMGHLDLAIELGSRAHRMWSLLRNPNKYQMVLCRLSKPLFLKSRYKHLVQVLGWLWDLSVTEEDIFSKAFFYFVCLDIMLYSGFIYRTFEECLEFIHHNEDNRILKFQSGLLLGLYSCIAVWYARLQEWDNFNKFSDRAKHLVTRRTPTVLYYEGISRYMEGQVLHLQKQIEEQAENAQDSGVEILKALETLVAQNTTGPVFYPRLYHLMAYVCILMGDGHSCDFFLNTALELSETHGNLLEKCWLSMSKEWWYSASELTGDQWLQTVLSLPSWDKIVSGKGGQRKRSWSWFCPPNFSMVSWSQPQCA 1614 Q866F4 Adenylate ADCY10 9986 None SL-0198 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}. UNIPROT Q866F4 Pfam PF00211 PROSITE PS50125 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}. GO:0005929 GO:0005856 GO:0005576 GO:0005634 GO:0048471 GO:0005886 GO:0004016 GO:0005524 GO:0071890 GO:0000287 GO:0006171 GO:0071241 GO:0003351 GO:0035556 GO:0007283 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q96PN6} MNTRKEELQDRAIVRIAAHLPDLIVYGDFSPQRPSVDYFDGVLMFVDISGFTAMTEKFSTAMYMDRGAEQLVEILNYYISAIVEKVLIFGGDILKFAGDALLALWKVERKQLKNIITVVIKCSLEIHGLFGTQESEEGLDIRVKIGLAAGHISMLVFGDETRNHFLVIGQAVDDVRLAQNMARMNDVILSPNCWQLCDRSMIEIERIPDQRAVKVNFLKPPPSFNFDEFFNKCMTFMDYYPSGDHKNLLRLACMLESDPDLELSLQKYVMESILKQIDDKQLRGYLSELRPVTIVFVNLMFQDQNKAEVIGSAIQDACVHISSVLKVFRGQINKVFMFDKGCSFLCVFGFPGEKAPDEVTHALESAVDIFDFCSQVHKIHTVSIGVASGIVFCGIVGHTVRHEYTVIGQKVNIAARMMMYYPGIVTCDSVTYNGSNLPPYFFKELPKKLMKGVGDSGPVYQCLGLNEKVMFGMAYLTCNRNEGYPLLGRDKEIKYFMCTMKEFLMSNCSRVLMYEGLSGFGKSRILMEIEYLAQGENHRTIAIALTKVSFHQNFYTIQILMANVLGLDTCKHYKERQTNLQNKVKTLLDEKFHCLLNDIFHVQFPISREISKMSTFRKQKQLEALFMKILEQTVKEERIIFIIDEAQFVDYASWIFMEKLIRTVPIFIIMSLSPFTEIPCAAASAIMKNRNTTYVTLGAVQPNDIRNKVCLDLNVSSIPKELDLYLVEGSCGIPFYCEELVKNLDHHRVLVFQQMETEEKTKVTWNNLFKNFIKPTEEFKMSGLGNEEGTEEICKLASGVRLKNLSPPASLKEISLVQLDSMSLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKALATLVESNIFDCFRDGKDLRLALKQNAASFEVHNRSLSLQPTEGIAHGEEEELRELESEVIECHIIRFCKPMMQKTAYELWLKDQKKAMHLKCARFLEENAHRCDHCRSGDFIPYHHFTVDIRLNTLDMDTIKKMATSHGFETEEEIKISRAGIPKNSELFSENLSPEEIGERILGFFDVILTKMKTSKEDIIPLESCQCEEILEIVILPLAQHFLALGENNKALYYFLEITSAYLTLGDNYMAYMYLNEGERLLKTLKKEKSWSQTFESATFYSLKGQVCFNMGQMVLAKKMLRKALKLLNRIFPYNLISLFLHTHMEKNRHFHYVTQQAQESSPPGKKRLAHLYQQTACFSLLWQIYSLNYFFHHKYYGHLAAMMELNTALETQNDFQIIKAYLDYAMYHHLAGYQGVWFKYEVKAMEQIFNLPLKGEGIEIVAYVAGKLSYIKLMMGYLDLAIELGARAHKMWALLQNPNQHYVVLCRLSKSLFLKNRYKHLIQMLRRLWDLSVAEGHIISKAFFYLVCLDIMLYSGFVYRTFEECLEFIIQNEDNRILKFQSGLLLGLYSSIAIWYGRLQEWDNFYVFSNRAKTLVSRRTPTILYYDGVSRYMEGQVLQLQKQIEEQSETAQDSGVELLKSLESLVAQNTTGPVFYPRLYHLMAYICILMGDGQNCDLFLNTALKLSEIQGNVLEKCWLNMSKEWWYSNCTLTEDQWLHTILSLPAWEKIVSGKVNIHDVQKNKFLMRVNILDNPF 1610 Q9Z286 Adenylate Adcy10 10116 None SL-0198 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}. UNIPROT Q9Z286 Pfam PF00211 PROSITE PS50125 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}. GO:0045177 GO:0016324 GO:0030424 GO:0045178 GO:0005737 GO:0005829 GO:0030425 GO:0005576 GO:0030426 GO:0016020 GO:0015630 GO:0005739 GO:0031514 GO:0043025 GO:0005634 GO:0048471 GO:0004016 GO:0005524 GO:0051117 GO:0071890 GO:0000287 GO:0030145 GO:0006171 GO:0071241 GO:0003351 GO:0035556 GO:0043065 GO:0007283 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q96PN6} MSARRQELQDRAIVKIAAHLPDLIVYGDFSPERPSVKCFDGVLMFVDISGFTAMTEKFSTAMYMDRGAEQLVEILNYYISAIVEKVLIFGGDILKFAGDALLALWKVERKQLKNIITVVIKCSLEIHGLFEAKEVEEGLDIRVKIGLAAGHITMLVFGDETRNYFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIERIPDQRAVKVSFLKPPPTFNFDEFFAKCMAFMDYYPSGDHKNFLRLACMLESDPELELSLQKYVMEIILKQIDDKQLRGYLSELRPVTIVFVNLMFKEQDKAEVIGSAIQAACVHITSVLKVFRGQINKVFMFDKGCSFLCVFGFPGEKAPDEITHALESAVDIFDFCSQVHKIRTVSIGVASGIVFCGIVGHTVRHEYTVIGQKVNIAARMMMYYPGIVTCDSVTYDGSNLPAYFFKELPKKVMKGVADPGPVYQCLGLNEKVMFGMAYLICNRYEGYPLLGRVREIDYFMSTMKDFLMTNCSRVLMYEGLPGYGKSQVLMEIEYLASQHENHRAVAIALTKISFHQNFYTIQILMANVLGLDTCKHYKERQTNLQNRVKTLLDDKYHCLLNDIFHVQFPVSREMSRMSKIRKQKQLEALFMKILEQTVREERIIFIIDEAQFVDVASWAFIEKLIRSMPIFIVMSLCPFPETPCAAANAIMKNRNTTYITLGTMQPQEIRDKVCVDLSVSSIPRELDSYLVEGSCGIPYYCEELLKNLDHHRILIFQQAEAEEKTNVTWNNLFKYSVKPTEDMYLYTSIAAGQKEACYLTSGVRLKNLSPPASLKEISLVQLDSMSLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKALATLVESNVFDCFRSSKDLQLALKQNVTTFEVHYRSLSLKSKEGLAYSEEEQLREMEGEVIECRILRFCRPIMQKTAYELWLKDQKKVLHLKCARFLEESAHRCNHCRNRDFIPYHHFIADIRLNTLDMDTVKKMVKSHGFKTEDEVIFSKSEIPRKFKFPENISITETREKILHFFDNVIIKMRTSQDDVIPLESCHCEELLQIVILPLAQHFVALEENNKALYYFLELASAYLILGDNYNAYMYLGEGERLLKSLTNEDSWSQTFEYATFYSLKGEICFNMGQMVLAKKMLRKALKLLNRMFPCNLLSLTFQMHIEKNRLSHFMNQHTQEGSLPGKKLAQLFLQSSCFSLLWKIYSLNFFFHYKYYGRLAAIMQMNTSLETQNNFQIIKAFLDFSLYRHLAGYEGVWFKYEILVMEQLLNLPLKGEAFEIMAYAADALGHIKFLTGHLDLAIELGSRAHKMWSLLRNPNKYHMVLCRLSKPLFLKSRYKHLVQVLGWLWDLSVTEEHIFSKAFFYFVCLDIMLYSGFIYRTFEECLEFIHHNEDNRILKFQSGLLLGLYSCIAVWYARLQEWDNFYKFSNRAKTLVTRRTPTVLYYEGISRYMEGQVLHLQKQIEEQAENAQDSGVELLKALETLVAQNTTGPVFYPRLYHLMAYVCILMGDGHSCDFFLNTALELSETQGNLLEKCWLSMSKEWWYSAPELTGDQWLQTVLSLPSWDKIVSGNVTLQDVQKNKFLMRVNILDNPF 1608 P24935 Adenovirus ADP 10515 None SL-0415 SL-0418 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}. UNIPROT P24935 Pfam PF05393 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}. GO:0044167 GO:0044178 GO:0044200 GO:0016021 GO:0044659 Transmembrane UniProt Sequence Analysis {ECO:0000255} MTGSTIAPTTDYRNTTATGLTSALNLPQVHAFVNDWASLDMWWFSIALMFVCLIIMWLICCLKRRRARPPIYRPIIVLNPHNEKIHRLDGLKPCSLLLQYD 101 Q99222 ARF3-interacting AFI1 559292 None SL-0198 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. UNIPROT Q99222 UNIPROT D6W2I7 UNIPROT Q92274 Pfam PF07792 PROSITE PS50211 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}. P53865 EBI-1781812 0.55 P29366 EBI-7365092 0.37 P11484 EBI-3700856 0.35 P32589 EBI-3732939 0.35 GO:0005938 GO:0005935 GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0051666 GO:0000282 Unknown UniProt Sequence Analysis MLRRELNNSISNRSIENESFPFERPNVSYIISAEFDNKLGPILKHQYPKDIPGFNQFSHEQRNGNTSVSMNLASLMIPSSIERNPGKQDITVFTLYYNKFTQNYQLFPVPKDPRFSFNLHHREQSDGSVTNSIYYDAENHQDAKNNRYTIVLEDDELECQEVQNNQKAIDNEPLFFINVANTVLDTTNDRGAVIKSIAIGTPLKTFFAFKNIIVLVLDLYMKAPTQAAATDILLDCFNMLNSIDLTLINDIHSKSSIQEVLHSIHDESIITKVFLDPDSTLKKLFCINGFDTKDKYGNIVTFHDQLIQYHFTRFQPKTLPPFLLKIPLQFNMIRREPIYIENDYNELVLKFLDKFVPYLLKAGQKVNAWKLVINSTKLSKEDLCAFILSLANITATYASDPQSYFKGNAALIFPYMDISLVDGLRAYVASNSDFVGCFAIIGTANPIFRYQLDIWDYYYDVDEGVFYENNSPEKEKPDTVAEVKIGPNPLRKIFNRPHFSTNAVNESQVNLGQKLFSLLIDEYHDSDTIMSVLRRLNVLQLENLLDALKRREIPPNIALKDEYIMFYKDFFIFPEFFDYFTLHSIELLSNLDNCLFSLGNTCQLFSTEQIYSQLSQILDIVKELFRMVSVSRTNIEKFLNACLNYSPFKILPTAQLHGDNISRWSFESEVRQGFDNFNSYMGIEKDPHGVIVSAIDLFTQIYSFDILAFFLTFITKESGQDLPFTKSLSRRRTYLTRIAQSSSLRQFLQLSTRPNIRILGGNGQGTGNSNYPEFTNASSVISPKLRASPLLERRASKICYAITKLLYRLECHPIGMALLKKYLHNQLREAYLESKRHFISKKGDSTNTSSTIASSSFAGASVPLSSNESGMLNGLKQINEQQESTLETTQKED 893 Q6ULP2 Aftiphilin AFTPH 9606 None SL-0198 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}. UNIPROT Q6ULP2 UNIPROT D6W5E9 UNIPROT Q6ZM66 UNIPROT Q86VW3 UNIPROT Q8TCF3 UNIPROT Q9H7E3 UNIPROT Q9HAB9 UNIPROT Q9NXS4 Pfam PF15045 OMIM 619628 DisGeNET 54812 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}. Q8ZJ79 EBI-2848711 0.00 A0A380PPP8 EBI-2876267 0.00 A0A3N4B631 EBI-2876260 0.00 P51692 EBI-3940316 0.37 Q05086 EBI-7412469 0.37 P41241 EBI-11013851 0.35 P56377 EBI-11037753 0.53 Q6P5F9 EBI-11603310 0.35 O95292 EBI-21550215 0.35 Q9P0L0 EBI-21550773 0.35 Q9Y6Q5 EBI-21760726 0.35 P03372 EBI-21301141 0.35 P63010 EBI-30816846 0.44 Q9H492 EBI-30829101 0.44 Q9GZQ8 EBI-30831123 0.44 O75381 EBI-30835687 0.44 Q6ZMQ8 EBI-32723474 0.27 GO:0030121 GO:0005829 GO:0005794 GO:0043231 GO:0005654 GO:0048471 GO:0032588 GO:0030276 GO:0046907 GO:0015031 Unknown UniProt Sequence Analysis MEPDIIRMYSSSPPPLDNGAEDDDDDEFGEFGGFSEVSPSGVGFVDFDTPDYTRPKEEFVPSNHFMPIHEFSENVDSLTSFKSIKNGNDKDITAELSAPVKGQSDVLLSTTSKEIISSEMLATSIDGMERPGNLNKVVEQRQNVGTLESFSPGDFRTNMNVVHQNKQLESCNGEKPPCLEILTNGFAVLETVNPQGTDDLDNVADSKGRKPLSTHSTEYNLDSVPSPAEEFADFATFSKKERIQLEEIECAVLNDREALTIRENNKINRVNELNSVKEVALGRSLDNKGDTDGEDQVCVSEISIVTNRGFSVEKQGLPTLQQDEFLQSGVQSKAWSLVDSADNSEAIRREQCKTEEKLDLLTSKCAHLCMDSVKTSDDEVGSPKEESRKFTNFQSPNIDPTEENDLDDSLSVKNGDSSNDFVTCNDINEDDFGDFGDFGSASGSTPPFVTGTQDSMSDATFEESSEHFPHFSEPGDDFGEFGDINAVSCQEETILTKSDLKQTSDNLSEECQLARKSSGTGTEPVAKLKNGQEGEIGHFDSVPNIQDDCNGFQDSDDFADFSSAGPSQVVDWNAFEDEQKDSCSWAAFGDQQATESHHRKEAWQSHRTDENIDTPGTPKTHSVPSATSKGAVASGHLQESATSVQTALLNRLERIFEACFPSILVPDAEEEVTSLKHLLETSTLPIKTREALPESGELLDVWTELQDIHDAHGLRYQWGGSHSNKKLLSSLGIDTRNILFTGNKKQPVIVPMYAAGLGMLEPTKEPLKPLSAAEKIASIGQTATMSPDMNTCTSDQFQESLPPVQFDWSSSGLTNPLDASGGSTLLNLDFFGPVDDSSSSSSTTIPGVDPELYELTTSKLEISTSSLKVTDAFARLMSTVEKTSTSTRKPKREEHLSEEAIKVIAGLPDLTFMHAKVLMFPATLTPSTSSQEKADG 936 Q80WT5 Aftiphilin Aftph 10090 None SL-0198 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}. UNIPROT Q80WT5 UNIPROT Q5SSE6 UNIPROT Q99KJ1 Pfam PF15045 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}. P18484 EBI-7578021 0.52 Q9R0Z7 EBI-7578129 0.56 P52303 EBI-7578394 0.40 GO:0030121 GO:0005829 GO:0005794 GO:0043231 GO:0005654 GO:0048471 GO:0032588 GO:0030276 GO:0046907 GO:0015031 Unknown UniProt Sequence Analysis MEPDIIRMYSSSPPPLDNGAEDDEEDEFGEFGGFSEVSPSGVGFVDFDTPDYTRPKEDFVPSNHFMPIHEYSEDVDSLTSFKSVQNGNDKDITAELSTPVKSQSDVVLSTTSKEMIPSKTLDPSIDGMESLEDLDKVVVQGPSTGQLRSFSPGDFRTDKNIVHQTKQLESCNGEKPPCLEILTNGFAGLETVNPQGTDDLDNVADSKGSKPLNTCGTECILESAASHATEFADFSTFSQTERTQLEEIECPVLNDGDTLTIQGNSKGPRVKELNCVKEVTLDGSFEDTGNTEREHQVCVSEIHAVADRGLSVEKQDLQTLQQDEFLNSRIQSEAWSLVDSSENSEAITKERCKMEKNDLFASKCADLSMDSVKTSDVNEIGSSKEENRKLTNPKSPDPDPTGQNALDDSAASMKNGDSGNGFVTCHDTNEDDFGDFGTANGTTPPFVTSTQDSMSDVTFEDSSEHFLHLSEPGDDFGEFEDTNAVSCQEEMRFTESDLRQTSDGLSEECPLAGESGGKDSKPDSKLKNGQDSEFGDFDSVPNTQGSAFQDSDDFADFSSAGPSQAVDWNAFEDEQKDGCSWAAFGDQQETESHHLKEVWQSQRTDETMGTLGTPKMHSVSSAASKGAVASGHLQEPGTSVQTALLNRLERIFEACFPSVFVPDVEEEVSSLKHLLETHSSPAKTREALADRGELRGVWTELQDIHDAHGLRYQWGGSHSNKKLLCSLGIDTRNILFTGNKKQPVIVPMYAAGLGMLEPTKEPLKPLSAAEKIASIGQTTVMTPEINTCTSDPFQESLPPVQFDWSSSGLTNPLDASGGSTLLNLDFFGPVDDSSSSSSTIPGVDPELYELTTAKLETSTSSLRVTDAFAKLMSTVEKTSTSTRKPKREEHLSEEAMKVIASLPDLTFMHAKVLMFPATLTPSMSSQEQADA 931 P14998 Agnoprotein AGNO 10631 None SL-0415 SL-0418 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}. UNIPROT P14998 Pfam PF01736 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}. GO:0044200 GO:0020002 GO:0044169 GO:0016021 GO:0044385 GO:0003677 GO:0005216 GO:0039707 GO:0051259 Transmembrane UniProt Sequence Analysis {ECO:0000255} MFCEPKNLVVLRQLSRQASVKVGKTWTGTKKRAQRIFIFILELLLEFCRGEDSVDGKNKSTTALPAVKDSVKDS 74 P03085 Agnoprotein AGNO 1891762 None SL-0415 SL-0418 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}. UNIPROT P03085 Pfam PF01736 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}. GO:0044200 GO:0020002 GO:0044169 GO:0016021 GO:0044385 GO:0003677 GO:0005216 GO:0039707 GO:0051259 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVLRQLSRQASVKVGKTWTGTKKRAQRIFIFILELLLEFCRGEDSVDGKNKSTTALPAVKDSVKDS 66 P03086 Agnoprotein AGNO 10632 None SL-0415 SL-0418 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}. UNIPROT P03086 PDB 2MJ2 PDB 5NHQ Pfam PF01736 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}. GO:0044200 GO:0020002 GO:0044169 GO:0016021 GO:0044385 GO:0003677 GO:0005216 GO:0039707 GO:0051259 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVLRQLSRKASVKVSKTWSGTKKRAQRILIFLLEFLLDFCTGEDSVDGKKRQRHSGLTEQTYSALPEPKAT 71 Q3L6L9 Agnoprotein AGNO 557605 None SL-0415 SL-0418 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}. UNIPROT Q3L6L9 UNIPROT Q1W5X4 Pfam PF01736 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}. GO:0044200 GO:0020002 GO:0044169 GO:0016021 GO:0044385 GO:0003677 GO:0005216 GO:0039707 GO:0051259 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVLRQLSRQASVKVGKTWTGTKRRAQRIFIFILELLLDFCRGEDSVDGKKKKDSLTDKTETVTEKKES 68 P03084 Agnoprotein AGNO 1891767 None SL-0415 SL-0418 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}. UNIPROT P03084 Pfam PF01736 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}. GO:0044200 GO:0020002 GO:0044169 GO:0016021 GO:0044385 GO:0003677 GO:0005216 GO:0039707 GO:0051259 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVLRRLSRQASVKVRRSWTESKKTAQRLFVFVLELLLQFCEGEDTVDGKRKKPERLTEKPES 62 O95831 Apoptosis-inducing AIFM1 9606 None SL-0198 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}. UNIPROT O95831 UNIPROT A4QPB4 UNIPROT B1ALN1 UNIPROT B2RB08 UNIPROT D3DTE9 UNIPROT E9PRR0 UNIPROT Q1L6K4 UNIPROT Q1L6K6 UNIPROT Q2QKE4 UNIPROT Q5JUZ7 UNIPROT Q6I9X6 UNIPROT Q9Y3I3 UNIPROT Q9Y3I4 PDB 1M6I PDB 4BUR PDB 4BV6 PDB 4FDC PDB 4LII PDB 5FMH PDB 5FS6 PDB 5FS7 PDB 5FS8 PDB 5FS9 PDB 5KVH PDB 5KVI Pfam PF14721 Pfam PF07992 OMIM 300169 OMIM 300232 OMIM 300614 OMIM 300816 OMIM 310490 DisGeNET 9131 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}. 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. A0A142I5B9 EBI-20625330 0.35 O00165 EBI-16786283 0.42 O15027 EBI-16786589 0.42 O75821 EBI-7083391 0.60 P08107 EBI-7947560 0.54 Q13233 EBI-361788 0.00 Q99759 EBI-362055 0.00 Q00653 EBI-362688 0.00 Q04206 EBI-363205 0.00 Q9Y572 EBI-363715 0.00 P20333 EBI-364540 0.00 Q15628 EBI-364813 0.00 Q9NX70 EBI-394875 0.35 Q15047 EBI-732770 0.00 O76061 EBI-732773 0.00 Q8NC60 EBI-737306 0.00 Q8IX03 EBI-737309 0.00 Q9Y3Q8 EBI-946353 0.51 O75365 EBI-1060356 0.00 Q15773 EBI-16786283 0.60 Q9HAW0 EBI-1070570 0.00 Q9BRX2 EBI-1071657 0.00 Q92956 EBI-1075816 0.00 P01889 EBI-1077732 0.00 Q9BUV8 EBI-1083497 0.00 O95831 EBI-5651205 0.40 P13569 EBI-1170380 0.35 P83887 EBI-2561869 0.40 P16104 EBI-2564373 0.35 Q8N0X7 EBI-2643801 0.35 P03372 EBI-2878124 0.35 P40692 EBI-2932395 0.37 Q9H492 EBI-3044058 0.35 Q9GZQ8 EBI-3045543 0.35 Q9H0R8 EBI-3048562 0.35 O95166 EBI-3050465 0.35 Q14197 EBI-7825470 0.35 Q96HA7 EBI-8522027 0.35 P62937 EBI-4533343 0.46 P0DOE9 EBI-6138583 0.35 Q8JPQ9 EBI-6159460 0.35 Q63ZY3 EBI-6223407 0.60 O95747 EBI-6255369 0.35 Q13418 EBI-6256400 0.53 Q77M19 EBI-6270503 0.35 Q86VP6 EBI-21322532 0.35 Q13616 EBI-21323857 0.35 Q92905 EBI-21325777 0.35 Q13617 EBI-21327106 0.35 Q13618 EBI-21329068 0.35 Q93034 EBI-21331078 0.35 Q96DB2 EBI-6598272 0.35 P21860 EBI-8770321 0.57 Q96KQ7 EBI-8832899 0.35 Q96JM2 EBI-8837110 0.35 Q5S007 EBI-9515510 0.53 P57078 EBI-12503575 0.35 O75807 EBI-9976880 0.35 P10398 EBI-10101513 0.35 P51617 EBI-10103481 0.35 Q96FW1 EBI-10770028 0.35 P19838 EBI-11322719 0.35 P05412 EBI-11323169 0.35 O43920 EBI-10762907 0.57 P03220 EBI-11722152 0.35 P03225 EBI-11722220 0.35 P06460 EBI-11723082 0.35 P0CK49 EBI-11725356 0.35 P0CK56 EBI-11725466 0.35 Q2MG95 EBI-11733653 0.35 Q5T3F8 EBI-11155257 0.35 Q5JTV8 EBI-11159793 0.53 Q96NL6 EBI-11376636 0.27 O94905 EBI-11425731 0.35 Q13509 EBI-11897134 0.35 Q71U36 EBI-11897791 0.35 O14829 EBI-14023711 0.35 Q05322 EBI-16214737 0.35 Q400G9 EBI-21768785 0.35 O95470 EBI-21820286 0.35 Q05209 EBI-21820311 0.35 Q8NI37 EBI-21820367 0.35 Q8WY91 EBI-21820422 0.35 Q9HAS0 EBI-21820465 0.35 Q6UXV4 EBI-21859075 0.35 Q9BV35 EBI-21859075 0.35 Q6JQN1 EBI-21859075 0.35 Q658Y4 EBI-21859075 0.35 Q08357 EBI-21859075 0.35 P55789 EBI-21859075 0.35 P54819 EBI-16786283 0.42 P24468 EBI-21859075 0.35 Q9UID3 EBI-16150241 0.35 P36405 EBI-16180991 0.35 O43615 EBI-16786283 0.27 Q8IXI1 EBI-16786283 0.42 Q7Z434 EBI-16786283 0.27 P00403 EBI-16786283 0.42 O75431 EBI-16786283 0.27 Q9Y3D9 EBI-16786283 0.27 Q9NVH1 EBI-16786283 0.42 Q9BYN8 EBI-16786283 0.27 Q99618 EBI-16786283 0.27 Q96EY7 EBI-16786283 0.27 Q8N4Q1 EBI-16786283 0.42 Q16891 EBI-16786283 0.42 Q16775 EBI-16786283 0.27 Q13011 EBI-16786283 0.27 Q02952 EBI-16786283 0.27 P82650 EBI-16786283 0.27 P50454 EBI-16786283 0.27 P36542 EBI-16786283 0.42 P31689 EBI-16786283 0.27 P18085 EBI-16786283 0.27 P16615 EBI-16786283 0.27 P13804 EBI-16786283 0.27 O95721 EBI-16786283 0.27 O76031 EBI-16786283 0.42 O75683 EBI-16786283 0.27 A8MXV4 EBI-16786283 0.27 Q9Y5L4 EBI-16786283 0.42 Q9Y5J9 EBI-16786283 0.42 Q9Y512 EBI-16786283 0.42 Q9Y4W6 EBI-16786283 0.27 Q9Y2W6 EBI-16786283 0.27 Q9Y2S7 EBI-16786283 0.42 Q9Y2Q9 EBI-16786283 0.27 Q9ULX6 EBI-16786283 0.27 Q9UJS0 EBI-16786283 0.27 Q9P0J0 EBI-16786283 0.42 Q9P032 EBI-16786283 0.27 Q9NX63 EBI-16786283 0.27 Q9NX40 EBI-16786283 0.27 Q9NX14 EBI-16786283 0.27 Q9NVI7 EBI-16786283 0.27 Q9NSE4 EBI-16786283 0.42 Q9NS69 EBI-16786283 0.27 Q9NPL8 EBI-16786283 0.27 Q9H845 EBI-16786283 0.27 Q9H078 EBI-16786283 0.42 Q9BW72 EBI-16786283 0.27 Q9BSH4 EBI-16786283 0.27 Q9BPX6 EBI-16786283 0.27 Q99714 EBI-16786283 0.27 Q96TA2 EBI-16786283 0.27 Q96EX1 EBI-16786283 0.27 Q96EL2 EBI-16786283 0.27 Q96E52 EBI-16786283 0.41 Q96C36 EBI-16786283 0.27 Q96C01 EBI-16786283 0.27 Q96BR5 EBI-16786283 0.27 Q96A73 EBI-16786283 0.27 Q92667 EBI-16786283 0.27 Q92665 EBI-16786283 0.27 Q8IYU8 EBI-16786283 0.27 Q8IUX1 EBI-16786283 0.27 Q86TX2 EBI-16786283 0.27 Q7L0Y3 EBI-16786283 0.27 Q7KZN9 EBI-16786283 0.27 Q70CQ3 EBI-16786283 0.27 Q6UB35 EBI-16786283 0.42 Q6KCM7 EBI-16786283 0.27 Q6DKK2 EBI-16786283 0.42 Q5TC12 EBI-16786283 0.27 Q5T9A4 EBI-16786283 0.27 Q5JTJ3 EBI-16786283 0.27 Q4VC31 EBI-16786283 0.27 Q49B96 EBI-16786283 0.27 Q3ZCQ8 EBI-16786283 0.27 Q16795 EBI-16786283 0.27 Q16740 EBI-16786283 0.27 Q16718 EBI-16786283 0.27 Q14249 EBI-16786283 0.27 Q14061 EBI-16786283 0.27 Q12849 EBI-16786283 0.27 Q04837 EBI-16786283 0.27 P99999 EBI-16786283 0.27 P83111 EBI-16786283 0.41 P62072 EBI-16786283 0.27 P61088 EBI-16786283 0.27 P56381 EBI-16786283 0.27 P56277 EBI-16786283 0.27 P53701 EBI-16786283 0.27 P51970 EBI-16786283 0.42 P49821 EBI-16786283 0.27 P49753 EBI-16786283 0.27 P48047 EBI-16786283 0.27 P46199 EBI-16786283 0.27 P38117 EBI-16786283 0.27 P36957 EBI-16786283 0.27 P36551 EBI-16786283 0.27 P35232 EBI-16786283 0.27 P34897 EBI-16786283 0.27 P32322 EBI-16786283 0.27 P31930 EBI-16786283 0.27 P31040 EBI-16786283 0.27 P30405 EBI-16786283 0.27 P28331 EBI-16786283 0.27 P25705 EBI-16786283 0.27 P24539 EBI-16786283 0.27 P22695 EBI-16786283 0.27 P20674 EBI-16786283 0.27 P19404 EBI-16786283 0.27 P19367 EBI-16786283 0.27 P18859 EBI-16786283 0.27 P14854 EBI-16786283 0.42 P13073 EBI-16786283 0.27 P10606 EBI-16786283 0.27 P10599 EBI-16786283 0.42 P09669 EBI-16786283 0.27 P08574 EBI-16786283 0.27 P07919 EBI-16786283 0.27 P06576 EBI-16786283 0.27 P05023 EBI-16786283 0.27 P00367 EBI-16786283 0.27 O96008 EBI-16786283 0.42 O96000 EBI-16786283 0.27 O95202 EBI-16786283 0.27 O94925 EBI-16786283 0.27 O94826 EBI-16786283 0.27 O75964 EBI-16786283 0.27 O75947 EBI-16786283 0.27 O75746 EBI-16786283 0.27 O75616 EBI-16786283 0.42 O75489 EBI-16786283 0.27 O75380 EBI-16786283 0.27 O75306 EBI-16786283 0.27 O60313 EBI-16786283 0.27 O60220 EBI-16786283 0.42 O43819 EBI-16786283 0.42 O43715 EBI-16786283 0.27 O43464 EBI-16786283 0.41 O00429 EBI-16786283 0.27 O00217 EBI-16786283 0.27 Q69YU5 EBI-16786283 0.27 P27694 EBI-16786589 0.35 P35244 EBI-16786589 0.35 P15927 EBI-16786589 0.35 Q9UHB6 EBI-16786589 0.35 Q9BSD7 EBI-16786589 0.35 Q96HS1 EBI-16786589 0.35 Q6PI48 EBI-16786589 0.35 Q10713 EBI-16786589 0.35 P49411 EBI-16786589 0.35 P18887 EBI-16786589 0.35 P0DMV8 EBI-16786589 0.35 P00374 EBI-16786589 0.35 O43813 EBI-16786589 0.35 P45880 EBI-16786589 0.35 Q02539 EBI-16786761 0.27 P53004 EBI-16786761 0.27 Q9HAV7 EBI-16786761 0.27 Q9H0I3 EBI-16786761 0.27 Q92522 EBI-16786761 0.27 P83881 EBI-16786761 0.27 P61604 EBI-16786761 0.27 P09622 EBI-20304669 0.35 P08559 EBI-20306509 0.35 P35610 EBI-20307233 0.35 P21796 EBI-20307902 0.35 Q9UI95 EBI-20219138 0.35 P51957 EBI-20721387 0.35 Q8IYE1 EBI-20902736 0.40 Q9HCD5 EBI-20905384 0.40 O75311 EBI-20905664 0.40 P08621 EBI-20907472 0.40 Q86X27 EBI-20908104 0.40 Q9Y6X8 EBI-20910808 0.40 Q9H2G2 EBI-20932552 0.40 Q13061 EBI-20932784 0.40 P14404 EBI-21026252 0.35 Q9BZR8 EBI-21258469 0.35 Q8IY21 EBI-21259607 0.35 F5H1C8 EBI-21264930 0.35 Q9H1C4 EBI-21266770 0.35 P05067 EBI-21132308 0.35 O60260 EBI-21135687 0.35 Q13153 EBI-25379067 0.35 P05129 EBI-25379555 0.35 Q05513 EBI-25380056 0.35 Q13322 EBI-25382050 0.35 P04049 EBI-25382473 0.35 Q13547 EBI-25394148 0.35 P0DOF2 EBI-25603126 0.35 P69479 EBI-25568051 0.35 P0DTD1 EBI-25509687 0.35 Q5EP34 EBI-25772822 0.61 C3W5S0 EBI-26452157 0.35 P15659 EBI-26452167 0.35 Q6DNN3 EBI-25773258 0.35 Q6DNT7 EBI-25773258 0.35 Q8TB24 EBI-26518569 0.35 Q6ZNK6 EBI-26453464 0.35 O60303 EBI-26582514 0.35 P34972 EBI-26880846 0.35 Q96T52 EBI-27049069 0.27 Q96LU5 EBI-27049466 0.27 Q9H300 EBI-27049982 0.27 Q8N488 EBI-27111302 0.35 Q8NCK7 EBI-27103180 0.35 A4FU01 EBI-27113520 0.35 Q99952 EBI-27114698 0.35 Q9Y603 EBI-29000341 0.35 P41162 EBI-29000231 0.35 P48742 EBI-29000712 0.35 Q9BXK1 EBI-29019783 0.35 O95600 EBI-29020196 0.35 Q86V87 EBI-34575191 0.27 GO:0005737 GO:0005829 GO:0005743 GO:0005758 GO:0005739 GO:0005634 GO:0048471 GO:0003677 GO:0071949 GO:0016174 GO:0003954 GO:0016651 GO:0072572 GO:0046983 GO:0006919 GO:0006915 GO:1904045 GO:0071392 GO:0070301 GO:0071732 GO:0090650 GO:0030261 GO:0070059 GO:0033108 GO:0032981 GO:0051402 GO:0030182 GO:0043065 GO:0060545 GO:0043525 GO:0012501 GO:0045041 GO:1902510 GO:0002931 GO:1902065 GO:0009636 Unknown UniProt Sequence Analysis MFRCGGLAAGALKQKLVPLVRTVCVRSPRQRNRLPGNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLSTVGAGAYAYKTMKEDEKRYNERISGLGLTPEQKQKKAALSASEGEEVPQDKAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALGRKARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED 613 Q9Z0X1 Apoptosis-inducing Aifm1 10090 None SL-0198 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}. UNIPROT Q9Z0X1 UNIPROT Q1L6K5 PDB 1GV4 PDB 3GD3 PDB 3GD4 PDB 5MIU PDB 5MIV Pfam PF14721 Pfam PF07992 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}. P10909 EBI-11065573 0.35 P17742 EBI-5326750 0.40 P27661 EBI-5326744 0.56 P16104 EBI-5326687 0.44 Q9Z0X1 EBI-5326701 0.44 Q8BP00 EBI-4282570 0.35 P09874 EBI-4412377 0.44 P10111 EBI-4533329 0.40 P62937 EBI-4533382 0.44 Q9EQN3 EBI-8296981 0.50 P14854 EBI-11065573 0.35 P09429 EBI-11065573 0.35 Q9UJZ1 EBI-11065573 0.35 P54819 EBI-11065573 0.35 Q9BRQ6 EBI-11065573 0.35 Q9Y266 EBI-11065573 0.35 P35232 EBI-11065573 0.35 Q16891 EBI-11065573 0.35 Q99623 EBI-11065573 0.35 Q8N4Q1 EBI-11065573 0.35 P21796 EBI-11065573 0.35 Q9NX63 EBI-11065573 0.35 Q16082 EBI-15182189 0.35 P51637 EBI-20565496 0.35 Q9NRI5 EBI-26612017 0.35 GO:0005737 GO:0005829 GO:0005743 GO:0005758 GO:0005741 GO:0005739 GO:0005634 GO:0048471 GO:0003677 GO:0004174 GO:0071949 GO:0016174 GO:0003954 GO:0016651 GO:0072572 GO:0046983 GO:0006919 GO:0008637 GO:0006915 GO:1904045 GO:0071392 GO:0070301 GO:0071732 GO:0090650 GO:0070059 GO:0033108 GO:0032981 GO:0051402 GO:0030182 GO:0043065 GO:0060545 GO:0043525 GO:0012501 GO:0045041 GO:1902510 GO:0002931 GO:1902065 GO:0006979 GO:0009636 Unknown UniProt Sequence Analysis MFRCGGLAGAFKQKLVPLVRTVYVQRPKQRNRLPGNLFQQWRVPLELQMARQMASSGSSGGKMDNSVLVLIVGLSTIGAGAYAYKTIKEDQKRYNERVMGLGLSPEEKQRRAIASATEGGSVPQIRAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLQFRQWNGKERSIYFQPPSFYVSAQDLPNIENGGVAVLTGKKVVHLDVRGNMVKLNDGSQITFEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRALEKISREVKSITVIGGGFLGSELACALGRKSQASGIEVIQLFPEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGRLLIKLKDGRKVETDHIVTAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSAPAVPQVPVEGEDYGKGVIFYLRDKVVVGIVLWNVFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED 612 Q9JM53 Apoptosis-inducing Aifm1 10116 None SL-0198 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}. UNIPROT Q9JM53 UNIPROT Q548E3 Pfam PF14721 Pfam PF07992 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}. GO:0005737 GO:0005829 GO:0005743 GO:0005758 GO:0005739 GO:0005634 GO:0048471 GO:0003677 GO:0071949 GO:0016174 GO:0003954 GO:0016651 GO:0072572 GO:0046983 GO:0006919 GO:0006915 GO:1904045 GO:0071392 GO:0070301 GO:0071732 GO:0090650 GO:0070059 GO:0033108 GO:0032981 GO:0051402 GO:0010942 GO:0060545 GO:0043525 GO:0012501 GO:0045041 GO:1902510 GO:0002931 GO:1902065 GO:0009636 Unknown UniProt Sequence Analysis MFRCGGLAGAFKQKLVPLVRSVCVQRPKQRNRLPGNLFQQWRVPLELQMARQMASSGPSGGKMDNSVLVLIVGLSTIGAGAYAYKTIKEDQKRYNERIMGLGLSPEEKQRRAIASAAEGGSVPPIRVPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLQFRQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVHLDVRGNMVKLNDGSQITFEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRALEKISREVKSITVIGGGFLGSELACALGRKSQASGIEVIQLFPEKGNMGKILPEYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGKLLIKLKDGRKVETDHIVTAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSDPAVPQVPVEGEDYGKGVIFYLRDKVVVGIVLWNVFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED 612 Q13023 A-kinase AKAP6 9606 None SL-0178 SL-0182 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. UNIPROT Q13023 UNIPROT A7E242 UNIPROT A7E2D4 UNIPROT O15028 OMIM 604691 DisGeNET 9472 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. P00519 EBI-1957451 0.40 P12931 EBI-1960946 0.40 Q06787 EBI-21392373 0.00 Q96EV8 EBI-1105409 0.00 P46108 EBI-1959534 0.40 P06241 EBI-1961210 0.40 P62993 EBI-1964442 0.40 P16333 EBI-1968724 0.40 P27986 EBI-1970517 0.40 A0A6L8PLI9 EBI-2838568 0.00 Q96CV9 EBI-5357521 0.45 Q92736 EBI-8758107 0.27 P14404 EBI-21028244 0.35 Q99459 EBI-21392414 0.00 Q9NRI5 EBI-21392402 0.00 Q8TDR0 EBI-21392387 0.00 GO:0034704 GO:0005901 GO:0005737 GO:0014704 GO:0014701 GO:0005635 GO:0031965 GO:0048471 GO:0016529 GO:0030315 GO:0008179 GO:0060090 GO:0051018 GO:0034237 GO:0043495 GO:0044325 GO:0001508 GO:0019933 GO:0071320 GO:0071345 GO:0070886 GO:0030307 GO:0061051 GO:1902261 GO:1901381 GO:0051281 GO:0060316 GO:0006605 GO:0060306 GO:0010738 GO:0010880 Unknown UniProt Sequence Analysis MLTMSVTLSPLRSQDLDPMATDASPMAINMTPTVEQGEGEEAMKDMDSDQQYEKPPPLHTGADWKIVLHLPEIETWLRMTSERVRDLTYSVQQDSDSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLVLRERILQGLQDANGNYTRQTDILQAFSEETKEGRLDSLTEVDDSGQLTIKCSQNYLSLDCGITAFELSDYSPSEDLLSGLGDMTSSQVKTKPFDSWSYSEMEKEFPELIRSVGLLTVAADSISTNGSEAVTEEVSQVSLSVDDKGGCEEDNASAVEEQPGLTLGVSSSSGEALTNAAQPSSETVQQESSSSSHHDAKNQQPVPCENATPKRTIRDCFNYNEDSPTQPTLPKRGLFLKEETFKNDLKGNGGKRQMVDLKPEMSRSTPSLVDPPDRSKLCLVLQSSYPNSPSAASQSYECLHKVGNGNLENTVKFHIKEISSSLGRLNDCYKEKSRLKKPHKTSEEVPPCRTPKRGTGSGKQAKNTKSSAVPNGELSYTSKAIEGPQTNSASTSSLEPCNQRSWNAKLQLQSETSSSPAFTQSSESSVGSDNIMSPVPLLSKHKSKKGQASSPSHVTRNGEVVEAWYGSDEYLALPSHLKQTEVLALKLENLTKLLPQKPRGETIQNIDDWELSEMNSDSEIYPTYHVKKKHTRLGRVSPSSSSDIASSLGESIESGPLSDILSDEESSMPLAGMKKYADEKSERASSSEKNESHSATKSALIQKLMQDIQHQDNYEAIWEKIEGFVNKLDEFIQWLNEAMETTENWTPPKAEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRMIASQWKELQRQIKRQHSWILRALDTIKAEILATDVSVEDEEGTGSPKAEVQLCYLEAQRDAVEQMSLKLYSEQYTSSSKRKEEFADMSKVHSVGSNGLLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEKVDSINEKWELLGKTLGEKIQDTMAGHSGSSPRDLLSPESGSLVRQLEVRIKELKGWLRDTELFIFNSCLRQEKEGTMNTEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRETCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESETLNVIDPGLMDLNGMSEDALEWDEMDISNKLISLNEESNDLDQELQPVIPSLKLGETSNEDPGYDEEADNHGGSQYASNITAPSSPHIYQVYSLHNVELYEDNHMPFLKNNPKVTGMTQPNVLTKSLSKDSSFSSTKSLPDLLGGSNLVKPCACHGGDMSQNSGSESGIVSEGDTETTTNSEMCLLNAVDGSPSNLETEHLDPQMGDAVNVLKQKFTDEGESIKLPNSSQSSISPVGCVNGKVGDLNSITKHTPDCLGEELQGKHDVFTFYDYSYLQGSKLKLPMIMKQSQSEKAHVEDPLLRGFYFDKKSCKSKHQTTELQPDVPPHERILASASHEMDRISYKSGNIEKTFTGMQNAKQLSLLSHSSSIESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFTGQMSLDIASSINEDSAASLTELSSSDELSLCSEDIVLHKNKIPESNASFRKRLTRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCIKDEDDDSSIATDDEIYEDCTLMSGLDYIKNELQTWIRPKLSLTRDKKRCNVSDEMKGSKDISSSEMTNPSDTLNIETLLNGSVKRVSENNGNGKNSSHTHELGTKRENKKTIFKVNKDPYVADMENGNIEGIPERQKGKPNVTSKVSENLGSHGKEISESEHCKCKALMDSLDDSNTAGKEFVSQDVRHLPKKCPNHHHFENQSTASTPTEKSFSELALETRFNNRQDSDALKSSDDAPSMAGKSAGCCLALEQNGTEENASISNISCCNCEPDVFHQKDAEDCSVHNFVKEIIDMASTALKSKSQPENEVAAPTSLTQIKEKVLEHSHRPIQLRKGDFYSYLSLSSHDSDCGEVTNYIEEKSSTPLPLDTTDSGLDDKEDIECFFEACVEGDSDGEEPCFSSAPPNESAVPSEAAMPLQATACSSEFSDSSLSADDADTVALSSPSSQERAEVGKEVNGLPQTSSGCAENLEFTPSKLDSEKESSGKPGESGMPEEHNAASAKSKVQDLSLKANQPTDKAALHPSPKTLTCEENLLNLHEKRHRNMHR 2319 Q9WVC7 A-kinase Akap6 10116 None SL-0178 SL-0182 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. UNIPROT Q9WVC7 Pfam PF00435 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}. P20651 EBI-7559869 0.52 P48453 EBI-7559943 0.44 F1LMY4 EBI-16420846 0.35 GO:0034704 GO:0005901 GO:0005737 GO:0014704 GO:0014701 GO:0005635 GO:0031965 GO:0005634 GO:0048471 GO:0032991 GO:0042383 GO:0016529 GO:0030315 GO:0008179 GO:0019899 GO:0060090 GO:0051018 GO:0034237 GO:0051721 GO:0043495 GO:0044325 GO:0071320 GO:0071345 GO:0071872 GO:0007194 GO:0070886 GO:2000481 GO:0030307 GO:0061051 GO:1902261 GO:1901381 GO:0001934 GO:0051281 GO:0060316 GO:0045727 GO:0031503 GO:0086004 GO:0060306 GO:0010738 GO:1901897 GO:0010880 Unknown UniProt Sequence Analysis MLTMSVTLSPLRSQGPDPMATDASPMAINMTPTVEQEEGEGEEAVKAIDAEQQYGKPPPLHTAADWKIVLHLPEIETWLRMTSERVRDLTYSVQQDADSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLVLRERILQGLQDANGNYTRQTDILQAFSEETTEGRLDSLTEVDDSGQLTIKCSQDYLSLDCGITAFELSDYSPSEDLLGGLGDMTTSQAKTKSFDSWSYSEMEKEFPELIRSVGLLTVATEPVPSSCGEANEDSSQASLSDDHKGEHGEDGAPVPGQQLDSTVGMSSLDGTLANAAEHPSETAKQDSTSSPQLGAKKTQPGPCEITTPKRSIRDCFNYNEDSPTQPTLPKRGLFLKETQKNERKGSDRKGQVVDLKPELSRSTPSLVDPPDRSKLCLVLQSSYPSSPSAASQSYECLHKVGLGNLENIVRSHIKEISSSLGRLTDCHKEKLRLKKPHKTLAEVSLCRIPKQGGGSGKRSESTGSSAGPSMVSPGAPKATMRPETDSASTASGGLCHQRNRSGQLPVQSKASSSPPCSHSSESSLGSDSIKSPVPLLSKNKSQKSSPPAPCHATQNGQVVEAWYGSDEYLALPSHLKQTEVLALKLESLTKLLPQKPRGETIQDIDDWELSEMNSDSEIYPTYHIKKKHTRLGTVSPSSSSDIASSLGESIESGPLSDILSDEDLCLPLSSVKKFTDEKSERPSSSEKNESHSATRSALIQKLMHDIQHQENYEAIWERIEGFVNKLDEFIQWLNEAMETTENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVSHKAGLKDTLRMIASQWKELQRQIKRQHSWILRALDTIKAEILATDVSVEDEEGTGSPKAEVQLCHLETQRDAVEQMSLKLYSEQYTSGSKRKEEFANMSKAHAEGSNGLLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKSELLSKVEALKKGGLSLPDDILEKVDSINEKWELLGKTLREKIQDTIAGHSGSGPRDLLSPESGSLVRQLEVRIKELKRWLRDTELFIFNSCLRQEKEGTSAEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESETLNVIDPGLMDLNGMSEDALEWDETDISNKLISVHEESNDLDQDPEPMLPAVKLEETHHKDSGYEEEAGDCGGSPYTSNITAPSSPHIYQVYSLHNVELHEDSHTPFLKSSPKFTGTTQPTVLTKSLSKDSSFSSTKSLPDLLGGSGLVRPYSCHSGDLSQNSGSESGIVSEGDNEMPTNSDMSLFSMVDGSPSNPETEHPDPQMGDAANVLEQKFKDNGESIKLSSVSRASVSPVGCVNGKAGDLNSVTKHTADCLGEELQGKHDVFTFYDYSYLQGSKLKLPMIMKQPQSEKAHVEDPLLGGFYFDKKSCKAKHQASESQPDAPPHERILASAPHEMGRSAYKSSDIEKTFTGIQSARQLSLLSRSSSVESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDMTLQSSSQKMPFAGQMSLDVASSINEDSPASLTELSSSDELSLCSEDIVLHKNKIPESNASFRKRLNRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCLKDEDDDSSIATDDEIYEESNLMSGLDYIKNELQTWIRPKLSLTREKKRSGVTDEIKVNKDGGGNEKANPSDTLDIEALLNGSIRCLSENNGNGKTPPRTHGSGTKGENKKSTYDVSKDPHVADMENGNIESTPEREREKPQGLPEVSENLASNVKTISESELSEYEAVMDGSEDSSVARKEFCPPNDRHPPQMGPKLQHPENQSGDCKPVQNPCPGLLSEAGVGSRQDSNGLKSLPNDAPSGARKPAGCCLLEQNETEESASISSNASCCNCKPDVFHQKDDEDCSVHDFVKEIIDMASTALKSKSQPESEVAAPTSLTQIKEKVLEHSHRPIHLRKGDFYSYLSLSSHDSDCGEVTNYIDEKSSTPLPPDAVDSGLDDKEDMDCFFEACVEDEPVNEEAGLPGALPNESAIEDGAEQKSEQKTASSPVLSDKTDLVPLSGLSPQKGADDAKEGDDVSHTSQGCAESTEPTTPSGKANAEGRSRMQGVSATPEENAASAKPKIQAFSLNAKQPKGKVAMRYPSPQTLTCKEKLVNFHEDRHSNMHR 2314 Q148F2 Arachidonate ALOX5AP 9913 None SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q148F2 Pfam PF01124 PROSITE PS01297 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}. GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0050544 GO:0008047 GO:0004602 GO:0004364 GO:0004464 GO:0019370 Transmembrane UniProt By Similarity {ECO:0000250} MDQEAVGNIVLLAIVTLISVVQNGFFAHKVEHESKTHNGRSFQRTGTLAFERVYTANQNCVDAYPTFLVMLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFAMSLAGILNYFFIALFGSDFENYIKTVTTTISPLLLIP 161 P30353 Arachidonate ALOX5AP 9796 None SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT P30353 Pfam PF01124 PROSITE PS01297 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}. GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0050544 GO:0008047 GO:0004602 GO:0004364 GO:0004464 GO:0019370 Transmembrane UniProt By Similarity {ECO:0000250} MDQETVGNVVLLAIVTLISVIQNGFFAHKVEHESKTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLVMLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERRQSTPGYIFGKRIILFLFLMSLAGIFNYYLILFFGSDFENYIKTITTT 153 P20292 Arachidonate ALOX5AP 9606 None SL-0178 SL-0182 Nucleus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. UNIPROT P20292 UNIPROT Q5VV04 PDB 2Q7M PDB 2Q7R PDB 6VGC PDB 6VGI Pfam PF01124 PROSITE PS01297 OMIM 601367 OMIM 603700 DisGeNET 241 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}. 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}. A0PK00 EBI-24765164 0.56 O00299 EBI-3904626 0.37 Q9H115 EBI-24738406 0.56 Q96FB2 EBI-24768960 0.56 O15529 EBI-24778364 0.56 P35372 EBI-24571720 0.56 Q13520 EBI-24799898 0.56 O15552 EBI-24808129 0.56 Q70Z53 EBI-21893005 0.40 P20292 EBI-26452342 0.40 GO:0005829 GO:0005783 GO:0005789 GO:0016021 GO:0016020 GO:0005635 GO:0031965 GO:0004051 GO:0050544 GO:0008047 GO:0019899 GO:0004602 GO:0004364 GO:0042802 GO:0004464 GO:0047485 GO:0044877 GO:0071277 GO:0019370 GO:0002540 GO:0019372 GO:0002675 GO:0070207 Transmembrane UniProt Sequence Analysis MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTISTTISPLLLIP 161 Q2PG08 Arachidonate ALOX5AP 9541 None SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q2PG08 Pfam PF01124 PROSITE PS01297 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}. GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0050544 GO:0008047 GO:0047485 GO:0071277 GO:0019370 GO:0002540 GO:0070207 Transmembrane UniProt By Similarity {ECO:0000250} MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQVPAAFAGLMYLLVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTVTTTISPLLLIP 161 P30354 Arachidonate ALOX5AP 9544 None SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT P30354 Pfam PF01124 PROSITE PS01297 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}. GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0050544 GO:0008047 GO:0004602 GO:0004364 GO:0004464 GO:0019370 Transmembrane UniProt By Similarity {ECO:0000250} MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQVPAAFAGLMYLLVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTVTTT 153 P30355 Arachidonate Alox5ap 10090 None SL-0178 SL-0182 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}. UNIPROT P30355 UNIPROT Q9D138 Pfam PF01124 PROSITE PS01297 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}. GO:0005829 GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0005634 GO:0004051 GO:0050544 GO:0008047 GO:0019899 GO:0004602 GO:0004364 GO:0042802 GO:0004464 GO:0047485 GO:0044877 GO:0071277 GO:0019370 GO:0002540 GO:0019372 GO:0002675 GO:0070207 Transmembrane UniProt By Similarity {ECO:0000250} MDQEAVGNVVLLALVTLISVVQNAFFAHKVEHESKAHNGRSFQRTGTLAFERVYTANQNCVDAYPTFLVVLWTAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSFAGILNHYLIFFFGSDFENYIRTVSTTISPLLLIP 161 P30356 Arachidonate ALOX5AP 9823 None SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT P30356 Pfam PF01124 PROSITE PS01297 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}. GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0050544 GO:0008047 GO:0004602 GO:0004364 GO:0004464 GO:0019370 Transmembrane UniProt By Similarity {ECO:0000250} MDQEAMGNIVLLAIVTLISVVQNAFFAHKVEHESKTHNGRSFQRTGTPAFERVYTANQNCVDAYPTFLVVLWSAGLFCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGIFNYFLILFFGSDFENYIKTITTT 153 P30357 Arachidonate ALOX5AP 9986 None SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT P30357 Pfam PF01124 PROSITE PS01297 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}. GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0050544 GO:0008047 GO:0019370 Transmembrane UniProt By Similarity {ECO:0000250} MDQEAVGNVVLLAIVTLISVVQNGFFAHKVEHESRNQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWTAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGILNYCLILLFGSDFENYIKTISTT 153 P20291 Arachidonate Alox5ap 10116 None SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT P20291 UNIPROT Q5RJL3 Pfam PF01124 PROSITE PS01297 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}. P12527 EBI-15746644 0.49 P20291 EBI-15746661 0.40 GO:0005829 GO:0005783 GO:0005789 GO:0016021 GO:0016020 GO:0005635 GO:0031965 GO:0005634 GO:0050544 GO:0008047 GO:0019899 GO:0004602 GO:0004364 GO:0042802 GO:0004464 GO:0047485 GO:0044877 GO:0071277 GO:0019370 GO:0002540 GO:0019372 GO:0002675 GO:0070207 Transmembrane UniProt By Similarity {ECO:0000250} MDQEAVGNVVLLAIVTLISVVQNAFFAHKVELESKAQSGRSFQRTGTLAFERVYTANQNCVDAYPTFLVVLWTAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGILNHYLIFFFGSDFENYIRTITTTISPLLLIP 161 P30358 Arachidonate ALOX5AP 9940 None SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT P30358 Pfam PF01124 PROSITE PS01297 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}. GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0050544 GO:0008047 GO:0019370 Transmembrane UniProt By Similarity {ECO:0000250} MDQETVGNIVLLAIVTLISVVQNGFFAHKVEHESKTHNGRSFQRTGPLAFERVYTANQNCVDAYPTFLVMLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFAMSLAGILNYFLIAFFGSDFENYIKTVTTT 153 Q750Y9 UDP-N-acetylglucosamine ALG14 284811 None SL-0178 SL-0182 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}. UNIPROT Q750Y9 Pfam PF08660 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}. GO:0030176 GO:0031965 GO:0043541 GO:0004577 GO:0043495 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAWLAIVCLLAATTALCVRMAALAPGVYGPAVCGGRSGGGRGPPRHVMIFLGSGGHTGEMLRLLEVYGAALVAGATVRVGYTDEASAERGRQSAALRAARGVEYVPLLKAREVGAGAGAAVRSTVRAAAQAFSAVRRARRALHTGPHVVVLNGPGTSVVVLFWLRVLDLLSLRRTRVVYVESLARTESLSLSGRLAYPFADEFVVQWPDLAQRYRRARWFGALV 224 Q4WNB5 UDP-N-acetylglucosamine alg14 330879 None SL-0178 SL-0182 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}. UNIPROT Q4WNB5 Pfam PF08660 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}. GO:0016021 GO:0031965 GO:0043541 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MFSMLRRMKLDPSTYTYRTYVVSSGDNFSAARAVEFETEWLKQSPKLSFPANGSNSTESYAVVTVPRARRVHQSYLTAPLSTLQCFYACFLVLCGRHPEQKSPLPTTNSPYPDVILTNGPATAVCMVLAAKSLRLFHYLKSLFYIKDHQDRDSSRSSQVKRSEDAPAPVHFQLRTIYVESWARVTTFSLSGKLLLPFADRFLVQWPDLAGKQAWRGMRETEYAGTLVD 228 Q5A5N6 UDP-N-acetylglucosamine ALG14 237561 None SL-0178 SL-0182 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}. UNIPROT Q5A5N6 UNIPROT A0A1D8PIT0 Pfam PF08660 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}. GO:0016021 GO:0031965 GO:0043541 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDIETAACFSIAFIATPILIVLVRLLFILPSLRLPTSVKKKKKLIQECQLSILLGSGGHTGEMMRIISKLDMGKVSRTWIYTSGDNASLAKAQDYERKSGTSSQYIPIPRARTVGQSYISSIPTTIYSFLFSAIAMLKHRPAVILLNGPGTCVPVAYILFLYKLLGLCNTKIIYIESLARVNKLSLSGLLLLPISDRFIVQWESLYQQYSRVEYYGILI 219 Q6FV75 UDP-N-acetylglucosamine ALG14 284593 None SL-0178 SL-0182 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}. UNIPROT Q6FV75 Pfam PF08660 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}. GO:0030176 GO:0031965 GO:0043541 GO:0004577 GO:0043495 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPFLSTAHLCALLLILGCFYIGRLIKVIPILRFACAGEAEIKPLFIQPKSNDGIHLFVFLGSGGHTGEMLRLLQNHQEVLLNKRNTFYIGYSDDDSKARFLSMVEKYDFKAERIHFYPFAKAREVNAGPIASIVTISKTLLTGFTNVLSIKMNTLGQPHLTLLNGPGTCCIINFWLKLLEWLIYIPYLSNGSNVVYIESLARIESLSLTGKILYLLADVFVVQWEELKVRKAPRSEYYGILV 242 P0CM11 UDP-N-acetylglucosamine ALG14 283643 None SL-0178 SL-0182 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}. UNIPROT P0CM11 UNIPROT Q55XH5 UNIPROT Q5KMF9 Pfam PF08660 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}. GO:0005789 GO:0016021 GO:0031965 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSLGRYIGWSILAFTYLVLAILLRLIFLQPSKTSRASYRPKDAKCSLGVFLGSGGHTSEMKALLSTLDYERYQPRTYIYCHGDDLSLRAVSDIESSKGGLISSKMYYLLSLPRARRVGQPLLSTMVSVLKTLYIAALRLFLIPLLKNPRRPFVDLLIVNGPGTCVVLVLVSYIRRVRLEYTRIIYVESFARVKSLSLSGKMIRPLADRFLVQWPDASDSDNVIHKGLLV 229 P0CM10 UDP-N-acetylglucosamine ALG14 214684 None SL-0178 SL-0182 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}. UNIPROT P0CM10 UNIPROT Q55XH5 UNIPROT Q5KMF9 Pfam PF08660 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}. GO:0016021 GO:0031965 GO:0043541 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSLGRYIGWSILAFTYLVLAILLRLIFLQPSKTSRASYRPKDAKCSLGVFLGSGGHTSEMKALLSTLDYERYQPRTYIYCHGDDLSLRAVSDIESSKGGLISSKMYYLLSLPRARRVGQPLLSTMVSVLKTLYIAALRLFLIPLLKNPRRPFVDLLIVNGPGTCVVLVLVSYIRRVRLEYTRIIYVESFARVKSLSLSGKMIRPLADRFLVQWPDASDSDNVIHKGLLV 229 Q6BMD0 UDP-N-acetylglucosamine ALG14 284592 None SL-0178 SL-0182 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}. UNIPROT Q6BMD0 Pfam PF08660 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}. GO:0005789 GO:0016021 GO:0031965 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDFESQLCIKVVLLLLPFFIIGIRLLWVLPAVNSPAMGSEKEKGLSQIPSELRGSNIMIFLGSGGHTGEMMRILANVDLNNFNRTWVTSSGDSTSILKCKKYEDERLTSGQNKSDYLVLHRARTVGESIISSVFSTVRSLISTIKHLYELPQFPSILLLNGPGTSVPLAYIIFLLKFLGLCKTRIIYIESLARVKQLSVSGLLILPITDRFIVQWKQLAVKYKRAEYYGILI 232 Q96F25 UDP-N-acetylglucosamine ALG14 9606 None SL-0178 SL-0182 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}. UNIPROT Q96F25 UNIPROT A8K030 Pfam PF08660 OMIM 612866 OMIM 616227 OMIM 619031 OMIM 619036 DisGeNET 199857 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}. 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. Q99871 EBI-21670231 0.35 Q9Y5Q0 EBI-21766826 0.35 P0DTD8 EBI-25687199 0.53 Q7TFA1 EBI-25688644 0.35 GO:0005789 GO:0016021 GO:0031965 GO:0043541 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVCVLVLAAAAGAVAVFLILRIWVVLRSMDVTPRESLSILVVAGSGGHTTEILRLLGSLSNAYSPRHYVIADTDEMSANKINSFELDRADRDPSNMYTKYYIHRIPRSREVQQSWPSTVFTTLHSMWLSFPLIHRVKPDLVLCNGPGTCVPICVSALLLGILGIKKVIIVYVESICRVETLSMSGKILFHLSDYFIVQWPALKEKYPKSVYLGRIV 216 Q6CJG3 UDP-N-acetylglucosamine ALG14 284590 None SL-0178 SL-0182 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}. UNIPROT Q6CJG3 Pfam PF08660 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}. GO:0030176 GO:0031965 GO:0043541 GO:0004577 GO:0043495 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLLTTAWCLLIWSVTLLLVRICLVIPIFHSSREAGPLTKDKDNVGGRMKNLVLFIFLGSGGHTGEMLRLIEHYQGMLLESAVTIHVGYSDDDSIIKFKNKIHQISVSNTLRAKVIYHRFDKARDVGSSLAGSIKSIIKTAIRSMVLTYRIKSSMRGHPNLTLLNGPGTCCIITFWLKLYHIFLWQPSKIVYVESLARTNRLSLTGMILYPLADEFVVQWADLLPIYPKAKYYGVLV 236 Q9D081 UDP-N-acetylglucosamine Alg14 10090 None SL-0178 SL-0182 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}. UNIPROT Q9D081 UNIPROT Q8CEP2 Pfam PF08660 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}. GO:0016021 GO:0031965 GO:0043541 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLSILILAATAAGLVILLFQRLWTVLGPHHVTPRESLRLLIVAGSGGHTTEILRLVGSLSNAYSPRHYVIAESDEMSAKKIHSLEELSRAQNDSTTEYPKYHLHRIPRSREVRQSWLSSVFTTFYSMWFSFPLVLRIKPDLVLCNGPGTCVPICVSALLLGILGVKKVIIVYVESICRVETLSLSGKILRHLSDYFIVQWPTLKEKYPKSVYLGRIV 217 Q6AY85 UDP-N-acetylglucosamine Alg14 10116 None SL-0178 SL-0182 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}. UNIPROT Q6AY85 Pfam PF08660 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}. GO:0016021 GO:0031965 GO:0043541 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVCVLTLAASAGGLAVLLIVRLWAVLRSHPVTPRQSLGLLIVAGSGGHTAEILRLVGSLSGAYSPRHYVIAESDEMSAKKIHSLELARAQNDSTTEHTEYYLHRIPRSREVRQSWLSSVFTTLYSIWFSFPLVHRIKPDLVLCNGPGTCVPICVSALLLGILGIKKVIIVYVESICRVETLSLSGKILWHLSDYFIVQWPTLKEKYPKSVYLGRIV 216 O14199 UDP-N-acetylglucosamine alg14 284812 None SL-0178 SL-0182 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}. UNIPROT O14199 Pfam PF08660 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}. GO:0005783 GO:0030176 GO:0031965 GO:0043541 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNTYVLTAIAVLASLIILLVGRNAIKSSKKKPFQKHLLVFFGSGGHTGEMLNLLNALDDKLYSVRSYVAGSDDTMSVSKASLLSNSLPSVKSKIFKVPRARYVKQSWLTTPFTAFWSLLGSISVIFWNPFGIPDVILCNGPGTCVFICLLGYLAKFLGKNVKIVYVESFARVKSLSLSGKILMPFVDRFLVQWPDLATKYKRAEYIGIVA 210 Q6CF02 UDP-N-acetylglucosamine ALG14 284591 None SL-0178 SL-0182 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}. UNIPROT Q6CF02 Pfam PF08660 Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). {ECO:0000250}. GO:0016021 GO:0031965 GO:0043541 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVTTILIAASAILVLLLLRLLFVLPASNRFGFLYRPKHSNPKLMVMMGSGGHTGEMLRMLKTLKLQSYAKRVYVSSSGDVDSLEKVKVLESTTKTDIKTMVLENIPRARKVGQSYPSSVITSAVSFAVAVKLVHKHKPHVIVCNGPATCVMLCYAAFLLRFMALIDTRIIYVESLARVNRLSLSGLILLPFCDRFLVQWPQLAEKYPRAEYHGILV 216 P38242 UDP-N-acetylglucosamine ALG14 559292 None SL-0178 SL-0182 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}. UNIPROT P38242 UNIPROT D6VQ69 Pfam PF08660 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}. P11484 EBI-804270 0.53 P10592 EBI-804270 0.35 P40069 EBI-804270 0.35 P53178 EBI-989509 0.46 P53223 EBI-6336679 0.00 P25294 EBI-3660139 0.35 P10591 EBI-3667000 0.35 P32589 EBI-3723318 0.35 GO:0005789 GO:0030176 GO:0031227 GO:0031965 GO:0042175 GO:0043541 GO:0043495 GO:0006488 Transmembrane UniProt Sequence Analysis {ECO:0000255} MKTAYLASLVLIVSTAYVIRLIAILPFFHTQAGTEKDTKDGVNLLKIRKSSKKPLKIFVFLGSGGHTGEMIRLLENYQDLLLGKSIVYLGYSDEASRQRFAHFIKKFGHCKVKYYEFMKAREVKATLLQSVKTIIGTLVQSFVHVVRIRFAMCGSPHLFLLNGPGTCCIISFWLKIMELLLPLLGSSHIVYVESLARINTPSLTGKILYWVVDEFIVQWQELRDNYLPRSKWFGILV 237 Q9UTK5 Nucleoporin alm1 284812 None SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000269|PubMed:28974540}. Nucleus envelope {ECO:0000269|PubMed:28974540}. UNIPROT Q9UTK5 UNIPROT O13313 UNIPROT Q9UTT8 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}. GO:0005635 GO:0005643 GO:0044615 GO:0140602 GO:0005634 GO:0017056 GO:0006406 GO:0015031 Unknown UniProt Sequence Analysis MSSGGLEDDIQLVHEFLDVSFEDIKPLVSVNGFAVFISAIKTKVKDINALKDQLVLQEVNHEHKENVLTKKINFLEQQLQSSNNQAEESRNLISVLRNENESLKTNLENQNKRFDALTTENQSLRRANSELQEQSKIASEQLSIAKDQIEALQNENSHLGEQVQSAHQALSDIEERKKQHMFASSSSRVKEEILVQEKSALVSDLASLQSDHSKVCEKLEVSSRQVQDLEKKLAGLAQQNTELNEKIQLFEQKRSNYSSDGNISKILETDPTSIKELEEEVETQKRLTALWESKSSELQSEVAALQEKLTSQQSLYNNVTEELNNNKQQLLISENSLRELQEKYDSVVSELQVVKENKNTSVSAGVGLFSPLAQKLSAVQNPEFSFTKVYSDNMKLQQKVSSLKLQLDRLTNKFSSFCEQVKQRIPVVKQQRSEIVRNNIYMNFLSESLETSNNNLTKVQAELLSTKMRQEACYLQLTASRTQCSDLSREVICLMAELDHLNETKSRNVPATVQVALDEYAQNPSTASETLVNKELANFSSIKEAVSKTLELREKVRALECDVEIQKQTVQYQISNAVKENSNTLSEQIKNLESELNSSKIKNESLLNERNLLKEMLATSRSSILSHNSSAGNIDDKMKSIDESTRELEKNYEVYRNEMTAIQESLSKRNQDLLSEMEAIRKELENSKYQQQLSTDRLTNANNDVEAFKKEAKELRSINQNLQDIISRQDQRASKFAEELLHVNSLAERLKGELNASKGEKDLRKRTQERLISENDKLLAERERLMSLVSDLQTFLNQQQLSDAARKVKFESEKESLSLSLQKLKESNEKMSNDLHSLQKSLEKSGIEYSSRIKTLMLEKQSLSEDNRKLLDNQQMMEIKLQELNGVIELEKQRFSTLEAKFTQQKNTSYSEREALLESSLSDLQSKHTSLESQYNYSLRNIEQLQAASKLAEEMVERVKTEYDEYRLQTSESLEKNHLKITSLEQRIVILQDEIASSSLRCENITKDSETRVALLLEENKHLNNELSSHRNAEKQHLEKENDYKQQLLLVTEDLRKTREDYEKELLRHADARSTLQKLREDYTKALEQVEDLNKEIALKAGINESQPFPISEKEDPLRQEVYVLKKQNAMLLTQLQSSNLNFAEITSPSPDLDSVMKLGLSDLQNHVKRISKEMEIISCQRQLLFLENKKLKRTVESSNRVIADLQRGITEKDVSSTSESVGERSNYLNMVALLNESNKSLRENLERNEEVITELREKIETLKTDLANFRLNKEQLESQLQTEKAAVKKLENSNEEYKRHNQEILLSLNSSTSTSSDASRLKNELVSKENLIEELNQEIGHLKSELETVKSKSEDLENERAQNQSKIEQLELKNTKLAAAWRTKYEQVVNKSLEKHNQIRQQLSQKTSELEAKVAECHQLNEQLNKPSATPTATTQSEPSTVSLEEFNSTKEELSSTQRKLSEIMDILNTTKEELEKVRQNSNKSEGTSKDTEIPNEEEMERKKVMQQEVLRLRSRIAKELQKNELLRKQNQVLQDQVKALQETVVSSEEAESASVHADTKDLENLKKTEEMLSVTFQVIFNESISDFSTSTADFTTFVQKEWEKRREILQKDVEEQVAQSHQKQLDNIRKELEMRNKLKLSMLEKNLARVRAELEQSKKKDSPAILSLEASKNTDSNKSNSEVPAAQVKEKKLIAKTHSVDTNSPPKRSSSDAGMDVSNDVKKAK 1727 P00978 Trypstatin AMBP 9913 None SL-0178 SL-0182 [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}. UNIPROT P00978 UNIPROT P35420 UNIPROT Q28020 UNIPROT Q3SZZ4 Pfam PF00014 Pfam PF00061 PROSITE PS00280 PROSITE PS50279 PROSITE PS00213 [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}. GO:0009986 GO:0005829 GO:0005783 GO:0005576 GO:0005615 GO:0031314 GO:0005743 GO:0031965 GO:0005886 GO:0016209 GO:0035374 GO:0098633 GO:0020037 GO:0019862 GO:0016491 GO:0016653 GO:0042803 GO:0004867 GO:0098869 GO:0034614 GO:1903606 GO:0020027 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P02760} MRSLSGLLLLLTACLAVNASSVPTLPDDIQVQENFDLSRIYGKWFNVAVGSTCPWLKRFKEKMTMSTVVLIAGPTSKEISVTNTHRRKGVCESISGTYEKTSADGKFLYHKAKWNITMESYVVHTNYDEYAIFLTKKLSRRHGPTITVKLYGREPQLRESLLEEFREVALGVGIPEDAIFTMPDRGECVPGEQDPVPTPLSRARRAVLTQEEEGSGAGQPVTNFSKKADSCQLDYSQGPCLGLFKRYFYNGTSMACETFLYGGCMGNGNNFLSEKECLQTCRTVEACNLPIVQGPCRSYIQLWAFDAVKGKCVRFSYGGCKGNGNKFYSEKECKEYCGIPGEADEELLRFSN 352 P02760 Trypstatin AMBP 9606 None SL-0178 SL-0182 [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}. UNIPROT P02760 UNIPROT P00977 UNIPROT P02759 UNIPROT P78491 UNIPROT Q2TU33 UNIPROT Q5TBD7 UNIPROT Q9UC58 UNIPROT Q9UDI8 PDB 1BIK PDB 3QKG PDB 4ES7 PDB 4U30 PDB 6EJ7 PDB 6EJ8 PDB 6EJ9 PDB 6EJA PDB 6EJB PDB 6EJC PDB 6EJD Pfam PF00014 Pfam PF00061 PROSITE PS00280 PROSITE PS50279 PROSITE PS00213 OMIM 176870 DisGeNET 259 [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}. P69616 EBI-7810311 0.53 P07858 EBI-7970369 0.60 Q92569 EBI-2115171 0.00 P62993 EBI-2115716 0.00 P42336 EBI-2116612 0.00 P10176 EBI-3904736 0.37 Q9Y4D1 EBI-3908964 0.37 P40763 EBI-3926609 0.37 Q99XU0 EBI-8852714 0.35 Q13643 EBI-10193895 0.56 P14335 EBI-11422579 0.37 Q99IB8 EBI-11599534 0.35 P05067 EBI-16716791 0.40 GO:0072562 GO:0009986 GO:0062023 GO:0005829 GO:0005783 GO:0070062 GO:0005576 GO:0005615 GO:0031314 GO:0005743 GO:0031965 GO:0005886 GO:0016209 GO:0019855 GO:0046904 GO:0030246 GO:0035374 GO:0098633 GO:0020037 GO:0019862 GO:0016491 GO:0016653 GO:0042803 GO:0004867 GO:0007155 GO:0098869 GO:0034614 GO:1903606 GO:0007565 GO:0042167 GO:0020027 GO:0050777 GO:0046329 GO:0030163 Peripheral UniProt Curator Inference {ECO:0000305|PubMed:23157686} MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN 352 Q62577 Trypstatin AMBP 10047 None SL-0178 SL-0182 [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}. UNIPROT Q62577 UNIPROT Q62576 Pfam PF00014 Pfam PF00061 PROSITE PS00280 PROSITE PS50279 [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}. GO:0005829 GO:0005783 GO:0005576 GO:0005615 GO:0031314 GO:0005743 GO:0031965 GO:0005886 GO:0016209 GO:0035374 GO:0098633 GO:0020037 GO:0019862 GO:0016491 GO:0016653 GO:0042803 GO:0004867 GO:0098869 GO:0034614 GO:1903606 GO:0020027 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P02760} MKGLGTLFLLLTACLASRADDAATLPDIQVQENFIESLIYGKWFNLAVGSTCPWLRRIKDKMSMSTLVLQEGATEAEISMTSTRWRRGVCEEISGAYEKTDIDGKFLYHKSKWNITLETYVVHTNYDEYAIFLTKKFSHYHGPTITLKLYGREPKLRDSLLLEFREVALSMGIPENSIVFMADKGECVPGDQEVKPSPHLRARRAVLPQENEGSGSEPLVTGILKKEDSCQLTYSEGPCLGMMERYHYNGTSMACETFQYGGCLGNGNNFISEKECLQTCRTVAACNLPIVQGPCRAYIKLWAFDAAQGKCIQFTYGGCKGNGNKFYSEKECKEYCGVPGDGDKTN 346 Q60559 Trypstatin AMBP 10036 None SL-0178 SL-0182 [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}. UNIPROT Q60559 UNIPROT Q60558 UNIPROT Q9QW86 UNIPROT Q9QW87 Pfam PF00014 Pfam PF00061 PROSITE PS00280 PROSITE PS50279 PROSITE PS00213 [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}. GO:0005829 GO:0005783 GO:0005576 GO:0005615 GO:0031314 GO:0005743 GO:0031965 GO:0005886 GO:0016209 GO:0035374 GO:0098633 GO:0020037 GO:0019862 GO:0016491 GO:0016653 GO:0042803 GO:0004867 GO:0098869 GO:0034614 GO:1903606 GO:0020027 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P02760} MLGLGTLFLLLAACPASRADPVPALPDIQVQENFNESRIYGKWFNLAVGSTCPWLSRIKNKMSMSTLVLREGATGAEISTTSTRWRRGVCEEVSGTYEKTDMDGKFLYHKSKWNVTLESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGREPQLRDSLLQEFREVALSVGIPENSIVFMEDRGECVPGDLEQKSTSLLRARRAVLPQENEGSGTGPLVTDVLKKEDSCQLSYSEGPCLGMIEKYYYNGASMACETFHYGGCLGNGNNFNSEKECLQTCRTVAACSLPIVQGPCRAYVELWAFDAAQGKCVQFSYGGCKGNGNKFYSEKECKEYCGVPGDGYEELTRS 349 Q07456 Trypstatin Ambp 10090 None SL-0178 SL-0182 [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}. UNIPROT Q07456 UNIPROT Q61294 UNIPROT Q925W1 UNIPROT Q9DBJ9 Pfam PF00014 Pfam PF00061 PROSITE PS00280 PROSITE PS50279 PROSITE PS00213 [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}. GO:0009986 GO:0062023 GO:0005829 GO:0005783 GO:0005615 GO:0031314 GO:0043231 GO:0031965 GO:0005886 GO:0016209 GO:0035374 GO:0098633 GO:0020037 GO:0019862 GO:0016653 GO:0042803 GO:0004867 GO:0098869 GO:0034614 GO:1903606 GO:0020027 GO:0030163 GO:0051604 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P02760} MQGLRTLFLLLTACLASRADPASTLPDIQVQENFSESRIYGKWYNLAVGSTCPWLSRIKDKMSVSTLVLQEGATETEISMTSTRWRRGVCEEITGAYQKTDIDGKFLYHKSKWNITLESYVVHTNYDEYAIFLTKKSSHHHGLTITAKLYGREPQLRDSLLQEFKDVALNVGISENSIIFMPDRGECVPGDREVEPTSIARARRAVLPQESEGSGTEPLITGTLKKEDSCQLNYSEGPCLGMQERYYYNGASMACETFQYGGCLGNGNNFISEKDCLQTCRTIAACNLPIVQGPCRAFIKLWAFDAAQGKCIQFHYGGCKGNGNKFYSEKECKEYCGVPGDGYEELIRS 349 P04366 Trypstatin AMBP 9823 None SL-0178 SL-0182 [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}. UNIPROT P04366 UNIPROT P34954 Pfam PF00014 Pfam PF00061 PROSITE PS00280 PROSITE PS50279 PROSITE PS00213 [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}. GO:0009986 GO:0005829 GO:0005783 GO:0005576 GO:0005615 GO:0031314 GO:0005743 GO:0031965 GO:0005886 GO:0016209 GO:0035374 GO:0098633 GO:0020037 GO:0019862 GO:0016491 GO:0016653 GO:0042803 GO:0004867 GO:0098869 GO:0034614 GO:1903606 GO:0020027 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P02760} AVSASPVLTLPNDIQVQENFDLSRIYGKWFHVAVGSTCPWLKRFKDKMTMGTLMLGEGATEREISVTKTHRRKGICEVISGAYEKTSTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRRHGPTLTAKLYGREPQLRESLLEEFREVALGVGIPEDSIFTMPDRGECVPGEQEPEPTLLSRARRAVLPQEEEGSGAGQPVADFSKKEDSCQLGYSQGPCLGMIKRYFYNGSSMACETFHYGGCMGNGNNFVSEKECLQTCRTVEACSLPIVSGPCRGFFQLWAFDAVQGKCVLFNYGGCQGNGNQFYSEKECKEYCGVPGEEDEELLRSSN 337 Q64240 Trypstatin Ambp 10116 None SL-0178 SL-0182 [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}. UNIPROT Q64240 UNIPROT P19603 UNIPROT Q63336 Pfam PF00014 Pfam PF00061 PROSITE PS00280 PROSITE PS50279 PROSITE PS00213 [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}. GO:0009986 GO:0005829 GO:0005783 GO:0005615 GO:0031314 GO:0043231 GO:0031965 GO:0005886 GO:0016209 GO:0035374 GO:0098633 GO:0020037 GO:0019862 GO:0016491 GO:0016653 GO:0042803 GO:0004867 GO:0098869 GO:0034614 GO:1903606 GO:0020027 GO:0030163 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P02760} MQGLGALFLLLTACLTLKADNVPTLPDIQVQENFNEARIYGKWFNLAVGSTCPWLRRIKNKMSVSTLVLQEGATEAEISVTSTQWRKGVCEEISGVYQKTDIDGKFLYHKSKWNATLESYVVHTNYDEYAIFLTKKFSHRHGPTITAKLYGREPQLRDSLLQEFREVALSVGIPENSIVFMADRGECVPGDREVESTSFARARRAVLPQENEGSGSEPLITGTLKKEDSCQLNYSEGPCLGMQQKYYYNGASMACETFQYGGCLGNGNNFASEKECLQTCRTIAACNLPIVQGPCRAFAELWAFDAAQGKCIQFIYGGCKGNGNKFYSEKECKEYCGVPGDGYEELTRS 349 G0S381 Nucleoporin AMO1 759272 None SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S381 UNIPROT G0ZGU0 PDB 6B4G PDB 6B4H Pfam PF00642 PROSITE PS50103 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}. GO:0031965 GO:0005643 GO:0046872 GO:0034641 GO:0043170 GO:0051028 GO:0044238 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P49686} MTVCRFWQQGYCRNGNACKFEHPPKGGQNYNRFGALSGSGQGMGGRVSEPPHYPGLSEDAIQKDLTSELPTWILSCYGPGRDAPEQLFGGYPREQSFEEIRLHFYNGLMAGNPQGALNEIQAAYQAAQQQIQNTLQNIPAAVQFILDAANKHPNRIDICRESSKGSSTGGSVFGRNVNPFQQSSAAPLNPFGAPSTPSTSAFGQPSPLGQKSSAFGTPAFGQPSQPVSAFGKPSALGGGSAFGSPQTGSTFGQPSVLGAKPSAFGQPAFGQPAFGQPAFGQSAFGQPSALGPKPGAFGTSAGSAFGASTTTAPSPFGAAAQATQPANPFGQPSQQAANSFGKPAAPASAFGQPSTTTAQNPFGQPSTQSSAFGQQQPQQAGTFGSPSLFGQQQQQPSNVFGQPSTTSAFGSQAATSGFSQLGNATSTIGASPAGAQAPASKSPYHPGSTRQHPDLLSYATKNPAGGLDTFKGKPVVYETPKGAAKPVPHIRQFDGTLVRIWMPDGAPAYTADTEAEDPKVYEDEGVKRQWQSFLEKGRFEGGMPEVPPRREWCVWDF 557 Q9N4M4 Nuclear anc 6239 None SL-0178 SL-0182 SL-0183 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}. UNIPROT Q9N4M4 UNIPROT O61841 UNIPROT O61842 UNIPROT Q6IMP3 Pfam PF00307 Pfam PF10541 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS51049 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}. GO:0005737 GO:0005856 GO:0016021 GO:0005635 GO:0005640 GO:0048471 GO:0003779 GO:0051087 GO:0007010 GO:0051179 GO:0051647 GO:0006997 GO:0035046 Transmembrane UniProt Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385} MSSSPPARPCCVCFRFRPHEDEKAQKNTFTRWINFHLEEHSSSGRIEDLFEDIRDGVLLCHLIEVLTGEALAVHKGRVSKRVHHIANLTTALTVLRRRGLELINNNAADIADGNPRIVLGLIWQIILHFQIETNMILLREWGWAATGTEEPTSSAQPEVVVTAPSPTPSSKKSHSKVSSLSGSKTSLASGEKAPSSPLRQRIASFLTPTKKAPKLTAQPVKQSVEQVFLRWINAEIGDLVGGRRVENMDKQWRDGILFCALVSRWRPDVISMREVTNANPRDNLELAFNLAHQHLGVRRLLAVEDMMIEKPDKRSVITYVSQFVRMFGERSPMQGREQHEIFLAWLEATYLLCTRHELNSQECSRIRREFIEHRPLFNTIIVTKVNYDVEELVEIEKKWDCIRETLEKYARRSERDLPEPFASIATWIAGAEHILSRPLDLDATDAKKTVTMLQKLISEHQKYMEDLPKRQEDFEEAVKHGGLGGRPVAPEFSEPLRARFAQIEEENEPRISTLRILTTHYILLQYLQHIDEKIILWRTADSVTLLLRWIKEYTQLNAENPQAKCASYINKITLTMANDQNSKLDKEAILNTSNEKTAETLKRFESLWIELKLLKVEWVEWETHVSQLEEIIEERRRNGVPPTPEDEQALAVITAGADQLAPKLGASARLSNNQRLDVLTHSFKKLTKTTIKIGGRLVVELEPSTSEQASKISYSWQASDELLKVEMQLRDRIQRDADSSDREQLEYRAETFRNIRDKLIELERLNEIYDNHSRDQVDTPNRNLIRHDMGTIIYGLQAGQYANFVDLSCYAFVYDEYNQVPVNLTENVLSEDYVREIVNRKKAILTRRENNEDEIRESIRDMEECDRIIEGWQSTEIEELRAEWNIKLSEFESWHEMMQQVEVLSQTIQTRLDVTVIQTIWILKERSYDIKHSELGGTLRESLEQLATTSETSVNRHLQNLELSNEQDCPDAIEFLEEVGRESVSKLSAAVDDRYIYTLHVLRTKMELFRRLQNFCDAVKILRSQNTKWNGIKISQIDQVQSEIDTLIVRLDEEWTQDANQLRAELASIHGSFFQLEFDRLNEKLNMLIHDKDKLRELMVHRRHYLTAANELITDSKTDLAQRATSSDHPDDILRATDEVTKALDIKGEELRRLGELAEMNITDLVVVALILSFRRRQLGSEGEPEVEELRRALREIIARPITEPRDVSPDAIVADILRMKDEKKRDEKTIDEIQATTLTDEQRASFAPLIEDYRRRADRHRIVFEHLVMIYLDWLSRQFDELEDEIGMTIQTSRADDLRRMNSTEWNKWKTDLANIERQVGPDTKKALSAELADLHRKRDSMEARINKYLTHSAKINAKLTQFEKWLNAIEEDIEQTERQFEDPERSYRFGSLHEVALAKQRLVAKLERLNVANKEEVLRLCERYHTIMHKLTPFQTAVGLPLHVSTNLDRNGPFQSQISVSSIASSELERPESVMSLTSSIGVIPADVAELSPFEAKINKLLQKLHIIEDSYLKGPKPIDTVREDVKQLEKYRNRGAEILQQLSTSNIEDAEKEGLKHRFVLMLNNYDDILRSIENEIRDDNELTAKNQEILAELSNAEQTLQNSPLEDLDISAELDRLQMQLDLVKVMCNKPRKYVECELIDSSREGSPQERRRRKKKVMVMVSNTITTIIHVVEERLEASDISRNPDVQQKLVAVKENLRELDTTTVTPHPPSIMSPLGTENRNDLEEVKRLAAEIDRAIDTASSMYEDAPTDEDALKSAIHLLDDQKVTLNHLHVVLEGIPEKNEQDRTDAIDIASSVGEKLGNLKSAVEEVYEEVLASTNPVKEDQPLQHIQEVQTTPAEQSNWDTDEFSRQPPVLSDERIELKTDPSAIDKFEVRSDEDPVPKIIDLFGQLQTAVNEASPLACEGTDDVDALQVASDKLTKQDRTIRKIHAILDTIDDPVQKPAIIESLDKIKDQINNARDNINRQIDNLNYNQTPVVVPKESTKTPLNEIEDAVRQASTVVSDELCNTEKLLSARQTLANVKPQVDSVEANVWSNPETIETVTPILEEYTTLVDNIEKKLANEIEVPTNDPSRQDLVQQLQDVILECEEVVVNCDNIEKLEESKLKLEKARPLLDQIGDNVEKLSREQSPDTSDAIDALSNVHQQYNATIMSIDDKIDELKNPEEDTSAADQLISELHVISEMPAVTIDLSMLNAIEEGLSTLPAHQAENVQAKIDELRQKKEVADQTEQILSDLNAFGDMPAITLDLDLLKSVEDGIAVLPVEDSERIKAKIVDLRKKKEDADQAEALLQELSVISDMPISTLDLNMLQGIEDNLNSLPAEESDEIREKLNELRRRKQESDQAEALLQELSVISDMPISTLDLNMLQGVEDNLNSLPTEEADKIREKINDLRRRKQESDLAEALLQELSVIYDMPTSTIDLNMLQGIEDNLNSLPAEESDKIREKINDLRRRKQESDLAEALLQELSVIYDMPTSTIDLNMLQGIEDNLNSLPAEESDKIREKINDLRRRKQESDQAEALLQELSVVSDMPASTIDINMLQSIEDGLSTLLSEDRSKIQQAIDSLRKKKSDSDLAQHALEALSVQSKLPSVSINLEELKKLEETLSTVPVEDSKVIRDKIAELKTEKALADHAENYLVELKKIEDMPISAVGSDVLATIEDQILQMPVQYQPSVKETLDKLKQAKEEDDKLAGVYDELEKIAKLPARDYDNKLLAKIDEKLNSLPKDQIAETHRKVEDIKVTKADIVAQIDVLDKLPAKDIDEHLLNSIEEKLPTIPSDSSDQLQIAIGKLRDRKQANIDEGKKILNELAEIQKMPADSLNEHALNLLATESDKFGSEISDKIMQEIDVLREKQNNHEVARLNAESVLQQLDKISEEPHLSLTEERLAPFLQNIDTVPACFVDKIRNKINEVQKLHDEAVQDEKDELKEKLVAKVQNIGKTSIDDVNVSDFEEIEREINGSLEAFEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDDGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDRGRSTGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDRLNKLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQLGSAVGEKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERASIWERFVKAKDDLYDYLEKLENNVSDVLNRPRLPVSQAQQRFNKLKEQSYLLDRIRDLKIDFDDLGEALLPLTVAEDELRFMHVHVESIERQYEDTMDKLNAEITAEVELLRTLDILSNELSQCKEDINNPSVDVDELSRATMLNDAIAHLENQKVVVARSEKDRKFVESSTSIDLDQLLAEAKRLLKEIEPRLQLAQPDHDNEDDEDEEKGSDEKPYDVRAAAEVLSALYPDEHPHNVLRNIGFEELPSDSESRSEFDSLDSRSDGLLSPIPDDSTLSEEQLRRQRSRWRRVLRTALPLQALLVLLMGAACLVPHCDDEYCCQLLNNFAKSFDPSLEFVNGPPPF 8545 H2KZB2 Ankyrin lem 6239 None SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:22770216}; Single-pass membrane protein {ECO:0000269|PubMed:22770216}. UNIPROT H2KZB2 UNIPROT Q5W7E5 PROSITE PS50297 PROSITE PS50088 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}. Q03565 EBI-6258976 0.44 Q19848 EBI-6258976 0.56 GO:0005783 GO:0016021 GO:0005635 GO:0031965 GO:0051721 GO:0051301 GO:0007084 GO:0042326 GO:0035307 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGRKSAILAVILAIIYFRSNFSKMSNTPVQETEGPVYVAYSMEDMLKSPRDLYKSVKEVAKFVNSAEGKSMSARFKKFGTPREAMDFLAYGDAPTTPKTVPPVAPTEPNSPFSGVNRIQMNEFKKYVEKGDMENFLRLVDSNPRFLVNTGGDVASIVMEGFRYNALHIAAKAGQTEIIAKILELIQNIDFLIRLYGTGADDVTLRKINILDSYLNTPDKGNSDTPLHFASKFGKIGVVRVLTENSATDRTLLNKSGKSALDCAGERYTGEDKDMVQRDIHLAIEGFYVFLHRNPTTGSTQLTVSQKPPATYSTSPTTATVTVSAQAGPFFTEREARDFAKSWQTAGKELKRTDFDKGWERVGRVLAEQSEAMWRETWHFLGSMELLDLGSEQGLGVLEAFLREKRRGNLRNSEISEISTKKSIFRRGIHARKLDFGILDGEKSAEISENLTPDGSDSADDEDDDDIFYDTFSEIPAAAEKSINDPDDTLGSLTDRFAAISIFSPLPPPPPPQWSNSPNFDYSEGEDSFATPPTTPPPTFVADDEPCKIDNDLFEVLAQISSELISKFPLTQDYVQKLGKLTAHDRSTWRPIDSPARCDSRRKI 603 Q8MQX9 Ankyrin Ankle2 7227 None SL-0178 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}. UNIPROT Q8MQX9 UNIPROT Q0KHR1 UNIPROT Q9VX44 UNIPROT X2JCC5 Pfam PF13637 PROSITE PS50297 PROSITE PS50088 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}. Q9VXY7 EBI-9936142 0.35 GO:0005737 GO:0012505 GO:0005783 GO:0005635 GO:0051721 GO:0055059 GO:0045167 GO:0000902 GO:0007029 GO:0042326 GO:0031468 GO:0035307 GO:0051653 Unknown UniProt Sequence Analysis MSTYFGVYIPTSKAGCFEGSVSQCIGSIAAVNIKPSNPASGSASVASGSPSGSAASVQTGNADDGSAATKYEDPDYPPDSPLWLIFTEKSKALDILRHYKEARLREFPNLEQAESYVQFGFESIEALKRFCKAKPESKPIPIISGSGYKSSPTSTDNSCSSSPTGNGSGFIIPLGSNSSMSNLLLSDSPTSSPSSSSNVIANGRQQQMQQQQQQQPQQPDVSGEGPPFRAPTKQELVEFRKQIEGGHIDRVKRIIWENPRFLISSGDTPTSLKEGCRYNAMHICAQVNKARIAQLLLKTISDREFTQLYVGKKGSGKMCAALNISLLDYYLNMPDKGRGETPLHFAAKNGHVAMVEVLVSYPECKSLRNHEGKEPKEIICLRNANATHVTIKKLELLLYDPHFVPVLRSQSNTLPPKVGQPFSPKDPPNLQHKADDYEGLSVDLAISALAGPMSREKAMNFYRRWKTPPRVSNNVMSPLAGSPFSSPVKVTPSKSIFDRSAGNSSPVHSGRRVLFSPLAEATSSPKPTKNVPNGTNECEHNNNNVKPVYPLEFPATPIRKMKPDLFMAYRNNNSFDSPSLADDSQILDMSLSRSLNASLNDSFRERHIKNTDIEKGLEVVGRQLARQEQLEWREYWDFLDSFLDIGTTEGLARLEAYFLEKTEQQADKSETVWNFAHLHQYFDSMAGEQQQQLRKDKNEAAGATSPSAGVMTPYTCVEKSLQVFAKRITKTLINKIGNMVSINDTLLCELKRLKSLIVSFKDDARFISVDFSKVHSRIAHLVASYVTHSQEVSVAMRLQLLQMLRSLRQLLADERGREQHLGCVCASLLLMLEQAPTSAVHLPDTLKTEELCCAAWETEQCCACLWDANLSRKTSRRKRTKSLRAAAVVQSQGQLQDTSGSTGSSALHASLGVGSTSLGASRVVASASKDAWRRQQSDDEDYDSDEQVIFFDCTNVTLPYGSSSEDEENFRTPPQSLSPGISMDLEPRYELFIFGNEPTKRDLDVLNALSNVDIDKETLPHVYAWKTAMESYSCAEMNLFPSPRNVKVQKPEPWYSGTSSSHNSQPLLHPKRLLATPKLNAVVSGRRGSGPLTAPVTPRLARTPSAASIQVASETNGESVGTAVTPASPILSFAALTAATQSFQTPLNKVRGLFSQYRDQRSYNEGDTPLGNRN 1174 P27214 Annexin ANXA11 9913 None SL-0178 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}. UNIPROT P27214 UNIPROT P27215 UNIPROT Q0VD55 Pfam PF00191 PROSITE PS00223 PROSITE PS51897 Binds specifically to calcyclin in a calcium-dependent manner. Required for midbody formation and completion of the terminal phase of cytokinesis. {ECO:0000250}. GO:0042470 GO:0016020 GO:0030496 GO:0005635 GO:0005654 GO:0005819 GO:0005509 GO:0005544 GO:0044548 GO:0032506 GO:0006909 Unknown UniProt Sequence Analysis MSYPGYPPPAGGYPPGAPGGGAWGGAGYPPPTMPPIGLDNVANYAGQFNQDYLSGVAANMSGTFGGANVPNLYPGAPGGGYPPVPPGGFGQPPPAQQPVPSYGMYPPPGGNPTSGMPSYPPYPGAPVPGQPMLPPGQQPPGVYPGQPPMTYPGQSPVPPPGQQPVPSYPGYSGSGTVTPAVSPAQFGNRGTITDASGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDAYEIKEAIKGAGTDEACLIEILASRSNEHIRELNRVYKTEFKKTLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMTLVQRDVQELYAAGENRLGTDESKFNAILCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSEIDLLDIRAEYKRLYGKSLYHDITGDTSGDYRKILLKICGGND 503 P50995 Annexin ANXA11 9606 None SL-0178 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}. UNIPROT P50995 UNIPROT B4DVE7 Pfam PF00191 PROSITE PS00223 PROSITE PS51897 OMIM 602572 OMIM 617839 DisGeNET 311 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}. 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. O15162 EBI-752707 0.55 P00533 EBI-34582286 0.35 P09104 EBI-731812 0.00 P31942 EBI-734775 0.00 O75340 EBI-2338752 0.75 Q5NHS4 EBI-2808973 0.00 A0A6L8PQC3 EBI-2838236 0.00 A0A380PL96 EBI-2843651 0.00 Q99459 EBI-7954144 0.35 Q93034 EBI-21331078 0.35 Q8IUH5 EBI-9090498 0.37 P05412 EBI-11324725 0.35 P08563 EBI-11477906 0.40 Q9WVM1 EBI-11008211 0.35 Q80UG5 EBI-11121465 0.35 Q91ZJ0 EBI-11131714 0.35 Q8NI38 EBI-24751877 0.56 Q96AE4 EBI-24374647 0.56 Q53EZ4 EBI-24386584 0.78 Q3LI66 EBI-24537226 0.56 Q9NZC7 EBI-24573309 0.56 Q52LG2 EBI-24587720 0.56 P15289 EBI-24600393 0.56 Q92734 EBI-12700650 0.67 P36810 EBI-26503730 0.49 P60033 EBI-20568535 0.35 Q15828 EBI-21887792 0.40 Q12888 EBI-20207896 0.27 O60260 EBI-21135687 0.35 P83105 EBI-25745135 0.35 Q9C0B5 EBI-25636144 0.35 GO:0042582 GO:0062023 GO:0005737 GO:0005829 GO:0070062 GO:0042470 GO:0016020 GO:0030496 GO:0005635 GO:0005654 GO:0045335 GO:0042581 GO:0005819 GO:0005509 GO:0005544 GO:0048306 GO:0023026 GO:0008429 GO:0003723 GO:0044548 GO:0032506 GO:0006909 GO:0051592 Unknown UniProt Sequence Analysis MSYPGYPPPPGGYPPAAPGGGPWGGAAYPPPPSMPPIGLDNVATYAGQFNQDYLSGMAANMSGTFGGANMPNLYPGAPGAGYPPVPPGGFGQPPSAQQPVPPYGMYPPPGGNPPSRMPSYPPYPGAPVPGQPMPPPGQQPPGAYPGQPPVTYPGQPPVPLPGQQQPVPSYPGYPGSGTVTPAVPPTQFGSRGTITDAPGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDIYEIKEAIKGVGTDEACLIEILASRSNEHIRELNRAYKAEFKKTLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLAQRDAQELYAAGENRLGTDESKFNAVLCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEEGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSETDLLDIRSEYKRMYGKSLYHDISGDTSGDYRKILLKICGGND 505 P97384 Annexin Anxa11 10090 None SL-0178 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}. UNIPROT P97384 UNIPROT Q921F1 Pfam PF00191 PROSITE PS00223 PROSITE PS51897 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}. GO:0042582 GO:0062023 GO:0005737 GO:0005829 GO:0042470 GO:0030496 GO:0005635 GO:0005654 GO:0045335 GO:0042581 GO:0005819 GO:0005509 GO:0005544 GO:0048306 GO:0008429 GO:0044548 GO:0032506 GO:0006909 GO:0051592 Unknown UniProt Sequence Analysis MSYPGYPPPAGGYPPAAPGGGPWGGAGYPPPSMPPIGLDNVANYAGQFNQDYLSGMAANMSGTFGGANVPNLYPGAPGGGYPPVPPGGFGQPPPAQQPVPPYGMYPPPGGNPPPGMPSYPAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSYPGYSGSSTITPAVPPAQFGNRGTITAASGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDVYEIKEAIKGAGTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLVQRDVQELYAAGENRLGTDESKFNAILCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSELDLLDIRAEYKRMYGKSLYHDITGDTSGDYRKILLKICGGND 503 P33477 Annexin ANXA11 9986 None SL-0178 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}. UNIPROT P33477 Pfam PF00191 PROSITE PS00223 PROSITE PS51897 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}. GO:0042470 GO:0030496 GO:0005635 GO:0005654 GO:0005819 GO:0005509 GO:0005544 GO:0044548 GO:0032506 Unknown UniProt Sequence Analysis MSYPGYPPPPGGYPPAPGGGAWGGAGYPPPSMPPIGLDNVANYAGQFNQDYLSGMAANMSGTFGGANVPPNLYPGAPGGGYPPVPPGGFGQPPPTQPSVPPYGVYPPPGGNPPSGVPSYPPFPGAPVPGQPMPPPGHQPPGPYPGQLPVTYPGQSPVPPPGQQPMPSYPGYPGSGTVTPAVPPVQFGNRGTITDASGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILALMKTPILFDAYEIKEAIKGAGTDEACLIEILASRSNEHIRELNKAYKTEFKKTLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLVQRDVQELYAAGENRLGTDESKFNAVLCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAVVKCLKNTPAFFAERLNRAMRGAGTKDRTLIRIMVSRSEIDLLDIRAEYKRMYGKSLYHDISGDTSGDYRKILLKICGGND 503 O43747 AP-1 AP1G1 9606 None SL-0198 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}. UNIPROT O43747 UNIPROT O75709 UNIPROT O75842 UNIPROT Q9UG09 UNIPROT Q9Y3U4 PDB 1IU1 Pfam PF01602 Pfam PF02883 PROSITE PS50180 OMIM 603533 OMIM 619467 OMIM 619548 DisGeNET 164 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}. 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. O18973 EBI-447608 0.37 Q15276 EBI-448309 0.51 Q9DB50 EBI-516318 0.37 P61967 EBI-516322 0.37 P61106 EBI-6962654 0.27 Q6VY07 EBI-6971116 0.44 Q96G01 EBI-7141935 0.27 Q9JIF3 EBI-7048115 0.40 A0A6L7H5N1 EBI-2811290 0.00 A0A6L8P1I7 EBI-2813482 0.00 Q81MS2 EBI-2817920 0.00 Q81LQ9 EBI-2817913 0.00 A0A2C3GDM9 EBI-2838167 0.00 A0A2P0HDJ9 EBI-2838153 0.00 A0A6L7HG24 EBI-2838146 0.00 Q81S14 EBI-2838160 0.00 A0A2U2GVV5 EBI-2848665 0.00 A0A380SBC9 EBI-2875986 0.00 Q77M19 EBI-6268389 0.35 Q10567 EBI-6868018 0.27 P56377 EBI-10185817 0.67 Q96S82 EBI-10185831 0.72 Q9NYZ3 EBI-11081743 0.35 Q9NYX4 EBI-10918009 0.40 Q10589 EBI-10960854 0.27 P19554 EBI-10960854 0.27 Q6P5F9 EBI-11603310 0.35 Q6PD74 EBI-24507122 0.67 Q6IQ23 EBI-16398399 0.35 Q96CW1 EBI-21520588 0.35 A0JP26 EBI-21540656 0.35 O75170 EBI-21664775 0.35 Q9Y6Q5 EBI-21760726 0.35 Q01968 EBI-16412116 0.35 O43493 EBI-16800265 0.27 P46013 EBI-20562326 0.35 P14404 EBI-21026252 0.35 P03372 EBI-21301141 0.35 P10644 EBI-25387530 0.35 P20339 EBI-25391898 0.35 P0DOF2 EBI-25603126 0.35 P54253 EBI-25978906 0.56 P0DTC5 EBI-27127936 0.27 GO:0030121 GO:0030136 GO:0030665 GO:0005737 GO:0030659 GO:0005829 GO:0005769 GO:0005794 GO:0000139 GO:0043231 GO:0005765 GO:0016020 GO:0048471 GO:0055037 GO:0032588 GO:0140312 GO:0035615 GO:0030742 GO:0019894 GO:0031267 GO:0110010 GO:0035646 GO:0090160 GO:0006896 GO:0006886 GO:1903232 GO:0032438 GO:0060155 GO:0043323 GO:0045954 GO:0006898 GO:0016192 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:12773381} MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPTEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPVIPTAPTSKPSSAGGELLDLLGDINLTGAPAAAPAPASVPQISQPPFLLDGLSSQPLFNDIAAGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ 822 P22892 AP-1 Ap1g1 10090 None SL-0198 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}. UNIPROT P22892 PDB 1GYU PDB 1GYV PDB 1GYW PDB 1W63 PDB 2A7B PDB 3ZY7 PDB 4HMY PDB 4P6Z PDB 6CM9 PDB 6CRI PDB 6D83 PDB 6D84 PDB 6DFF Pfam PF01602 Pfam PF02883 PROSITE PS50180 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}. Q07113 EBI-7855082 0.44 P52303 EBI-1040301 0.40 Q14677 EBI-7071326 0.54 Q9JIF3 EBI-7048197 0.40 P46096 EBI-7837071 0.27 Q62277 EBI-7837084 0.27 Q10567 EBI-6863559 0.74 P84077 EBI-6864775 0.35 Q96PC3 EBI-6864775 0.35 P35585 EBI-6864775 0.66 O75379 EBI-6868249 0.35 O54774 EBI-9103779 0.35 P18242 EBI-9103779 0.35 Q68FD5 EBI-9103779 0.35 P11438 EBI-9103779 0.35 Q8BKC8 EBI-9103779 0.35 Q9CQD1 EBI-9103779 0.35 O88384 EBI-9103735 0.35 P61966 EBI-10960176 0.40 GO:0030121 GO:0030136 GO:0005829 GO:0005769 GO:0005794 GO:0043231 GO:0005765 GO:0048471 GO:0055037 GO:0005802 GO:0032588 GO:0140312 GO:0035615 GO:0030742 GO:0019894 GO:0031267 GO:0110010 GO:0035646 GO:0090160 GO:0006896 GO:0006886 GO:1903232 GO:0060155 GO:0043323 GO:0045954 GO:0006898 GO:0016192 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:O43747} MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPSEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPVIPTAPTSKPASAGGELLDLLGDITLTGAPAAAPTPASVPQISQPPFLLDGLSSQPLFNDIAPGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ 822 Q5R5M2 AP-1 AP1G1 9601 None SL-0198 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}. UNIPROT Q5R5M2 Pfam PF01602 Pfam PF02883 PROSITE PS50180 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}. GO:0030121 GO:0048471 GO:0006886 GO:0016192 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:O43747} MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMPAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVRTDHNTVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEYGDLLVSGQCEEEGPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPTEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPVIPTAPTSKPSSAGGELLDLLGDINLTGAPAAAPAPASVPQISQPPFLLDGLSSQPLFNDIAAGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ 822 Q02410 Amyloid-beta APBA1 9606 None SL-0198 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}. UNIPROT Q02410 UNIPROT O14914 UNIPROT O60570 UNIPROT Q5VYR8 PDB 1AQC PDB 1U37 PDB 1U38 PDB 1U39 PDB 1U3B PDB 1X11 PDB 1X45 PDB 1Y7N Pfam PF00595 Pfam PF00640 PROSITE PS50106 PROSITE PS01179 OMIM 602414 DisGeNET 320 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}. P05067 EBI-368901 0.65 P49768 EBI-7693425 0.70 Q00975 EBI-7693446 0.44 Q02410 EBI-7693492 0.37 Q5NGR3 EBI-2808888 0.00 Q8ZD84 EBI-2840135 0.00 A0A2S9PLH1 EBI-2875941 0.00 P97887 EBI-6674509 0.40 Q9NRW1 EBI-8840227 0.62 P20340 EBI-8840230 0.62 P35279 EBI-8841337 0.27 O14936 EBI-9084378 0.40 Q9NUP9 EBI-21627409 0.35 Q99767 EBI-21817505 0.35 K9N5R3 EBI-26973521 0.40 GO:0005737 GO:0005829 GO:0043197 GO:0098978 GO:0005794 GO:0005634 GO:0048471 GO:0005886 GO:0048787 GO:0098685 GO:0008021 GO:0001540 GO:0008088 GO:0007155 GO:0007268 GO:0014051 GO:0014047 GO:0001701 GO:0006886 GO:0007626 GO:0035264 GO:0007399 GO:0065003 GO:0010468 GO:2000300 Unknown UniProt Sequence Analysis MNHLEGSAEVEVTDEAAGGEVNESVEADLEHPEVEEEQQQPPQQQHYVGRHQRGRALEDLRAQLGQEEEERGECLARSASTESGFHNHTDTAEGDVIAAARDGYDAERAQDPEDESAYAVQYRPEAEEYTEQAEAEHAEATHRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRGEDEPYSEPYADYGGLQEHVYEEIGDAPELDARDGLRLYEQERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERPPTPAGGRPDSPGLQAPAGQQRAVGPAGGGEAGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPMDGDSPSPGSSSPLGAESSSTSLHPSDPVEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKMAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQETMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI 837 B2RUJ5 Amyloid-beta Apba1 10090 None SL-0198 Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. [Isoform 3]: Golgi apparatus. UNIPROT B2RUJ5 UNIPROT Q3UH49 UNIPROT Q8BMF2 PDB 6LNM Pfam PF00595 Pfam PF00640 PROSITE PS50106 PROSITE PS01179 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}. P61294 EBI-8840212 0.27 P20340 EBI-8840609 0.44 GO:0005737 GO:0005829 GO:0043197 GO:0098978 GO:0005794 GO:0016020 GO:0005634 GO:0048471 GO:0005886 GO:0048787 GO:0032991 GO:0098685 GO:0008021 GO:0001540 GO:0030165 GO:0005546 GO:0044877 GO:0007268 GO:0051649 GO:0014051 GO:0014047 GO:0001701 GO:0006886 GO:0007626 GO:0035264 GO:0065003 GO:0010468 GO:2000300 Unknown UniProt Sequence Analysis MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVVEGQQPSPSPPPPAGHEPEDHRGHPAPPPPPPPQEEEEEERGECLARSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHVEAAQRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGLPAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPVDGDSPSPGSSSPLGAESSSIPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI 842 O35430 Amyloid-beta Apba1 10116 None SL-0198 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}. UNIPROT O35430 PDB 4DBB PDB 6KMH Pfam PF00595 Pfam PF00640 PROSITE PS50106 PROSITE PS01179 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. P26010 EBI-8611689 0.44 P05106 EBI-8611732 0.44 P05556 EBI-8611776 0.44 Q99PW8 EBI-7293493 0.64 Q00975 EBI-7076778 0.51 Q02294 EBI-7076897 0.40 Q62889 EBI-7414748 0.44 Q63373 EBI-7414873 0.27 P49768 EBI-8513481 0.40 P05067 EBI-8513444 0.52 P52188 EBI-704679 0.35 P32851 EBI-8545713 0.66 P61765 EBI-2027999 0.62 Q24008 EBI-4307047 0.56 GO:0005737 GO:0005829 GO:0043197 GO:0098978 GO:0005794 GO:0016020 GO:0005634 GO:0048471 GO:0005886 GO:0048787 GO:0032991 GO:0098685 GO:0008021 GO:0001540 GO:0030165 GO:0005546 GO:0044877 GO:0007268 GO:0051649 GO:0014051 GO:0014047 GO:0001701 GO:0006886 GO:0007626 GO:0035264 GO:0065003 GO:0010468 GO:2000300 GO:0016079 Unknown UniProt Sequence Analysis MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVEEEQQPSPPPPAGHAPEDHRAHPAPPPPPPPQEEEEERGECLARSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHAEAAQRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGLPAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPVDGDSPSPGSSSPLGAESSITPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDAKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI 839 O96018 Amyloid-beta APBA3 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:19726677}. UNIPROT O96018 UNIPROT O60483 UNIPROT Q9UPZ2 PDB 2YT7 PDB 2YT8 PDB 5UWS Pfam PF00595 Pfam PF00640 PROSITE PS50106 PROSITE PS01179 OMIM 604262 DisGeNET 9546 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}. P11274 EBI-7358205 0.61 P00533 EBI-7877395 0.44 Q9QYP6 EBI-6115837 0.50 A7MCY6 EBI-6116450 0.50 Q92844 EBI-6116592 0.50 Q9H6Z9 EBI-12503146 0.35 P16152 EBI-11153984 0.35 Q6P5F9 EBI-11603310 0.35 Q96P71 EBI-15098872 0.60 Q8NCP5 EBI-15098805 0.37 Q06481 EBI-15098809 0.37 P78545 EBI-15098813 0.37 P14061 EBI-15098817 0.37 Q9UN79 EBI-15098821 0.37 Q9H6I2 EBI-15098825 0.37 P52747 EBI-15098829 0.37 Q9NWT6 EBI-15099018 0.75 P78552 EBI-21604776 0.35 Q9UHD2 EBI-21604776 0.35 Q9NSD9 EBI-21604776 0.35 Q9H6S1 EBI-21604776 0.35 Q9BY42 EBI-21604776 0.35 Q9BSJ5 EBI-21604776 0.35 Q99590 EBI-21604776 0.35 Q99569 EBI-21604776 0.35 Q8TEU7 EBI-21604776 0.35 Q8TBX8 EBI-21604776 0.35 Q8N9R8 EBI-21604776 0.35 Q6PD62 EBI-21604776 0.35 Q6P5Z2 EBI-21604776 0.35 Q5JTD0 EBI-21604776 0.35 Q12986 EBI-21604776 0.35 Q08AH1 EBI-21604776 0.35 P55789 EBI-21604776 0.35 P29803 EBI-21604776 0.35 P17029 EBI-21604776 0.35 P05067 EBI-25936284 0.56 O94985 EBI-21604776 0.35 O75319 EBI-21604776 0.35 Q96BW9 EBI-21604776 0.35 P32320 EBI-21622979 0.35 Q86VW1 EBI-21721972 0.35 Q9BZB8 EBI-21821951 0.35 Q9H492 EBI-30828353 0.44 Q93009 EBI-30841267 0.44 GO:0005737 GO:0043197 GO:0048471 GO:0005886 GO:0001540 GO:0019899 GO:0004857 GO:0007268 GO:0001701 GO:0043086 GO:0015031 GO:0010468 Unknown UniProt Sequence Analysis MDFPTISRSPSGPPAMDLEGPRDILVPSEDLTPDSQWDPMPGGPGSLSRMELDESSLQELVQQFEALPGDLVGPSPGGAPCPLHIATGHGLASQEIADAHGLLSAEAGRDDLLGLLHCEECPPSQTGPEEPLEPAPRLLQPPEDPDEDSDSPEWVEGASAEQEGSRSSSSSPEPWLETVPLVTPEEPPAGAQSPETLASYPAPQEVPGPCDHEDLLDGVIFGARYLGSTQLVSERNPPTSTRMAQAREAMDRVKAPDGETQPMTEVDLFVSTKRIKVLTADSQEAMMDHALHTISYTADIGCVLVLMARRRLARRPAPQDHGRRLYKMLCHVFYAEDAQLIAQAIGQAFAAAYSQFLRESGIDPSQVGVHPSPGACHLHNGDLDHFSNSDNCREVHLEKRRGEGLGVALVESGWGSLLPTAVIANLLHGGPAERSGALSIGDRLTAINGTSLVGLPLAACQAAVRETKSQTSVTLSIVHCPPVTTAIIHRPHAREQLGFCVEDGIICSLLRGGIAERGGIRVGHRIIEINGQSVVATPHARIIELLTEAYGEVHIKTMPAATYRLLTGQEQPVYL 575 O88888 Amyloid-beta Apba3 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT O88888 UNIPROT Q3TDI1 UNIPROT Q8BR09 Pfam PF00595 Pfam PF00640 PROSITE PS50106 PROSITE PS01179 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}. P0C6X9 EBI-25509102 0.37 GO:0005737 GO:0043197 GO:0048471 GO:0005886 GO:0001540 GO:0019899 GO:0004857 GO:0007268 GO:0001701 GO:0043086 GO:0015031 GO:0010468 Unknown UniProt Sequence Analysis MEFLPGPQHPPGPPTMDLEEPKGPEVPSENHPSNTQSALGPGGPVTLSEMELDTSSVQELVQQLEALPSDLGGPFPDGAPCPLHIATGQGLATQENPDAGGLLSAEAGGDDLLGLLRDEASSPAQSVPQDPAQTAPRLLQPPEDPDGDPGWMEGASAEPADSRSSSSSPEPWLETAPLVTQQEPPVGTQSRETLASCPAVTEVPGPCGPEELMDGVIFGAKYLGSTQLLSERSPAPSTRMGQAQEAMDRVKAPEGETQPMVEVDIFISTKRVKVLAADSQDALMDHALQTISYIADIGPVLVLMARRRLARRTTPQDRQRRLYKMLCHVFHSEDAQLIAQAIGQAFSIAYSQFLQENRIDPSQVGTQPSTAASHPHNGDLDHFCNSQNCREVCIQKRPGEGLGVALVESGWGSLLPTAVIANLLHGGPAERCGALSIGDRVTAINGTSLVGLSLAACQAAVREVRRLSSVTLSIIHCPPVTTAVIRRPHVREQLGFCVEDGIICSLLRGGAAERGGVRVGHRIIEVNGQSVVAMPHARIIQLLTETREIHIKTMPAATYRLLTGQEQPVYL 571 O70248 Amyloid-beta Apba3 10116 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT O70248 UNIPROT B1WBQ3 Pfam PF00595 Pfam PF00640 PROSITE PS50106 PROSITE PS01179 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}. P05067 EBI-8513424 0.52 P49768 EBI-8513544 0.40 Q16832 EBI-22241781 0.35 P04626 EBI-22242478 0.35 P11362 EBI-22243924 0.35 P06241 EBI-22245123 0.35 GO:0005737 GO:0043197 GO:0048471 GO:0005886 GO:0045202 GO:0001540 GO:0019899 GO:0004857 GO:0007268 GO:0001701 GO:0043086 GO:0015031 GO:0010468 Unknown UniProt Sequence Analysis MEFLPEPQHPPGPPTMDLEEPKGPEVPSEDHPSNTQWALGPRGPDTLSEMELDTSSVRALVQQLEALPSDLGGQFPDGAPCPLHIATGQGLATQENLDAGGLLSAEAGGDNLLGLLRCEASLPAQSVPPDPAQAAPRLLQPPEDPGGDPGWMEGTEPADNRSSSSSPELWLETAPLVTHRDPPVGTQSQETLASCPAVSEVPGPCGQEELMDGVLFGAKYLGSTQLLSERNPPPSTRMGQAQEAMDRVKAPEGETQPMTEVDIFISTKRVKVLAADSQDALMDHALQTISYIADIGPVLVLMARRRLAKRTTSQDRQRQLYKMLCHVFHSEDAQLIAQAIGQAFSIAYSQFLQENRIDPSQVGMQPSASASHPHNGDLDHFCNSQNCREVCIQKRPGEGLGVALVESGWGSLLPTAVIANLLHGGPAERCGALSIGDRVTAINGTSLVGLSLAACQAAVREVRRHSSVTLSIIHCPPVTTAVIHRPHVREQLGFCVENGIICSLLRGSAAERGGVRVGHRIIEVNGQSVVAMPHARIIQLLTETREIHIKTMPAATYRLLTGQEQPVYL 569 O95996 Adenomatous APC2 9606 None SL-0198 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}. UNIPROT O95996 UNIPROT Q05BW4 UNIPROT Q9UBZ1 UNIPROT Q9UEM8 UNIPROT Q9UQJ8 UNIPROT Q9UQJ9 UNIPROT Q9Y632 Pfam PF05956 Pfam PF16689 Pfam PF05923 Pfam PF18797 Pfam PF00514 Pfam PF05924 OMIM 612034 OMIM 617169 OMIM 618677 DisGeNET 10297 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}. 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. P16035 EBI-1077756 0.00 P67809 EBI-5325180 0.35 Q13625 EBI-8830464 0.54 Q9UPY8 EBI-8842039 0.61 Q15691 EBI-8840634 0.53 P51957 EBI-20721387 0.35 Q9NRI5 EBI-21369738 0.00 P51114 EBI-26509879 0.37 Q9NZ94 EBI-26513299 0.37 P51531 EBI-26515204 0.37 P46934 EBI-30832261 0.44 P46937 EBI-30846273 0.44 GO:0005884 GO:0030877 GO:0016342 GO:0005737 GO:0005829 GO:0005794 GO:0045171 GO:0031258 GO:0005874 GO:0015630 GO:0030496 GO:0048471 GO:0098794 GO:0008013 GO:0045295 GO:0008017 GO:0090630 GO:0001708 GO:0016477 GO:0000226 GO:0090090 GO:0007026 GO:0007399 GO:0007389 GO:0045732 GO:0043161 GO:0045595 GO:0016055 Unknown UniProt Sequence Analysis MASSVAPYEQLVRQVEALKAENSHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQMDITSLYNLKFQPPTLGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDRERCFLLNEIEKEEKEKLWYYSQLQGLSKRLDELPHVETQFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQALLAVKSVPVDEDPETEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQILHGTEAAAGGRAGAPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDGGPEGGGAGSAPIPIEPQICQATCAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTRDPLNLALRRYAGMTLTNLTFGDVANKATLCARRGCMEAIVAQLASDSEELHQVVSSILRNLSWRADINSKKVLREAGSVTALVQCVLRATKESTLKSVLSALWNLSAHSTENKAAICQVDGALGFLVSTLTYKCQSNSLAIIESGGGILRNVSSLVATREDYRQVLRDHNCLQTLLQHLTSHSLTIVSNACGTLWNLSARSARDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKHQAAATAVSPGSCVPSLYVRKQRALEAELDARHLAQALEHLEKQGPPAAEAATKKPLPPLRHLDGLAQDYASDSGCFDDDDAPSSLAAAAATGEPASPAALSLFLGSPFLQGQALARTPPTRRGGKEAEKDTSGEAAVAAKAKAKLALAVARIDQLVEDISALHTSSDDSFSLSSGDPGQEAPREGRAQSCSPCRGPEGGRREAGSRAHPLLRLKAAHASLSNDSLNSGSASDGYCPREHMLPCPLAALASRREDPRCGQPRPSRLDLDLPGCQAEPPAREATSADARVRTIKLSPTYQHVPLLEGASRAGAEPLAGPGISPGARKQAWLPADHLSKVPEKLAAAPLSVASKALQKLAAQEGPLSLSRCSSLSSLSSAGRPGPSEGGDLDDSDSSLEGLEEAGPSEAELDSTWRAPGATSLPVAIPAPRRNRGRGLGVEDATPSSSSENYVQETPLVLSRCSSVSSLGSFESPSIASSIPSEPCSGQGSGTISPSELPDSPGQTMPPSRSKTPPLAPAPQGPPEATQFSLQWESYVKRFLDIADCRERCRLPSELDAGSVRFTVEKPDENFSCASSLSALALHEHYVQQDVELRLLPSACPERGGGAGGAGLHFAGHRRREEGPAPTGSRPRGAADQELELLRECLGAAVPARLRKVASALVPGRRALPVPVYMLVPAPAPAQEDDSCTDSAEGTPVNFSSAASLSDETLQGPPRDQPGGPAGRQRPTGRPTSARQAMGHRHKAGGAGRSAEQSRGAGKNRAGLELPLGRPPSAPADKDGSKPGRTRGDGALQSLCLTTPTEEAVYCFYGNDSDEEPPAAAPTPTHRRTSAIPRAFTRERPQGRKEAPAPSKAAPAAPPPARTQPSLIADETPPCYSLSSSASSLSEPEPSEPPAVHPRGREPAVTKDPGPGGGRDSSPSPRAAEELLQRCISSALPRRRPPVSGLRRRKPRATRLDERPAEGSRERGEEAAGSDRASDLDSVEWRAIQEGANSIVTWLHQAAAATREASSESDSILSFVSGLSVGSTLQPPKHRKGRQAEGEMGSARRPEKRGAASVKTSGSPRSPAGPEKPRGTQKTTPGVPAVLRGRTVIYVPSPAPRAQPKGTPGPRATPRKVAPPCLAQPAAPAKVPSPGQQRSRSLHRPAKTSELATLSQPPRSATPPARLAKTPSSSSSQTSPASQPLPRKRPPVTQAAGALPGPGASPVPKTPARTLLAKQHKTQRSPVRIPFMQRPARRGPPPLARAVPEPGPRGRAGTEAGPGARGGRLGLVRVASALSSGSESSDRSGFRRQLTFIKESPGLRRRRSELSSAESAASAPQGASPRRGRPALPAVFLCSSRCEELRAAPRQGPAPARQRPPAARPSPGERPARRTTSESPSRLPVRAPAARPETVKRYASLPHISVARRPDGAVPAAPASADAARRSSDGEPRPLPRVAAPGTTWRRIRDEDVPHILRSTLPATALPLRGSTPEDAPAGPPPRKTSDAVVQTEEVAAPKTNSSTSPSLETREPPGAPAGGQLSLLGSDVDGPSLAKAPISAPFVHEGLGVAVGGFPASRHGSPSRSARVPPFNYVPSPMVVAATTDSAAEKAPATASATLLE 2303 Q9Z1K7 Adenomatous Apc2 10090 None SL-0198 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}. UNIPROT Q9Z1K7 Pfam PF05956 Pfam PF16689 Pfam PF05923 Pfam PF18797 Pfam PF00514 Pfam PF05924 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}. P35922 EBI-16728828 0.35 GO:0005884 GO:0030877 GO:0016342 GO:0005737 GO:0005881 GO:0005829 GO:0031941 GO:0005794 GO:0045171 GO:0031258 GO:0015630 GO:0030496 GO:0048471 GO:0098794 GO:0008013 GO:0045295 GO:0008017 GO:0090630 GO:0001708 GO:0016477 GO:0000226 GO:0090090 GO:0007026 GO:0007399 GO:0007389 GO:0045732 GO:0043161 GO:0045595 GO:0016055 Unknown UniProt Sequence Analysis MTSSMASYEQLVRQVEALKAENTHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQTDISSLYNLKFHAPALGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDQERCFLLSEIEKEEKEKLWYYSQLQGLSKRLDELPHVDTFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQALLAVKPVAVEEEQEAEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQILHGTEAGSVGRAGIPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDSGTETPVPIEPQICQATCAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTRDPLNLALRRYAGMTLTNLTFGDVANKATLCARRGCMEAIVAQLGSESEELHQVVSSILRNLSWRADINSKKVLREVGSMTALMECVLRASKESTLKSVLSALWNLSAHSTENKAAICQVDGALGFLVSTLTYRCQGNSLAVIESGGGILRNVSSLIATREDYRQVLRDHNCLQTLLQHLTSHSLTIVSNACGTLWNLSARSPRDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKYQAAAMAVSPGTCVPSLYVRKQRALEAELDTRHLVHALGHLEKQSLPEAETTSKKPLPPLRHLDGLVQDYASDSGCFDDDDAPSLAAAATTAEPASPAVMSMFLGGPFLQGQALARTPPARQGGLEAEKEAGGEAAVAAKAKAKLALAVARIDRLVEDISALHTSSDDSFSLSSGDPGQEAPREGRAQSCSPCRGTEGGRREAGSRAHPLLRLKAAHTSLSNDSLNSGSTSDGYCTREHMTPCPLAALAEHRDDPVRGQTRPRRLDLDLPSRAELPARDTAATDARVRTIKLSPTYQHVPLLDGAAGAGVRPLVGPGTSPGARKQAWIPADSLSKVPEKLVASPLPIASKVLQKLVAQDGPMSLSRCSSLSSLSSTGHAVPSQAENLDSDSSLEGLEEAGPGEAELGRAWRASGSTSLPVSIPAPQRGRSRGLGVEDATPSSSSENCVQETPLVLSRCSSVSSLGSFESRSIASSIPSDPCSGLGSGTVSPSELPDSPGQTMPPSRSKTPPAPPGQPETSQFSLQWESYVKRFLDIADCRERCQPPSELDAGSVRFTVEKPDENFSCASSLSALALHELYVQQDVELRLRPPACPERAVGGGGHRRRDEAASRLDGPAPAGSRARSATDKELEALRECLGAAMPARLRKVASALVPGRRSLPVPVYMLVPAPARGDDSGTDSAEGTPVNFSSAASLSDETLQGPSRDKPAGPGDRQKPTGRAAPARQTRSHRPKAAGAGKSTEHTRGPCRNRAGLELPLSRPQSARSNRDSSCQTRTRGDGALQSLCLTTPTEEAVYCFYDSDEEPPATAPPPRRASAIPRALKREKPAGRKETPSRAAQPATLPVRAQPRLIVDETPPCYSLTSSASSLSEPEAPEQPANHARGPEQGSKQDSSPSPRAEEELLQRCISLAMPRRRTQVPGSRRRKPRALRSDIRPTEITQKCQEEVAGSDPASDLDSVEWQAIQEGANSIVTWLHQAAAKASLEASSESDSLLSLVSGVSAGSTLQPSKLRKGRKPAAEAGGAWRPEKRGTTSTKINGSPRLPNGPEKAKGTQKMMAGESTMLRGRTVIYSAGPASRTQSKGISGPCTTPKKTGTSGTTQPETVTKAPSPEQQRSRSLHRPGKISELAALRHPPRSATPPARLAKTPSSSSSQTSPASQPLPRRSPLATPTGGPLPGPGGSLVPKSPARALLAKQHKTQKSPVRIPFMQRPARRVPPPLARPSPEPGSRGRAGAEGTPGARGSRLGLVRMASARSSGSESSDRSGFRRQLTFIKESPGLLRRRRSELSSADSTASTSQAASPRRGRPALPAVFLCSSRCDELRVSPRQPLAAQRSPQAKPGLAPLAPRRTSSESPSRLPVRASPGRPETVKRYASLPHISVSRRSDSAVSVPTTQANATRRGSDGEARPLPRVAPPGTTWRRIKDEDVPHILRSTLPATALPLRVSSPEDSPAGTPQRKTSDAVVQTEDVATSKTNSSTSPSLESRDPPQAPASGPVAPQGSDVDGPVLTKPPASAPFPHEGLSAVIAGFPTSRHGSPSRAARVPPFNYVPSPMAAATMASDSAVEKAPVSSPASLLE 2274 O94353 Nuclear apq12 284812 None SL-0178 SL-0182 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}. UNIPROT O94353 Pfam PF12716 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}. GO:0005783 GO:0005789 GO:0016021 GO:0140599 GO:0005635 GO:0031965 GO:0042175 GO:0097038 GO:0006643 GO:0007077 GO:0051028 GO:0006998 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSLTSVLWNFVAKLAVDHGLNTNPDQVFQTVENVGKSFEKYETSFLKSLFNGNLGLSLPSAINILTLIIVLYFSLVIVNKTTSIALALFKTLAVISFFLLIGCLFAYWFINNGSF 115 P40532 Nuclear APQ12 559292 None SL-0178 SL-0182 Nucleus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. UNIPROT P40532 UNIPROT D6VVP2 Pfam PF12716 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}. P11484 EBI-3685195 0.35 P32589 EBI-3723382 0.35 GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0055088 GO:0051028 GO:0006998 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDATQPQYELSVVTQCLKSAIDVIQWLIPTITKFSQSHPLVFQLLFIFFTFYVFYKLLMNFITLVKRFLYLTLVVTCIGIYMRGSQQFLTVDLLNFYNFVMSNRYYAFKIYTLFINALEREINTVYHLAQMKMEQLLK 138 F6S3G9 Aquaporin-11 AQP11 9796 None SL-0198 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}. UNIPROT F6S3G9 Pfam PF00230 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}. GO:0009986 GO:0005737 GO:0030659 GO:0005783 GO:0005789 GO:0016021 GO:0048471 GO:0005886 GO:0015267 GO:0015254 GO:0015250 GO:0009992 GO:0048388 GO:0080170 GO:0050680 GO:1904293 GO:0032364 GO:0008284 GO:0006486 GO:0051260 GO:0006612 GO:0072014 Transmembrane UniProt Sequence Analysis {ECO:0000255} MTALRALWSEMQDTCTSLGLMLSVVLLAGLARVVARQQQLHRPMAHAFVLEFLATLQLCCCTHELLLLSEQEPAHPTWPLTLIYFFTLVHGLTLVGTSSNPCGVMMQMMLGGMSPEMGAVRLLAQLIGALGSRYCIGALWSLGLTKYHVSERSFACKNPIQVDLPKAVIVEALCSFIFHSALLNFQEVRPKLRIHLLAALITFLVYAGGSLTGAVFNPALALSLHFKCFDEAFLQFFIVYWLAPSLGILLMILMFSFFLPWLYNNHTINKKE 272 Q8NBQ7 Aquaporin-11 AQP11 9606 None SL-0198 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}. UNIPROT Q8NBQ7 Pfam PF00230 OMIM 609914 DisGeNET 282679 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}. P42229 EBI-3943260 0.37 GO:0009986 GO:0005737 GO:0030659 GO:0005783 GO:0005789 GO:0016021 GO:0048471 GO:0005886 GO:0015267 GO:0015254 GO:0015250 GO:0009992 GO:0048388 GO:0015793 GO:0080170 GO:0050680 GO:1904293 GO:1903573 GO:0032364 GO:0008284 GO:0006486 GO:0051260 GO:0006612 GO:0072014 GO:0030104 GO:0006833 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSPLLGLRSELQDTCTSLGLMLSVVLLMGLARVVARQQLHRPVAHAFVLEFLATFQLCCCTHELQLLSEQHPAHPTWTLTLVYFFSLVHGLTLVGTSSNPCGVMMQMMLGGMSPETGAVRLLAQLVSALCSRYCTSALWSLGLTQYHVSERSFACKNPIRVDLLKAVITEAVCSFLFHSALLHFQEVRTKLRIHLLAALITFLVYAGGSLTGAVFNPALALSLHFMCFDEAFPQFFIVYWLAPSLGILLMILMFSFFLPWLHNNHTINKKE 271 Q8BHH1 Aquaporin-11 Aqp11 10090 None SL-0198 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}. UNIPROT Q8BHH1 UNIPROT Q8JZU1 Pfam PF00230 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}. GO:0009986 GO:0005737 GO:0030659 GO:0005829 GO:0030425 GO:0005783 GO:0005789 GO:0016021 GO:0048471 GO:0005886 GO:0015267 GO:0015254 GO:0042802 GO:0015250 GO:0009992 GO:0048388 GO:0015793 GO:0080170 GO:0001822 GO:0050680 GO:1904293 GO:1903573 GO:0032364 GO:0008284 GO:0006486 GO:0051260 GO:0006612 GO:0072014 GO:0030104 GO:0006833 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSALLGLRPEVQDTCISLGLMLLFVLFVGLARVIARQQLHRPVVHAFVLEFLATFQLCCCTHELQVLSEQDSAHPTWTLTLIYFFSLVHGLTLVGTASNPCGVMMQMILGGMSPEMGAVRLLAQLVSALCSRYCISALWSLSLTKYHYDERILACRNPIHTDMSKAIIIEAICSFIFHSALLHFQEVRTKLRIHLLAALITFLAYAGGSLTGALFNPALALSLHFPCFDELFYKFFVVYWLAPSVGVLMMILMFSFFLPWLHNNQMTNKKE 271 Q8CHM1 Aquaporin-11 Aqp11 10116 None SL-0198 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}. UNIPROT Q8CHM1 UNIPROT Q6AZ79 Pfam PF00230 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}. GO:0009986 GO:0005737 GO:0030659 GO:0005829 GO:0030425 GO:0005783 GO:0005789 GO:0016021 GO:0048471 GO:0005886 GO:0015267 GO:0015254 GO:0042802 GO:0015250 GO:0009992 GO:0048388 GO:0015793 GO:0080170 GO:0001822 GO:0050680 GO:1904293 GO:1903573 GO:0032364 GO:0008284 GO:0006486 GO:0051260 GO:0006612 GO:0072014 GO:0055085 GO:0030104 GO:0006833 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSALLGLPPEVQDTCISLGLMLLVVLFMGLARVIARQQLHRPMVHAFVLEFLATFQLCYCTHELQLLSEQDSGHPTWTLTLIYFFSLVHGLTLVGTASNPCGVMMQMILGGMSPEMGAVRLMAQLVSALCSRYCISALWSLSLTKYHFDERILACRNPINTDISKAIIIEAICSFIFHSALLHFQEVRTKLRIHVLAALITFLAYAGGSLTGALFNPALALSLHFPCFDESFYKFFVVYWVAPSLGVLLMILMFSFFLPWLHNNQLSNKKE 271 Q3MHM8 ADP-ribosylation ARL6IP6 9913 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:Q8BH07}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q3MHM8 Pfam PF15062 GO:0016021 GO:0005637 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSFVESGRRSAPLRRRPGTPVPFARPAYSVFSQGDSWGEGEVEEEEGCDQVARDLRAEFSAGSSSKLRKDPVLQPDGDGSPVLPDKRNGIFSADAGGKALARRWPVQVLSILCSLLFAILLACLLAITYLIVKELHAENLKNEDDVNTGLLGFWSLLIISLTAGFSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKMTGHSFHMGYSMAILNGIVAALTVAWCLM 226 Q8N6S5 ADP-ribosylation ARL6IP6 9606 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:Q8BH07}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q8N6S5 UNIPROT B2RDS6 UNIPROT Q7Z4G7 Pfam PF15062 OMIM 616495 DisGeNET 151188 Q15125 EBI-24694418 0.56 Q5NEB4 EBI-2808841 0.00 P36895 EBI-11008521 0.35 Q9BZJ8 EBI-24509770 0.56 A0PK11 EBI-25264604 0.56 Q14973 EBI-24664535 0.56 Q96HE8 EBI-24679228 0.56 Q13520 EBI-23703606 0.56 Q96GQ5 EBI-24752673 0.56 Q6UW68 EBI-24780992 0.56 Q0VAB0 EBI-25279584 0.56 O14880 EBI-25284176 0.56 Q8TAZ6 EBI-24555520 0.56 P48165 EBI-24802824 0.56 Q9NPL8 EBI-24809431 0.56 Q8N661 EBI-25273194 0.56 O43291 EBI-21587968 0.35 Q9NVS9 EBI-21736268 0.35 Q9GZZ1 EBI-21736268 0.35 Q9BY43 EBI-21736268 0.35 Q15126 EBI-21736268 0.35 Q13951 EBI-21736268 0.35 P55957 EBI-21736268 0.35 P51452 EBI-21736268 0.35 P30043 EBI-21736268 0.35 P09488 EBI-21736268 0.35 O60493 EBI-21736268 0.35 O60361 EBI-21736268 0.35 O15498 EBI-21736268 0.35 Q16853 EBI-21784415 0.35 P14416 EBI-20805470 0.37 P0DTC3 EBI-25491278 0.64 P46108 EBI-30820700 0.44 GO:0016021 GO:0005637 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSFAESGWRSALRRRGPGTPGPVARPSYSSFTQGDSWGEGEVDEEEGCDQVARDLRAEFSAGAWSEPRKRSVLPPDGNGSPVLPDKRNGIFPAAAGSRAQPRRWPVQVLSILCSLLFAILLAFLLAIAYLIVKELHAENLKNEDDVDTGLLGFWTLLIISLTAGFSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKLTGHSFHMGYSMAILNGIVAALTVAWCLM 226 Q8BH07 ADP-ribosylation Arl6ip6 10090 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:31142202}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q8BH07 UNIPROT Q8BSK7 UNIPROT Q8VCL3 UNIPROT Q9CY07 UNIPROT Q9D4R5 UNIPROT Q9WUH0 Pfam PF15062 GO:0016021 GO:0005637 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSFVESWRFAGARRRRQVTPGPATRPGYSDYTQGDSWGEGEGDEDEGCDQVARDLRAEFSARASSETKRAPLLPRVGDGSPVLPDKRNGIFPATAAKRTQARRWPIQALSILCSLLFAVLLAFLLAIAYMIVKELHAENLKNEDDIHTGLLGFWSLLIISLTAGLSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKLTGHSFHMGYSMAILNGIVAALTVAWCLM 226 Q68FV2 ADP-ribosylation Arl6ip6 10116 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:Q8BH07}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q68FV2 Pfam PF15062 GO:0016021 GO:0005637 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSFVESWRSVGPRRRRQVTPGPVTRSVYSDYTQGNSWSEDGDEGCDQVARDLRAEFSARASSESKRAPLLPRIGDGSPVLPDKRNGIFPATAAKRTQARRWPIQALSILCSLLFAVLLAFLLAIAYLIVKELHTENSKNEDVVDTGLLGFWSLLIISLTAGLSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKLTGHSFHMGYSMAILNGVVAALTVAWCLM 223 A3KNS9 All-trans atraid 7955 None SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:Q6UW56}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6UW56}. UNIPROT A3KNS9 UNIPROT Q502E7 UNIPROT Q5RID6 PROSITE PS00022 Involved in osteoblast cell differentiation. May play a role in inducing the cell cycle arrest (By similarity). {ECO:0000250}. GO:0016021 GO:0043231 GO:0005635 GO:0048471 GO:0005886 GO:0048856 GO:0030154 GO:0033689 GO:0042177 GO:0030501 GO:0045669 GO:0010468 Transmembrane UniProt Sequence Analysis {ECO:0000255} MTANVTVSSMYLFTVLLLLFNVYVNSQDTDAQLCQMCEGTIRHDSPVWSFCITKGYVKGHCCFKNNTSDVDTIIGLDLSNCSISHVEHLYNSSTALIIDLSNNPISNLSDYVFQGFSQLTQLLLPSKLECPGGRASWEKVEVKSITRICEGQKNACNQTVQMPLVCPENSLCSPYGPGFFECSCLNNFHGYKCMRQGEFPLVKVLGILTASTVVVSSVLWFTQRRKVKNT 230 Q6UW56 All-trans ATRAID 9606 None SL-0178 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). UNIPROT Q6UW56 UNIPROT A8C1S2 UNIPROT A8K779 UNIPROT Q96FF6 UNIPROT Q96RT2 UNIPROT Q9Y2R7 UNIPROT Q9Y5L7 PROSITE PS00022 PROSITE PS01186 PROSITE PS50026 OMIM 619682 DisGeNET 51374 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}. Q93052 EBI-736289 0.00 Q9Y5X1 EBI-7876576 0.52 A0A6L8PDJ5 EBI-2838097 0.00 Q92832 EBI-7001256 0.61 Q00013 EBI-24627560 0.56 Q8NCC5 EBI-21822465 0.35 Q16236 EBI-22030894 0.35 Q14145 EBI-22030903 0.35 GO:0016021 GO:0043231 GO:0005765 GO:0005635 GO:0048471 GO:0005886 GO:0030154 GO:0033689 GO:0042177 GO:0030501 GO:0045669 GO:0010468 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAPHDPGSLTTLVPWAAALLLALGVERALALPEICTQCPGSVQNLSKVAFYCKTTRELMLHARCCLNQKGTILGLDLQNCSLEDPGPNFHQAHTTVIIDLQANPLKGDLANTFRGFTQLQTLILPQHVNCPGGINAWNTITSYIDNQICQGQKNLCNNTGDPEMCPENGSCVPDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGATTLSVSILLWATQRRKAKTS 229 Q6PGD0 All-trans Atraid 10090 None SL-0178 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}. UNIPROT Q6PGD0 UNIPROT Q3UAH4 UNIPROT Q810Q3 UNIPROT Q9DD14 PROSITE PS00022 PROSITE PS01186 PROSITE PS50026 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}. GO:0016021 GO:0043231 GO:0005765 GO:0005635 GO:0048471 GO:0005886 GO:0030154 GO:0033689 GO:0042177 GO:0030501 GO:0045669 GO:0010468 Transmembrane UniProt Sequence Analysis {ECO:0000255} MASRESGGSRAAALLLVLGVERALALPEICTLCPGGMHNLSRVAAYCEDTSKLMQARCCLNQKGTILGLDLQNCSLKDPGPNFLQAYTAIIIDLQANPLKDDLANTFRGFTQLQTLILPQDVPCPGGSNAWDNVTSFKDKQICQGQRDLCNSTGSPEMCPENGSCASDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGSTTLAISILLWGTQRRKAKAS 223 Q5E9I6 ADP-ribosylation ARF3 9913 None SL-0198 Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5E9I6 UNIPROT Q0VCG1 Pfam PF00025 PROSITE PS51417 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}. GO:0005794 GO:0048471 GO:0005886 GO:0005525 GO:0003924 GO:0006886 GO:0006890 GO:0016192 Lipid-Anchored UniProt Sequence Analysis {ECO:0000255} MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLANQLKNKK 181 P61204 ADP-ribosylation ARF3 9606 None SL-0198 Golgi apparatus {ECO:0000269|PubMed:17555535}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}. UNIPROT P61204 UNIPROT A8K6G8 UNIPROT B7ZB63 UNIPROT P16587 PDB 6II6 Pfam PF00025 PROSITE PS51417 OMIM 103190 DisGeNET 377 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. P54259 EBI-951076 0.00 P53365 EBI-640718 0.37 O15264 EBI-2255044 0.35 O35071 EBI-2557531 0.40 P97302 EBI-2559511 0.40 Q8VD62 EBI-2562857 0.40 Q5PRE5 EBI-2563058 0.40 Q14186 EBI-8836223 0.35 Q8TBB1 EBI-24495699 0.56 A2A935 EBI-21024514 0.35 P14404 EBI-21028244 0.35 Q5S007 EBI-21360986 0.35 P0DOF2 EBI-25603126 0.35 P53367 EBI-25568957 0.40 Q96CS3 EBI-25770166 0.35 P05067 EBI-25937879 0.56 Q01995 EBI-26878675 0.35 P34972 EBI-26880846 0.35 Q9BXK1 EBI-29019783 0.35 Q96ED9 EBI-34575530 0.27 GO:0070062 GO:0000139 GO:0048471 GO:0005886 GO:0005525 GO:0003924 GO:0006886 GO:0006890 GO:0016192 Lipid-Anchored UniProt Sequence Analysis {ECO:0000255} MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLANQLKNKK 181 P61205 ADP-ribosylation Arf3 10090 None SL-0198 Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT P61205 UNIPROT P16587 Pfam PF00025 PROSITE PS51417 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. P35922 EBI-16728828 0.35 Q62108 EBI-16724752 0.53 Q7TMB8 EBI-16727444 0.35 F6SEU4 EBI-16733301 0.53 Q9D415 EBI-16725590 0.35 Q4ACU6 EBI-16726570 0.35 Q9NRI5 EBI-26612017 0.35 GO:0005794 GO:0048471 GO:0005886 GO:0005525 GO:0003924 GO:0006886 GO:0015031 GO:0006890 GO:0016192 Lipid-Anchored UniProt Sequence Analysis {ECO:0000255} MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLANQLKNKK 181 Q5R5P7 ADP-ribosylation ARF3 9601 None SL-0198 Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5R5P7 Pfam PF00025 PROSITE PS51417 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}. GO:0005794 GO:0048471 GO:0005525 GO:0003924 GO:0015031 GO:0016192 Lipid-Anchored UniProt Sequence Analysis {ECO:0000255} MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLANQLKNKK 181 P61206 ADP-ribosylation Arf3 10116 None SL-0198 Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT P61206 UNIPROT P16587 Pfam PF00025 PROSITE PS51417 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. P19357 EBI-921030 0.35 P80386 EBI-16400563 0.35 P19332 EBI-26374040 0.35 GO:0005794 GO:0048471 GO:0005886 GO:0005525 GO:0003924 GO:0006886 GO:0006890 GO:0016192 Lipid-Anchored UniProt Sequence Analysis {ECO:0000255} MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLANQLKNKK 181 P84085 ADP-ribosylation ARF5 9606 None SL-0198 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}. UNIPROT P84085 UNIPROT P26437 PDB 2B6H Pfam PF00025 PROSITE PS51417 OMIM 103188 DisGeNET 381 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}. P04626 EBI-25367743 0.37 Q13573 EBI-7950968 0.35 P19320 EBI-6191076 0.35 Q96FW1 EBI-10770198 0.35 Q96GX1 EBI-11375285 0.27 P61006 EBI-11822843 0.35 Q96HD9 EBI-24488061 0.56 Q8N9I9 EBI-25277416 0.56 Q8WVK2 EBI-21500567 0.35 Q9UNA3 EBI-21543010 0.35 P35414 EBI-21559824 0.35 P46059 EBI-21560916 0.35 Q9UHF4 EBI-21590820 0.35 P54219 EBI-21609589 0.35 P30550 EBI-21613281 0.35 Q9Y5M8 EBI-21633655 0.35 Q9NU53 EBI-21700986 0.35 P56559 EBI-21709189 0.35 P21589 EBI-21722916 0.35 P55290 EBI-21736384 0.35 P25445 EBI-21766342 0.35 Q96GM1 EBI-21806142 0.35 O60259 EBI-21828465 0.35 P09923 EBI-21831497 0.35 O94955 EBI-21879222 0.35 Q86YS3 EBI-15605267 0.40 P62491 EBI-15605371 0.35 O75154 EBI-15605449 0.40 Q71U36 EBI-16800060 0.27 P14854 EBI-21933521 0.35 O00746 EBI-21934323 0.35 Q9H944 EBI-25472954 0.35 Q5S007 EBI-21360986 0.35 P05067 EBI-21132574 0.35 P13569 EBI-25416349 0.35 P0DOF2 EBI-25603126 0.35 O95931 EBI-25477072 0.35 Q96CS3 EBI-25770808 0.35 Q96LU5 EBI-27050332 0.35 Q96T52 EBI-27050444 0.35 Q8N488 EBI-27110926 0.35 GO:0070062 GO:0005794 GO:0048471 GO:0005886 GO:0005525 GO:0003924 GO:0006886 GO:0006890 GO:0016192 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:25255805} MGLTVSALFSRIFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVQESADELQKMLQEDELRDAVLLVFANKQDMPNAMPVSELTDKLGLQHLRSRTWYVQATCATQGTGLYDGLDWLSHELSKR 180 P84084 ADP-ribosylation Arf5 10090 None SL-0198 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}. UNIPROT P84084 UNIPROT A2RTC5 UNIPROT P26437 Pfam PF00025 PROSITE PS51417 GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. {ECO:0000269|PubMed:11950392}. P68510 EBI-8586548 0.35 Q9JKK1 EBI-7569455 0.27 Q8BYR5 EBI-7569528 0.60 F6SEU4 EBI-16733301 0.53 Q62108 EBI-16724752 0.35 Q9D415 EBI-16725590 0.35 GO:0005737 GO:0005794 GO:0048471 GO:0005886 GO:0005525 GO:0003924 GO:0006886 GO:0015031 GO:0006890 GO:0016192 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:P84085} MGLTVSALFSRIFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVQESADELQKMLQEDELRDAVLLVFANKQDMPNAMPVSELTDKLGLQHLRSRTWYVQATCATQGTGLYDGLDWLSHELSKR 180 P84083 ADP-ribosylation Arf5 10116 None SL-0198 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}. UNIPROT P84083 UNIPROT P26437 Pfam PF00025 PROSITE PS51417 GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. {ECO:0000250|UniProtKB:P84084}. P00533 EBI-22241891 0.35 P19357 EBI-921030 0.35 P09619 EBI-22248078 0.35 GO:0005737 GO:0005794 GO:0048471 GO:0005886 GO:0005525 GO:0003924 GO:0006886 GO:0006890 GO:0016192 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:P84085} MGLTVSALFSRIFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVQESADELQKMLQEDELRDAVLLVFANKQDMPNAMPVSELTDKLGLQHLRSRTWYVQATCATQGTGLYDGLDWLSHELSKR 180 P54074 ERAD-associated ASI1 559292 None SL-0178 SL-0179 SL-0182 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}. UNIPROT P54074 UNIPROT D6VZU2 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}. P53895 EBI-10096457 0.46 P53983 EBI-10096480 0.56 P02829 EBI-3810442 0.35 P10614 EBI-10096413 0.40 Q969F0 EBI-11533969 0.56 GO:0097658 GO:0016021 GO:0005637 GO:0034399 GO:0046872 GO:0061630 GO:0004842 GO:0071230 GO:0016567 GO:0036369 GO:0006511 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNSSTSSENVFINSFSYLNQTSQAVISGNSTFANVINFPYRLGLSFIGAVNLQYEQTVKSEEIPPTLRSVFDTIGFFFSPYAIFCFVIAIVLNRFVVFYAVLNNGSRRTLPLWLSNVFHVSAVVVLAMVSLGPLTLGKDFKILGDPAFAQEKFLLNIFYAFAYSYCVETIFTIMRNSSPLEGTDYSLFELSIQFYTMTNNNTKFLDSPDYIIDCSMAILSRILIHLVEIFRLRNYRLLFSTIMNLCHICYLGIRVKQGGWKSLPFSVKFRHFPKLFSVSIICLSLLIFKLSCLIRWDPFGKSRNSCELLQFYPLSRNWKKYLNYTGEEDFSAMATKFALLLCSGTELMEKGIRREFPAINIPDNVNEKFFISGYLNELSKPYKENTSISFPKKNSSILKQRFFLMFPKSIIWIMKKLVGQVFFGFRDNKDEDIPDNDPSKMLKITKTNSLNNSAGHKEDIELELLNTSDDEYSEDYEPSEVESLGDSDEENLEEDSLIFNETRDALLDLFSSEDNEVHTDYNWIMSTSRILQQKLLSDKTLTRASILDTKLSEVDETFGTESDFDLSCAVCKVNERNTVLWPCRCFAICEDCRISLGLRGFSTCVCCRSKVHGYCKVHPVSDSK 624 P53895 Protein ASI2 559292 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:17085444}; Multi-pass membrane protein {ECO:0000269|PubMed:17085444}. UNIPROT P53895 UNIPROT D6W124 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}. P38074 EBI-855745 0.00 P25294 EBI-3762277 0.35 P10592 EBI-3793098 0.35 P10614 EBI-10096421 0.40 P53983 EBI-10096480 0.46 P54074 EBI-10096457 0.46 GO:0097658 GO:0005783 GO:0016021 GO:0005637 GO:0071230 GO:0036369 GO:0006511 Transmembrane UniProt Curator Inference {ECO:0000305|PubMed:17085444} MARPQNHRRSNWTERDDNDDYLFQRFLEESETRHSREPSPVTEQSQQELQQDVQQAIDGIFNSLRRNMSSTSNINRAANMDATTNGNGGINADTIRATNANTADSPFTARQQSPLRTFLRNLFILDYFIGLILFPFSVYNILRSGFNSMTFSENDFIIEIVGYWKFAKIFGSGGTTLIAYKDTGKLGLLGKFHNIIVFYSSPVIKHIMKSRDGNEPNLNWIRLMFAKAFELFVKVSTILIYLAYGVSGTVYMVTAGFFFVLCLLFTVIRRYKGVHRMLVSQRITGPGVF 289 P53983 Probable ASI3 559292 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17085444}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17085444}. UNIPROT P53983 UNIPROT D6W1G9 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}. P25491 EBI-3763707 0.35 P53895 EBI-10096480 0.46 P25346 EBI-7752898 0.37 P38156 EBI-7752951 0.37 P49626 EBI-787273 0.35 P0C2I0 EBI-787273 0.35 Q02159 EBI-860284 0.00 P25294 EBI-3660235 0.35 P10591 EBI-3667430 0.35 P11484 EBI-3777888 0.35 P39077 EBI-3824502 0.35 P54074 EBI-10096480 0.56 P10614 EBI-10096429 0.40 P53846 EBI-16291965 0.35 GO:0097658 GO:0016021 GO:0005637 GO:0034399 GO:0046872 GO:0004842 GO:0071230 GO:0036369 GO:0006511 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSTNILQHVKQLLHNRDVFSFFHNKTGNLNYLDNTTQKPEVFVSPNSTIVSAPTLDSFQALMEKGNFTTLQLAKVGIRMFFSYSVSKYAVLCFSTAIILNRLTVMSSLRSNSTNIRLPLWSKTLLHLVATLSLVKALLQILSQFGLMHELHVSDTDFYALSVYLFVALSDCIEIFISSTTNVPSLICSDFSIWGLSLNLYIISKMPAGQQHIGDNVELLGAVFHRLVIHLVELFHIRAYRLCGEVILNAGFFTAFVTRTYLNGLDFINICLIHNYFPGFFYISTILLASIGIFLKALFTSNPFRSLYSRYKNLEKWWRSNNYNGEEEFNEIALSLCLLLTSNDYKIFKKSDNVKSVDEVAAFSNSYVVSGHLNQLQSTPEDLLSRKEMTTDSQLPGFARTYLGLFELVRTIILTYSRLLKNLLWSKNFESSIDKKPRVGKRKKRDLNKYVTEKNYKKFLYKPDVKELNIESDLRSLELLLPEDDSSKDYFPPRKIDESVSDEEFDSDMESQLIIDEEKELTHLSSNAVDSDDLEEIAWNISMWSILNYEMDVHNKVNGPLTRSQYGKRNPQGVLVDVVIERLLHHTNSRYMYKRLNMKDDDKLEFKFDFAFDSCDEVEEMDLSCLICKVNKRNIVTWPCRCLALCDDCRISLGYKGFATCVSCDSEVKGYSKLNIV 676 Q13625 Apoptosis-stimulating TP53BP2 9606 None SL-0198 Cytoplasm, perinuclear region. Nucleus. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. Sequester in the cytoplasm on overexpression of DDX42. UNIPROT Q13625 UNIPROT B4DG66 UNIPROT Q12892 UNIPROT Q86X75 UNIPROT Q96KQ3 PDB 1YCS PDB 2UWQ PDB 4A63 PDB 4IRV PDB 6GHM PDB 6HKP Pfam PF12796 Pfam PF00018 PROSITE PS50297 PROSITE PS50088 PROSITE PS50002 OMIM 602143 DisGeNET 7159 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}. O95996 EBI-8830464 0.54 P10415 EBI-15723849 0.65 P27958 EBI-9389968 0.64 P29991 EBI-8828390 0.37 P49790 EBI-9688225 0.35 P61970 EBI-9688225 0.35 P62826 EBI-9692277 0.64 Q07817 EBI-15723914 0.56 Q12840 EBI-731035 0.00 P05067 EBI-77660 0.58 P62136 EBI-7267006 0.86 P68104 EBI-731032 0.00 P21246 EBI-731038 0.00 Q9BVJ6 EBI-731041 0.00 Q13432 EBI-731044 0.00 Q9BYC9 EBI-733610 0.00 Q13107 EBI-736082 0.00 O15265 EBI-952468 0.00 P04637 EBI-1026207 0.90 P46937 EBI-6912563 0.78 P46936 EBI-7804125 0.40 P63104 EBI-7195756 0.67 P46108 EBI-1960202 0.40 Q04917 EBI-1644092 0.64 Q04206 EBI-1749490 0.56 P35570 EBI-1751169 0.57 P81122 EBI-1751281 0.48 O08724 EBI-1751296 0.35 O14654 EBI-1751296 0.35 P35569 EBI-1751450 0.52 Q13625 EBI-7907803 0.62 P36873 EBI-7908028 0.85 Q92843 EBI-7908070 0.68 Q81ZG1 EBI-2838000 0.00 Q14457 EBI-3257986 0.35 P31016 EBI-7966630 0.44 Q09472 EBI-8632299 0.50 Q8IUQ4 EBI-10261292 0.56 P67870 EBI-7137665 0.37 Q13387 EBI-7240832 0.37 P53350 EBI-7314465 0.37 Q8NEY8 EBI-7317291 0.37 Q8TEW0 EBI-6911368 0.53 A6NKD9 EBI-6911368 0.35 P41236 EBI-6911368 0.35 O75901 EBI-6911368 0.35 Q9H3G5 EBI-6911368 0.35 P34932 EBI-6911368 0.35 P62140 EBI-6911368 0.67 Q8NHQ8 EBI-6911368 0.53 Q92598 EBI-6911368 0.35 Q02833 EBI-6911368 0.35 Q15834 EBI-6911368 0.35 P04083 EBI-6911368 0.35 A6NK89 EBI-6912271 0.35 P31946 EBI-8796749 0.35 Q9Y2J4 EBI-8797381 0.35 Q7TSJ6 EBI-8798662 0.27 Q4VCS5 EBI-8799893 0.27 Q9WMX2 EBI-9082105 0.37 Q2TBE0 EBI-10175037 0.56 Q8WWY3 EBI-10177388 0.56 O14777 EBI-10181501 0.56 P17031 EBI-10199685 0.56 P40222 EBI-10207929 0.56 P56279 EBI-10215275 0.56 P57075 EBI-10215824 0.56 P61968 EBI-10219004 0.56 P62807 EBI-10219796 0.56 P62875 EBI-10219932 0.56 P62993 EBI-10220253 0.56 Q86Y26 EBI-10230509 0.56 Q494U1 EBI-10241572 0.56 Q53HC0 EBI-10242635 0.56 Q8N5A5 EBI-10265979 0.56 Q8N5M1 EBI-10266628 0.56 Q8NCE2 EBI-10269256 0.56 Q92844 EBI-10279575 0.56 Q96DC9 EBI-10284602 0.56 Q96GG9 EBI-10286368 0.56 Q9BUJ2 EBI-10298924 0.56 Q9BUZ4 EBI-10299140 0.56 Q9NU19 EBI-10313701 0.56 Q9UBU9 EBI-10319914 0.56 Q9UQB8 EBI-10324972 0.56 Q9Y2D8 EBI-10326054 0.56 Q96J02 EBI-10635597 0.40 Q9BYG5 EBI-11002976 0.35 Q9NPB6 EBI-11011731 0.35 Q9JK83 EBI-11052294 0.35 P46938 EBI-11138299 0.35 O75665 EBI-11365691 0.27 Q15154 EBI-11366535 0.27 Q5BJF6 EBI-11367291 0.27 Q5JU00 EBI-11367780 0.27 Q6ZU80 EBI-11370150 0.27 Q7Z7A1 EBI-11371427 0.27 Q8N4C6 EBI-11374469 0.27 Q8TES7 EBI-11374846 0.27 Q96KN7 EBI-11376202 0.27 Q96NL6 EBI-11376636 0.27 Q96ST8 EBI-11377220 0.27 Q9Y2I6 EBI-11379511 0.27 O60308 EBI-11380299 0.27 O94986 EBI-11381405 0.27 Q5TB80 EBI-11385924 0.27 Q66GS9 EBI-11386281 0.27 Q68CZ1 EBI-11386978 0.27 Q8IW35 EBI-11391901 0.27 Q8N137 EBI-11392655 0.27 Q8N960 EBI-11393386 0.27 Q9C0F1 EBI-11397104 0.27 Q9HC77 EBI-11397411 0.27 Q15435 EBI-12451625 0.51 O43295 EBI-21563971 0.35 Q7Z4N8 EBI-21583801 0.35 Q86YM7 EBI-21671273 0.35 Q9UMS4 EBI-21763056 0.35 Q96ES7 EBI-21781962 0.35 Q96NE9 EBI-21880697 0.35 P61981 EBI-21905461 0.35 Q8N3R9 EBI-21911830 0.35 Q9H3D4 EBI-15685239 0.44 O15350 EBI-15685344 0.44 P12830 EBI-16124887 0.35 P35222 EBI-16124887 0.58 Q05086 EBI-16814851 0.35 P16403 EBI-20919284 0.40 Q15149 EBI-20926194 0.40 Q9NPJ6 EBI-25472202 0.27 Q6NSK7 EBI-21387894 0.00 P0DOF2 EBI-25603126 0.35 F1PAA9 EBI-27079701 0.27 P46934 EBI-30832503 0.44 P11362 EBI-32721578 0.27 GO:0030054 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0042802 GO:0051059 GO:0002039 GO:0017124 GO:0007049 GO:0072332 GO:0045786 GO:1900119 GO:0007165 Unknown UniProt Sequence Analysis MMPMFLTVYLSNNEQHFTEVPVTPETICRDVVDLCKEPGESDCHLAEVWCGSERPVADNERMFDVLQRFGSQRNEVRFFLRHERPPGRDIVSGPRSQDPSLKRNGVKVPGEYRRKENGVNSPRMDLTLAELQEMASRQQQQIEAQQQLLATKEQRLKFLKQQDQRQQQQVAEQEKLKRLKEIAENQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNNLFQQKQRELVLAVSKVEELTRQLEMLKNGRIDSHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVNELRDRLWKKKAALQQKENLPVSSDGNLPQQAASAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLVIQASEGPMKIQTLPNMRSGAASQTKGSKIHPVGPDWSPSNADLFPSQGSASVPQSTGNALDQVDDGEVPLREKEKKVRPFSMFDAVDQSNAPPSFGTLRKNQSSEDILRDAQVANKNVAKVPPPVPTKPKQINLPYFGQTNQPPSDIKPDGSSQQLSTVVPSMGTKPKPAGQQPRVLLSPSIPSVGQDQTLSPGSKQESPPAAAVRPFTPQPSKDTLLPPFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTHTRGPHFSSVYGKPVIAAAQNQQQHPENIYSNSQGKPGSPEPETEPVSSVQENHENERIPRPLSPTKLLPFLSNPYRNQSDADLEALRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSYPSKSASVTASSESPVEIQNPYLHVEPEKEVVSLVPESLSPEDVGNASTENSDMPAPSPGLDYEPEGVPDNSPNLQNNPEEPNPEAPHVLDVYLEEYPPYPPPPYPSGEPEGPGEDSVSMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYEPQNDDELPMKEGDCMTIIHREDEDEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA 1128 Q8CG79 Apoptosis-stimulating Tp53bp2 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. {ECO:0000250}. UNIPROT Q8CG79 UNIPROT Q3UYM7 UNIPROT Q8K2L5 Pfam PF12796 Pfam PF14604 PROSITE PS50297 PROSITE PS50088 PROSITE PS50002 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}. O35626 EBI-4325310 0.37 Q9EQ32 EBI-654281 0.37 P35569 EBI-1751427 0.40 Q80YT7 EBI-16732484 0.35 Q3UHD9 EBI-16750831 0.35 GO:0030054 GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0042802 GO:0051059 GO:0002039 GO:0017124 GO:0007049 GO:0007417 GO:0009792 GO:0007507 GO:0072332 GO:1900119 GO:1901216 GO:0010212 Unknown UniProt Sequence Analysis MMPMFLTVYLSNSEQHFTEVPVTPETICRDVVDLCKEPGENDCHLAEVWCGSERPVADNERMFDVLQRFGSQRNEVRFFLRHERPPNRDIVSGPRSQDPSVKRNGVKVPGEHRRKENGVNSPRLDLTLAELQEMASRQQQQIEAQQQMLATKEQRLKFLKQQDQRQQQQAAEQEKLKRLREIAESQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNSLFQQKQRELVLAVSKVEELTRQLEMLKNGRIDGHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVSELRDRLWKKKAALQQKENLPVSPDGNLPQQAVSAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLLMQSAEGPMKIQTLPNMRSGAASQSKGSKAHPASPDWNPSNADLLPSQGSSVPQSAGTALDQVDDGEIAVREKEKKVRPFSMFDTVDQCAAPPSFGTLRKNQSSEDILRDAQAVNKNVAKVPPPVPTKPKQIHLPYFGQTAQSPSDMKPDGNAQQLPIAATSVGAKLKPAGPQARMLLSPGAPSGGQDQVLSPASKQESPPAAAVRPFTPQPSKDTFPPAFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTQPRGPHFSSVYGKPVIAAAQNPQQHPENIYSCSQGKPGSPEPETETVSSVHESHENERIPRPLSPTKLLPFLSNPYRNQSDADLEALRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSHPSKSPGSVTVNPESSVEIPNPYLHVEPEKEVGSLVPEPLSPEDMGSASTENSDVPAPSAGLEYVSEGVTDSSTNLQNNVEETNPEAPHLLEVYLEEYPPYPPPPYPSGEPEVSEEDSARMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYEPQHDDELLMKEGDCMTVIRREDEEEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA 1128 Q9N0Z4 Phospholipid-transporting ATP11B 9986 None SL-0178 SL-0179 SL-0182 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}. UNIPROT Q9N0Z4 UNIPROT Q8WMR2 Pfam PF16212 Pfam PF16209 PROSITE PS00154 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}. GO:0005769 GO:0005783 GO:0005794 GO:0016021 GO:0005637 GO:0055038 GO:0005524 GO:0016887 GO:0000287 GO:0090555 GO:0090556 GO:0015917 Transmembrane UniProt Sequence Analysis {ECO:0000255} LGFDPPHQSDTRTIYIANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLFEQFRRVANFYFLIIFLVQLMIDTPTSPITSGLPLFFVITVTAIKQGYEDWLRHNSDNEVNGAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDGSCHVTTASLDGETNLKTHVAVPETAVLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPESLLLRGARLKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLIILISEAIISTILKYTWQAEEKWDEPWYNQKTEHQRNSSKILRFISDFLAFLVLYNFIIPISLYVTVEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDKTGTLTENEMQFRECSIHGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHVNSLSHLTSSSSFRTSPENDTELIKEHDLFFKAVSLCHTVQISSVQTDGIGDGPWQSSLAPSQLEYYASSPDEKALVEAAARIGIVFVGNTEETMEVKILGKLERYKLLHVLEFDSDRRRMSVIVQAPSGERFLFAKGAESSILPKCIGGEIEKTRIHVDEFALKGLRTLCVAYRQFTSKEYEVIDRRLFEARTALQQREEKLADVFHYIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSCGHFHRTMNILELTNQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLFMEVCRNCSAVLCCRMAPLQKAKVIRLIKISPEKPITIGCWDGANDVSMIQEAHVGIGIMGKERRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVCFITPQFLYQFYCLFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHIDPHILQNKPTLYRDISKNRLLSIKTFLYWTILGFSRSFIFLFGSYFLIGKDASLLGNGQMFGNWTFGTLVFTVMVITVTVKMALETHFWTWINHLVTWGSIIFYFVFSLFYGGILWPFLGSQNMYFVFIQLVSSGSAWFAIILMVVTCLFLDVMKKVFDRQLHPTSTEKAQLTETNSSIKCVDSLCCFPEGETTCTSVRRMLERVIGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC 1169 A7MB71 Protein ATP1B4 9913 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Detected in nuclear envelops. {ECO:0000250}. UNIPROT A7MB71 Pfam PF00287 PROSITE PS00390 PROSITE PS00391 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}. GO:0005637 GO:0005890 GO:0006813 GO:0006355 GO:0006814 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRRQLRSRRAPALPYGYRYRLDDQDEVNQNYLADEEEEAEEEARVMVVPDLEEEEEEEEEKEEEEKEEEDSHSQETDSAWWRKLQIVNEYLWDPEKRTSLARTGQSWSLILVIYFFFYASLAAVITLCMYTLFLTISPYMPTFTERVKPPGVMIRPFAHSLNFNFNVSEPDTWQHYVISLNGFLQGYNDSLQEEMNVDCPPGQYFIQDGDEDEDKKACQFKRSFLKNCSGLEDPTFGYSTGQPCILLKMNRIVGFRPERGDPVKVSCKVQRGDENDIRSINYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVKNQAVPVQCQLKGKGIINDVINDRFVGRVIFTLNIET 355 Q9UN42 Protein ATP1B4 9606 None SL-0178 SL-0179 SL-0182 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}. UNIPROT Q9UN42 UNIPROT Q17RR0 UNIPROT Q9UN41 Pfam PF00287 PROSITE PS00390 PROSITE PS00391 OMIM 301073 DisGeNET 23439 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}. Q9H1E5 EBI-21789423 0.35 Q5BVD1 EBI-24610156 0.56 P07306 EBI-24622793 0.56 Q7Z2K6 EBI-24534258 0.56 Q9BZL3 EBI-24550199 0.56 O60636 EBI-24576756 0.56 Q8N6G5 EBI-24583309 0.56 Q07325 EBI-24593256 0.56 Q8WVV5 EBI-21789423 0.35 Q9Y219 EBI-21789423 0.35 Q9UK28 EBI-21789423 0.35 Q9NQZ7 EBI-21789423 0.35 Q9HCN3 EBI-21789423 0.35 Q9BZ76 EBI-21789423 0.35 Q96J42 EBI-21789423 0.35 Q8TCT7 EBI-21789423 0.35 Q8N766 EBI-21789423 0.35 Q86UD1 EBI-21789423 0.35 Q5HYA8 EBI-21789423 0.35 Q14393 EBI-21789423 0.35 Q13733 EBI-21789423 0.35 Q13683 EBI-21789423 0.35 Q03167 EBI-21789423 0.35 P55899 EBI-21789423 0.35 O75298 EBI-21789423 0.35 Q9CSN1 EBI-15644307 0.40 GO:0005887 GO:0005635 GO:0005637 GO:0005890 GO:0022890 GO:0006813 GO:0006355 GO:0006814 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRRQLRSRRAPSFPYSYRYRLDDPDEANQNYLADEEEEAEEEARVTVVPKSEEEEEEEEKEEEEEEEKEEEEGQGQPTGNAWWQKLQIMSEYLWDPERRMFLARTGQSWSLILLIYFFFYASLAAVITLCMYTLFLTISPYIPTFTERVKPPGVMIRPFAHSLNFNFNVSEPDTWQHYVISLNGFLQGYNDSLQEEMNVDCPPGQYFIQDGNEDEDKKACQFKRSFLKNCSGLEDPTFGYSTGQPCILLKMNRIVGFRPELGDPVKVSCKVQRGDENDIRSISYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVKNQAVPVQCQLKGKGVINDVINDRFVGRVIFTLNIET 357 Q99ME6 Protein Atp1b4 10090 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Detected in nuclear envelops. {ECO:0000250}. UNIPROT Q99ME6 UNIPROT Q543D0 UNIPROT Q99ME5 Pfam PF00287 PROSITE PS00390 PROSITE PS00391 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}. Q6ZWR6 EBI-15644511 0.37 Q921T2 EBI-15644413 0.37 Q9CSN1 EBI-15644494 0.37 GO:0000785 GO:0005635 GO:0005637 GO:0005634 GO:0005890 GO:0006813 GO:0006355 GO:0006814 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRRQLRSRRAPAFPYGYRYRLDDQDEANHNYLADEEEEAEEEAQVMMVPGLEEEEEEEEGKEEEEEREEEEGQGQSTGSAWWRKLQIVNEYLWDPEKRMSLARTGQSRSLILVIYFFFYASLAAVITLFIYMLFLAISPYMPTFTEQVKPPGVMIRPFAHSLNFNFNVSEPETWQRYVISLNGFLQGYNDSLQEEMNIDCPPGRYFIQDGDEDEDKKACQFKRSFLKNCSGLEDPTFGYSTGQPCILLKMNRIVGFRPEFGDPVKVSCKVQKGDENDIRSINYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVKNQAVPVQCQLKGKGIVNDVINDRFVGRIIFTLNIET 356 Q9BDK6 Protein ATP1B4 9823 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:14656723}; Single-pass type II membrane protein {ECO:0000269|PubMed:14656723}. Note=Detected in nuclear envelops. UNIPROT Q9BDK6 UNIPROT Q9BDK5 Pfam PF00287 PROSITE PS00390 PROSITE PS00391 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}. GO:0005635 GO:0005637 GO:0005890 GO:0006813 GO:0006355 GO:0006814 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRRQLRSRRAPAFPYGYGYRLDDQDEVNQNYLADEEEEAEEARVMVVPDLEEEEKEEEEEKEEDEKEEEESHHQDTRSAWWQKLQIVNEYLWDPEKRMSLARTGQSLSLLLVIYFFFYASLAAVITLCMYTLFLTISPYVPTFTERVKPPGVMIRPFAHSLNFNFNVSEPDTWQHYVISLNGFLQGYNDSLQEEMNVDCPPGQYFIQDGDEDEDKKACQFKRSFLKNCSGLEDPTFGYSTGQPCILLKMNRIVGFRPELGDPVKVSCKVQRGDENDIRSISYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVKNQAVPVQCQLKGKGIINDVINDRFVGRVIFTLNIET 355 Q9R193 Protein Atp1b4 10116 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Detected in nuclear envelops. {ECO:0000250}. UNIPROT Q9R193 UNIPROT Q9R192 Pfam PF00287 PROSITE PS00390 PROSITE PS00391 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}. Q5PQX1 EBI-15644460 0.40 D4A8G7 EBI-15644371 0.40 GO:0000785 GO:0005637 GO:0005634 GO:0005890 GO:0006813 GO:0006355 GO:0006814 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRRQLRSRRAPAFPYGYRYRLDDQDEMNHNYLADEEEEAEEEAQVMMVPGLEEEEEEEEGKEEEEEREEEEGQGQSTGNAWWRKLQIVNEYLWDPEKRMSLARTGQSRSLILVIYFFFYASLAAVITLFIYMLFLAISPYMPTFTEQVKPPGVMIRPFAHSLNFNFNVSEPETWQRYVISLNGFLQGYNDSLQEEMNIDCPPGQYFIQDGDEDEDKKACQFKRSFLKNCSGLEDPTFGYSTGQPCILLKMNRIVGFRPEFGDPVKVSCKVQKGDENDIRSINYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVKNQEVPVQCQLKGKGIVNDVINDRFVGRIIFTLNIET 356 Q93084 Sarcoplasmic/endoplasmic ATP2A3 9606 None SL-0178 SL-0182 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}. UNIPROT Q93084 UNIPROT A8MZG0 UNIPROT D3DTJ8 UNIPROT O60900 UNIPROT O60901 UNIPROT O75501 UNIPROT O75502 UNIPROT Q16115 UNIPROT Q6JHX1 UNIPROT Q8TEX5 UNIPROT Q8TEX6 Pfam PF00689 Pfam PF00690 PROSITE PS00154 OMIM 601929 DisGeNET 489 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}. P04626 EBI-8770853 0.35 P0DTD1 EBI-26496082 0.35 Q9HAW0 EBI-1064949 0.00 Q9P2S5 EBI-1079489 0.00 P04439 EBI-1079517 0.00 P13569 EBI-1171098 0.35 P16333 EBI-1967197 0.40 P15336 EBI-5529812 0.35 P04578 EBI-6177436 0.35 Q96DB2 EBI-6598272 0.35 Q20MH8 EBI-12586007 0.35 P22460 EBI-21505491 0.35 Q86UE6 EBI-21507777 0.35 Q9UN75 EBI-21537575 0.35 Q7KYR7 EBI-21541130 0.35 Q2Y0W8 EBI-21566582 0.35 Q9C099 EBI-21571999 0.35 Q6UXE8 EBI-21583647 0.35 Q9UN71 EBI-21584146 0.35 O43291 EBI-21587968 0.35 Q8TDD5 EBI-21589012 0.35 Q8WW62 EBI-21589315 0.35 P58658 EBI-21588759 0.35 Q9BQ31 EBI-21590203 0.35 Q96FT7 EBI-21589962 0.35 Q9NRJ7 EBI-21590428 0.35 Q96FV3 EBI-21591007 0.35 Q9Y5M8 EBI-21633655 0.35 Q9Y5F2 EBI-21658599 0.35 Q16281 EBI-21687526 0.35 Q8NAC3 EBI-21687716 0.35 Q9Y5H8 EBI-21695064 0.35 Q9Y5G8 EBI-21697051 0.35 P14778 EBI-21700570 0.35 P08754 EBI-21709056 0.35 Q86XK7 EBI-21739948 0.35 Q8IV01 EBI-21748151 0.35 Q6P9F7 EBI-21762226 0.35 P40967 EBI-21773380 0.35 Q99675 EBI-21775037 0.35 Q5T2D2 EBI-21777947 0.35 Q8NAU1 EBI-21799562 0.35 A5X5Y0 EBI-21800698 0.35 O43521 EBI-21803818 0.35 Q9NRM6 EBI-21807235 0.35 Q16445 EBI-21828581 0.35 O76096 EBI-21835330 0.35 Q8TEQ8 EBI-21840858 0.35 Q9Y5E4 EBI-21877083 0.35 Q9Y227 EBI-21891924 0.35 P51957 EBI-20721387 0.35 P22626 EBI-20937172 0.40 P0DTC5 EBI-25685699 0.53 P37173 EBI-25892533 0.56 Q8NCK7 EBI-27103180 0.35 GO:0005783 GO:0005789 GO:0016021 GO:0031965 GO:0031090 GO:0031095 GO:0016529 GO:0033017 GO:0005524 GO:0016887 GO:0015085 GO:0030899 GO:0008656 GO:0046872 GO:0005388 GO:0015662 GO:0044325 GO:0006919 GO:0070588 GO:0006816 GO:1903515 GO:0006874 GO:0070059 GO:0034220 GO:1900121 GO:1903779 GO:0150104 Transmembrane UniProt By Similarity {ECO:0000250} MEAAHLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTTLRVDQSILTGESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGSCLLHEFTISGTTYTPEGEVRQGDQPVRCGQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLQALSRVERAGACNTVIKQLMRKEFTLEFSRDRKSMSVYCTPTRPHPTGQGSKMFVKGAPESVIERCSSVRVGSRTAPLTPTSREQILAKIRDWGSGSDTLRCLALATRDAPPRKEDMELDDCSKFVQYETDLTFVGCVGMLDPPRPEVAACITRCYQAGIRVVMITGDNKGTAVAICRRLGIFGDTEDVAGKAYTGREFDDLSPEQQRQACRTARCFARVEPAHKSRIVENLQSFNEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKSAAEMVLSDDNFASIVAAVEEGRAIYSNMKQFIRYLISSNVGEVVCIFLTAILGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMEKLPRSPREALISGWLFFRYLAIGVYVGLATVAAATWWFVYDAEGPHINFYQLRNFLKCSEDNPLFAGIDCEVFESRFPTTMALSVLVTIEMCNALNSVSENQSLLRMPPWMNPWLLVAVAMSMALHFLILLVPPLPLIFQVTPLSGRQWVVVLQISLPVILLDEALKYLSRNHMHEEMSQK 999 P54259 Atrophin-1 ATN1 9606 None SL-0198 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}. UNIPROT P54259 UNIPROT Q99495 UNIPROT Q99621 UNIPROT Q9UEK7 Pfam PF03154 OMIM 125370 OMIM 607462 OMIM 618494 DisGeNET 1822 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}. 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. O15162 EBI-956422 0.00 P14335 EBI-11422698 0.37 Q9UQB8 EBI-6997364 0.63 Q06455 EBI-955342 0.00 Q01844 EBI-955350 0.00 Q96CN9 EBI-955358 0.00 Q96PV6 EBI-955366 0.00 Q99750 EBI-955374 0.00 Q9BSW2 EBI-955382 0.00 O43639 EBI-955390 0.00 P61964 EBI-8836498 0.74 O00308 EBI-955406 0.00 Q9BQ66 EBI-956398 0.00 Q9HAU0 EBI-946360 0.51 P61289 EBI-956430 0.00 Q93062 EBI-956438 0.00 Q15654 EBI-946367 0.51 Q9NWB1 EBI-946549 0.51 O00468 EBI-950710 0.00 P54259 EBI-950716 0.00 P46379 EBI-950722 0.00 Q02641 EBI-950728 0.00 O43439 EBI-950734 0.00 Q9HC77 EBI-950740 0.00 Q9H2X0 EBI-950746 0.00 P52943 EBI-950752 0.00 O14641 EBI-950758 0.00 Q12805 EBI-950764 0.00 O95967 EBI-950770 0.00 O75095 EBI-950776 0.00 Q7Z7M0 EBI-950782 0.00 P23142 EBI-950794 0.00 Q5ZEY4 EBI-950800 0.00 P28799 EBI-950806 0.00 P98160 EBI-950812 0.00 Q9Y219 EBI-950818 0.00 O60290 EBI-950824 0.00 Q14766 EBI-950830 0.00 Q8N2S1 EBI-950836 0.00 P02686 EBI-950842 0.00 A6BM72 EBI-950848 0.00 Q92832 EBI-950854 0.00 Q99435 EBI-950860 0.00 O75420 EBI-950866 0.00 P17858 EBI-950872 0.00 Q96PM5 EBI-950878 0.00 O75093 EBI-950884 0.00 Q6ZWJ1 EBI-950890 0.00 Q86TM6 EBI-950896 0.00 Q99973 EBI-950902 0.00 Q9ULU4 EBI-950914 0.00 P98175 EBI-950926 0.00 Q9NP73 EBI-950944 0.00 Q9UBX5 EBI-950980 0.00 P98164 EBI-951010 0.00 Q92824 EBI-951040 0.00 P25788 EBI-951046 0.00 Q9H0M0 EBI-951064 0.00 Q08117 EBI-951070 0.00 P61204 EBI-951076 0.00 P48634 EBI-951088 0.00 Q9H9J5 EBI-951100 0.00 Q09013 EBI-951106 0.00 Q16610 EBI-951112 0.00 P98095 EBI-951130 0.00 Q3KQU3 EBI-951142 0.00 Q5JSZ5 EBI-951148 0.00 A7E2V4 EBI-951154 0.00 Q15323 EBI-951160 0.00 Q92794 EBI-951166 0.00 Q8WYB5 EBI-951172 0.00 O43251 EBI-951190 0.00 Q9P2R6 EBI-951196 0.00 Q96EP0 EBI-951202 0.00 Q8IUQ4 EBI-3928819 0.55 O43255 EBI-951214 0.00 Q96R06 EBI-951220 0.00 Q9Y4B4 EBI-951226 0.00 Q70EL1 EBI-951232 0.00 O75081 EBI-1190259 0.37 A0A6L8P747 EBI-2817819 0.00 A0A6L7HHZ0 EBI-2837958 0.00 A0A5P8YJG2 EBI-2848559 0.00 A0A3N4BEU0 EBI-2875462 0.00 A0A0H2W2I9 EBI-2875448 0.00 A0A3N4AY03 EBI-2875455 0.00 Q8ZA76 EBI-2875469 0.00 P31016 EBI-7968802 0.44 O75360 EBI-9030447 0.37 Q14457 EBI-14690094 0.35 Q9ULD9 EBI-15637634 0.44 Q8WXX7 EBI-16135059 0.35 P61417 EBI-20817140 0.37 Q8ZG77 EBI-20818229 0.37 P51114 EBI-26509906 0.37 P51116 EBI-26511575 0.37 Q9BYB0 EBI-26513830 0.37 Q92574 EBI-26515443 0.37 P10275 EBI-26965611 0.27 P46934 EBI-30832404 0.44 Q99816 EBI-30839191 0.44 P46937 EBI-30846537 0.44 O15178 EBI-29014443 0.27 P55771 EBI-29704799 0.27 Q8TDD2 EBI-29740517 0.27 P31314 EBI-29779038 0.27 GO:0070161 GO:0005737 GO:0016363 GO:0005654 GO:0005634 GO:0048471 GO:0019904 GO:0003713 GO:0003714 GO:0001906 GO:0016477 GO:0007417 GO:0008340 GO:0030011 GO:0008584 GO:0035264 GO:0000122 GO:0051402 GO:0009791 GO:0032094 GO:0007283 Unknown UniProt Sequence Analysis MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEEASTPKVNKQGRSEEISESESEETNAPKKTKTEQELPRPQSPSDLDSLDGRSLNDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPQPPDSTPRQPEASFEPHPSVTPTGYHAPMEPPTSRMFQAPPGAPPPHPQLYPGGTGGVLSGPPMGPKGGGAASSVGGPNGGKQHPPPTTPISVSSSGASGAPPTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLNNASASPPGLGAQPLPGHLPSPHAMGQGMGGLPPGPEKGPTLAPSPHSLPPASSSAPAPPMRFPYSSSSSSSAAASSSSSSSSSSASPFPASQALPSYPHSFPPPTSLSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANSNAHPGPFPPSTGAQSTAHPPVSTHHHHHQQQQQQQQQQQQQQQQQQQHHGNSGPPPPGAFPHPLEGGSSHHAHPYAMSPSLGSLRPYPPGPAHLPPPHSQVSYSQAGPNGPPVSSSSNSSSSTSQGSYPCSHPSPSQGPQGAPYPFPPVPTVTTSSATLSTVIATVASSPAGYKTASPPGPPPYGKRAPSPGAYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASGPPLSATQIKQEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL 1190 O35126 Atrophin-1 Atn1 10090 None SL-0198 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}. UNIPROT O35126 UNIPROT P70200 UNIPROT Q80YQ0 Pfam PF03154 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}. GO:0070161 GO:0031252 GO:0005737 GO:0016363 GO:0005654 GO:0005634 GO:0048471 GO:0008432 GO:0019904 GO:0003713 GO:0003714 GO:0001906 GO:0016477 GO:0008340 GO:0030011 GO:0008584 GO:0035264 GO:0000122 GO:0051402 GO:0009791 GO:0045664 GO:0032094 GO:0007283 Unknown UniProt Sequence Analysis MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARIEEPSAPKASKQGRSEEISESESEETSAPKKTKTEQELPRPQSPSDLDSLDGRSINDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPPPPDSTPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHPQLYPGNASGGVLSGPPMGPKGGAAASSVGAPSGGKQHPPPTTPIPISSSGASGAPPAKPPSAPVGGGSLPSAPPPASFPHVTPNLPPPPALRPLNNASASPPGMGAQPIPGHLPSPHAMGQGMSGLPPGPEKGPTLAPSPHPLPPASSSAPGPPMRYPYSSSSSSAAASSSSSSSSASQYPASQALPSYPHSFPPPTSMSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANNNTHPGPFPPTGGQSTAHPAAPTHHHHQQQPQQQHHHGNSGPPPPGAYPHPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPPHGQVSYNQAGPNGPPVSSSNSSGSSSQASYSCSHPSSSQGPQGASYPFPPVPPVTTSSATLSTVIATVASSPAGYKTASPPGPPQYSKRAPSPGSYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTGPPLTATQIKQEPAEEYEPPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL 1175 Q5IS70 Atrophin-1 ATN1 9598 None SL-0198 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}. UNIPROT Q5IS70 Pfam PF03154 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}. GO:0070161 GO:0005634 GO:0048471 GO:0003714 Unknown UniProt Sequence Analysis MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEEASTPKVNKQGRSEEISESESEETNAPKKTKTEELPRPQSPSDLDSLDGRSLNDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPQPPDSTPRQPEASFEPHPSVTPTGYHAPMEPPTSRMFQAPPGAPPPHPQLYPGGTGGVLSGPPMGPKGGGAASSVGGPNGGKQHPPPTTPISVSSSGASGAPPTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLNNASASPPGLGAQPLPGHLPSPHAMGQGMGGLPPGPEKGPTLAPSPHSLPPASSSAPAPPMRFPYSSSSSSSAAASSSSSSSSSSASPFPASQALPSYPHSFPPPTSLSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANSNAHPGPFPPSTGAQSTAHPPVSTHHHHHQQQQQQQQQQQQQQQQHHGNSGPPPPGAFPHPLEGGSSHHAHPYAMSPSLGSLRPYPPGPAHLPPPHSQVSYSQAGPNGPPVSSSSNSSSSTSQGSYPCSHPSPSQGPQGAPYPFPPVPTVTTSSATLSTVIATVASSPAGYKTASPPGPPPYGKRAPSPGAYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASGPPLSATQIKQEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL 1186 P54258 Atrophin-1 Atn1 10116 None SL-0198 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}. UNIPROT P54258 Pfam PF03154 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}. Q6GMN2 EBI-6997460 0.40 Q9BYV2 EBI-21999534 0.35 GO:0070161 GO:0031252 GO:0005737 GO:0016363 GO:0005634 GO:0048471 GO:0008432 GO:0019904 GO:0090729 GO:0003713 GO:0003714 GO:0001906 GO:0016477 GO:0008340 GO:0030011 GO:0008584 GO:0035264 GO:0045892 GO:0000122 GO:0051402 GO:0045893 GO:0009791 GO:0045664 GO:0032094 GO:0007283 GO:0009404 Unknown UniProt Sequence Analysis MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEETSTPKANKQGRSEEISESESEETSAPKKTKTEELPRPQSPSDLDSLDGRSINDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPPPPDSIPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPPHPQLYPGSAGGGVLSGPPMGPKGGAAASSVGPPSGGKQHPPPTTPIPISSSGASGAPPAKPPNTPVGAGNLPSAPPPATFPHVTPNLPPPPALRPLNNASASPPGMGAQPIPGHLPSPHAMGQGMSGLPPGPEKGPTLAPSPHPLPPASSSAPGPPMRYPYSSCSSSSVAASSSSSAATSQYPASQTLPSYPHSFPPPTSMSVSNQPPKYTQPSLPSQAVWSQGPPPPPPPYGRLLPNNNTHPGPFPPTGGQSTAHPPAPAHHHHQQQQQPQPQPQPQQHHHGNSGPPPPGAYPHPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPSHGQVSYSQAGPNGPPVSSSSNSSGSSSQAAYSCSHPSSSQGPQGASYPFPPVPPITTSSATLSTVIATVASSPAGYKTASPPGPPQYSKRAPSPGSYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTGPPLTATQIKQEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL 1183 Q2TBW0 Ataxin-10 ATXN10 9913 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q2TBW0 Pfam PF09759 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}. GO:0048471 Unknown UniProt Sequence Analysis MAAPRPPPGRLSGVMMPAPIQDLEALRALTALFKEQRNRDTAPRTIFQRVLDILKKSSHAVELACRDPSQVEHLASSLQLITECFRCLRNACIECSVNQNSIRNLGTIGVAVDLILLFRELRVEQDSLLTAFRCGLQFLGNIASRNEDSQSVVWMHAFPELFLSCLNHPDRKIVAYSSMILFTSLNSERMKELEENLNIAIDVVEAHQKQPESEWPFLIITDHFLKSPELVKAMYAKMSNQERVTLLDLMIAKIVGDEPLTKDDAPVFLSHAELIASTFVDQCKIVLKLTSEQHTDDEEALATIRLLDVLCEKTANTDLLGYLQVFPGLLERVIDLLRLIHVAGNDSTNIFSACASIKADGDVSSVAEGFKSHLIRLIGNLCYKNKDNQDKVNELDGIPLILDSCGLDDSNPFLTQWVVYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKMGFEVEKRGDKLILKSTSDTPQL 475 Q9UBB4 Ataxin-10 ATXN10 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:16498633}. UNIPROT Q9UBB4 UNIPROT A6NLC4 UNIPROT B4DG05 UNIPROT O14998 UNIPROT O15009 UNIPROT Q6I9X4 Pfam PF09759 OMIM 603516 OMIM 611150 DisGeNET 25814 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}. 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}. P00533 EBI-702075 0.35 Q14693 EBI-25917615 0.56 Q15049 EBI-25917631 0.56 Q99IB8 EBI-11613941 0.35 O75365 EBI-1060045 0.00 Q9Y5J5 EBI-1060584 0.00 Q9BUV8 EBI-1061278 0.00 P43360 EBI-1067847 0.00 Q13418 EBI-1068425 0.00 Q9Y6J8 EBI-1071021 0.00 P35613 EBI-1071495 0.00 Q9Y5V3 EBI-1075883 0.00 Q92956 EBI-1076016 0.00 Q99623 EBI-1079000 0.00 Q9Y2Q3 EBI-1079777 0.00 Q9P2S5 EBI-1079870 0.00 O00422 EBI-1083812 0.00 P48059 EBI-5660392 0.00 P05919 EBI-6175288 0.46 Q77M19 EBI-6270503 0.35 Q13618 EBI-21329068 0.35 P04792 EBI-6870186 0.37 Q16666 EBI-9995438 0.35 Q9Z1B5 EBI-10996176 0.35 Q8BFY9 EBI-11018381 0.35 P49459 EBI-11040518 0.35 P83887 EBI-11057297 0.35 Q9D1H7 EBI-11064973 0.35 P01106 EBI-11105437 0.67 Q13751 EBI-11135011 0.35 Q9BQE3 EBI-11139064 0.35 Q6ZU80 EBI-11370150 0.27 Q96NL6 EBI-11376636 0.27 O94986 EBI-11381405 0.27 Q5TB80 EBI-11385924 0.27 Q9HC77 EBI-11397411 0.27 Q9WMX2 EBI-11513409 0.35 P27105 EBI-12452286 0.51 P03452 EBI-12577294 0.35 P03485 EBI-12577388 0.35 P06821 EBI-12577493 0.35 P03468 EBI-12577881 0.35 Q6DPW5 EBI-12582145 0.35 I6T1Z2 EBI-12581941 0.35 C5E519 EBI-12583021 0.35 C5E526 EBI-12584981 0.35 C5E527 EBI-12585279 0.35 Q20MH8 EBI-12586007 0.35 Q8IWL3 EBI-13943458 0.35 F5HFG5 EBI-14063444 0.35 P11142 EBI-16794405 0.42 P09622 EBI-20304669 0.35 P46013 EBI-20562326 0.35 P50406 EBI-20809027 0.37 P35408 EBI-20811409 0.37 Q5S007 EBI-21360986 0.35 P05067 EBI-21132308 0.35 Q9NRI5 EBI-21376713 0.00 P0DOF2 EBI-25603126 0.35 Q969R5 EBI-25480413 0.35 P69479 EBI-25568051 0.35 Q9C0B5 EBI-25636144 0.35 P19739 EBI-25685423 0.35 Q5EP34 EBI-25773054 0.35 P63010 EBI-25917448 0.56 O75925 EBI-25917565 0.56 Q9BZZ5 EBI-25917557 0.56 Q9UNS2 EBI-25917549 0.56 Q96E88 EBI-25917541 0.56 Q13772 EBI-25917531 0.56 Q9UNY5 EBI-25917523 0.56 Q16611 EBI-25917456 0.56 Q04724 EBI-25917507 0.56 O14974 EBI-25917499 0.56 P55198 EBI-25917481 0.56 P61978 EBI-25917473 0.56 P29017 EBI-25917464 0.56 P08670 EBI-25917515 0.56 Q12891 EBI-25917573 0.56 Q6NX45 EBI-25917763 0.56 Q7Z7K6 EBI-25917755 0.56 Q8N6K7 EBI-25917747 0.56 Q96KN4 EBI-25917739 0.56 Q2TBE0 EBI-25917729 0.56 Q8IYU4 EBI-25917719 0.56 Q71DI3 EBI-25917711 0.56 Q8IUW3 EBI-25917703 0.56 Q8WVJ9 EBI-25917695 0.56 Q8NHS9 EBI-25917687 0.56 Q9GZS3 EBI-25917679 0.56 Q9H347 EBI-25917671 0.56 Q9UHD9 EBI-25917663 0.56 Q5T6S3 EBI-25917655 0.56 Q9BR01 EBI-25917647 0.56 Q9Y2L8 EBI-25917639 0.56 Q14689 EBI-25917623 0.56 Q9BVJ6 EBI-25917607 0.56 O95391 EBI-25917599 0.56 O94851 EBI-25917591 0.56 Q9UJX2 EBI-25917581 0.56 Q8NCK7 EBI-27103180 0.35 Q8NCE2 EBI-27113554 0.35 P23771 EBI-29000509 0.35 GO:0005737 GO:0005829 GO:0030425 GO:0005615 GO:0016020 GO:0043025 GO:0048471 GO:0005886 GO:0060271 GO:0007399 GO:0031175 Unknown UniProt Sequence Analysis MAAPRPPPARLSGVMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSSHAVELACRDPSQVENLASSLQLITECFRCLRNACIECSVNQNSIRNLDTIGVAVDLILLFRELRVEQESLLTAFRCGLQFLGNIASRNEDSQSIVWVHAFPELFLSCLNHPDKKIVAYSSMILFTSLNHERMKELEENLNIAIDVIDAYQKHPESEWPFLIITDLFLKSPELVQAMFPKLNNQERVTLLDLMIAKITSDEPLTKDDIPVFLRHAELIASTFVDQCKTVLKLASEEPPDDEEALATIRLLDVLCEMTVNTELLGYLQVFPGLLERVIDLLRVIHVAGKETTNIFSNCGCVRAEGDISNVANGFKSHLIRLIGNLCYKNKDNQDKVNELDGIPLILDNCNISDSNPFLTQWVIYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKVGFEVEKKGEKLILKSTRDTPKP 475 Q4R4Y2 Ataxin-10 ATXN10 9541 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q4R4Y2 Pfam PF09759 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}. GO:0048471 Unknown UniProt Sequence Analysis MAAPRPPPARLSGIMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSSHAVELACRDPSQVENLASSLQLITECFRCLRNACIECSVNQNSIRNLDTIGVAVDLILLFRELRVEQEALLTAFRCGLQFLGNIASRNEDSQSIVWVHAFPELFLSCLNHPDKKIVAYSSMILFTSLNHERMKELEENLNIAIDVIDAYQKHPESEWPVLIITDLFLKSPELVQAMFPKLNNQERVTLLDLMIAKITSDEPLTTDDIPVFLRHAELIASTFVDQCKTVLKLASEEPPDDEEALATIRLLDVLCEMTANTELLGYLQVFPGLLERVIDLLRVIHVTGKETTNIFSNCGCVRAEGDISNVAEGFKSHLIRLIGNLCYKNKDNQDKVNELDGIPLILDNCNISDSNPFLTQWVIYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKVGFEVEKKGEKLILKSTRDTPKP 475 P28658 Ataxin-10 Atxn10 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT P28658 UNIPROT Q543S3 UNIPROT Q99LP5 UNIPROT Q9D1I1 Pfam PF09759 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}. Q8BP00 EBI-4283417 0.50 Q8CG73 EBI-4284701 0.35 Q83B01 EBI-21287600 0.37 Q83A33 EBI-21288114 0.37 Q83A11 EBI-21288333 0.37 Q6P1J9 EBI-20729673 0.35 GO:0005737 GO:0005829 GO:0030425 GO:0043025 GO:0048471 GO:0005886 GO:0019899 GO:0042802 GO:0060271 GO:0007399 GO:0031175 Unknown UniProt Sequence Analysis MAAPRMPPSRLSGIMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSTHAVELACRDPSQVEHLASSLQLITECFRCLRNACIECSVNQNSIRNLDTIGVAVDLVLLFRELRVEQDSLLTAFRCGLQFLGNVASRNEESQSIVWVHAFPELFMSCLNHPDKKIVAYCSMILFTSLNAERMKDLEENLNIAINVIEAHQKHPASEWPFLIISDHFLKSPELVEAMYGKLSNQERITLLDIVIAKLVGEEQLTKDDISIFVRHAELIANSFMDQCRNVLKLTSEPHTEDKEALVTIRLLDVLCEMTSNTELLGYLQVFPGLMERVIDVLRVIHEVGKESTNIFSPSDSLKAEGDIEHMTEGFKSHLIRLIGNLCYKNKENQDKVNELDGIPLILDSSNIDDNNPFMMQWVVYAVRNLTEDNSQNQDVIAKMEEQGLADASLLKKMGFEIEKSGDKLILKSNNDIPPP 475 Q5RE06 Ataxin-10 ATXN10 9601 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5RE06 Pfam PF09759 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}. GO:0048471 Unknown UniProt Sequence Analysis MAAPRLPPARALSGVMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSSHAVELACRDPSQVENLASSLQLITECFRCLRNACIECSVNQNSIRNLDAIGVAVDLILLFRELRVEQESLLTAFRCGLQFLGNIASRNEDSQSIVWVHAFPELFLSCLNHPDKKIVAYSSMILFTSLNHERMKELEENLNIAIDVIDAYQKHPESEWPFLIITDLFLKSPELVQAMFPKLNNQERVTLLDLMIAKITSDEPLTKDDIPVFLRHAELIASTFVDQCKTVLKLASEEPPDDEEALATIRLLDVLCEMTVNTELLGYLQVFPGLLERVIDLLRVIHVAGKETTNIFSNCGCVRAEGDISNVAEGFKSHLIRLIGNLCYKNKDNQDKVNELDGIPLILDNCNISDSNPFLTQWVIYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKVGFEVEKKGEKLILKSTRDTPKP 476 Q9ER24 Ataxin-10 Atxn10 10116 None SL-0198 Cytoplasm {ECO:0000269|PubMed:15201271}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q9ER24 Pfam PF09759 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}. Q969Q1 EBI-21997483 0.35 P35968 EBI-22252817 0.35 Q92835 EBI-22260778 0.35 P42681 EBI-22265546 0.35 GO:0005737 GO:0005829 GO:0030425 GO:0043025 GO:0048471 GO:0019899 GO:0042802 GO:0060271 GO:0007399 GO:0031175 Unknown UniProt Sequence Analysis MAAPRMPPSRLSGIMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSTQAVELACRDPSQVEHLASSLQLITECFRCLRNACIECSVNQNSIRNLDTIGVAVDLVLLFRELRVEQDSLLTAFRCGLQFLGNVASRNEDSQSIVWVHAFPELFMSCLNHPDKKIVAYCSMILFTSLNSERMKDLEENLNIAINVIEAHQKHPESEWPFLIITDHFLKSPELVEAMYGKLSNQERVTLLDIMIAKIVGDEQLTKDDISIFLRHAELIANSFVDQCRNVLKLTSEPQTEDKEALVTIRLLDVLCEMTSNTELLGYLQVFPGLMERVIDVLRVIHSVGKDSTNIFSPSDSLKAEGDIEHMTEGFKSHLIRLIGNLCYKNKENQDKVNELDGIPLILDSSNIDDNNPFMMQWVVYAVRNLTEDNSQNQDFIAKMEEQGLADASLLKKMGFEVEKSGDKLILKSNNDIPPP 475 Q5FVB0 Ataxin-10 atxn10 8364 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5FVB0 Pfam PF09759 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}. GO:0005829 GO:0048471 GO:0031175 Unknown UniProt Sequence Analysis MAAPVERLAGVCAELEQWLGEESGQRNDWAEGEGIVWRLSELFREAQYRELAEPRIFRLILQILSRVSCEIKVATLPAGAFTDTHCQLPAECFRCLRNACVQCASNQDSVRNVGLIEESVRLIQIFGAPHVLQEPALVAFRCGLQFLGNTAAGNRDSQNAVWACAFPDLFLSCLVHDDEKVVTYSSMVLFTCINREKVSTLQDPSKLDVALSVVTAYSKYPDAEWMYLIVMDHFLLCPDLVKAVYLSQSSPERVTLLELILGKISQKEPLSAEESEALQAIAAFLSDCFQTQCKTILKLTSPSACDEEEPIVVTRLLDILCEVTSKNEHLSCLQTCPGLLEAAVDILRLTHLAGKQSMNVFTAAHTMSMGQDLTHAAVGFKAHLIRLIGNLCYQNKENQEKVYQLDGIALILDNCSIDDNNPFLNQWAVFAIRNLTENNDKNQELIASMERQGLADSSLLKSMGLQAEERDGKLLLKSVKKSPAL 485 Q9C5X4 Histone ATX1 3702 None SL-0198 [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}. UNIPROT Q9C5X4 UNIPROT Q84WP4 UNIPROT Q9SIP3 Pfam PF05965 Pfam PF05964 Pfam PF09465 Pfam PF00855 Pfam PF00856 PROSITE PS51805 PROSITE PS51543 PROSITE PS51542 PROSITE PS50868 PROSITE PS50812 PROSITE PS50280 PROSITE PS50081 PROSITE PS01359 PROSITE PS50016 [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}. GO:0000785 GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0048188 GO:0003682 GO:0018024 GO:0046872 GO:0010314 GO:0008276 GO:0000976 GO:0009738 GO:0030036 GO:0051568 GO:0080182 GO:0009910 GO:0018022 GO:1904961 GO:0006355 GO:0009909 GO:0040029 GO:2000023 GO:2000280 GO:2000067 GO:0090333 GO:0006357 GO:0009414 GO:0010093 GO:0010228 Unknown UniProt Sequence Analysis MACFSNETQIEIDVHDLVEAPIRYDSIESIYSIPSSALCCVNAVGSHSLMSKKVKAQKLPMIEQFEIEGSGVSASDDCCRSDDYKLRIQRPEIVRVYYRRRKRPLRECLLDQAVAVKTESVELDEIDCFEEKKRRKIGNCELVKSGMESIGLRRCKENNAFSGNKQNGSSRRKGSSSKNQDKATLASRSAKKWVRLSYDGVDPTSFIGLQCKVFWPLDALWYEGSIVGYSAERKRYTVKYRDGCDEDIVFDREMIKFLVSREEMELLHLKFCTSNVTVDGRDYDEMVVLAATLDECQDFEPGDIVWAKLAGHAMWPAVIVDESIIGERKGLNNKVSGGGSLLVQFFGTHDFARIKVKQAISFIKGLLSPSHLKCKQPRFEEGMQEAKMYLKAHRLPERMSQLQKGADSVDSDMANSTEEGNSGGDLLNDGEVWLRPTEHVDFRHIIGDLLIINLGKVVTDSQFFKDENHIWPEGYTAMRKFTSLTDHSASALYKMEVLRDAETKTHPLFIVTADSGEQFKGPTPSACWNKIYNRIKKVQNSDSPNILGEELNGSGTDMFGLSNPEVIKLVQDLSKSRPSSHVSMCKNSLGRHQNQPTGYRPVRVDWKDLDKCNVCHMDEEYENNLFLQCDKCRMMVHAKCYGELEPCDGALWLCNLCRPGAPDMPPRCCLCPVVGGAMKPTTDGRWAHLACAIWIPETCLSDVKKMEPIDGVNKVSKDRWKLMCTICGVSYGACIQCSNNSCRVAYHPLCARAAGLCVELENDMSVEGEEADQCIRMLSFCKRHRQTSTACLGSEDRIKSATHKTSEYLPPPNPSGCARTEPYNCFGRRGRKEPEALAAASSKRLFVENQPYVIGGYSRLEFSTYKSIHGSKVSQMNTPSNILSMAEKYRYMRETYRKRLAFGKSGIHGFGIFAKLPHRAGDMMIEYTGELVRPSIADKREQLIYNSMVGAGTYMFRIDDERVIDATRTGSIAHLINHSCVPNCYSRVITVNGDEHIIIFAKRHIPKWEELTYDYRFFSIGERLSCSCGFPGCRGVVNDTEAEEQHAKICVPRCDLIDWTAE 1062 Q9M077 Serine/threonine-protein AUR1 3702 None SL-0178 SL-0182 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. UNIPROT Q9M077 UNIPROT Q8LBX4 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0009504 GO:0032133 GO:0005874 GO:0031965 GO:0005730 GO:0005634 GO:0009524 GO:0005819 GO:0005876 GO:0051233 GO:0000922 GO:0005524 GO:0035175 GO:0035174 GO:0106310 GO:0004674 GO:0051301 GO:0007052 GO:0006468 GO:0032465 Unknown UniProt Sequence Analysis MAIPTETQHQEKEASDASAAAAQKRWTLSDFDIGKPLGRGKFGHVYLAREKRSNHVVALKVLFKSQLQQSQVEHQLRREVEIQSHLRHPNILRLYGYFYDQKRVYLILEYAARGELYKDLQKCKYFSERRAATYVASLARALIYCHGKHVIHRDIKPENLLIGAQGELKIADFGWSVHTFNRRRTMCGTLDYLPPEMVESVEHDASVDIWSLGILCYEFLYGVPPFEAMEHSDTYRRIVQVDLKFPPKPIISASAKDLISQMLVKESSQRLPLHKLLEHPWIVQNADPSGIYRV 294 Q683C9 Serine/threonine-protein AUR2 3702 None SL-0178 SL-0182 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. UNIPROT Q683C9 UNIPROT O82309 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. O23160 EBI-25517190 0.56 Q9SSA8 EBI-25519383 0.56 GO:0032133 GO:0005737 GO:0031965 GO:0005634 GO:0005876 GO:0051233 GO:0000922 GO:0005524 GO:0035175 GO:0035174 GO:0106310 GO:0007052 GO:0006468 GO:0032465 Unknown UniProt Sequence Analysis MLYQAASEAAQKRWTTSDFDIGKPLGRGKFGHVYLAREKRSDHIVALKVLFKAQLQQSQVEHQLRREVEIQSHLRHPNILRLYGYFYDQKRVYLILEYAVRGELYKELQKCKYFSERRAATYVASLARALIYCHGKHVIHRDIKPENLLIGAQGELKIADFGWSVHTFNRRRTMCGTLDYLPPEMVESVEHDASVDIWSLGILCYEFLYGVPPFEAREHSETYKRIVQVDLKFPPKPIVSSSAKDLISQMLVKESTQRLALHKLLEHPWIVQNADPSGLYRG 282 O64629 Serine/threonine-protein AUR3 3702 None SL-0198 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}. UNIPROT O64629 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0032133 GO:0000775 GO:0005634 GO:0048471 GO:0005819 GO:0005876 GO:0051233 GO:0005524 GO:0035175 GO:0044022 GO:0035174 GO:0106310 GO:0007059 GO:0007052 GO:0016310 GO:0006468 GO:0032465 Unknown UniProt Sequence Analysis MSKKSTESDAGNTEKQWSLADFEIGRPLGKGKFGRVYLAREAKSKYIVALKVIFKEQIEKYKIHHQLRREMEIQTSLRHPNILRLFGWFHDNERIFLILEYAHGGELYGVLKQNGHLTEQQAATYIASLSQALAYCHGKCVIHRDIKPENLLLDHEGRLKIADFGWSVQSSNKRKTMCGTLDYLAPEMVENRDHDYAVDNWTLGILCYEFLYGNPPFEAESQKDTFKRILKIDLSFPLTPNVSEEAKNLISQLLVKDPSKRLSIEKIMQHPWIVKNADPKGVCASIDI 288 P14975 Protein AV2 10818 None SL-0382 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}. UNIPROT P14975 Pfam PF01524 Pfam PF03716 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}. GO:0044220 GO:0019048 GO:0060967 Unknown UniProt Sequence Analysis MWDPLVNEFPDSVHGLRCMLAIKYLQALEDTYEPSTLGHELVRDLVSVIRARNYVEATRRYHHFHSRIQGSSKTELRQPIQEPCYCPHCPRHKSKTGLGEQAHVQKAHDVQDV 113 P14967 Uncharacterized AV2 222073 None SL-0382 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}. UNIPROT P14967 Pfam PF01524 Pfam PF03716 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}. GO:0044220 GO:0019048 GO:0060967 Unknown UniProt Sequence Analysis MWDPLVNEFPDSVHGLRCMLAIKYLQALEDTYEPSTLGHDLVRDLISVIRARNYVEATRRYHHFHSRLEGSSKAELRQPIQEPCYCPHCPRHKSKTGLDEQAHVQKAHDVQDV 113 Q08593 Protein AV2 31600 None SL-0382 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}. UNIPROT Q08593 Pfam PF01524 Pfam PF03716 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}. GO:0044220 GO:0019048 GO:0060967 Unknown UniProt Sequence Analysis MWDPLLNEFPESVHGFRCMLAVKYLQLVECTYSPDTLGYDLIRDLFSVIRAKNYVEATSRYHNFYSRLEGSSPSELRQPIQQPCGCPYCPRHKKTILDKQTHQSEAQVVSDV 112 Q9YPS6 Protein AV2 223295 None SL-0382 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}. UNIPROT Q9YPS6 Pfam PF01524 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}. GO:0044220 GO:0019048 GO:0060967 Unknown UniProt Sequence Analysis MWDPLVNDFPKSLHGFRCMLAIKYLQYIQENYPSNSLGFVYLTELIQVLRIRKHAKAELRYRLLYPDVECAEEADLRHPAFLTCHCGKCPCQREKEEVDQPTHVEETEILSVIPLS 116 P36282 Protein V2 223353 None SL-0382 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}. UNIPROT P36282 Pfam PF01524 Pfam PF03716 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}. GO:0044220 GO:0019048 GO:0060967 Unknown UniProt Sequence Analysis MWDPLVHEFPETVHGFRCMLANKYLLAVESKYAPDTLGYELIRDCIGVVRSRNYEQATSRYRDIYTRLQGATEAELQQSVQERCCCPHCPRHKKADMGESAHVQKAHDVQAVQKP 115 P61512 Protein V2 37139 None SL-0382 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}. UNIPROT P61512 UNIPROT P27270 Pfam PF01524 Pfam PF03716 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}. GO:0044220 GO:0019048 GO:0060967 Unknown UniProt Sequence Analysis MWDPLLNEFPDSVHGLRCMLAIKYLQLVEETYEPNTLGHDLIRDLISVIRARDYAEANRRYTNFNARLEGSSKTELRQPVYQPCCCPHCPRHQASIMDLQAHVSKAADVQNVQKP 115 Q67616 Protein V2 221538 None SL-0382 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}. UNIPROT Q67616 Pfam PF01524 Pfam PF03716 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}. GO:0044220 GO:0019048 GO:0060967 Unknown UniProt Sequence Analysis MWDPLLNEFPDSVHGLRCMLAIKYLQLVEETYEPNTLGHDLIRDLISVIRARDYAEANRRYTNVKPALEVSSKTELRQPVYQPCCCPHCPRHQASIMDLQAHVSKAADVQNVQKP 115 P61511 Protein V2 123735 None SL-0382 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}. UNIPROT P61511 UNIPROT P27270 Pfam PF01524 Pfam PF03716 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}. GO:0044220 GO:0019048 GO:0060967 Unknown UniProt Sequence Analysis MWDPLLNEFPDSVHGLRCMLAIKYLQLVEETYEPNTLGHDLIRDLISVIRARDYAEANRRYTNFNARLEGSSKTELRQPVYQPCCCPHCPRHQASIMDLQAHVSKAADVQNVQKP 115 Q9DXE9 Protein V2 185793 None SL-0382 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}. UNIPROT Q9DXE9 Pfam PF01524 Pfam PF03716 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}. GO:0044220 GO:0019048 GO:0060967 Unknown UniProt Sequence Analysis MWDPLLNEFPETVHGFRCMLAIKYLQLVENTYSPDTLGYDLIRDLISVIRARDYGETSRRYCHFHSRLEGASPAELRQPLYGSCCCPHCPRHQKTNVVKQAHVPEAHDVPDVQKP 115 P27269 Protein V2 66366 None SL-0382 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. UNIPROT P27269 Pfam PF01524 Pfam PF03716 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}. GO:0044220 GO:0019048 GO:0060967 Unknown UniProt Sequence Analysis MWDPLLNEFPESVHGFRCMLAIKYLQSVEETYEPNTLGHDLIRDLISVVRARDYVEATRRYNHFHARLEGSPKAELRQPIQQPCCCPHCPRHKQATIMDVQAHVPKAQNIQNVSKP 116 Q96A70 Antizyme AZIN2 9606 None SL-0198 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}. UNIPROT Q96A70 UNIPROT B2RDU5 UNIPROT D3DPQ9 UNIPROT Q5TIF4 UNIPROT Q5TIF5 UNIPROT Q5TIF6 UNIPROT Q8TF56 UNIPROT Q96L54 UNIPROT Q96L55 UNIPROT Q96L56 UNIPROT Q96L57 UNIPROT Q96MD9 Pfam PF02784 Pfam PF00278 PROSITE PS00878 PROSITE PS00879 OMIM 608353 DisGeNET 113451 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}. Q9UMX2 EBI-10281607 0.56 Q9NZC9 EBI-21811703 0.35 Q96FC9 EBI-21811703 0.35 Q8ND04 EBI-21811703 0.35 Q5T3J3 EBI-21811703 0.35 Q16890 EBI-21811703 0.35 P78395 EBI-21811703 0.35 P57737 EBI-21811703 0.35 P54368 EBI-21811703 0.35 O95190 EBI-21811703 0.35 GO:0030424 GO:0005801 GO:0005737 GO:0031410 GO:0005829 GO:0030425 GO:0033116 GO:1990005 GO:0005739 GO:0005634 GO:0043204 GO:0048471 GO:0005802 GO:0030133 GO:0008792 GO:0042978 GO:0097055 GO:0042177 GO:0043085 GO:1902269 GO:0033387 GO:0007283 GO:0098629 Unknown UniProt Sequence Analysis MAGYLSESDFVMVEEGFSTRDLLKELTLGASQATTDEVAAFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEGAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQPGREEENGSTSKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQACHITYAMSRVAWEALRRQLMAAEQEDDVEGVCKPLSCGWEITDTLCVGPVFTPASIM 460 Q8BVM4 Antizyme Azin2 10090 None SL-0198 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}. UNIPROT Q8BVM4 UNIPROT A2A823 Pfam PF02784 Pfam PF00278 PROSITE PS00879 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}. Q9R109 EBI-9656867 0.59 P54369 EBI-9660716 0.40 O08608 EBI-9660680 0.40 GO:0030424 GO:0005801 GO:0005737 GO:0031410 GO:0005829 GO:0030425 GO:0033116 GO:1990005 GO:0005739 GO:0005634 GO:0043204 GO:0048471 GO:0005802 GO:0030133 GO:0003824 GO:0042978 GO:0042177 GO:0006591 GO:0043085 GO:1902269 GO:0033387 GO:0098629 Unknown UniProt Sequence Analysis MAGYLSESDFVMVEEGFSTRDLLEELTLGASQATSGKVAAFFVADLGAVVRKHFCFLKHLPRVRPFYAVGCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQVAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKMVLCIATQDSHSLNHLSLRFGASLKSCRHLLENAKKSHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFQMGEELGHTMNILDLGGGFPGLEGAKVRFEEMASVINSALDLYFPEGCGVDILAELGRYYVTSAFTVAVSIVAKREVLDQASREEQTGAAPKSIVYYLDEGVYGVFNSVLFDNTCPTPALQKKPSADQPLYSSSLWGPAVEGCDCVAEGLWLPQLQVGDWLVFDNMGAYTVDTKSLLGGTQARRVTYAMSRLAWEALRGQLLPAEEDQDAEGVCKPLSCGWEITDTLCVGPVFTPASIM 459 D4A693 Antizyme Azin2 10116 None SL-0198 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}. UNIPROT D4A693 Pfam PF02784 Pfam PF00278 PROSITE PS00879 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}. GO:0030424 GO:0005801 GO:0005737 GO:0031410 GO:0030425 GO:0033116 GO:1990005 GO:0005739 GO:0005634 GO:0043204 GO:0048471 GO:0005802 GO:0030133 GO:0003824 GO:0042978 GO:0042177 GO:0006591 GO:0043085 GO:1902269 GO:0033387 GO:0050790 GO:0098629 Unknown UniProt Sequence Analysis MAGYLSESDFVMVEEGFSTRDLLEELTLGASQATTGKVAAFFVADAVVRKHFCFLKYLPRVRPFYAVRCNSSLGVLKVLAELGLGFSCASKAEMELVQHIGVPASKIICANPCKQVAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKSWGEVLTLDALGLHHTHRRVGCSLMFQASVIASVAQGYLELVCQPFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPGLEGAKVRFEEVTSVIGKNIPFYTPPPCHVPLRTHATKKMTSSDFCCRVHVTAKEKPLFSPFLTEQTGAAPKSIVYHLDEGVYGVFNSVLFDNTCPTPALQKKPSADQPLYSSSLWGPAVDGCDCVAEGLWLPQLQVGDWLVFDNMGAYTVDTKSLLGGTQACRVTYAMSRLAWEALQGQLLPAEEDQDAEGVCKPLSCGWEITDSLCVGPVFTPASIM 457 Q9I8S4 Antizyme azin2 8355 None SL-0198 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}. UNIPROT Q9I8S4 Pfam PF02784 Pfam PF00278 PROSITE PS00878 PROSITE PS00879 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}. GO:0030424 GO:0005801 GO:0005737 GO:0031410 GO:0030425 GO:0033116 GO:1990005 GO:0005634 GO:0043204 GO:0048471 GO:0005802 GO:0030133 GO:0016831 GO:0042978 GO:0006596 GO:0043085 GO:1902269 GO:0098629 Unknown UniProt Sequence Analysis MQGYIQESDFNLVEEGFLARDLMEEIINEVSQTEDRDAFFVADLGDVVRKHLRFLKALPRVKPFYAVKCNSSKGVVKILAELGAGFDCASKTEIELVQDVGVAPERIIYANPCKQISQIKYAAKNGVQMMTFDNEVELSKVSRSHPNARMVLRIATDDSKSSARLSVKFGAPLKSCRRLLEMAKNLSVDVIGVSFHVGSGCTDSKAYTQAISDARLVFEMASEFGYKMWLLDIGGGFPGTEDSKIRFEEIAGVINPALDMYFPESSDVQIIAEPGRYYVASAFSLAVNVIAKKEVEHSVSDDEENESSKSIMYYVNDGVYGSFNCLVFDHAHPKPILHKKPSPDQPLYTSSLWGPTCDGLDQIAERVQLPELHVGDWLLFENMGAYTIAASSNFNGFQQSPVHYAMPRAAWKAVQLLQRGLQQTEEKENVCTPMSCGWEISDSLCFTRTFAATSII 456 Q07816 Bcl-2-like BCL2L1 9031 None SL-0178 SL-0182 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}. UNIPROT Q07816 UNIPROT Q98908 Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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}. GO:0070161 GO:0097136 GO:0005813 GO:0005829 GO:0005783 GO:0016021 GO:0005759 GO:0005741 GO:0031965 GO:0030672 GO:0051434 GO:0046982 GO:0042803 GO:0019901 GO:0071839 GO:0071312 GO:0071230 GO:0071480 GO:0051607 GO:0097048 GO:0044565 GO:0035234 GO:0050673 GO:0097192 GO:0009566 GO:0007281 GO:0097284 GO:0008630 GO:0008584 GO:0070584 GO:2000669 GO:0051093 GO:1902236 GO:1900118 GO:1902042 GO:2001243 GO:1902230 GO:0043524 GO:1903077 GO:2000242 GO:0051402 GO:0001541 GO:0032946 GO:0032465 GO:0040008 GO:0046902 GO:0051881 GO:0001836 GO:0046898 GO:0034097 GO:0007283 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSSSNRELVIDFVSYKLSQRGHCWSELEEEDENRTDTAAEAEMDSVLNGSPSWHPPAGHVVNGATVHRSSLEVHEIVRASDVRQALRDAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFHDGVNWGRIVAFFSFGGALCVESVDKEMRVLVGRIVSWMTTYLTDHLDPWIQENGGWERFVDLYGNNAAAELRKGQETFNKWLLTGATVAGVLLLGSLLSRK 229 Q07817 Bcl-2-like BCL2L1 9606 None SL-0178 SL-0182 [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}. UNIPROT Q07817 UNIPROT E1P5L6 UNIPROT Q5CZ89 UNIPROT Q5TE65 UNIPROT Q92976 PDB 1BXL PDB 1G5J PDB 1LXL PDB 1MAZ PDB 1R2D PDB 1R2E PDB 1R2G PDB 1R2H PDB 1R2I PDB 1YSG PDB 1YSI PDB 1YSN PDB 2B48 PDB 2LP8 PDB 2LPC PDB 2M03 PDB 2M04 PDB 2ME8 PDB 2ME9 PDB 2MEJ PDB 2O1Y PDB 2O2M PDB 2O2N PDB 2P1L PDB 2PON PDB 2YJ1 PDB 2YQ6 PDB 2YQ7 PDB 2YXJ PDB 3CVA PDB 3FDL PDB 3FDM PDB 3INQ PDB 3IO8 PDB 3PL7 PDB 3QKD PDB 3R85 PDB 3SP7 PDB 3SPF PDB 3WIZ PDB 3ZK6 PDB 3ZLN PDB 3ZLO PDB 3ZLR PDB 4A1U PDB 4A1W PDB 4AQ3 PDB 4BPK PDB 4C52 PDB 4C5D PDB 4CIN PDB 4EHR PDB 4HNJ PDB 4IEH PDB 4PPI PDB 4QVE PDB 4QVF PDB 4QVX PDB 4TUH PDB 4Z9V PDB 5AGW PDB 5AGX PDB 5B1Z PDB 5C3G PDB 5FMJ PDB 5FMK PDB 5VAY PDB 5VX3 PDB 6BF2 PDB 6DCN PDB 6DCO PDB 6F46 PDB 6HJL PDB 6IJQ PDB 6LHD PDB 6O0K PDB 6O0L PDB 6O0M PDB 6O0O PDB 6O0P PDB 6RNU PDB 6ST2 PDB 6UVC PDB 6UVD PDB 6UVE PDB 6UVF PDB 6UVG PDB 6UVH PDB 6VWC PDB 6X7I PDB 6YLI PDB 6ZHC PDB 7CA4 PDB 7JGV PDB 7JGW PDB 7LH7 Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 OMIM 600039 DisGeNET 598 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. P00519 EBI-8488890 0.40 P10415 EBI-2126646 0.44 P10909 EBI-4322676 0.61 P30429 EBI-494146 0.40 P49810 EBI-7072489 0.54 P49768 EBI-7072509 0.37 P70444 EBI-15708450 0.44 Q92934 EBI-7986686 0.97 O54918 EBI-15616455 0.59 Q9NP97 EBI-526396 0.35 P51572 EBI-78034 0.40 P45983 EBI-7497515 0.52 Q14318 EBI-7497660 0.44 Q07817 EBI-700842 0.59 Q64373 EBI-700869 0.40 Q07812 EBI-701131 0.97 Q16611 EBI-760384 0.95 O43521 EBI-701297 0.93 O00198 EBI-701309 0.70 Q9BXH1 EBI-707945 0.86 Q91ZE9 EBI-708056 0.44 Q13323 EBI-760279 0.91 P55957 EBI-708176 0.86 Q61337 EBI-709145 0.59 Q13794 EBI-709305 0.68 P02340 EBI-728086 0.50 Q99ML1 EBI-728086 0.50 P04637 EBI-727854 0.88 P62136 EBI-1206864 0.00 P36873 EBI-1207054 0.00 Q9C000 EBI-1246322 0.65 Q14457 EBI-5234817 0.70 Q9H2V7 EBI-1386556 0.46 O15304 EBI-1393098 0.57 O35303 EBI-1767441 0.40 O00429 EBI-1767523 0.44 A0A2S9PFE9 EBI-2874931 0.00 O43889 EBI-8645414 0.37 P48558 EBI-5275391 0.40 P60709 EBI-7102779 0.37 Q3B7T1 EBI-7102826 0.37 Q86XA0 EBI-7102889 0.37 Q96N67 EBI-7102942 0.37 P09467 EBI-7102996 0.37 Q9HC38 EBI-7103053 0.37 Q6PKG0 EBI-7103101 0.37 P13667 EBI-7103233 0.37 Q8IV08 EBI-7103438 0.37 Q8NEY8 EBI-7103564 0.37 P21246 EBI-7103628 0.37 P52756 EBI-7103707 0.37 Q04724 EBI-7103774 0.37 Q13625 EBI-15723914 0.56 Q8IWV7 EBI-7103907 0.37 Q9HBF4 EBI-7103940 0.37 Q9UKY1 EBI-7104013 0.37 Q9P2Y4 EBI-7104091 0.37 Q96PU4 EBI-6051471 0.40 Q86Y07 EBI-6476114 0.50 P99999 EBI-6589621 0.27 P04049 EBI-6592472 0.27 P55211 EBI-6593000 0.27 Q96LC9 EBI-10290553 0.81 Q61699 EBI-11091301 0.35 P49286 EBI-11577578 0.00 Q7L3V2 EBI-11509563 0.46 P03496 EBI-11519828 0.37 Q20MH3 EBI-11520043 0.37 Q0A2H0 EBI-11520223 0.37 Q8NBJ4 EBI-24661651 0.56 P56557 EBI-24667028 0.56 Q9GZR5 EBI-23702709 0.56 P22749 EBI-24691348 0.56 Q7KZS0 EBI-24702746 0.56 P27469 EBI-23766185 0.56 Q9Y282 EBI-24743336 0.56 Q9H2K0 EBI-24748533 0.56 Q9H6H4 EBI-24749484 0.56 Q8IYJ2 EBI-24779286 0.56 P78317 EBI-24796078 0.56 Q7Z5B4 EBI-23915698 0.56 P0C671 EBI-24555838 0.56 Q6NTF9 EBI-24646649 0.56 Q5T7V8 EBI-25269471 0.56 P24830 EBI-16046634 0.37 P06921 EBI-16047315 0.00 P06422 EBI-16048535 0.00 P36780 EBI-16049904 0.00 P04015 EBI-16050562 0.00 P06790 EBI-16051663 0.00 P06423 EBI-16052407 0.00 P03118 EBI-16053329 0.00 P36778 EBI-16054563 0.00 Q29RF7 EBI-21755538 0.35 Q99MI6 EBI-15572392 0.56 Q8BWF2 EBI-15572411 0.56 Q99104 EBI-15666413 0.35 Q07813 EBI-15666413 0.53 Q8VDD5 EBI-15666432 0.35 P42345 EBI-15828862 0.69 P21796 EBI-15828900 0.35 Q64010 EBI-15959690 0.40 O08734 EBI-16176197 0.35 Q14790 EBI-16211903 0.40 O15530 EBI-16594603 0.35 P59637 EBI-25487800 0.40 P59635 EBI-25494122 0.40 P37840 EBI-25940857 0.56 Q9HB09 EBI-27086218 0.37 Q9H492 EBI-30828681 0.44 Q9GZQ8 EBI-30830914 0.44 O75381 EBI-30835456 0.44 GO:0070161 GO:0097136 GO:0005813 GO:0005737 GO:0005829 GO:0005783 GO:0016021 GO:0005743 GO:0005759 GO:0005741 GO:0005739 GO:0031965 GO:0097143 GO:0030672 GO:0051434 GO:0042802 GO:0046982 GO:0042803 GO:0019901 GO:0008637 GO:0071839 GO:0071312 GO:0071230 GO:0071480 GO:0051607 GO:0097048 GO:0044565 GO:0035234 GO:0006897 GO:0050673 GO:0097192 GO:0009566 GO:0007281 GO:0097284 GO:0001701 GO:0008630 GO:0008584 GO:0070584 GO:2000811 GO:0043066 GO:0010507 GO:2000669 GO:0051093 GO:1902236 GO:1900118 GO:2001240 GO:1902042 GO:2001243 GO:1902230 GO:1901029 GO:0043524 GO:1903077 GO:0090201 GO:2000242 GO:0051402 GO:0001541 GO:0032946 GO:0032465 GO:0040008 GO:0046902 GO:0051881 GO:0001836 GO:0046898 GO:0034097 GO:0007283 GO:0019050 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK 233 Q64373 Bcl-2-like Bcl2l1 10090 None SL-0178 SL-0182 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. UNIPROT Q64373 UNIPROT O35844 UNIPROT Q60657 UNIPROT Q60658 UNIPROT Q61338 PDB 1PQ0 PDB 1PQ1 PDB 2BZW PDB 3IHC PDB 3IHD PDB 3IHE PDB 3IHF PDB 3IIG PDB 3IIH PDB 3ILB PDB 3ILC PDB 4YJ4 PDB 4YK9 PDB 5C3G Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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}. Q07817 EBI-700869 0.40 Q99ML1 EBI-727813 0.35 P02340 EBI-727813 0.35 O54918 EBI-1037127 0.44 P63087 EBI-1202891 0.00 O54926 EBI-1393194 0.40 O00198 EBI-6375860 0.40 Q61337 EBI-6693214 0.40 P59637 EBI-25487713 0.40 GO:0070161 GO:0097136 GO:0005813 GO:0005905 GO:0005737 GO:0005829 GO:0005783 GO:0016021 GO:0016020 GO:0005740 GO:0005743 GO:0005759 GO:0031966 GO:0005741 GO:0005739 GO:0031965 GO:0098793 GO:0097143 GO:0030672 GO:0051400 GO:0051434 GO:0030276 GO:0043027 GO:0051020 GO:0042802 GO:0097371 GO:0046982 GO:0042803 GO:0019901 GO:0044877 GO:0006915 GO:0071839 GO:0071312 GO:0071230 GO:0071480 GO:0051607 GO:0097048 GO:0044565 GO:0035234 GO:0050673 GO:0097192 GO:0009566 GO:0007281 GO:0097284 GO:0001701 GO:0008630 GO:0008584 GO:0070584 GO:2000811 GO:0043066 GO:2000669 GO:0051093 GO:1902236 GO:1900118 GO:1902042 GO:2001243 GO:1902230 GO:1901029 GO:0043524 GO:1903077 GO:0090201 GO:2000242 GO:0051402 GO:0001541 GO:0043065 GO:2001171 GO:0032946 GO:2000809 GO:1900244 GO:2000302 GO:0042981 GO:0032465 GO:0040008 GO:1900452 GO:0046902 GO:0051881 GO:0001836 GO:0046898 GO:0034097 GO:0002931 GO:0009314 GO:0009615 GO:0007283 GO:0019050 GO:0036466 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEAERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK 233 O77737 Bcl-2-like BCL2L1 9823 None SL-0178 SL-0182 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}. UNIPROT O77737 Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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}. GO:0070161 GO:0005813 GO:0005737 GO:0005829 GO:0016021 GO:0005759 GO:0005741 GO:0031965 GO:0030672 GO:0046982 GO:0042803 GO:0006897 GO:0097192 GO:0008630 GO:1902236 GO:1900118 GO:2001243 GO:0032465 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSQSNRELVVDFLSYKLSQKGYSWSQFTDVEENRTEAPEGTESEAETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVLNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIATWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTLAGVVLLGSLFSRK 233 P53563 Bcl-2-like Bcl2l1 10116 None SL-0178 SL-0182 [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}. UNIPROT P53563 UNIPROT P70613 UNIPROT P70614 UNIPROT Q52KS0 UNIPROT Q62678 UNIPROT Q62836 UNIPROT Q64087 UNIPROT Q64128 PDB 1AF3 PDB 4QNQ Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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. O88498 EBI-79058 0.37 O35303 EBI-1767505 0.56 O35147 EBI-15693744 0.40 P08081 EBI-16062715 0.50 Q4KM98 EBI-16062732 0.35 GO:0070161 GO:0097136 GO:0005813 GO:0005737 GO:0005829 GO:0005783 GO:0016021 GO:0016020 GO:0005740 GO:0005743 GO:0005759 GO:0031966 GO:0005741 GO:0005739 GO:0031965 GO:0098793 GO:0030672 GO:0051400 GO:0051434 GO:0030276 GO:0043027 GO:0051020 GO:0042802 GO:0097371 GO:0046982 GO:0042803 GO:0019901 GO:0044877 GO:0007568 GO:0006915 GO:0071839 GO:0008283 GO:0071312 GO:0071230 GO:1905218 GO:0071320 GO:0071549 GO:0036018 GO:0071480 GO:0071456 GO:0071347 GO:1990646 GO:1904579 GO:0071356 GO:0071466 GO:0021987 GO:0051607 GO:0097048 GO:0044565 GO:0035234 GO:0006897 GO:0050673 GO:0097192 GO:0009566 GO:0007281 GO:0097284 GO:0001701 GO:0008630 GO:0008584 GO:0070584 GO:0043066 GO:2000669 GO:0051093 GO:1902236 GO:1900118 GO:1902042 GO:2001243 GO:1902230 GO:0043524 GO:1903077 GO:2000242 GO:0051402 GO:0001541 GO:0043065 GO:2001171 GO:0008284 GO:0032946 GO:2000809 GO:1900244 GO:2000302 GO:0042981 GO:0032465 GO:0040008 GO:1900452 GO:0046902 GO:0051881 GO:0001836 GO:0046898 GO:0034097 GO:0051602 GO:0036017 GO:0042542 GO:0001666 GO:0010035 GO:0002931 GO:0010288 GO:0032496 GO:0014070 GO:0010243 GO:0006979 GO:0043434 GO:0009314 GO:0009615 GO:0009410 GO:0007283 GO:0036466 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEPERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK 233 Q9HD36 Bcl-2-like BCL2L10 9606 None SL-0178 SL-0182 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}. UNIPROT Q9HD36 UNIPROT Q3SX80 UNIPROT Q52LQ9 UNIPROT Q8TCS9 PDB 4B4S Pfam PF00452 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 OMIM 606910 DisGeNET 10017 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}. Q14643 EBI-22188044 0.66 P22736 EBI-2126371 0.40 Q14790 EBI-9064052 0.37 O43521 EBI-11304337 0.78 Q07812 EBI-11304362 0.40 Q13323 EBI-11304411 0.70 Q96LC9 EBI-24617832 0.56 Q5PRF9 EBI-24664926 0.56 Q99735 EBI-23758524 0.56 Q86VY9 EBI-24795275 0.56 Q14571 EBI-22188055 0.40 Q14573 EBI-22188066 0.40 O43865 EBI-22196627 0.59 GO:0005829 GO:0005783 GO:0016021 GO:0016020 GO:0044233 GO:0005741 GO:0005739 GO:0031965 GO:0005819 GO:0005509 GO:0089720 GO:0046982 GO:0042803 GO:0006919 GO:0006915 GO:0097192 GO:0007292 GO:0008630 GO:0031023 GO:0043066 GO:2001243 GO:0007283 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVDQLRERTTMADPLRERTELLLADYLGYCAREPGTPEPAPSTPEAAVLRSAAARLRQIHRSFFSAYLGYPGNRFELVALMADSVLSDSPGPTWGRVVTLVTFAGTLLERGPLVTARWKKWGFQPRLKEQEGDVARDCQRLVALLSSRLMGQHRAWLQAQGGWDGFCHFFRTPFPLAFWRKQLVQAFLSCLLTTAFIYLWTRLL 204 Q9Z0F3 Bcl-2-like Bcl2l10 10090 None SL-0178 SL-0182 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}. UNIPROT Q9Z0F3 UNIPROT Q3ULP5 UNIPROT Q7TPY8 PDB 2KUA Pfam PF00452 PROSITE PS50062 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}. O14727 EBI-8658689 0.51 GO:0005829 GO:0005783 GO:0016021 GO:0016020 GO:0044233 GO:0005741 GO:0005739 GO:0031965 GO:0005819 GO:0005509 GO:0089720 GO:0042802 GO:0046982 GO:0042803 GO:0006915 GO:0097192 GO:0097193 GO:0008630 GO:0031023 GO:0043066 GO:2001240 GO:2001243 GO:0043065 Transmembrane UniProt Sequence Analysis {ECO:0000255} MADSQDPLHERTRRLLSDYIFFCAREPDTPEPPPTSVEAALLRSVTRQIQQEHQEFFSSFCESRGNRLELVKQMADKLLSKDQDFSWSQLVMLLAFAGTLMNQGPYMAVKQKRDLGNRVIVTRDCCLIVNFLYNLLMGRRHRARLEALGGWDGFCRFFKNPLPLGFWRRLLIQAFLSGFFATAIFFIWKRL 191 Q99M66 Bcl-2-like Bcl2l10 10116 None SL-0178 SL-0182 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}. UNIPROT Q99M66 Pfam PF00452 PROSITE PS50062 PROSITE PS01258 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}. GO:0005829 GO:0005783 GO:0016021 GO:0016020 GO:0044233 GO:0005741 GO:0005739 GO:0031965 GO:0005819 GO:0005509 GO:0089720 GO:0042802 GO:0046982 GO:0042803 GO:0006915 GO:0097192 GO:0097193 GO:0008630 GO:0031023 GO:0043066 GO:2001240 GO:2001243 GO:0048709 GO:0043065 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGDPLQDRTRRLLTDYILFCARAPNTPEPLPTSVEAALLRSVTSQIQQEHQDLFNSFRDYQGNRLELVTQMADELLSNDQEFNWGRLVMLLAFVGTLMNQDRTVKRRRDQRNRLLLERDCYLIVSLLYNRLTGRHRSWLEAHGGWDGFCQFFKNPLPPGFWRRLLIRAILSCFFATAIFYIWKCL 185 Q6NTS2 Barrier-to-autointegration banf1 8355 None SL-0178 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}. UNIPROT Q6NTS2 UNIPROT A3KNC4 Pfam PF02961 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}. GO:0000785 GO:0005635 GO:0003677 GO:0010836 GO:0006979 Unknown UniProt Sequence Analysis MSSTSQKHRDFVAEPMGEKSVQCLAGIGEALGHRLEEKGFDKAYVVLGQFLVLKKDEELFKEWLKDICSANAKQSRDCYGCLKEWCDAFL 90 Q66KV4 Barrier-to-autointegration banf1 8355 None SL-0178 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}. UNIPROT Q66KV4 Pfam PF02961 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}. B9X187 EBI-12596342 0.46 Q7ZTB4 EBI-12596356 0.40 GO:0000785 GO:0005635 GO:0003677 GO:0010836 GO:0006979 Unknown UniProt Sequence Analysis MSSTSQKHRDFVAEPMGEKSVQCLAGIGDTLGRRLEEKGFDKAYVVLGQFLVLKKDEELFKEWLKDACSANAKQSRDCYGCLKEWCDAFL 90 P61283 Barrier-to-autointegration BANF1 9913 None SL-0178 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}. UNIPROT P61283 UNIPROT Q5E9E5 Pfam PF02961 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}. GO:0000785 GO:0005737 GO:0005635 GO:0005654 GO:0003677 GO:0006325 GO:0030261 GO:0007059 GO:0007084 GO:0010836 GO:0032480 GO:0006979 Unknown UniProt Sequence Analysis MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 89 Q6P026 Barrier-to-autointegration banf1 7955 None SL-0178 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}. UNIPROT Q6P026 Pfam PF02961 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}. GO:0000785 GO:0005737 GO:0005635 GO:0005654 GO:0003677 GO:0006325 GO:0030261 GO:0007059 GO:0007084 GO:0010836 GO:0032480 GO:0006979 Unknown UniProt Sequence Analysis MSSTSQKHKDFVAEPMGEKSVMALAGIGEVLGKRLEEKGFDKAYVVLGQFLVLRKDEELFREWLKDTCGANTKQQGDCYSCLREWCDSFL 90 O75531 Barrier-to-autointegration BANF1 9606 None SL-0178 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}. UNIPROT O75531 UNIPROT O60558 UNIPROT Q6FGG7 PDB 1CI4 PDB 1QCK PDB 2BZF PDB 2EZX PDB 2EZY PDB 2EZZ PDB 2ODG PDB 6GHD PDB 6RPR PDB 6UNT PDB 6URE PDB 6URJ PDB 6URK PDB 6URL PDB 6URN PDB 6URR PDB 6URZ PDB 6US0 PDB 6US1 PDB 6US7 PDB 6USB PDB 6USD PDB 6USI PDB 7ABM PDB 7NDY Pfam PF02961 OMIM 603811 OMIM 614008 DisGeNET 8815 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}. 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. Q96JB5 EBI-1076230 0.00 P01889 EBI-1083050 0.00 P38606 EBI-4324466 0.35 O95758 EBI-7851121 0.35 O14862 EBI-9995694 0.35 P50402 EBI-10759397 0.94 P60033 EBI-10766934 0.35 Q6ZWV7 EBI-10997876 0.35 Q9D752 EBI-11004099 0.35 P83917 EBI-11012671 0.35 P97470 EBI-11029414 0.35 P27635 EBI-11035646 0.35 Q9CPQ5 EBI-11051123 0.35 Q80UF4 EBI-11074854 0.35 Q8N0Z3 EBI-11392023 0.27 Q8N137 EBI-11392655 0.27 Q9H503 EBI-25251388 0.56 O75531 EBI-15556735 0.62 O15155 EBI-16788578 0.35 P02545 EBI-16795953 0.35 P51151 EBI-16798596 0.35 P27824 EBI-16789225 0.27 Q7KZN9 EBI-20304305 0.35 P09622 EBI-20304669 0.35 P31040 EBI-20306992 0.35 P35610 EBI-20307233 0.35 P00441 EBI-20307497 0.35 P21796 EBI-20307902 0.35 Q9HCE5 EBI-20595531 0.35 E7ELX2 EBI-20625922 0.35 Q96N64 EBI-20910224 0.40 Q8NEL9 EBI-20920812 0.40 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 P68431 EBI-25471577 0.27 Q9UBI1 EBI-21259462 0.35 Q9BWW4 EBI-21265722 0.35 P03372 EBI-21301141 0.35 Q8WUJ0 EBI-21945299 0.35 Q15311 EBI-25375541 0.35 Q01995 EBI-26878675 0.35 Q8NAG6 EBI-27052189 0.40 P42166 EBI-27052224 0.40 P35226 EBI-27109494 0.35 Q99502 EBI-27113432 0.35 P11831 EBI-28997377 0.35 P23769 EBI-29000495 0.35 P40763 EBI-29000558 0.35 P48431 EBI-29373058 0.35 P08047 EBI-29385496 0.35 P21709 EBI-32717758 0.35 P54764 EBI-32717864 0.35 P54756 EBI-32717888 0.35 Q15375 EBI-32718158 0.35 P29322 EBI-32718189 0.35 P29323 EBI-32718255 0.35 P21802 EBI-32718470 0.35 P22607 EBI-32718522 0.35 P17948 EBI-32718591 0.35 P36888 EBI-32718602 0.35 Q12866 EBI-32719029 0.35 Q16288 EBI-32719212 0.35 P08581 EBI-32723963 0.27 GO:0000785 GO:0000793 GO:0005737 GO:0005829 GO:0005635 GO:0005654 GO:0005634 GO:0003677 GO:0003690 GO:0019899 GO:0042802 GO:0097726 GO:0008022 GO:0042803 GO:0047485 GO:0006325 GO:0030261 GO:0007059 GO:0007084 GO:0045824 GO:0010836 GO:0032480 GO:0045071 GO:0006979 GO:0009615 Unknown UniProt Sequence Analysis MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 89 O54962 Barrier-to-autointegration Banf1 10090 None SL-0178 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}. UNIPROT O54962 UNIPROT Q542E6 Pfam PF02961 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}. P68510 EBI-8586548 0.35 P52927 EBI-9986179 0.35 Q8VI24 EBI-26885060 0.35 GO:0000785 GO:0000793 GO:0005737 GO:0005829 GO:0005635 GO:0005654 GO:0005634 GO:0003677 GO:0003690 GO:0019899 GO:0042802 GO:0097726 GO:0008022 GO:0042803 GO:0047485 GO:0006325 GO:0030261 GO:0007059 GO:0015074 GO:0075713 GO:0007084 GO:0045824 GO:0010836 GO:0032480 GO:0045071 GO:0006979 Unknown UniProt Sequence Analysis MTTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 89 Q5RBU9 Barrier-to-autointegration BANF1 9601 None SL-0178 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}. UNIPROT Q5RBU9 Pfam PF02961 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}. GO:0000785 GO:0000793 GO:0005829 GO:0005635 GO:0005654 GO:0003690 GO:0019899 GO:0097726 GO:0008022 GO:0042803 GO:0047485 GO:0006325 GO:0007084 GO:0045824 GO:0010836 GO:0032480 GO:0045071 GO:0006979 Unknown UniProt Sequence Analysis MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 89 Q9R1T1 Barrier-to-autointegration Banf1 10116 None SL-0178 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}. UNIPROT Q9R1T1 Pfam PF02961 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}. GO:0000785 GO:0000793 GO:0005737 GO:0005635 GO:0005654 GO:0005634 GO:0003677 GO:0003690 GO:0019899 GO:0042802 GO:0097726 GO:0008022 GO:0042803 GO:0047485 GO:0006325 GO:0030261 GO:0007059 GO:0015074 GO:0007084 GO:0045824 GO:0010836 GO:0032480 GO:0045071 GO:0006979 Unknown UniProt Sequence Analysis MTTSQKHRDFVAEPMGEKPVGSLAGIGDALGKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 89 O95999 B-cell BCL10 9606 None SL-0198 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}. UNIPROT O95999 UNIPROT Q5VUF1 PDB 2MB9 PDB 6BZE PDB 6GK2 Pfam PF00619 PROSITE PS50209 OMIM 137245 OMIM 603517 OMIM 616098 DisGeNET 8915 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}. 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. Q96LW7 EBI-7443946 0.60 P31749 EBI-958921 0.69 P20749 EBI-959017 0.52 Q14525 EBI-1077929 0.00 P62807 EBI-1084020 0.00 Q9Y6K9 EBI-7334387 0.79 Q04759 EBI-7334619 0.40 Q9BXL7 EBI-7661911 0.86 Q9UDY8 EBI-7661911 0.92 Q92905 EBI-7006208 0.35 P50750 EBI-3906788 0.37 Q13261 EBI-3910825 0.37 Q07955 EBI-3913288 0.37 Q8WUM9 EBI-3913379 0.37 O14745 EBI-3914094 0.37 Q9BZD6 EBI-3921644 0.37 Q8N6Y0 EBI-3941289 0.44 Q14790 EBI-6253103 0.35 Q9H257 EBI-6665220 0.55 Q9ULZ3 EBI-6253113 0.35 Q92688 EBI-8995108 0.37 Q14032 EBI-8995121 0.37 P09467 EBI-8995160 0.37 Q9BU70 EBI-8995134 0.37 O60729 EBI-8995147 0.37 Q9BXL5 EBI-8995173 0.37 Q9P1Z9 EBI-8995186 0.37 Q9NR45 EBI-8995209 0.37 P20936 EBI-8995222 0.37 P01137 EBI-8995235 0.37 Q12933 EBI-10193048 0.81 O95999 EBI-10483822 0.75 Q05513 EBI-10689973 0.52 P06930 EBI-11737514 0.37 P33215 EBI-10993316 0.35 O95684 EBI-11381827 0.27 Q6P5F9 EBI-11603310 0.35 Q9Y2V7 EBI-11773232 0.70 Q9H0F6 EBI-11692014 0.40 Q66677 EBI-11709450 0.51 Q9Y297 EBI-15618375 0.35 O14920 EBI-15618375 0.35 P48729 EBI-15748832 0.35 P17813 EBI-22197897 0.35 Q96PU8 EBI-26969026 0.35 GO:0032449 GO:0005737 GO:0005881 GO:0005829 GO:0001772 GO:0005764 GO:0045121 GO:0005634 GO:0048471 GO:0002096 GO:0032991 GO:0050700 GO:0019899 GO:0140296 GO:0042802 GO:0019900 GO:0051059 GO:0002020 GO:0008022 GO:0043422 GO:0019901 GO:0043621 GO:0044877 GO:0003713 GO:0031625 GO:0002250 GO:0061760 GO:0001783 GO:0008219 GO:0006968 GO:0071222 GO:0071260 GO:0007249 GO:0016064 GO:0045087 GO:0031663 GO:0002906 GO:0001843 GO:0043065 GO:0043280 GO:0045893 GO:2001238 GO:0043123 GO:0032755 GO:0032757 GO:0033674 GO:0032761 GO:0032765 GO:0051092 GO:0042327 GO:0031398 GO:0050870 GO:0050862 GO:0051260 GO:0032094 GO:0070231 GO:0050852 GO:0002224 Unknown UniProt Sequence Analysis MEPTAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLDTLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFPDGATNNLSRSNSDESNFSEKLRASTVMYHPEGESSTTPFFSTNSSLNLPVLEVGRTENTIFSSTTLPRPGDPGAPPLPPDLQLEEEGTCANSSEMFLPLRSRTVSRQ 233 Q9QYN5 B-cell Bcl10 10116 None SL-0198 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}. UNIPROT Q9QYN5 Pfam PF00619 PROSITE PS50209 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}. GO:0032449 GO:0005737 GO:0005881 GO:0005829 GO:0001772 GO:0005764 GO:0045121 GO:0005634 GO:0048471 GO:0002096 GO:0032991 GO:0050700 GO:0019899 GO:0140296 GO:0042802 GO:0019209 GO:0019900 GO:0051059 GO:0002020 GO:0008022 GO:0043422 GO:0019901 GO:0043621 GO:0044877 GO:0003713 GO:0031625 GO:0002250 GO:0061760 GO:0001783 GO:0008219 GO:0006968 GO:0071222 GO:0071260 GO:0007249 GO:0016064 GO:0045087 GO:0031663 GO:0002906 GO:0001843 GO:0043065 GO:0043280 GO:0001819 GO:0045893 GO:2001238 GO:0043123 GO:0032757 GO:0051092 GO:0042327 GO:0031398 GO:0050870 GO:0050862 GO:0051260 GO:0050856 GO:0032094 GO:0009620 GO:0070231 GO:0050852 GO:0002224 Unknown UniProt Sequence Analysis MEAPAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLDTLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFAAGATNNLSRSNSDESNFSEKQRPSTVIYHPEGESSTAPFFSTESSLNLPVLEVGRLENSSFSSASLPRPGDPGAPPLPPDLRLEEGGSCGNSSEMFLPLRSRALSRQ 233 O02718 Apoptosis BCL2 9913 None SL-0178 SL-0182 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}. UNIPROT O02718 Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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}. GO:0005789 GO:0016021 GO:0016020 GO:0005741 GO:0005739 GO:0031965 GO:0046982 GO:0042803 GO:0097192 GO:0008630 GO:0043066 GO:0010507 GO:0032848 GO:2001243 GO:0046902 GO:0051881 GO:0001836 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAHAGGTGYDNREIVMKYIHYKLSQRGYEWDAGDAGAAPPGAAPAPGILSSQPGRTPAPSRTSPPPPPAAAAGPAPSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARERFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDSIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKALLSLALVGACITLGAYLGHK 229 Q6R755 Apoptosis BCL2 9615 None SL-0178 SL-0182 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}. UNIPROT Q6R755 Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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}. GO:0005789 GO:0016021 GO:0005741 GO:0031965 GO:0046982 GO:0042803 GO:0097192 GO:0008630 GO:0010507 GO:2001243 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDVGDVDAAPLGAAPTPGIFSFQPESNPTPAVHRDMAARTSPLRPIVATTGPTLSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPTMQPLFDFSWLSLKALLSLALVGACITLGAYLGHK 236 Q00709 Apoptosis BCL2 9031 None SL-0178 SL-0182 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}. UNIPROT Q00709 Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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). GO:0005829 GO:0005789 GO:0005741 GO:0005739 GO:0043209 GO:0031965 GO:0005654 GO:0046930 GO:0051434 GO:0015267 GO:0016248 GO:0140297 GO:0002020 GO:0046982 GO:0042803 GO:0051721 GO:0043565 GO:0031625 GO:0007015 GO:0031103 GO:0007409 GO:0001783 GO:0001782 GO:0002326 GO:0042100 GO:0050853 GO:0001662 GO:0001658 GO:0060402 GO:0043375 GO:0098609 GO:0042149 GO:0071456 GO:0071310 GO:0021747 GO:0051607 GO:0097048 GO:0048546 GO:0043583 GO:0032469 GO:1904019 GO:0097192 GO:0008625 GO:0048041 GO:0000082 GO:0022612 GO:0032835 GO:0060218 GO:0048873 GO:0008630 GO:0070059 GO:0008631 GO:0070306 GO:0002320 GO:0008584 GO:0006582 GO:0030318 GO:0014031 GO:0001656 GO:0097049 GO:0033028 GO:2000811 GO:0043066 GO:0010507 GO:0002903 GO:0010523 GO:0030308 GO:0030336 GO:0032848 GO:2000669 GO:1904036 GO:2001240 GO:2000134 GO:2001243 GO:2000672 GO:0033033 GO:0030279 GO:0033689 GO:2000378 GO:0046671 GO:0070233 GO:0042551 GO:0048599 GO:0035265 GO:0001503 GO:0033687 GO:0001541 GO:0018105 GO:0018107 GO:0048753 GO:0030890 GO:0043085 GO:0030307 GO:0045636 GO:0040018 GO:0014042 GO:0033138 GO:0048743 GO:0014911 GO:0009791 GO:0006470 GO:0000209 GO:0072593 GO:0001952 GO:0010468 GO:0010559 GO:0046902 GO:0051881 GO:0006808 GO:0032880 GO:0031647 GO:0022898 GO:0045069 GO:0001836 GO:0003014 GO:0034097 GO:0010332 GO:0051384 GO:0042542 GO:0010039 GO:0002931 GO:1904373 GO:0035094 GO:0009636 GO:0010224 GO:0009410 GO:0046666 GO:0048741 GO:0014909 GO:0048536 GO:0048864 GO:0070231 GO:0033077 GO:0043029 GO:0048538 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAHPGRRGYDNREIVLKYIHYKLSQRGYDWAAGEDRPPVPPAPAPAAAPAAVAAAGASSHHRPEPPGSAAASEVPPAEGLRPAPPGVHLALRQAGDEFSRRYQRDFAQMSGQLHLTPFTAHGRFVAVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIATWMTEYLNRHLHNWIQDNGGWDAFVELYGNSMRPLFDFSWISLKTILSLVLVGACITLGAYLGHK 233 Q9JJV8 Apoptosis BCL2 10029 None SL-0178 SL-0182 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}. UNIPROT Q9JJV8 Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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}. Q14790 EBI-1749111 0.40 GO:0005829 GO:0005789 GO:0005741 GO:0043209 GO:0031965 GO:0005654 GO:0046930 GO:0051434 GO:0015267 GO:0016248 GO:0140297 GO:0042802 GO:0002020 GO:0046982 GO:0051721 GO:0043565 GO:0031625 GO:0007015 GO:0031103 GO:0007409 GO:0001783 GO:0001782 GO:0002326 GO:0042100 GO:0050853 GO:0001662 GO:0001658 GO:0060402 GO:0043375 GO:0098609 GO:0042149 GO:0071456 GO:0071310 GO:0021747 GO:0051607 GO:0097048 GO:0048546 GO:0043583 GO:0032469 GO:1904019 GO:0097192 GO:0008625 GO:0048041 GO:0000082 GO:0022612 GO:0032835 GO:0031069 GO:0060218 GO:0048873 GO:0008630 GO:0070059 GO:0008631 GO:0002320 GO:0008584 GO:0006582 GO:0030318 GO:0014031 GO:0001656 GO:0097049 GO:0033028 GO:2000811 GO:0010507 GO:0002903 GO:0010523 GO:0030308 GO:0030336 GO:0032848 GO:2000669 GO:1904036 GO:2001240 GO:2000134 GO:2001243 GO:2000672 GO:0033033 GO:0030279 GO:0033689 GO:2000378 GO:0046671 GO:0070233 GO:0042551 GO:0048599 GO:0035265 GO:0001503 GO:0033687 GO:0001541 GO:0018105 GO:0018107 GO:0048753 GO:0030890 GO:0043085 GO:0030307 GO:0045636 GO:0040018 GO:0014042 GO:0033138 GO:0048743 GO:0014911 GO:0009791 GO:0006470 GO:0000209 GO:0072593 GO:0001952 GO:0010468 GO:0010559 GO:0046902 GO:0051881 GO:0006808 GO:0032880 GO:0031647 GO:0022898 GO:0045069 GO:0001836 GO:0003014 GO:0034097 GO:0010332 GO:0051384 GO:0042542 GO:0010039 GO:0002931 GO:1904373 GO:0035094 GO:0009636 GO:0010224 GO:0009410 GO:0046666 GO:0048741 GO:0014909 GO:0048536 GO:0048864 GO:0070231 GO:0033077 GO:0043029 GO:0048538 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDVGDVDAAPLGAAPTPGIFSFQPESNPTPAVHRDMAARTSPLRPIVATTGPTLSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSVRPLFDFSWLSLKTLLSLALVGACITLGTYLGHK 236 P10415 Apoptosis BCL2 9606 None SL-0178 SL-0182 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}. UNIPROT P10415 UNIPROT C9JHD5 UNIPROT P10416 UNIPROT Q13842 UNIPROT Q16197 PDB 1G5M PDB 1GJH PDB 1YSW PDB 2O21 PDB 2O22 PDB 2O2F PDB 2W3L PDB 2XA0 PDB 4AQ3 PDB 4IEH PDB 4LVT PDB 4LXD PDB 4MAN PDB 5AGW PDB 5AGX PDB 5FCG PDB 5JSN PDB 5VAU PDB 5VAX PDB 5VAY PDB 6GL8 PDB 6IWB PDB 6O0K PDB 6O0L PDB 6O0M PDB 6O0O PDB 6O0P PDB 7LHB Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 OMIM 151430 DisGeNET 596 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}. 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}. O60238 EBI-850662 0.44 O54918 EBI-707531 0.44 Q9DAJ5 EBI-526356 0.35 P51572 EBI-77682 0.52 P28482 EBI-7210282 0.49 P67775 EBI-7210303 0.49 P45983 EBI-7497436 0.31 Q14318 EBI-7497544 0.51 P55957 EBI-519684 0.87 Q9BXH1 EBI-707957 0.82 P63098 EBI-7517885 0.49 Q07813 EBI-700706 0.40 Q07812 EBI-700753 0.94 Q16611 EBI-700762 0.61 Q92934 EBI-700785 0.81 Q13323 EBI-700803 0.82 P10415 EBI-700826 0.59 O43521 EBI-707839 0.92 Q91ZE9 EBI-708044 0.62 Q61337 EBI-709166 0.72 Q12982 EBI-849945 0.37 Q12983 EBI-849952 0.37 O60551 EBI-8173465 0.40 Q63690 EBI-8496082 0.40 P62136 EBI-1206840 0.00 P36873 EBI-1207036 0.00 P62140 EBI-1207176 0.00 Q86Y07 EBI-1207847 0.37 Q9C000 EBI-1246113 0.75 Q14457 EBI-5234827 0.95 Q9H2V7 EBI-1386538 0.46 O15304 EBI-1393040 0.40 Q14790 EBI-1749080 0.37 P22736 EBI-2126295 0.67 Q07817 EBI-2126646 0.44 P04637 EBI-7044574 0.56 O15151 EBI-7044604 0.50 Q8N5K1 EBI-7676229 0.54 Q0WGQ5 EBI-2874959 0.00 P27797 EBI-8537109 0.35 P38646 EBI-8537109 0.35 Q07820 EBI-8537109 0.35 Q9C0C7 EBI-8600088 0.66 Q13794 EBI-4370379 0.54 Q96LC9 EBI-5488187 0.40 P29117 EBI-6465503 0.40 P30405 EBI-6465542 0.37 Q9NYF8 EBI-6621256 0.50 P38398 EBI-8757170 0.38 P0DM65 EBI-8839562 0.40 A8MW95 EBI-8839552 0.40 Q5S007 EBI-10055396 0.44 Q7L3V2 EBI-11509550 0.35 Q13625 EBI-15723849 0.65 P11881 EBI-15801106 0.52 Q14643 EBI-15801089 0.40 P21796 EBI-15801214 0.40 Q92570 EBI-20939354 0.40 P59635 EBI-25495801 0.40 P00441 EBI-25934648 0.56 P05067 EBI-25936674 0.56 Q9HB09 EBI-27086233 0.37 Q13619 EBI-30863570 0.35 Q8WV16 EBI-30863977 0.35 GO:0005737 GO:0005829 GO:0005783 GO:0005789 GO:0016020 GO:0005741 GO:0005739 GO:0043209 GO:0031965 GO:0005654 GO:0005634 GO:0046930 GO:0032991 GO:0051434 GO:0015267 GO:0016248 GO:0140297 GO:0042802 GO:0060090 GO:0002020 GO:0046982 GO:0042803 GO:0051721 GO:0043565 GO:0031625 GO:0007015 GO:0006915 GO:0031103 GO:0007409 GO:0001783 GO:0001782 GO:0002326 GO:0042100 GO:0050853 GO:0001662 GO:0001658 GO:0060402 GO:0043375 GO:0098609 GO:0006974 GO:0042149 GO:0071456 GO:0071310 GO:0021747 GO:0051607 GO:0097048 GO:0048546 GO:0043583 GO:0032469 GO:1904019 GO:0097192 GO:0008625 GO:0007565 GO:0048041 GO:0000082 GO:0022612 GO:0032835 GO:0031069 GO:0060218 GO:0048873 GO:0006959 GO:0008630 GO:0070059 GO:0008631 GO:0002320 GO:0008584 GO:0006582 GO:0030318 GO:0014031 GO:0001656 GO:0097049 GO:0033028 GO:2000811 GO:0043066 GO:2001234 GO:0010507 GO:0002903 GO:0010523 GO:0030308 GO:0030336 GO:0032848 GO:2000669 GO:1904036 GO:2001240 GO:2000134 GO:2001243 GO:1902166 GO:0051902 GO:2000672 GO:0033033 GO:0043524 GO:0030279 GO:0033689 GO:2000378 GO:0046671 GO:0070233 GO:0051402 GO:0042551 GO:0048599 GO:0035265 GO:0001503 GO:0033687 GO:0001541 GO:0018105 GO:0018107 GO:0048753 GO:0030890 GO:0043085 GO:0030307 GO:0008284 GO:0045636 GO:0040018 GO:0014042 GO:0033138 GO:0048743 GO:0014911 GO:0009791 GO:0006470 GO:0000209 GO:0072593 GO:0051924 GO:0001952 GO:0010468 GO:0010559 GO:0046902 GO:0051881 GO:0006808 GO:0032880 GO:0031647 GO:0022898 GO:0045069 GO:0001836 GO:0003014 GO:0034097 GO:0010332 GO:0051384 GO:0042542 GO:0010039 GO:0002931 GO:1904373 GO:0035094 GO:0009314 GO:0009636 GO:0010224 GO:0009410 GO:0046666 GO:0048741 GO:0014909 GO:0048536 GO:0048864 GO:0070231 GO:0033077 GO:0043029 GO:0048538 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK 239 P10417 Apoptosis Bcl2 10090 None SL-0178 SL-0182 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}. UNIPROT P10417 UNIPROT P10418 UNIPROT Q4VBF6 Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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}. P70444 EBI-7986755 0.40 P62137 EBI-1202230 0.00 P63087 EBI-1202999 0.00 Q07813 EBI-8067327 0.57 O54918 EBI-8538239 0.51 O08734 EBI-5394637 0.40 Q61337 EBI-5395607 0.37 O88597 EBI-10714637 0.73 P63158 EBI-10714676 0.35 Q99MI6 EBI-15572329 0.56 Q8BWF2 EBI-15572373 0.56 GO:0005737 GO:0005829 GO:0005783 GO:0005789 GO:0016020 GO:0030061 GO:0031966 GO:0005741 GO:0005739 GO:0043209 GO:0031965 GO:0005654 GO:0005634 GO:0048471 GO:0046930 GO:0032991 GO:0051400 GO:0051434 GO:0015267 GO:0016248 GO:0140297 GO:0042802 GO:0002020 GO:0046982 GO:0042803 GO:0051721 GO:0019903 GO:0044877 GO:0043565 GO:0031625 GO:0007015 GO:0009887 GO:0008637 GO:0006915 GO:0031103 GO:0007409 GO:0001783 GO:0030183 GO:0001782 GO:0002326 GO:0042100 GO:0050853 GO:0001662 GO:0001658 GO:0060402 GO:0043375 GO:0016477 GO:0000902 GO:0008283 GO:0098609 GO:0006874 GO:0006974 GO:0042149 GO:0071456 GO:0071310 GO:0021747 GO:0051607 GO:0097048 GO:0048589 GO:0048066 GO:0048546 GO:0043583 GO:0032469 GO:1904019 GO:0051649 GO:0097192 GO:0008625 GO:0048041 GO:0000082 GO:0022612 GO:0032835 GO:0031069 GO:0060218 GO:0030097 GO:0048873 GO:0002520 GO:0008630 GO:0070059 GO:0008631 GO:0001822 GO:0001776 GO:0070227 GO:0002260 GO:0002320 GO:0008584 GO:0006582 GO:0030318 GO:0014031 GO:0001656 GO:0000278 GO:0097049 GO:0033028 GO:2000811 GO:0043066 GO:2001234 GO:0010507 GO:0002903 GO:0010523 GO:0010667 GO:0030308 GO:0030336 GO:0008285 GO:0032848 GO:2000669 GO:1904036 GO:2001240 GO:2000134 GO:2001243 GO:0070229 GO:0045930 GO:2000672 GO:0033033 GO:0043524 GO:1901215 GO:0030279 GO:0033689 GO:2000378 GO:0046671 GO:0070233 GO:0051402 GO:0070997 GO:0042551 GO:0048599 GO:0035265 GO:0001503 GO:0033687 GO:0001541 GO:0018105 GO:0018107 GO:0048753 GO:0043473 GO:0030890 GO:0043085 GO:0030307 GO:0008284 GO:0048087 GO:0045636 GO:0040018 GO:0014042 GO:0033138 GO:0048743 GO:0014911 GO:0009791 GO:0006470 GO:0000209 GO:0072593 GO:0042981 GO:0010506 GO:0051924 GO:0050790 GO:0051726 GO:0001952 GO:0048070 GO:0010468 GO:0010559 GO:0040008 GO:0046902 GO:0051881 GO:0006808 GO:0043067 GO:0032880 GO:0031647 GO:0022898 GO:0045069 GO:0001836 GO:0003014 GO:0034097 GO:0045471 GO:0010332 GO:0051384 GO:0042542 GO:0010039 GO:0002931 GO:1904373 GO:0035094 GO:0006979 GO:0048545 GO:0009636 GO:0010224 GO:0009410 GO:0046666 GO:0048741 GO:0014909 GO:0048536 GO:0048864 GO:0070231 GO:0030217 GO:0033077 GO:0043029 GO:0002360 GO:0048538 GO:0001657 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDADAAPLGAAPTPGIFSFQPESNPMPAVHRDMAARTSPLRPLVATAGPALSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK 236 P49950 Apoptosis Bcl2 10116 None SL-0178 SL-0182 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}. UNIPROT P49950 UNIPROT Q62837 UNIPROT Q64032 Pfam PF00452 Pfam PF02180 PROSITE PS50062 PROSITE PS01080 PROSITE PS01258 PROSITE PS01259 PROSITE PS01260 PROSITE PS50063 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}. O88498 EBI-79017 0.37 P29117 EBI-6465491 0.40 P06536 EBI-15756525 0.40 GO:0005737 GO:0005829 GO:0005783 GO:0005789 GO:0016020 GO:0030061 GO:0031966 GO:0005741 GO:0005739 GO:0043209 GO:0031965 GO:0005634 GO:0048471 GO:0046930 GO:0032991 GO:0051400 GO:0051434 GO:0015267 GO:0016248 GO:0140297 GO:0042802 GO:0002020 GO:0046982 GO:0042803 GO:0051721 GO:0019903 GO:0044877 GO:0043565 GO:0031625 GO:0007015 GO:0007568 GO:0009887 GO:0008637 GO:0006915 GO:0031103 GO:0007409 GO:0001783 GO:0030183 GO:0001782 GO:0002326 GO:0042100 GO:0050853 GO:0001662 GO:0007420 GO:0001658 GO:0060402 GO:0043375 GO:0016477 GO:0000902 GO:0008283 GO:0098609 GO:0006874 GO:0006974 GO:1902618 GO:0042149 GO:0071333 GO:0070301 GO:0071456 GO:0071407 GO:0071310 GO:0021987 GO:0021747 GO:0051607 GO:0097048 GO:0048589 GO:0048066 GO:0048546 GO:0043583 GO:0032469 GO:1904019 GO:0051649 GO:0097192 GO:0008625 GO:0048041 GO:0000082 GO:0022612 GO:0034349 GO:0032835 GO:0031069 GO:0060218 GO:0030097 GO:0048873 GO:0002520 GO:0008630 GO:0070059 GO:0008631 GO:0001822 GO:0001776 GO:0097421 GO:0070227 GO:0002260 GO:0002320 GO:0008584 GO:0006582 GO:0030318 GO:0014031 GO:0001656 GO:0000278 GO:0097049 GO:0033028 GO:2000811 GO:0043066 GO:2001234 GO:0010507 GO:0002903 GO:0010523 GO:0010667 GO:0030308 GO:0030336 GO:0008285 GO:0032848 GO:2000669 GO:1904036 GO:2001240 GO:2000134 GO:2001243 GO:0070229 GO:0045930 GO:2000672 GO:0033033 GO:0043524 GO:1901215 GO:0030279 GO:0033689 GO:2000378 GO:0046671 GO:0070233 GO:0051402 GO:0070997 GO:0042551 GO:0048709 GO:0048599 GO:0035265 GO:0001503 GO:0033687 GO:0001541 GO:0018105 GO:0018107 GO:0048753 GO:0043473 GO:0030890 GO:0043085 GO:0030307 GO:0008284 GO:0048087 GO:0045636 GO:0040018 GO:0014042 GO:0033138 GO:0048743 GO:0014911 GO:0009791 GO:0006470 GO:0000209 GO:0072593 GO:0042981 GO:0010506 GO:0051924 GO:0050790 GO:0051726 GO:0001952 GO:0048070 GO:0010468 GO:0010559 GO:0040008 GO:0046902 GO:0051881 GO:0006808 GO:0043067 GO:0032880 GO:0031647 GO:0022898 GO:0045069 GO:0001836 GO:0003014 GO:0010044 GO:1904645 GO:0031000 GO:0051591 GO:0046688 GO:0051412 GO:0034097 GO:0051602 GO:0036017 GO:0043627 GO:0045471 GO:0051593 GO:0010332 GO:0051384 GO:0009408 GO:0042542 GO:0001666 GO:0010035 GO:0032868 GO:0010039 GO:0002931 GO:1904373 GO:0033591 GO:0034284 GO:0035094 GO:0007584 GO:0014070 GO:0010033 GO:0006979 GO:0043434 GO:0080184 GO:0048545 GO:0009636 GO:0010224 GO:0033197 GO:0009410 GO:0046666 GO:0048741 GO:0014909 GO:0048536 GO:0048864 GO:0070231 GO:0030217 GO:0033077 GO:0043029 GO:0002360 GO:0048538 GO:0001657 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDTGDEDSAPLRAAPTPGIFSFQPESNRTPAVHRDTAARTSPLRPLVANAGPALSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK 236 P20749 B-cell BCL3 9606 None SL-0198 Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Ubiquitination via 'Lys-63'- linked ubiquitin chains is required for nuclear accumulation. {ECO:0000250}. UNIPROT P20749 PDB 1K1A PDB 1K1B Pfam PF12796 PROSITE PS50297 PROSITE PS50088 OMIM 109560 DisGeNET 602 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}. 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}. O95999 EBI-959017 0.52 P06239 EBI-7785707 0.59 P06241 EBI-7785768 0.40 P56545 EBI-3926425 0.51 O15084 EBI-5653696 0.00 O00625 EBI-10713595 0.44 Q92598 EBI-21258808 0.35 Q00653 EBI-21258808 0.35 P19838 EBI-21258808 0.35 P17066 EBI-21258808 0.35 Q9BVL2 EBI-25907809 0.56 Q13619 EBI-30863570 0.35 GO:0032996 GO:0033257 GO:0005737 GO:0005829 GO:0043231 GO:0030496 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0032991 GO:0140297 GO:0042826 GO:0030674 GO:0003713 GO:0003714 GO:0019730 GO:0006974 GO:0042742 GO:0042832 GO:0030330 GO:0030198 GO:0002268 GO:0002467 GO:0002455 GO:0007249 GO:0042771 GO:0002315 GO:0043066 GO:0045892 GO:0032717 GO:0032088 GO:0046426 GO:0070233 GO:0032720 GO:0045893 GO:0032729 GO:0032733 GO:0045944 GO:0045727 GO:0006606 GO:0042981 GO:0051101 GO:1901222 GO:0010225 GO:0009615 GO:0048536 GO:0070231 GO:0042088 GO:0045064 Unknown UniProt Sequence Analysis MPRCPAGAMDEGPVDLRTRPKAAGLPGAALPLRKRPLRAPSPEPAAPRGAAGLVVPLDPLRGGCDLPAVPGPPHGLARPEALYYPGALLPLYPTRAMGSPFPLVNLPTPLYPMMCPMEHPLSADIAMATRADEDGDTPLHIAVVQGNLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAAPGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILRGKATRPASTSQPDPSPDRSANTSPESSSRLSSNGLLSASPSSSPSQSPPRDPPGFPMAPPNFFLPSPSPPAFLPFAGVLRGPGRPVPPSPAPGGS 454 Q9Z2F6 B-cell Bcl3 10090 None SL-0198 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. UNIPROT Q9Z2F6 Pfam PF00023 Pfam PF12796 PROSITE PS50297 PROSITE PS50088 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}. Q80TQ2 EBI-943890 0.67 GO:0032996 GO:0033257 GO:0005737 GO:0005829 GO:0043231 GO:0030496 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0032991 GO:0140297 GO:0042826 GO:0030674 GO:0003713 GO:0003714 GO:0019730 GO:0006974 GO:0042742 GO:0042832 GO:0030330 GO:0030198 GO:0002268 GO:0002467 GO:0002455 GO:0007249 GO:0042771 GO:0002315 GO:0043066 GO:0045892 GO:0032717 GO:0032088 GO:0046426 GO:0070233 GO:0032720 GO:0045893 GO:0032729 GO:0032733 GO:0045944 GO:0045727 GO:0006606 GO:0042981 GO:0051101 GO:1901222 GO:0010225 GO:0009615 GO:0048536 GO:0070231 GO:0042088 GO:0045064 Unknown UniProt Sequence Analysis MPRCPAGAMDEGPVDLRTRPKGTPGAALPLRKRPLRPASPEPATTRSPAGPLDALRSGCDVPVVPGPPHCVARPEALYYQGPLMPIYSTPTMAPHFPLLNLPTHPYSMICPMEHPLSADIAMATRVDEDGDTPLHIAVVQNNIAAVYRILSLFKLGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSATSGSVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDIKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHNDTPLMVARSRRVIDILRGKASRAASGSQPEPSPDQSATNSPESSSRLSSNGLQSSPSSSPSLSPPKDAPGFPATPQNFFLPTTSTPAFLPFPGVLRGPGRPVPPSPAPGSS 448 O74907 Protein bcp1 284812 None SL-0178 Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}. UNIPROT O74907 Pfam PF13862 Involved in nuclear export, actin cytoskeleton organization and vesicular transport. {ECO:0000250}. GO:0005737 GO:0005783 GO:0005635 GO:0005634 GO:0006611 GO:0000055 Unknown UniProt Sequence Analysis MAKRHAEENEDTVMSESLKVVDTDFINVDFEFFDPQPIDFHAFKNLLKQLLGYDHTNVNLSALADLILSQPLLGSTVKVDGNNSDPYAMLSVINLNTRRDEPVIKQLTSYIISRLAKSNSRLENELQKLLEPNSGSQVGLIVNERLINMPVQVIPPMYNMLLEEMQWAINENEPYNFTHYLLLSRTYTEIESKLMDDERPSKKGKKSKKTSGEEVMFFHPEDEQFREVAIDIADYPFANQDFNPDANRVFQDAGIKPQGELLLMTNEDFKNLVPKLMEIYSA 282 P16278 Beta-galactosidase GLB1 9606 None SL-0198 [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}. UNIPROT P16278 UNIPROT B2R7H8 UNIPROT B7Z6B0 UNIPROT P16279 PDB 3THC PDB 3THD PDB 3WEZ PDB 3WF0 PDB 3WF1 PDB 3WF2 PDB 3WF3 PDB 3WF4 Pfam PF13364 Pfam PF01301 PROSITE PS01182 OMIM 230500 OMIM 230600 OMIM 230650 OMIM 253010 OMIM 611458 DisGeNET 2720 [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}. 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. P04985 EBI-989686 0.35 Q99519 EBI-989719 0.37 Q9NSA3 EBI-1066502 0.00 P01023 EBI-7183126 0.35 P16104 EBI-2564373 0.35 P02866 EBI-2908516 0.35 P01100 EBI-3909100 0.37 P67870 EBI-7133497 0.37 P53350 EBI-7312891 0.37 P04183 EBI-7398255 0.37 P24668 EBI-10999951 0.35 O75787 EBI-11037152 0.35 Q9P0L0 EBI-11120309 0.35 P08670 EBI-12452764 0.51 P62699 EBI-12452923 0.51 Q9BRI3 EBI-24521461 0.56 Q3KNW5 EBI-24662545 0.56 P30825 EBI-24732260 0.56 Q8NBJ4 EBI-25278037 0.56 Q9NQH7 EBI-11905895 0.00 P10619 EBI-11905886 0.00 Q8IWL3 EBI-13943458 0.35 O92597 EBI-14062645 0.35 Q9WRJ7 EBI-14062674 0.35 Q8IUR0 EBI-21546443 0.35 Q9Y5R8 EBI-21546787 0.35 Q03405 EBI-21577545 0.35 P24941 EBI-21606933 0.35 P51449 EBI-21635113 0.35 P25686 EBI-21643743 0.35 Q9UM11 EBI-21645901 0.35 Q9Y296 EBI-21692555 0.35 Q9UL33 EBI-21692555 0.35 Q96Q05 EBI-21692555 0.35 Q8WVR3 EBI-21692555 0.35 Q86SZ2 EBI-21692555 0.35 P48553 EBI-21692555 0.35 P04439 EBI-21692555 0.35 O43617 EBI-21692555 0.35 Q9UDY4 EBI-21720121 0.35 P08134 EBI-21721227 0.35 P61586 EBI-21721324 0.35 P25685 EBI-21801194 0.35 Q8TD22 EBI-21843206 0.35 Q8NEP7 EBI-21843169 0.35 Q96NY8 EBI-21851548 0.35 P50053 EBI-21851528 0.40 Q13363 EBI-27044482 0.35 Q8N5S9 EBI-28943380 0.35 Q9UL54 EBI-28946956 0.35 P03372 EBI-34581889 0.35 GO:0035578 GO:0005737 GO:0070062 GO:0005576 GO:1904813 GO:0005794 GO:0043231 GO:0043202 GO:0048471 GO:0005773 GO:0004565 GO:0016936 GO:0042803 GO:0044262 GO:0019388 GO:0006027 GO:0006687 GO:0042340 GO:0051413 GO:1904016 Unknown UniProt Sequence Analysis MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV 677 Q8TD16 Protein BICD2 9606 None SL-0178 SL-0185 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}. UNIPROT Q8TD16 UNIPROT O75181 UNIPROT Q5TBQ2 UNIPROT Q5TBQ3 UNIPROT Q96LH2 UNIPROT Q9BT84 UNIPROT Q9H561 PDB 6OFP PDB 6PSE Pfam PF09730 OMIM 609797 OMIM 615290 OMIM 618291 DisGeNET 23299 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}. 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. O75604 EBI-25254904 0.56 P0DTD1 EBI-27126939 0.35 P49792 EBI-15847951 0.40 P53350 EBI-2372594 0.53 Q9UGI0 EBI-2511131 0.40 Q9ERU9 EBI-2555617 0.40 Q9D0F1 EBI-2558810 0.40 Q07832 EBI-2560950 0.40 A0A5P8YL50 EBI-2841923 0.00 A0A380PMY4 EBI-2874899 0.00 Q9Q2G4 EBI-6176962 0.35 Q6ZU80 EBI-11370150 0.27 Q15154 EBI-11382763 0.27 Q6P5F9 EBI-11603310 0.35 P55081 EBI-24273176 0.56 Q8TBB1 EBI-24278102 0.56 Q8IVT4 EBI-24279124 0.56 Q96IZ5 EBI-24282407 0.56 Q96BR6 EBI-24299149 0.56 Q13573 EBI-24303486 0.56 O43602 EBI-24327875 0.56 P56524 EBI-24330514 0.56 O43309 EBI-24331439 0.56 Q3SY00 EBI-24333322 0.56 Q5T619 EBI-24351080 0.56 Q99633 EBI-24356006 0.56 Q96MY7 EBI-24361254 0.56 Q8TAU3 EBI-25251198 0.56 Q8TD31 EBI-25253133 0.56 Q96NC0 EBI-24494537 0.56 Q8N8B7 EBI-24371967 0.56 Q9NRW1 EBI-24383386 0.56 Q9P2J8 EBI-24385190 0.56 Q9Y247 EBI-24386038 0.56 Q6NYC8 EBI-24395125 0.56 Q3B820 EBI-24407148 0.56 Q3MJ62 EBI-24410326 0.56 P00540 EBI-25262612 0.56 Q6P1K2 EBI-24417481 0.67 Q8WUT1 EBI-24419281 0.56 Q9BQ89 EBI-24423630 0.56 Q8WWY3 EBI-24431378 0.56 Q5TAP6 EBI-24433469 0.56 P07947 EBI-24435343 0.56 Q15560 EBI-24438200 0.56 Q9BS34 EBI-24441307 0.56 Q969Z0 EBI-24460855 0.56 Q53FD0 EBI-24470675 0.56 O75828 EBI-24472069 0.56 Q92619 EBI-24473457 0.56 Q9Y6Q1 EBI-21501330 0.35 Q9Y3C0 EBI-21617288 0.35 Q8TDR4 EBI-21617027 0.35 Q9NYP9 EBI-21663541 0.35 Q9Y5N6 EBI-21663753 0.35 Q9Y2V7 EBI-21673529 0.35 Q8IV45 EBI-21699883 0.35 P07196 EBI-21716934 0.35 Q9HCH3 EBI-21757216 0.35 Q96GS4 EBI-21795617 0.35 P31146 EBI-21859808 0.35 Q8TD19 EBI-20908056 0.40 P16401 EBI-20908000 0.40 P16403 EBI-20911880 0.40 P10412 EBI-20912702 0.40 P61163 EBI-20912662 0.40 Q8N4N8 EBI-20913996 0.40 Q16695 EBI-20922400 0.40 Q8TE73 EBI-20924962 0.40 Q71DI3 EBI-20924954 0.40 Q16778 EBI-20924946 0.40 Q93079 EBI-20924938 0.40 O94989 EBI-20924930 0.40 O95858 EBI-20929440 0.40 Q02539 EBI-20931216 0.40 O15021 EBI-20934244 0.40 Q5S007 EBI-21360986 0.35 Q14204 EBI-21991405 0.40 O14576 EBI-21992400 0.52 P20340 EBI-21992535 0.46 P0DOF2 EBI-25603126 0.35 P69479 EBI-25568044 0.35 Q8NHP6 EBI-25617558 0.35 GO:0005642 GO:0005813 GO:0005737 GO:0031410 GO:0005829 GO:0005794 GO:0005635 GO:0005643 GO:0005886 GO:0008093 GO:0034452 GO:0070840 GO:0051959 GO:0031267 GO:0051642 GO:0072393 GO:0007018 GO:0072385 GO:0051028 GO:0034067 GO:0033365 GO:0015031 GO:0070507 GO:0006890 Unknown UniProt Sequence Analysis MSAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTPKKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYREGQGGAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRADGGTGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRRGRAKAAPKTKPATPSL 824 Q921C5 Protein Bicd2 10090 None SL-0178 SL-0185 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}. UNIPROT Q921C5 UNIPROT Q80TU1 UNIPROT Q8BTE3 UNIPROT Q9DCL3 Pfam PF09730 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}. P46060 EBI-15847893 0.35 P49792 EBI-15847872 0.63 Q12840 EBI-15847851 0.41 Q14203 EBI-7894652 0.35 Q8N1F7 EBI-15847893 0.35 Q9JL25 EBI-650530 0.37 P35279 EBI-7893837 0.51 O14576 EBI-7894652 0.35 Q8VHQ4 EBI-11569919 0.35 Q5SW79 EBI-15847893 0.35 O60447 EBI-15847893 0.35 O75122 EBI-15847893 0.35 O60333 EBI-15847893 0.35 P35579 EBI-15847893 0.35 O00159 EBI-15847893 0.35 Q86SQ0 EBI-15847893 0.35 O43896 EBI-15847893 0.35 P20340 EBI-15847968 0.41 Q8BUK6 EBI-25297227 0.36 GO:0005642 GO:0005813 GO:0005737 GO:0031410 GO:0005829 GO:0005794 GO:0005635 GO:0005643 GO:0005886 GO:0008093 GO:0034452 GO:0070840 GO:0051959 GO:0031267 GO:0051642 GO:0072393 GO:0007018 GO:0072385 GO:0051028 GO:0034067 GO:0033365 GO:0015031 GO:0070507 GO:0006890 Unknown UniProt Sequence Analysis MSAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDDTVTAEPNNDAEALVNGFEHSGLVKSSLDNKTSTPRKDGLAPPSPSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVNRLTENLSALRRLQAGKERQTSLDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKISLLEKASHQDRELLAHLEKELKKVSDVAGETQGSLNVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYREGQGKAGRTSPEGRGRRSPVLLPKGLLATEVGRADGGTGDNSPSPSSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRRGRSKAASKAKPASPSL 820 V6CJ04 Protein bicd 6239 None SL-0178 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}. UNIPROT V6CJ04 UNIPROT V6CK55 Pfam PF09730 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}. Q17902 EBI-2903351 0.51 Q23064 EBI-2905267 0.51 O01590 EBI-2414739 0.49 Q22771 EBI-2414746 0.49 Q9N4I1 EBI-6460281 0.37 Q9XVN3 EBI-6534816 0.37 GO:0005829 GO:0030425 GO:0005794 GO:0005875 GO:0043025 GO:0005635 GO:0043204 GO:0008093 GO:0034452 GO:0070840 GO:0072393 GO:0007399 GO:0030473 GO:0033365 GO:0048814 GO:0070507 Unknown UniProt Sequence Analysis MAESELEKLRQDIAILTEKYEQAKEDIHKAANAGLELLRQKEDLEKRLAEMQAELDLARTEIDKTNQTLAEYRSQHQRSTRSELENEESLLEESSAKEEEYLQRIAKLEADLKKKEQELAEKKEELESIEKKHSKEIDSGAALEDERRKLRAELKETKEREQRLISEYSELEEENIGLQKTVANLRGSQVEYESLRIDNNRLEETIEIMKMAAEEDEILRVIADKQLEEALLTAQQERDQRLAMKRELEQTRNAEHISSLNDMLFGLERLGEDGELPPPQPGASDLFSELQGSSDVKVRELEAAKEGLQEELKSREKIFIEFVTGLADTLNIHRPTNELDYMHARQQKDVVLEKIQNIARDTDRHDKEGEEKRSGILKADLRTLVLVAGEKSAQLAAAQDAMIQVSDQLYQFYHQMTQNQGVQTEKSVQEIVKKLRLLARANAEDVPRVSLADEGVESGTETDVNASRSIPLNSDRLVIAPSFAKEIEKKLASVKIGDVLSETDLRQRILTEGNAISETTESLKKMIQVVKRTSEQAFNQAVMASGAENEIEMQNMKLRSLLSTKRDQISTLRTVLKSNKLTAESALTSMREKYESEKKMMMEINDKMRRELKQLKEDAATFASHRAMFTARGEELKSKVEELSNELRANEEEKKTLNQLLRLAIQQKLTLTQRLEEVEVDRDRQVFKRSSTRAPTRETYQPPRAVRYPGSTTTAQQPAPSSSGGSRGGPRRGDNQQ 737 O46382 Brefeldin ARFGEF1 9913 None SL-0198 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}. UNIPROT O46382 Pfam PF16213 Pfam PF09324 Pfam PF01369 Pfam PF12783 PROSITE PS50190 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}. GO:0005829 GO:0000139 GO:0016363 GO:0005730 GO:0048471 GO:0030532 GO:0005802 GO:0005085 GO:0034237 GO:0010256 GO:0007030 GO:0030837 GO:0034260 GO:0090303 GO:0006486 GO:0015031 GO:0032012 GO:2000114 Unknown UniProt Sequence Analysis MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKERHRQHHHLLQSPVSHHEPESPQLRYLPPQTVDHIPQEHEGDLDPQTNDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNDILYDGENHDCEEKPQDIVQSIVEEMVNIVVGDTGERTTINVSADGNNGTIEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPIFGTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQETSEMKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFTKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPAKSSKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGAKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMNVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGYTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPISGETAPPTPSPVSENQLDTISQKSVDIHDSIQPRSADNRQQAPLASVSTVNEEISKIKPTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSRKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYTDESRASAWEEVQQRLLNVCSEALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGVVFQISQPPEQELGINKQ 1849 Q9Y6D6 Brefeldin ARFGEF1 9606 None SL-0198 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. UNIPROT Q9Y6D6 UNIPROT Q9NV46 UNIPROT Q9UFV2 UNIPROT Q9UNL0 PDB 3LTL PDB 5EE5 PDB 5J5C Pfam PF16213 Pfam PF09324 Pfam PF01369 Pfam PF12783 PROSITE PS50190 OMIM 604141 DisGeNET 10565 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}. D4A631 EBI-6251296 0.40 P0DTC7 EBI-25687011 0.35 P37198 EBI-15687558 0.35 Q13459 EBI-6251244 0.56 Q5SQN1 EBI-11294278 0.37 Q9Y6D5 EBI-6249183 0.79 O75365 EBI-1074175 0.00 P0DPB3 EBI-2679560 0.00 A0A6L7HGG4 EBI-2837534 0.00 A0A3N4AWL6 EBI-2848506 0.00 P0DOE9 EBI-6138583 0.35 P05919 EBI-6175288 0.46 Q7Z4S6 EBI-6251652 0.71 Q99417 EBI-6251879 0.54 Q9UQV4 EBI-21563011 0.35 P49146 EBI-21569349 0.35 Q8N7X8 EBI-21585341 0.35 P01889 EBI-21611619 0.35 P24530 EBI-21672284 0.35 O95988 EBI-21767396 0.35 Q6DKI7 EBI-21808409 0.35 Q8TDX6 EBI-21888284 0.35 P36873 EBI-15627579 0.40 P19338 EBI-15687524 0.50 P22087 EBI-15687576 0.35 P05455 EBI-15687649 0.35 Q14432 EBI-15766317 0.58 P10644 EBI-15766462 0.50 Q14678 EBI-15953570 0.63 O15155 EBI-16788067 0.27 Q00839 EBI-20927272 0.40 P05787 EBI-20930720 0.40 Q9NU19 EBI-21228134 0.35 Q9NRI5 EBI-21370268 0.00 P0DTC5 EBI-25685699 0.35 Q5EP34 EBI-25772822 0.35 GO:0005829 GO:0005794 GO:0000139 GO:0016363 GO:0005730 GO:0005654 GO:0048471 GO:0030532 GO:0005802 GO:0005085 GO:0017022 GO:0034237 GO:0010256 GO:0006887 GO:0007030 GO:0030837 GO:0034260 GO:0090303 GO:0006486 GO:0015031 GO:0032012 GO:2000114 Unknown UniProt Sequence Analysis MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKERHRQHHHLLQSPVSHHEPESPQLRYLPPQTVDHISQEHEGDLDLHTNDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNEVLYDGENHDCEEKPQDIVQNIVEEMVNIVVGDMGEGTTINASADGNIGTIEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPIFRTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQEMSEIKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPTKSSKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMNVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPNSGETAPPPPSPVSEKPLDTISQKSVDIHDSIQPRSVDNRPQAPLVSASAVNEEVSKIKSTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYMDESRVSAWEEVQQRLLNVCSEALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGVVFQISQPPEQELGINKQ 1849 G3X9K3 Brefeldin Arfgef1 10090 None SL-0198 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}. UNIPROT G3X9K3 UNIPROT Q8BKL2 Pfam PF16213 Pfam PF09324 Pfam PF01369 Pfam PF12783 PROSITE PS50190 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}. A0A0F6B5H5 EBI-27034767 0.46 GO:0005829 GO:0005794 GO:0000139 GO:0016363 GO:0005730 GO:0005654 GO:0048471 GO:0030532 GO:0005802 GO:0005085 GO:0017022 GO:0034237 GO:0010256 GO:0007030 GO:0030837 GO:0034260 GO:0031175 GO:0051897 GO:0090303 GO:0006486 GO:0015031 GO:0032012 GO:2000114 Unknown UniProt Sequence Analysis MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKVETEKQSPPHGEAKAGSGTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGRAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMERERHRQQQHLLQSPVSHHEPESPHLRYLPPQTVDHINQEHEGDLEPQTHDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNDILYDGDYEEKPLDIVQSIVEEMVNIIVGDMGEGMAISASTEGNTGTVEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPVFRTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQEISEVKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRLFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPTKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMSVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPTSGEAEPPSPSAVSEKPLDAISQKSVDIHDSIQPRSSDNRQQAPLVSVSTVSEEVSKVKSTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYMDESRVSAWEEVQQRLLNVCREALSYFLTLTSESHREAWTNLLLLFLTKVLKISDSRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGIVFQISQPPEQELGINRQ 1846 D4A631 Brefeldin Arfgef1 10116 None SL-0198 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}. UNIPROT D4A631 Pfam PF16213 Pfam PF09324 Pfam PF01369 Pfam PF12783 PROSITE PS50190 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}. Q63358 EBI-6251135 0.51 Q13459 EBI-6251284 0.40 Q9Y6D6 EBI-6251296 0.40 P00533 EBI-22084260 0.35 GO:0005829 GO:0000139 GO:0016363 GO:0005730 GO:0048471 GO:0030532 GO:0005802 GO:0005085 GO:0017022 GO:0034237 GO:0010256 GO:0007030 GO:0030837 GO:0034260 GO:0031175 GO:0051897 GO:0090303 GO:0006486 GO:0015031 GO:0032012 GO:2000114 Unknown UniProt Sequence Analysis MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKVETEKQSPPHGEAKAGSGTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGSAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMERERHRQQHHLLQSPVSHHEPESPHLRYLPPQTVDHIAQEQEGDLDPQTHDVDKSLQDDIEPENGSDISSAENEQTEADQATAAETLSKDDVLCDGECEEKPQDIVQSIVEEMVDIIVGDMGEGTAVSASADGNAGAVEDGSDSENVQANGIPGTPISAAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPVFRTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQEISEIKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQAGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRLFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPTKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTDVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTSGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMNVAPEDRVWVRGWFPILFELSCVINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPTSGEAAPPSPSAMSEKQLDAISQKSVDIHDSAQPRSSDNRQQAPLVSVSPASEEVSKGRPTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYTDESRVSAWEEVQQRLLNVCSEALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGIVFQISQPPEQELGINKQ 1846 Q9Y6D5 Brefeldin ARFGEF2 9606 None SL-0198 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. UNIPROT Q9Y6D5 UNIPROT Q5TFT9 UNIPROT Q9NTS1 PDB 3L8N PDB 3SWV Pfam PF16213 Pfam PF09324 Pfam PF01369 Pfam PF12783 PROSITE PS50190 OMIM 605371 OMIM 608097 DisGeNET 10564 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}. 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. P10909 EBI-21370252 0.00 O75400 EBI-7243480 0.37 A0A3P1UC63 EBI-2837508 0.00 A0A6L7HB40 EBI-2837541 0.00 A0A6L8PCK7 EBI-2837527 0.00 Q13573 EBI-7950968 0.35 P0DOE9 EBI-6138583 0.35 P05919 EBI-6175288 0.46 Q9Y6D6 EBI-6249183 0.79 Q9UPT5 EBI-6251422 0.51 P19438 EBI-6251604 0.46 Q99417 EBI-6251858 0.54 P31323 EBI-6258808 0.46 Q15116 EBI-21506827 0.35 Q13477 EBI-21555701 0.35 P06028 EBI-21557067 0.35 Q9UQV4 EBI-21563011 0.35 P05362 EBI-21568860 0.35 Q8N7X8 EBI-21585341 0.35 P01889 EBI-21611619 0.35 Q96G30 EBI-21633324 0.35 Q6EMK4 EBI-21651359 0.35 P40259 EBI-21668943 0.35 P24530 EBI-21672284 0.35 Q86XD5 EBI-21711466 0.35 Q9BRK5 EBI-21763329 0.35 Q9BZW8 EBI-21787892 0.35 Q9NQ34 EBI-21788287 0.35 Q8TDX6 EBI-21888284 0.35 P36873 EBI-15627562 0.40 Q14432 EBI-15766317 0.50 P10644 EBI-15766425 0.35 O43493 EBI-16800265 0.27 P0DTC5 EBI-26495256 0.53 GO:0070161 GO:0032279 GO:0005879 GO:0031410 GO:0005829 GO:0043197 GO:0005794 GO:0000139 GO:0043231 GO:0016020 GO:0005815 GO:0048471 GO:0055037 GO:0032280 GO:0005802 GO:0050811 GO:0005085 GO:0017022 GO:0034237 GO:0010256 GO:0007032 GO:0006887 GO:0006893 GO:0035556 GO:0032760 GO:0015031 GO:0001881 GO:0032012 Unknown UniProt Sequence Analysis MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAEIEKQRLGTAAPPKANFIEADKYFLPFELACQSKSPRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETICSCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTILQTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPIQSKPQSPVIQAAAVSPKFVRLKHSQAQSKPTTPEKTDLTNGEHARSDSGKVSTENGDAPRERGSSLSGTDDGAQEVVKDILEDVVTSAIKEAAEKHGLTEPERVLGELECQECAIPPGVDENSQTNGIADDRQSLSSADNLESDAQGHQVAARFSHVLQKDAFLVFRSLCKLSMKPLGEGPPDPKSHELRSKVVSLQLLLSVLQNAGPVFRTHEMFINAIKQYLCVALSKNGVSSVPDVFELSLAIFLTLLSNFKMHLKMQIEVFFKEIFLNILETSTSSFEHRWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRSGHELGMTPLQELSLRKKGLECLVSILKCMVEWSKDLYVNPNHQTSLGQERLTDQEIGDGKGLDMARRCSVTSMESTVSSGTQTTVQDDPEQFEVIKQQKEIIEHGIELFNKKPKRGIQFLQEQGMLGTSVEDIAQFLHQEERLDSTQVGDFLGDSARFNKEVMYAYVDQLDFCEKEFVSALRTFLEGFRLPGEAQKIDRLMEKFAARYIECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSSIYEEIEGKKIAMKETKELTIATKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHAKAPFTSATHLDHVRPMFKLVWTPLLAAYSIGLQNCDDTEVASLCLEGIRCAIRIACIFGMQLERDAYVQALARFSLLTASSSITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKTRYLSGSGREREGSLKGHTLAGEEFMGLGLGNLVSGGVDKRQMASFQESVGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSLQKIVEISYYNMNRIRLQWSRIWHVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKKNRSPTIRDMAIRCIAQMVNSQAANIRSGWKNIFAVFHQAASDHDGNIVELAFQTTCHIVTTIFQHHFPAAIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRFCGKYVSERPRVLQEYTSDDMNVAPGDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKSYGHTFEKHWWQDLFRIVFRIFDNMKLPEQLSEKSEWMTTTCNHALYAICDVFTQFYEALNEVLLSDVFAQLQWCVKQDNEQLARSGTNCLENLVISNGEKFSPEVWDETCNCMLDIFKTTIPHVLLTWRPVGMEEDSSEKHLDVDLDRQSLSSIDKNPSERGQSQLSNPTDDSWKGRPYANQKLFASLLIKCVVQLELIQTIDNIVFYPATSKKEDAEHMVAAQQDTLDADIHIETEDQGMYKYMSSQHLFKLLDCLQESHSFSKAFNSNYEQRTVLWRAGFKGKSKPNLLKQETSSLACCLRILFRMYVDENRRDSWEEIQQRLLTVCSEALAYFITVNSESHREAWTSLLLLLLTKTLKINDEKFKAHASMYYPYLCEIMQFDLIPELRAVLRKFFLRIGVVYKIWIPEEPSQVPAALSPVW 1785 A2A5R2 Brefeldin Arfgef2 10090 None SL-0198 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}. UNIPROT A2A5R2 Pfam PF16213 Pfam PF09324 Pfam PF01369 Pfam PF12783 PROSITE PS50190 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}. Q8BP00 EBI-4283417 0.35 Q91WZ8 EBI-16749137 0.35 GO:0070161 GO:0032279 GO:0005879 GO:0005737 GO:0031410 GO:0005829 GO:0043197 GO:0005794 GO:0000139 GO:0043231 GO:0016020 GO:0005815 GO:0048471 GO:0055037 GO:0032280 GO:0005802 GO:0050811 GO:0005085 GO:0017022 GO:0034237 GO:0010256 GO:0007032 GO:0006887 GO:0006893 GO:0035556 GO:0032760 GO:0015031 GO:0001881 GO:0032012 Unknown UniProt Sequence Analysis MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAELEKQRLGAAAPPKANFIEADKYFLPFELACQSKSPRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETICNCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTILQTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPMQSKPQSPVIQATAGSPKFSRLKQSQAQSKPTTPEKAELPNGDHAQSGLGKVSLENGEAPRERGSPVSGRAEPSRGTDSGAQEVVKDILEDVVTSAVKEAAEKHGLPEPDRALGALECQECAVPPGVDENSQTNGIADDRQSLSSADNLEPDVQGHQVAARFSHILQKDAFLVFRSLCKLSMKPLGEGPPDPKSHELRSKVVSLQLLLSVLQNAGPVFRSHEMFVTAIKQYLCVALSKNGVSSVPDVFELSLAIFLTLLSNFKMHLKMQIEVFFKEIFLNILETSTSSFEHRWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRSGHELGMTPLQELSLRKKGLECLVSILKCMVEWSKDLYVNPNHQATLGQERLPDQEMGDGKGLDMARRCSVTSVESTVSSGTQTAIQDDPEQFEVIKQQKEIIEHGIELFNKKPKRGIQFLQEQGMLGAAVEDIAQFLHQEERLDSTQVGEFLGDSTRFNKEVMYAYVDQLDFCEKEFVSALRTFLEGFRLPGEAQKIDRLMEKFAARYIECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSSIYDEIEGKKIAMKETKEHTIATKSTKQSVASEKQRRLLYNVEMEQMAKTAKALMEAVSHAKAPFTSATHLDHVRPMFKLVWTPLLAAYSIGLQNCDDTEVASLCLEGIRCAVRIACIFGMQLERDAYVQALARFSLLTASSSITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKTRYLSGSGREREGSLKGHSLAGEEFMGLGLGNLVSGGVDKRQMASFQESVGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSLQKIVEISYYNMNRIRLQWSRIWHVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKKNRSPTIRDMVIRCIAQMVSSQAANIRSGWKNIFAVFHQAASDHDGNIVELAFQTTGHIVSTIFQHHFPAAIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRFCGKYVSERPRVLQEYTSDDMNVAPGDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKSYGHTFAKHWWQDLFRIVFRIFDNMKLPEQQSEKSEWMTTTCNHALYAICDVFTQFYEALHEVLLSDVFAQLQWCVKQDNEQLARSGTNCLENLVISNGEKFSPAVWDETCNCMLDIFKTTIPHVLLTWRPAGMEEEVSDRHLDVDLDRQSLSSIDRNASERGQSQLSNPTDDSWKGAPYAHQKLLASLLIKCVVQLELIQTIDNIVFYPATSKKEDAEHMVAAQQDTLDAEIHIETENQGMYKFMSSQHLFKLLDCLQESHSFSKAFNSNYEQRTVLWRAGFKGKSKPNLLKQETSSLACCLRILFRMYVDENRRDSWDEIQQRLLRVCSEALAYFITVNSESHREAWTSLLLLLLTKTLKISDEKFKAHASMYYPYLCEIMQFDLIPELRAVLRKFFLRIGLVYKIWIPEEPSQVPAALSSTW 1792 Q7TSU1 Brefeldin Arfgef2 10116 None SL-0198 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}. UNIPROT Q7TSU1 Pfam PF16213 Pfam PF09324 Pfam PF01369 Pfam PF12783 PROSITE PS50190 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}. P15431 EBI-6257990 0.37 P63079 EBI-6257978 0.53 P63138 EBI-6258080 0.37 P62813 EBI-6258190 0.40 P14867 EBI-6258248 0.27 P28472 EBI-6258248 0.27 P40748 EBI-21282580 0.35 P22607 EBI-22244643 0.35 P15498 EBI-22257448 0.35 GO:0070161 GO:0032279 GO:0005879 GO:0005737 GO:0031410 GO:0005829 GO:0043197 GO:0000139 GO:0016020 GO:0005815 GO:0048471 GO:0055037 GO:0032280 GO:0005802 GO:0050811 GO:0005085 GO:0017022 GO:0034237 GO:0010256 GO:0007032 GO:0006887 GO:0006893 GO:0035556 GO:0032760 GO:0015031 GO:0001881 GO:0032012 Unknown UniProt Sequence Analysis MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAELEKQRLGAAAPPKANFIEADKYFLPFELACQSKSPRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETVCNCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTILQTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPIQSKPQSPVIQATAGSPKFSRLKQSQAQSKPTTPEKTELPNGDHARSSLGKVNSENGEAHRERGSSISGRAEPSGGSDNGAQEVVKDILEDVVTSAVKEAAEKQGLPEPDQAPGVPECQECTVPPAVDENSQTNGIADDRQSLSSADNLEPDAQGHPVAARFSHILQKDAFLVFRSLCKLSMKPLGEGPPDPKSHELRSKVVSLQLLLSVLQNAGPVFRSHEMFVTAIKQYLCVALSKNGVSSVPDVFELSLAIFLTLLSNFKMHLKMQIEVFFKEIFLNILETSTSSFEHRWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRSGHELGMTPLQELSLRKKGLECLVSILKCMVEWSKDLYVNPNHQATLGQERLPDQEMGDGKGLDMARRCSVTSVESTVSSGTQTAIPDDPEQFEVIKQQKEIIEHGIELFNKKPKRGIQFLQEQGMLGAAVEDIAQFLHQEERLDSTQVGEFLGDSTRFNKEVMYAYVDQLDFCEKEFVSALRTFLEGFRLPGEAQKIDRLMEKFAARYIECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSSIYEEIEGKKIAMKETKEHTMATKSTKQNVASEKQRRLLYNVEMEQMAKTAKALMEAVSHAKAPFTSATHLDHVRPMFKLVWTPLLAAYSIGLQNCDDTEVASLCLEGIRCAVRIACIFGMQLERDAYVQALARFSLLTASSSITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKTRYLSGSGREREGSLKGHSLAGEEFMGLGLGNLVSGGVDKRQMASFQESVGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSLQKIVEISYYNMNRIRLQWSRIWHVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKKNRSPTIRDMVIRCIAQMVSSQAANIRSGWKNIFAVFHQAASDHDGNIVELAFQTTGHIVSTIFQHHFPAAIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRFCGKYVSERPRVLQEYTSDDMNVAPGDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKSYGHTFAKHWWQDLFRIVFRIFDNMKLPEQQSEKSEWMTTTCNHALYAICDVFTQFYEALHEVLLSDVFAQLQWCVKQDNEQLARSGTNCLENLVISNGEKFSPAVWDETCNCMLDIFRTTIPHVLLTWRPAGMEEEVSDRHLDVDLDRQSLSSIDRNASERGQSQLSNPTDDSWKGAPYANQKLLASLLIKCVVQLELIQTIDNIVFYPATSKKEDAEHMVAAQQDTLDADIHIETENQGMYKFMSSQHLFKLLDCLQESHSFSKAFNSNYEQRTVLWRAGFKGKSKPNLLKQETSSLACCLRILFRMYVDENRRDSWGEIQQRLLTVCSEALAYFITVNSESHREAWTSLLLLLLTKTLKINDEKFKAHASVYYPYLCEMMQFDLIPELRAVLRKFFLRIGLVYKIWVPEEPSQVPAASTAW 1791 I6V1W0 Protein bmb 7955 None SL-0178 SL-0182 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. UNIPROT I6V1W0 Required for nuclear membrane fusion during karyogamy. {ECO:0000269|PubMed:22863006}. GO:0016021 GO:0031965 GO:0061472 GO:0007344 Transmembrane UniProt Sequence Analysis {ECO:0000255} MALWFVLLWVSSLQYAEVEAFFDWLKKADPAPTPPPAESIVPILLHGEAPAFEMSVVDEKFLAEAKQMELSPLDSCHFRVVAQLKATCSGLSEEQLAKLGVALFNCQSEVEGRRTYPCTEEMSIKECTADMDSDTWNAYHIVSNRARSVCYATRQQHFRKRAELTVNALISTATSQLDAMKDLKEGQKELRDMTAASLDKLLEGHGALQIQQGALKEGQEQLDASISENLQRLAQEKALISTGQQLVAQLIQGITQRMENVSGQLKDQTAEVQEGHQAILEDLAVVRGSAQDIYEKMELNLNGFLQQQNTTAHFYTELMRKLELMNGTLGYMLTYLDNMQTRLEDRLHMIQGYLGWAGLSLRALWTCVMHAGYFLLCAVLLSFLQCTTFSRVTLLLSVPINAIAEINQQAALDLISLTLLLFTLSLGRWFVLQLLWALSKIKGRTCSRPPHLSIYPPKEKTPEKQHEFGEKCPASSSTPVQSDPVCDLEVESFMMGDPCVLGVSPSRCPPKFSHHHLGGTPNHSTPRLKSRHSIAATELDNIPQRNLGVFLETVNRSRSSSPNQSLASSSSFSGRSLCSGITRLGQPCKKRAVVGQDYCRVHEGGHTSYSRL 612 Q3T013 BCL2/adenovirus BNIP3L 9913 None SL-0178 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}. UNIPROT Q3T013 UNIPROT A5D9C5 Pfam PF06553 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}. GO:0005783 GO:0016021 GO:0005741 GO:0005739 GO:0005635 GO:0005634 GO:0042802 GO:0051607 GO:0097345 GO:0035694 GO:0043065 GO:0043067 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSSHLVEQPPPPHNNNNNCEEGEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSKDHSSQSEEEVAEGEKEVDALKKSVDWVSDWSSRPENIPPKEFHFRHPKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY 219 O60238 BCL2/adenovirus BNIP3L 9606 None SL-0178 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. UNIPROT O60238 UNIPROT B0AZS9 UNIPROT Q5JW63 UNIPROT Q8NF87 Pfam PF06553 OMIM 605368 DisGeNET 665 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}. A0PK00 EBI-24405238 0.56 Q6NUQ1 EBI-737555 0.00 Q9P104 EBI-752488 0.37 Q01844 EBI-753931 0.37 O60238 EBI-755134 0.86 Q12983 EBI-757996 0.96 P17152 EBI-758767 0.84 P03247 EBI-849900 0.65 Q12982 EBI-849923 0.37 P02545 EBI-849933 0.37 Q92934 EBI-850652 0.44 P10415 EBI-850662 0.44 P38182 EBI-7679661 0.67 Q9H492 EBI-7680248 0.61 Q81X61 EBI-2817764 0.00 Q81TT4 EBI-2837471 0.00 A0A2U2GZW8 EBI-2848492 0.00 Q7CIP6 EBI-2874847 0.00 A0A380PE22 EBI-2874840 0.00 Q9NRQ5 EBI-8640186 0.78 Q9BXN2 EBI-8656262 0.67 P51452 EBI-3904946 0.37 Q16610 EBI-3904966 0.37 O14936 EBI-3906243 0.37 Q8IU85 EBI-3912671 0.37 P32456 EBI-7104878 0.37 O14775 EBI-7104942 0.37 Q8NBE8 EBI-7105008 0.37 Q9HCK4 EBI-7105110 0.37 Q9NQ11 EBI-6377441 0.51 Q5T700 EBI-10186247 0.67 Q969F0 EBI-10186257 0.56 Q9H2S6 EBI-24287972 0.56 Q13021 EBI-25259116 0.56 P60520 EBI-24378093 0.56 O43169 EBI-24422195 0.56 Q9H0R8 EBI-24427438 0.56 Q9NRS4 EBI-24447859 0.56 Q15848 EBI-12697535 0.56 Q9Y4P8 EBI-21766966 0.35 P22736 EBI-16085278 0.54 Q8NI37 EBI-21934639 0.35 P41595 EBI-20808451 0.37 Q96H55 EBI-25476634 0.35 Q9P0W8 EBI-25476634 0.35 O43464 EBI-25476634 0.35 Q96IX5 EBI-25476634 0.35 P0DTD8 EBI-25687199 0.35 Q7TFA1 EBI-25688644 0.35 A0A663DJA2 EBI-28953729 0.56 GO:0005783 GO:0016021 GO:0031224 GO:0005741 GO:0005739 GO:0005635 GO:0016607 GO:0005634 GO:0042802 GO:0005521 GO:0042803 GO:0071456 GO:0051607 GO:0097345 GO:0035694 GO:0043066 GO:0060548 GO:0043065 GO:0016239 GO:1903146 GO:0043067 GO:1903214 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY 219 Q9Z2F7 BCL2/adenovirus Bnip3l 10090 None SL-0178 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}. UNIPROT Q9Z2F7 UNIPROT Q545J6 Pfam PF06553 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}. Q69ZI1 EBI-1774643 0.58 Q9GZQ8 EBI-7679879 0.61 Q9H0R8 EBI-7679924 0.57 P60520 EBI-7679985 0.54 O95166 EBI-7679950 0.54 Q9H492 EBI-7680044 0.65 P38182 EBI-7680182 0.44 GO:0005829 GO:0005783 GO:0016021 GO:0005741 GO:0005739 GO:0005635 GO:0016607 GO:0005634 GO:0042802 GO:0005521 GO:0042803 GO:0071456 GO:0051607 GO:0097345 GO:0035694 GO:0043066 GO:0060548 GO:0010917 GO:0043065 GO:0016239 GO:0035794 GO:1903146 GO:0043067 GO:1903214 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSHLVEPPPPLHNNNNNCEEGEQPLPPPAGLNSSWVELPMNSSNGNENGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRAASLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY 218 Q12982 BCL2/adenovirus BNIP2 9606 None SL-0198 Cytoplasm. Cytoplasm, perinuclear region. Note=Localizes to the nuclear envelope region and to other cytoplasmic structures. UNIPROT Q12982 UNIPROT B4DS94 Pfam PF12496 Pfam PF13716 PROSITE PS50191 OMIM 603292 DisGeNET 663 Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins. O14681 EBI-24742623 0.56 O60238 EBI-849923 0.37 P03247 EBI-849887 0.37 P10415 EBI-849945 0.37 O43889 EBI-760141 0.37 Q8ZAE1 EBI-2874833 0.00 P42685 EBI-8640766 0.83 P08107 EBI-5659534 0.00 B2R9H7 EBI-10175714 0.56 Q07866 EBI-10224717 0.56 Q969F0 EBI-10227522 0.72 Q9ULV0 EBI-10227532 0.56 Q8IUY3 EBI-24286337 0.56 Q6FHY5 EBI-24288305 0.56 Q92520 EBI-24296511 0.56 O75477 EBI-24319282 0.56 P50221 EBI-24506124 0.56 O95070 EBI-24520784 0.56 O15499 EBI-24526443 0.56 Q9NRZ7 EBI-24609790 0.56 Q6P587 EBI-24614147 0.56 Q96Q45 EBI-24619126 0.56 P0C671 EBI-24627238 0.56 Q6ZPD8 EBI-24631723 0.56 H3BQL7 EBI-23670177 0.56 Q8TED1 EBI-24667727 0.56 Q9UH17 EBI-24673525 0.56 Q8TB40 EBI-23694319 0.56 Q8TDT2 EBI-24684836 0.56 Q7Z769 EBI-24696473 0.56 P00387 EBI-24717088 0.56 Q7Z7G2 EBI-24717755 0.56 P21579 EBI-24733989 0.56 Q9Y320 EBI-23808606 0.56 Q9NUM3 EBI-24742735 0.56 Q5T7V8 EBI-24753105 0.56 O95562 EBI-24755839 0.56 Q9BSY9 EBI-24793885 0.56 Q5JX71 EBI-25279273 0.56 Q8N9I0 EBI-25280067 0.56 Q12983 EBI-24385418 0.56 Q5T700 EBI-24407207 0.56 Q8TDF6 EBI-24570628 0.56 P32243 EBI-24572235 0.56 Q96LJ7 EBI-24573986 0.56 O15393 EBI-24575163 0.56 Q9H9P2 EBI-24641706 0.56 Q8TBB6 EBI-24647910 0.56 Q53GL0 EBI-24648150 0.56 Q9H400 EBI-24652262 0.56 O00623 EBI-24758990 0.56 O95279 EBI-24798641 0.56 Q07960 EBI-20733446 0.27 GO:0005737 GO:0005829 GO:0043231 GO:0005635 GO:0005730 GO:0048471 GO:0005509 GO:0005096 GO:0006915 GO:0043066 GO:0090649 Unknown UniProt Sequence Analysis MEGVELKEEWQDEDFPIPLPEDDSIEADILAITGPEDQPGSLEVNGNKVRKKLMAPDISLTLDPSDGSVLSDDLDESGEIDLDGLDTPSENSNEFEWEDDLPKPKTTEVIRKGSITEYTAAEEKEDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDGLNAIVVFAVCFMPESSQPNYRYLMDNLFKYVIGTLELLVAENYMIVYLNGATTRRKMPSLGWLRKCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQVDQELNGKQDEPKNEQ 314 O54940 BCL2/adenovirus Bnip2 10090 None SL-0198 Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localizes to the nuclear envelope region and to other cytoplasmic structures. {ECO:0000250}. UNIPROT O54940 UNIPROT Q8K4H0 Pfam PF12496 Pfam PF13716 PROSITE PS50191 Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins (By similarity). {ECO:0000250}. GO:0005814 GO:0005737 GO:0005829 GO:0043231 GO:0005635 GO:0005730 GO:0048471 GO:0031616 GO:0006915 GO:0001824 GO:0007098 GO:0043410 GO:0045666 GO:0051057 GO:0051146 Unknown UniProt Sequence Analysis MEGVELKEEWQDEDFPIPLPEDDSIEADTLDGTDPDRQPGSLEVNGNKVRKKLMAPDISLTLDPGEDSLWSDDLDEAGEVDLEGLDTPSENSDEFEWEDDLPKPKTTEVIRKGSITEYTATEEKGDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDGLNAIVVFAVCFMPESGQPNYRYLMDNLFKYVIGTLELLVAENYMIIYLNGATTRRKMPSLGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQYEEEKFKKRQKRVDQELNGKQEPPKSEQ 326 Q709R6 LEM bocks 7227 None SL-0178 SL-0179 SL-0182 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}. UNIPROT Q709R6 UNIPROT Q8SZZ5 UNIPROT Q9VHA7 Pfam PF03020 PROSITE PS50954 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}. O76454 EBI-256393 0.00 Q7JR34 EBI-268668 0.00 Q9VC86 EBI-279174 0.00 Q06559 EBI-281575 0.00 Q9VVQ1 EBI-282628 0.00 Q9VLU0 EBI-282809 0.00 O01666 EBI-283293 0.00 Q94524 EBI-26751768 0.49 GO:0005737 GO:0005783 GO:0016021 GO:0005635 GO:0005637 GO:0005654 GO:0007049 GO:0051301 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSDLSYLDTLGNKELLAKCLEHGLPGVPVTDSTRSVIIRRLKAKITGVPLNKSKSASKKAIPRRETVHGSQVTTPTSEPVRRTPGKSAGRTSSNNNKISEQSRRTIAYGLDNTSISGRSVQTTTTVSDMSSQSEDDDSYMVDSPVPNYSKDQQPRRYVSLAKSGVLTTSYTREVDQPLYEQEDIPRSYTYERPHVPAATLHALPTYEPRIEPSTYRPTDLGFSRPLLTQTNLNSTSYEESSTYNPKLSPISPRNTFSGSARPFGGPAPAPAPIRQRQSVPVSGSNLARGRLLQPTTAVNTLYPQLNEFYDQPNDAGEPMETESESEVEEVPINSHFQKNRFSPLARKPLVRHHDQVSPMAQFRALAVSLDQKYNLKFYLILVVSVMLATMVYVVLTPNA 399 Q9UMX3 Bcl-2-related BOK 9606 None SL-0178 SL-0182 SL-0183 [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}. UNIPROT Q9UMX3 PDB 6CKV Pfam PF00452 PROSITE PS50062 OMIM 605404 DisGeNET 666 [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}. Q8NC60 EBI-7105200 0.37 A2RU30 EBI-21861544 0.35 P13637 EBI-25832700 0.56 P50570 EBI-25844480 0.56 Q86V38 EBI-25846172 0.56 P10809 EBI-25872088 0.56 P16284 EBI-25881099 0.56 Q8TB36 EBI-25923268 0.56 GO:0033106 GO:0005737 GO:0031901 GO:0005783 GO:0005789 GO:0005794 GO:0016021 GO:0016020 GO:0005743 GO:0031966 GO:0005741 GO:0005739 GO:0005640 GO:0005634 GO:0055038 GO:0032588 GO:0051400 GO:0046982 GO:0042803 GO:0044877 GO:0005102 GO:0031625 GO:0006919 GO:0008635 GO:0006915 GO:0007420 GO:0006921 GO:0097192 GO:0072332 GO:0008630 GO:0008584 GO:0051902 GO:1901029 GO:0060546 GO:0043524 GO:0051402 GO:0048709 GO:0043065 GO:1902237 GO:1900119 GO:2001244 GO:1901030 GO:1903899 GO:0051259 GO:0010506 GO:1901382 GO:0051480 GO:1904708 GO:0001836 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERAAPVPGRLAEVCAVLLRLGDELEMIRPSVYRNVARQLHISLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYAVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKTLATWLRRRGGWTDVLKCVVSTDPGLRSHWLVAALCSFGRFLKAAFFVLLPER 212 O35425 Bcl-2-related Bok 10090 None SL-0178 SL-0182 SL-0183 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}. UNIPROT O35425 Pfam PF00452 PROSITE PS50062 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}. GO:0033106 GO:0005737 GO:0031901 GO:0005783 GO:0005789 GO:0005794 GO:0016021 GO:0016020 GO:0005743 GO:0031966 GO:0005741 GO:0005739 GO:0005640 GO:0005634 GO:0055038 GO:0032588 GO:0051400 GO:0046983 GO:0046982 GO:0042803 GO:0044877 GO:0005102 GO:0031625 GO:0006919 GO:0008635 GO:0006915 GO:0007420 GO:0006921 GO:0097192 GO:0072332 GO:0008630 GO:0008584 GO:0051902 GO:1901029 GO:0060546 GO:0043524 GO:0051402 GO:0048709 GO:0043065 GO:1902237 GO:1900119 GO:2001244 GO:1901030 GO:1903899 GO:0051259 GO:0010506 GO:1901382 GO:0051480 GO:1904708 GO:0001836 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQIRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKTLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER 213 Q792S6 Bcl-2-related Bok 10116 None SL-0178 SL-0182 SL-0183 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}. UNIPROT Q792S6 UNIPROT O88857 Pfam PF00452 PROSITE PS50062 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}. GO:0033106 GO:0005737 GO:0031901 GO:0005783 GO:0005789 GO:0005794 GO:0016021 GO:0016020 GO:0005743 GO:0031966 GO:0005741 GO:0005739 GO:0005640 GO:0005634 GO:0055038 GO:0032588 GO:0051400 GO:0046983 GO:0046982 GO:0042803 GO:0044877 GO:0005102 GO:0031625 GO:0006919 GO:0008635 GO:0006915 GO:0007420 GO:0006921 GO:0097192 GO:0072332 GO:0008630 GO:0008584 GO:0051902 GO:1901029 GO:0060546 GO:0043524 GO:0051402 GO:0048709 GO:0043065 GO:1902237 GO:1900119 GO:2001244 GO:1901030 GO:1903899 GO:0051259 GO:0010506 GO:1901382 GO:0051480 GO:1904708 GO:0001836 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQIRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKTLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER 213 P42674 Blastula BP10 7656 None SL-0198 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. UNIPROT P42674 Pfam PF01400 Pfam PF00431 PROSITE PS51864 PROSITE PS01180 PROSITE PS00022 PROSITE PS01186 PROSITE PS50026 PROSITE PS00142 Could be involved in the differentiation of ectodermal lineages and subsequent patterning of the embryo. GO:0005938 GO:0005615 GO:0048471 GO:0004222 GO:0008270 GO:0006508 Unknown UniProt Sequence Analysis MKLILFLSGLVSLVLCTLAAPTGDQKEIHTETPPPKKPSETTTPGALKTPQPEPKDEEPTPGAFQGDMMLTEDQQRESKEAIDDEMTGRKKRKATIYESQRWPYKVIPYVISPSSSGQSSLIRNAMDHWEQNTCLRFEPRTSSHSRQLGHNAYLSFFRGSGCWSYVGKAFNGEQQISIGNGCAYFGTIVHEIGHAIGFHHEQSRPDRDDYINVLYQNIQSGRQHNFAKYTWGRVTSRNVEYDVGSIMHYGGYGFSSNGRPTITTRDPRLNSRLGQRIALSPADIELANLIYECDDIEDCAGANECLNGGYHDTECNCVCPSGYNGDLCEDAVTTTRPDCSERFTEMTGVITSPNWPGRYEDNMACVYQIEGPPGSTIELTFTEMNIENHAACRYDAVEVRKDDINSDGEKFCGNTLPAVQISSGNQMLISFTSDPSITGRGFRATYRIVILTTTQIPDTTTISTTTPVPTTTQATTDETVVGSCGGSFGGTQGRVATPNYPNNYDNDLECVYVIEVEIGRRVELDFIDFVLEDETNCRWDSLSINLGDGIKIDMKMCGREYPAASLVSIGNNMELTLISDRSVTDRGFMADYRAIDL 597 O74510 Bouquet bqt3 284812 None SL-0178 SL-0179 SL-0182 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}. UNIPROT O74510 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}. GO:0005789 GO:0005637 GO:1990862 GO:0140473 GO:0051301 GO:0045141 GO:0032200 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSGSKCCSSSNTIKVSIYLFLHTLTYGLLNYHLNPRLLASTGVVESDIPYWMSYLSIIMHVGQSLLLQKFNLGYGWLLLTKYPVYVLLSTYYLTPLSQIAWAFIIDAISLLVARCFSRANPIKCSNQVNTQYSVSFLFTIMASVLISVLNYISQKIFLNGLILGNSHNVVTSLVAPPLPLQYLAHVPIGYVIQRVVFSERPIPQSLFLMIFLTLWNCFIPYSILFSMNWSAMFQVVGAYLSQIWIITFICWALSL 255 O60158 Bouquet bqt4 284812 None SL-0178 SL-0179 SL-0182 Cytoplasm {ECO:0000305}. Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. Nucleus inner membrane {ECO:0000269|PubMed:19948484}; Peripheral membrane protein {ECO:0000305}. UNIPROT O60158 UNIPROT Q9USF5 PDB 5YBX PDB 5YC2 PDB 5YCA PDB 6A6W PROSITE PS51299 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}. GO:0005737 GO:0005635 GO:0005637 GO:1990862 GO:0005634 GO:0003677 GO:0140473 GO:0051301 GO:0070197 GO:0045141 GO:0044820 GO:0000723 GO:0032200 Peripheral UniProt Curator Inference {ECO:0000305} MTENEKSRSLPAERNPLYKDDTLDHTPLIPKCRAQVIEFPDGPATFVRLKCTNPESKVPHFLMRMAKDSSISATSMFRSAFPKATQEEEDLEMRWIRDNLNPIEDKRVAGLWVPPADALALAKDYSMTPFINALLEASSTPSTYATPSRPTAQKSETSEGEPESSTSATTTSVARRTRQRLAEHLENSKKTILQHDNKEEDKEIHSEENETKDEIKSEKKEPEIKKQEGGSSTEKVGQPSSSDDKAKGSTSKDQPSEEEEKTSDIQDRKIKTPIKPSLLGKIRSSVNKGMTDVASQVNRGMTDVASQVNKGVNGVASQVNKGMNGVANQVNKGVTGVASQVRKPVGKLEKKFENLEKSIGDTLKSSIRSSPKSKKRSREDFEENEDYNAMVPVKRSRITKLESEVYYEKRKVRALGGIAIGLGVGAILPFLF 432 Q32L83 Brain BRI3 9913 None SL-0198 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}. UNIPROT Q32L83 Pfam PF10164 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}. GO:0016021 GO:0005765 GO:0048471 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDHKPLLQERPPAYNLEAGQGEFACAPHGYGAIAAAPPPPYPYLVTGIPTHHPRVYNIHSRNVTRYPANSIVVVGGCPVCRVGVLEDSFTFLGIFLAIVLFPFGFICCFALRKRRCPNCGANFT 124 Q99N46 Brain I3 10141 None SL-0198 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}. UNIPROT Q99N46 Pfam PF10164 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}. GO:0016021 GO:0005765 GO:0048471 GO:0042802 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDHKPLLQERPPAYNLEAGQGDYACGAPGYGAIPSAPPPPPYPYLVTGIPTPHPRVYSIHSRTVTRYPANSIVVVGGCPVCRVGVLEDCFTFLGIFLAIILFPFGFICCFALRKRRCPNCGATFT 125 O95415 Brain BRI3 9606 None SL-0198 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}. UNIPROT O95415 UNIPROT D6W5R8 UNIPROT F5GXW6 UNIPROT Q8WV52 UNIPROT Q9UIC6 Pfam PF10164 OMIM 615628 DisGeNET 25798 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}. A0A380PDF6 EBI-2874795 0.00 Q13021 EBI-24525743 0.56 O95870 EBI-24537575 0.56 Q01628 EBI-25503997 0.54 P26572 EBI-25504004 0.54 P16871 EBI-25507926 0.37 Q8WY22 EBI-25504211 0.57 P46934 EBI-30832228 0.44 P46937 EBI-30846229 0.44 GO:0035577 GO:0016021 GO:0005634 GO:0048471 GO:0005886 GO:0042802 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDHKPLLQERPPAYNLEAGQGDYACGPHGYGAIPAAPPPPPYPYLVTGIPTHHPRVYNIHSRTVTRYPANSIVVVGGCPVCRVGVLEDCFTFLGIFLAIILFPFGFICCFALRKRRCPNCGATFA 125 P28662 Brain Bri3 10090 None SL-0198 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}. UNIPROT P28662 UNIPROT Q501N3 UNIPROT Q9Z1S1 Pfam PF10164 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}. GO:0016021 GO:0005765 GO:0048471 GO:0042802 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDHKPLLQERPPAYNLEAGQGDYACGPHGYGAIPTAPPPPPYPYLVTGIPTSHPRVYNIHSRTVTRYPANSIVVVGGCPVCRVGVLEYCFTCLGIFLAIVLFPFGFLCCFALRKRRCPNCGAVFT 125 Q5PPK1 Brain Bri3 10116 None SL-0198 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}. UNIPROT Q5PPK1 Pfam PF10164 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}. GO:0016021 GO:0005765 GO:0048471 GO:0042802 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDHKPLLQERPPAYNLEAGQGDYACGPHGYGAIPTAPPPPPYPYLVTGIPTSHPRVYNIHSRAVTRYPANSIVVVGGCPVCRVGVLEYCFTCLGIFLAIVLFPFGFLCCFALRKRRCPNCGAVFT 125 P38770 Nucleus BRL1 559292 None SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:15882446}; Multi-pass membrane protein {ECO:0000269|PubMed:15882446}. UNIPROT P38770 UNIPROT D3DKY3 Pfam PF10104 Involved in mRNA and protein export from nucleus. {ECO:0000269|PubMed:15882446}. P16140 EBI-800112 0.35 P09733 EBI-800112 0.35 P32589 EBI-800112 0.53 P11484 EBI-800112 0.53 P10592 EBI-800112 0.53 P12709 EBI-800112 0.35 P06169 EBI-800112 0.35 P04147 EBI-800112 0.35 P15108 EBI-800112 0.35 P47088 EBI-856804 0.00 P02829 EBI-864646 0.00 P13393 EBI-7738433 0.44 P29056 EBI-8224002 0.22 P46985 EBI-2347758 0.37 P10591 EBI-3667891 0.35 P33416 EBI-3743771 0.35 Q12329 EBI-3750479 0.35 Q9UJW9 EBI-11529461 0.56 Q9BXL8 EBI-11529452 0.56 GO:0005783 GO:0016021 GO:0005635 GO:0031965 GO:0055088 GO:0051028 GO:0006998 GO:0015031 Transmembrane UniProt Sequence Analysis {ECO:0000255} MESFENLSIRDSFTSGMEHVDEELGGLSDLSISKQGPTLSPQLINRFMPHFPSSPSPLRNTLDFSAAKADEEEDDRMEIDEVDDTSFEEEYNNEPIETHTEATENAVVEEIEATPEERQKQEKNESQDQSVEEVENIVSPHRSTVIKALLSPTDLGVAAATKVEGVVPLPPSANQDDNESSNNNAEGEDIIRNEEVEDEIKSSLGNHKSSQYANAFDSEIIKRELRSRSKYQPIQVSFNTHNYFYSDKDGIKTYSLTKPNHNKIDEFYDQNEAFKLPKPWSPNSHPASRASYALMSYLQLFLNAITTVVIFSFILSFIIALQKDLKSTWEQRKHELQYESRICQEQYLTNRCNQTPGLPALGEQCAIWKQCMDRNNDIFFRARSTLSAKLFGDIINSFIDPLNWKTLFVIFCGVITWCFSSNFLLGFVRAKSYYGNGIKTYPLPSSPKSPTSEETHSSMTASGEDSHLLKQ 471 Q9UT30 Nucleus brr6 284812 None SL-0178 SL-0182 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}. UNIPROT Q9UT30 Pfam PF10104 Involved in mRNA and protein export from nucleus. {ECO:0000250|UniProtKB:P38770, ECO:0000269|PubMed:17993570}. GO:0005789 GO:0016021 GO:0044732 GO:0005635 GO:0031965 GO:1990578 GO:0055088 GO:0140480 GO:0051028 GO:0006998 GO:0015031 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEMYVEDVPMPDIGPDSVLNTPIRPKYEILKSKKKTQNENDPEPMDISMSPDEKNLKKSTVRRKLRKSKPNSSSNQVSSRTRALTKRSNSSNAIIKANNQDSVYVSDWTNVHRDIPIVVSGYLQLMFNACVASIFLYFLFKIVFGIQNDVRNRVEYHKILQEEQAADCQREYLSINCDSPGPAIFEVCQKLKQCKMESSNNVGSTKLAALVFAEIIDAFISHISYKTMVFSLILVFGSLLTSNYAFGLYRARHSQNIHDYAANAIPAMIPSSRFLPSNLSDISNRNLIEAASQEEEI 297 P53062 Nucleus BRR6 559292 None SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:14562095}. UNIPROT P53062 UNIPROT D6VV88 Pfam PF10104 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}. P25611 EBI-2347149 0.37 P11484 EBI-3778254 0.35 GO:0071944 GO:0005783 GO:0016021 GO:0005635 GO:0031965 GO:0055088 GO:0051028 GO:0006998 Transmembrane UniProt Sequence Analysis {ECO:0000255} MELRSFSRQPDGILANPRLGREEVLEGEHPQDARLARQSIWLSPSLIAEYIQLFFNFIIGTIGLSLAIKFILMIRNDVNLKLEHNVREELDKIATCKSRYFENQCEPHMRVPALEVRCNEWSKCMNKEIVSGSDYQWAKAWARTLAEVINAFFEAFSIRSFLFILISIIGIIFVTNTSFGSYRVYLNNKDTKSVRHA 197 Q8IWQ3 Serine/threonine-protein BRSK2 9606 None SL-0198 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. UNIPROT Q8IWQ3 UNIPROT B3KVE9 UNIPROT E9PLM7 UNIPROT O60843 UNIPROT O95099 UNIPROT Q5J5B4 UNIPROT Q6ZMQ4 UNIPROT Q8TB60 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 609236 DisGeNET 9024 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}. Q8WVZ9 EBI-3232144 0.35 Q99PL5 EBI-11066888 0.35 Q9Y4K3 EBI-24471109 0.56 Q96RY5 EBI-28942454 0.35 P61769 EBI-28942454 0.35 P02452 EBI-28942454 0.35 Q8TDC3 EBI-28943702 0.35 Q92905 EBI-30872909 0.64 GO:0005813 GO:0005737 GO:0150034 GO:0005783 GO:0048471 GO:0005524 GO:0051117 GO:0060590 GO:0000287 GO:0019901 GO:0106310 GO:0004674 GO:0048156 GO:0050321 GO:0031532 GO:0007409 GO:0051301 GO:0042149 GO:0036503 GO:0030010 GO:0006887 GO:0000086 GO:0035556 GO:0070059 GO:0090176 GO:0030182 GO:0018105 GO:0006468 GO:0043462 GO:0050770 GO:0061178 GO:0010975 GO:1904152 GO:2000807 Unknown UniProt Sequence Analysis MTSTGKDGGAQHAQYVGPYRLEKTLGKGQTGLVKLGVHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSQEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRARLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFISLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPSLSHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDPPAAQHLSDTTNCMEMMTGRLSKCGSPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGPGGDAEYPTGKDTAKMGPPTARREQP 736 Q69Z98 Serine/threonine-protein Brsk2 10090 None SL-0198 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}. UNIPROT Q69Z98 UNIPROT Q699J3 UNIPROT Q699J4 UNIPROT Q6DMN7 UNIPROT Q6PHM0 PDB 4YNZ PDB 4YOM Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0005813 GO:0005737 GO:0150034 GO:0005783 GO:0048471 GO:0005524 GO:0051117 GO:0000287 GO:0019901 GO:0106310 GO:0004674 GO:0050321 GO:0031532 GO:0007409 GO:0051301 GO:0042149 GO:0036503 GO:0030010 GO:0006887 GO:0000086 GO:0035556 GO:0070059 GO:0090176 GO:0030182 GO:0048812 GO:0018105 GO:0006468 GO:0050770 GO:0061178 GO:0010975 Unknown UniProt Sequence Analysis MTSTGKDGGGAQHAQYVGPYRLEKTLGKGQTGLVKLGIHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDERNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSHEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRTRLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFINLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPSLSHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDQPSAQHLSDTTNCMEVMTGRLSKCGTPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGGDTEYPMGKDMAKMGPPAARREQP 735 D3ZML2 Serine/threonine-protein Brsk2 10116 None SL-0198 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}. UNIPROT D3ZML2 UNIPROT E9PTC7 UNIPROT Q4A1P4 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. P49286 EBI-11578535 0.00 GO:0005813 GO:0005737 GO:0150034 GO:0005783 GO:0005634 GO:0048471 GO:0005524 GO:0051117 GO:0000287 GO:0019901 GO:0106310 GO:0004674 GO:0050321 GO:0031532 GO:0007409 GO:0051301 GO:0006974 GO:0042149 GO:0036503 GO:0030010 GO:0006887 GO:0000086 GO:0035556 GO:0070059 GO:0090176 GO:0007095 GO:0030182 GO:0048812 GO:0018105 GO:0006468 GO:0050770 GO:0061178 GO:0010975 GO:0009411 Unknown UniProt Sequence Analysis MTSTGKDGGGAQHAQYVGPYRLEKTLGKGQTGLVKLGIHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDERNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSHEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRTRLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELGHLQLFGNPVSKVRSVAMELVILVQTLAYTSFRLLGTFLPVRYLRHSVLSRPPERARLVLRGAPCTHMGPVWNMVGMAYTQNPPIMGETGVYGSQWVMSSAPSKHYTSLGLSVPSPSCSLSPSLFPFCAPDTTNCMEVMTGRLSKCGTPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGGDTEYPMGKDMAKMGPPAARREQP 735 Q58DP0 Probable BUD23 9913 None SL-0198 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}. UNIPROT Q58DP0 UNIPROT Q2TBN2 Pfam PF08241 Pfam PF12589 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}. GO:0005730 GO:0005654 GO:0048471 GO:0046982 GO:0016435 GO:0006325 GO:2000234 GO:0070476 Unknown UniProt Sequence Analysis MAFRGRRPELRGPPELYYDKNEARKYVRNSRMIDVQIKMTGRALELLCVPEDKPCYVLDIGCGTGLSGDYLSDEGHYWVGIDISPAMLDEALDRETQGDVILGDMGQGIPFKPGTFDACISISAVQWLCNANKKSDIPAKRLYCFFSSLYSVLVRGGRAVLQLYPENSEQLELITTQATRAGFTGGVVVDYPNSAKAKKFYLCLFSGPSTSLPEGLSEDTEEEKPAESTFTADRIPYRIARRGVVRKSREWVLEKKARRRRQGKEVCPDTQYTGRKRKPRF 281 Q55DA6 Probable DDB_G0269722 44689 None SL-0198 Nucleus {ECO:0000250|UniProtKB:O43709}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O43709}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43709}. Cytoplasm {ECO:0000250|UniProtKB:O43709}. UNIPROT Q55DA6 Pfam PF08241 Pfam PF12589 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}. GO:0005730 GO:0005654 GO:0048471 GO:0016435 GO:0070476 Unknown UniProt Sequence Analysis MSRPEHIAPPEIFYDDVESKKYSSNSRIIEIQTKMAERAYELLAIPETAEGLMLLDIGCGSGISGDVITDAGHYWIGCDISQHMLDVAIDREVEGDVMLRDIGQGFPFRAGSFDAAISISAIQWLCNAEKSHHNPRKRLHTFFQSLFNVLTRGGKAILQFYPENSAQIEMITASALRCGFSGGLLIDFPNSSKAKKYFLVLFTGNNNIMPSAKGVEGEEYEQQEEEDSNEVKYSNRKRDRRRVTKSKGSAQHKTKEWIMNKKDRQRKQGREIKNDSKFSGRKRGPKF 287 O43709 Probable BUD23 9606 None SL-0198 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}. UNIPROT O43709 UNIPROT A8K501 UNIPROT C9K060 UNIPROT Q96P12 UNIPROT Q9BQ58 UNIPROT Q9HBP9 PDB 6G4W Pfam PF08241 Pfam PF12589 OMIM 194050 OMIM 615733 DisGeNET 114049 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}. 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}. Q9Y478 EBI-1079549 0.00 P01100 EBI-2692676 0.00 Q5NHY6 EBI-2799823 0.00 P00973 EBI-3942303 0.37 Q16512 EBI-3942313 0.37 P55072 EBI-3942323 0.37 Q13618 EBI-21329068 0.35 Q6ZWV7 EBI-10997876 0.35 P06748 EBI-11145880 0.35 Q9UI30 EBI-23853163 0.83 D0UZS0 EBI-14064021 0.35 Q9C0C9 EBI-21894427 0.35 Q8IUE6 EBI-21894427 0.35 Q9IK91 EBI-25747231 0.35 P0DTC9 EBI-27129711 0.35 P59595 EBI-27129966 0.35 P15130 EBI-27131516 0.35 Q0ZME3 EBI-27131755 0.35 Q6Q1R8 EBI-27132003 0.35 K9N4V7 EBI-27132270 0.35 P33469 EBI-27132272 0.35 Q9BXK1 EBI-29019783 0.35 O95600 EBI-29020196 0.35 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0008168 GO:0046982 GO:0003723 GO:0016435 GO:0006325 GO:2000234 GO:0070476 Unknown UniProt Sequence Analysis MASRGRRPEHGGPPELFYDETEARKYVRNSRMIDIQTRMAGRALELLYLPENKPCYLLDIGCGTGLSGSYLSDEGHYWVGLDISPAMLDEAVDREIEGDLLLGDMGQGIPFKPGTFDGCISISAVQWLCNANKKSENPAKRLYCFFASLFSVLVRGSRAVLQLYPENSEQLELITTQATKAGFSGGMVVDYPNSAKAKKFYLCLFSGPSTFIPEGLSENQDEVEPRESVFTNERFPLRMSRRGMVRKSRAWVLEKKERHRRQGREVRPDTQYTGRKRKPRF 281 Q9CY21 Probable Bud23 10090 None SL-0198 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}. UNIPROT Q9CY21 UNIPROT Q3U915 Pfam PF08241 Pfam PF12589 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}. GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0046982 GO:0016435 GO:0006325 GO:2000234 GO:0070476 Unknown UniProt Sequence Analysis MASRSRRPEHSGPPELFYDQNEARKYVRNSRMIDIQTKMTERALELLCLPEGQPSYLLDIGCGSGLSGDYISEEGHYWVGIDISPAMLDAALDRDTEGDLLLGDMGQGVPFRPGSFDGCISISAVQWLCNANKKSDVPARRLYCFFSSLYSALVRGARAVLQLYPENSEQLELITTQATRAGFTGGVVVDFPNSAKAKKFYLCLFSGPSTSLPKGLTESQDADQASESMFTSERAPHKKARRDLVKKSREWVLEKKERRRRQGKEVRPDTQYTGRKRKPRF 281 O22873 bZIP BZIP18 3702 None SL-0198 Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27896439}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27896439}. Cytoplasm {ECO:0000269|PubMed:27896439}. UNIPROT O22873 UNIPROT O23726 Pfam PF00170 PROSITE PS50217 Transcription factor that may participate with bZIP34 in the gametophytic control of pollen development. {ECO:0000269|PubMed:27896439}. Q94AY3 EBI-4509008 0.37 Q9LZW4 EBI-25522576 0.56 GO:0005737 GO:0005654 GO:0005634 GO:0048471 GO:0031490 GO:0003700 GO:0043621 GO:0000976 Unknown UniProt Sequence Analysis MEDPSNPQPNQSNLSQCPPLATAPTPAPVRGPYHRRAHSEVQFRLPEDLDLSEPFGGFDELGSEDDLFCSYMDIEKLGSGSGSASDSAGPSAPRSDNPFSAENGGAEAGNSRPRHRHSLSVDGSSTLESIEAKKAMAPDKLAELWVVDPKRAKRIIANRQSAARSKERKARYILELERKVQTLQTEATTLSAQLSLFQRDTTGLSSENTELKLRLQVMEQQAKLRDALNEQLKKEVERLKFATGEVSPADAYNLGMAHMQYQQQPQQSFFQHHHQQQTDAQNLQQMTHQFHLFQPNNNQNQSSRTNPPTAHQLMHHATSNAPAQSHSYSEAMHEDHLGRLQGLDISSCGRGSNFGRSDTVSESSSTM 367 Q9FWS3 Zinc CG1 3702 None SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT Q9FWS3 UNIPROT F4HZ22 UNIPROT Q94C30 Pfam PF18044 PROSITE PS50103 Q9XFM0 EBI-25527299 0.56 GO:0005635 GO:0005643 GO:0005634 GO:0003677 GO:0046872 GO:0061630 GO:0051028 GO:0015031 GO:0016567 Unknown UniProt Sequence Analysis MRKELCRNFQRGSCRYGENCRFLHPQQAKPNNPFGFGTQNQQQQQQQQQQNSSNPFGFGVQSGGSSRPNQFQNTWSRTASTPTGGGAAASTQQTGKQTQPADHKCTDPAACKRVMQDDFKNERPMWKLTCYGHWKYFPCDVTGDISYEELRAVAYEEAKRGIPLQSIVERERNLQNSKIAEFENFLRNPYKGSVTANQSPFAATTPSIFPQSSQINSPSPAFSGFNQQTAFSNTNAGGLSSSGPPNAFASFNQQTTFPNTNAGGVSSSGPPNPFASFTQQSNNQQTAFSNTNAGGLSSSGPPNAFASFNKQPNAFSVNTPQPVPSGPSGFQTNPSTTFKPASFGPGPGFATTPQNNNIFGQSTPTPATNTSQNNQTAFNFNVPVASFTAPAINTTNTSSGTELQIGGDPVDSSIWLKEKWNPGEIPEQAPPDAFV 435 Q9N1R0 Calcium-binding CABP1 9913 None SL-0198 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}. UNIPROT Q9N1R0 UNIPROT Q9N1R1 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0070161 GO:0005737 GO:0005856 GO:0005794 GO:0048471 GO:0005886 GO:0014069 GO:0005246 GO:0005509 GO:0048306 GO:0008139 GO:0042308 GO:1901385 GO:0050896 GO:0007601 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:Q9NZU7} MGNCVKSPLRNLSRKMRQEETSYTVVQTSEEGLAASGELPGPLLMLAQNCAVMHNLLGPACIFLRKGFAENRQPDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR 226 Q9NZU7 Calcium-binding CABP1 9606 None SL-0198 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. UNIPROT Q9NZU7 UNIPROT O95663 UNIPROT Q8N6H5 UNIPROT Q9NZU8 PDB 2K7B PDB 2K7C PDB 2K7D PDB 2LAN PDB 2LAP PDB 3OX5 PDB 3OX6 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 605563 DisGeNET 9478 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}. P06623 EBI-907917 0.40 Q13936 EBI-15896764 0.54 P08047 EBI-2679915 0.00 P01100 EBI-2681402 0.00 Q13107 EBI-21883326 0.40 GO:0070161 GO:0005938 GO:0005737 GO:0005856 GO:0005615 GO:0000139 GO:0048471 GO:0005886 GO:0014069 GO:0005246 GO:0005509 GO:0048306 GO:0004857 GO:0008139 GO:0042308 GO:1901385 GO:0050896 GO:0007601 Lipid-Anchored UniProt Sequence Analysis {ECO:0000255} MGGGDGAAFKRPGDGARLQRVLGLGSRREPRSLPAGGPAPRRTAPPPPGHASAGPAAMSSHIAKSESKTSLLKAAAAAASGGSRAPRHGPARDPGLPSRRLPGSCPATPQSSGDPSSRRPLCRPAPREEGARGSQRVLPQAHCRPREALPAAASRPSPSSPLPPARGRDGEERGLSPALGLRGSLRARGRGDSVPAAASEADPFLHRLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR 370 Q9N1Q9 Calcium-binding CABP2 9913 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. UNIPROT Q9N1Q9 Pfam PF00036 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0005737 GO:0005794 GO:0048471 GO:0005886 GO:0005246 GO:0005509 GO:1901385 GO:0050896 GO:0007605 GO:0007601 Lipid-Anchored UniProt By Similarity {ECO:0000250} MGNCAKRPRHRAPKDRELRPEEIEELQAAFQEFDRDRDGYIGYQELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDAFREFDTNGDGCISLGELRAALKALLGERLSQREVDEILRDIDLNGDGLVDFEEFVRMMSR 163 Q9NPB3 Calcium-binding CABP2 9606 None SL-0198 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}. UNIPROT Q9NPB3 Pfam PF00036 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 607314 OMIM 614899 DisGeNET 51475 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}. 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. Q7Z3Z2 EBI-24796266 0.56 Q5JST6 EBI-24280036 0.56 Q9H257 EBI-24349898 0.56 A6NEM1 EBI-24354781 0.56 Q96ED9 EBI-24363653 0.56 P86480 EBI-25247799 0.56 Q96M29 EBI-25252219 0.56 Q9NPE3 EBI-23679380 0.56 Q5T686 EBI-23682258 0.56 Q9H1P6 EBI-24667738 0.56 Q8IZF2 EBI-23695711 0.56 Q9BRK3 EBI-23698200 0.56 Q5JTJ3 EBI-23706738 0.56 Q6NX45 EBI-24681698 0.56 A8K8V0 EBI-23728536 0.56 P52738 EBI-23735866 0.56 O43623 EBI-24705441 0.56 Q9BU61 EBI-24705993 0.56 Q9BRJ7 EBI-24717821 0.56 Q8NCR6 EBI-24726274 0.56 Q8N6D5 EBI-24738691 0.56 O00746 EBI-23809170 0.56 P19237 EBI-24741126 0.56 Q9UPQ4 EBI-24765776 0.56 A0A0U1RQF7 EBI-25278632 0.56 Q9H9P5 EBI-24548110 0.56 Q8TBB0 EBI-24654317 0.56 Q68EA5 EBI-24654686 0.56 Q9H0A9 EBI-24789004 0.56 Q6P5X5 EBI-25202133 0.56 Q08117 EBI-25267170 0.56 P35452 EBI-25241483 0.56 Q8TAG6 EBI-25275160 0.56 GO:0005737 GO:0005794 GO:0048471 GO:0005886 GO:0005246 GO:0005509 GO:1901385 GO:0007605 GO:0007165 GO:0007601 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:10625670} MGNCAKRPWRRGPKDPLQWLGSPPRGSCPSPSSSPKEQGDPAPGVQGYSVLNSLVGPACIFLRPSIAATQLDRELRPEEIEELQVAFQEFDRDRDGYIGCRELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDAFREFDTNGDGRISVGELRAALKALLGERLSQREVDEILQDVDLNGDGLVDFEEFVRMMSR 220 Q9JLK4 Calcium-binding Cabp2 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. UNIPROT Q9JLK4 UNIPROT Q3KNX9 UNIPROT Q9JLK5 Pfam PF00036 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0005737 GO:0005794 GO:0048471 GO:0005886 GO:0005246 GO:0005509 GO:1901385 GO:0050896 GO:0007605 GO:0007601 Lipid-Anchored UniProt By Similarity {ECO:0000250} MGNCAKTPWHRGSKERWQWPGSPLGGSRPSPGPRTEEQEGTQGYSVLGSLVGPACIFLRPSIAATQLDRELRPEEIEELQIAFQEFDRDRDGYIGYRELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDAFREFDTNGDGCISVGELRAALKALLGERLSQREVDEILQDIDLNGDGLVDFEEFVRMMSR 216 Q86V35 Calcium-binding CABP7 9606 None SL-0198 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}. UNIPROT Q86V35 PDB 2LV7 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 618759 Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. {ECO:0000250}. Q9H2K0 EBI-23900572 0.56 GO:0016021 GO:0048471 GO:0005886 GO:0032588 GO:0005509 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPFHPVTAALMYRGIYTVPNLLSEQRPVDIPEDELEEIREAFKVFDRDGNGFISKQELGTAMRSLGYMPNEVELEVIIQRLDMDGDGQVDFEEFVTLLGPKLSTSGIPEKFHGTDFDTVFWKCDMQKLTVDELKRLLYDTFCEHLSMKDIENIIMTEEESHLGTAEECPVDVETCSNQQIRQTCVRKSLICAFAIAFIISVMLIAANQVLRSGMK 215 Q91ZM8 Calcium-binding Cabp7 10090 None SL-0198 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}. UNIPROT Q91ZM8 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. {ECO:0000250}. GO:0016021 GO:0048471 GO:0005886 GO:0032588 GO:0005509 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPFHPVTAALMYRGIYTVPNLLSEQRPVDIPEDELEEIREAFKVFDRDGNGFISKQELGTAMRSLGYMPNEVELEVIIQRLDMDGDGQVDFEEFVTLLGPKLSTSGIPEKFHGTDFDTVFWKCDMQKLTVDELKRLLYDTFCEHLSMKDIENIIMTEEESHLGTAEECPVDVETCSNQQIRQTCVRKSLICAFAIAFIISVMLIAANQVLRSGMK 215 Q866X0 Calcium-binding CABP7 9555 None SL-0198 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}. UNIPROT Q866X0 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. {ECO:0000250}. GO:0016021 GO:0048471 GO:0005886 GO:0032588 GO:0005509 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPFHPVTAALMYRGIYTVPNLLSEQRPVDIPEDELEEIREAFKVFDRDGNGFISKQELGTAMRSLGYMPNEVELEVIIQRLDMDGDGQVDFEEFVTLLGPKLSTSGIPEKFHGTDFDTVFWKCDMQKLTVDELKRLLYDTFCEHLSMKDIENIIMTEEESHLGTAEECPVDVETCSNQQIRQTCVRKSLICAFAIAFIISVMLIAANQVLRSGMK 215 Q66H96 Calcium-binding Cabp7 10116 None SL-0198 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}. UNIPROT Q66H96 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. {ECO:0000269|PubMed:19458041}. GO:0016021 GO:0048471 GO:0005886 GO:0032588 GO:0005509 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPFHPVTAALMYRGIYTVPNLLSEQRPVDIPEDELEEIREAFKVFDRDGNGFISKQELGTAMRSLGYMPNEVELEVIIQRLDMDGDGQVDFEEFVTLLGPKLSTSGIPEKFHGTDFDTVFWKCDMQKLTVDELKRLLYDTFCEHLSMKDIENIIMTEEESHLGTAEECPVDVETCSNQQIRQTCVRKSLICAFAIAFIISVMLIAANQVLRSGMK 215 Q9BXU9 Calcium-binding CALN1 9606 None SL-0198 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}. UNIPROT Q9BXU9 UNIPROT J3KQA7 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 607176 DisGeNET 83698 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}. P62166 EBI-21458640 0.27 Q96LL9 EBI-24625155 0.56 Q9NZ43 EBI-24630791 0.56 Q969F0 EBI-24388353 0.56 Q96IW7 EBI-24542608 0.56 P60201 EBI-24602587 0.56 P21145 EBI-24638394 0.56 P03973 EBI-24807681 0.56 Q9H400 EBI-25271079 0.56 Q58WW2 EBI-21889878 0.40 P21554 EBI-21458285 0.38 GO:0016021 GO:0048471 GO:0005886 GO:0032588 GO:0005509 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRLPEQPGEGKPENEKKGDGGALGGGEEPPRSQAPDFPTWEKMPFHHVTAGLLYKGNYLNRSLSAGSDSEQLANISVEELDEIREAFRVLDRDGNGFISKQELGMAMRSLGYMPSEVELAIIMQRLDMDGDGQVDFDEFMTILGPKLVSSEGRDGFLGNTIDSIFWQFDMQRITLEELKHILYHAFRDHLTMKDIENIIINEEESLNETSGNCQTEFEGVHSQKQNRQTCVRKSLICAFAMAFIISVMLIAANQILRSGME 261 Q9JJG7 Calcium-binding Caln1 10090 None SL-0198 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}. UNIPROT Q9JJG7 UNIPROT F8WHE1 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. P47746 EBI-21458692 0.27 GO:0016021 GO:0048471 GO:0005886 GO:0032588 GO:0005509 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRLPEQPGDGKPENETKGDQETPERGEEPRRSPAPDFPTWEKMPFHHVTAGLLYKGNYLNRSLSAGSDSEQLANISVEELDEIREAFRVLDRDGNGFISKQELGMAMRSLGYMPSEVELAIIMQRLDMDGDGQVDFDEFMTILGPKLVSSEGRDGFLGNTIDSIFWQFDMQRVTLEELKHILYHAFRDHLTMKDIENIIINEEESLNETSGNCQTEFEGVHSQKQNRQTCVRKSLICAFAMAFIISVMLIAANQILRSGME 261 Q06BI3 Calcium-binding Caln1 10116 None SL-0198 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}. UNIPROT Q06BI3 UNIPROT Q06BI2 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0016021 GO:0048471 GO:0005886 GO:0032588 GO:0005509 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRLPEQPGDGKPENETKGDQETPERGEEPRRSPAPDFPTWEKMPFHHVTAGLLYKGNYLNRSLSAGSDSEQLANISVEELDEIREAFRVLDRDGNGFISKQELGMAMRSLGYMPSEVELAIIMQRLDMDGDGQVDFDEFMTILGPKLVSSEGRDGFLGNTIDSIFWQFDMQRVTLEELKHILYHAFRDHLTMKDIENIIINEEESLNETSGNCQTEFEGVHSQKQNRQTCVRKSLICAFAMAFIISVMLIAANQILRSGME 261 O18737 Calcium-binding CALCOCO2 9913 None SL-0198 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}. UNIPROT O18737 Pfam PF17751 PROSITE PS51905 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}. GO:0005776 GO:0000421 GO:0031410 GO:0005856 GO:0048471 GO:0016605 GO:0046872 GO:1901098 GO:0098792 Peripheral UniProt Curator Inference {ECO:0000305} MEETVDDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDITCYYTLTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPVDLNSESAKQQEVQFKAYYLPKDDEYYQFCYVDQDGVVRGASIPFQFRPENEEDILVVTTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRLLSYMGLDCDSLSYQVPTSNQGGTRQDPGLVFGNPYSGIQESSAPSLLSIKKCPTCKSDFAADVFDHNLALEQHLQTLSLNCPICDKTFPAKEKQIFEDHVFCHTL 450 Q13137 Calcium-binding CALCOCO2 9606 None SL-0198 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}. UNIPROT Q13137 UNIPROT B2RBT0 UNIPROT B4DDC4 UNIPROT B4DDT4 UNIPROT B4DP36 UNIPROT B4E0C0 UNIPROT E7ENK0 UNIPROT E7ETP5 UNIPROT E9PBE5 UNIPROT Q53FQ5 UNIPROT Q53HB5 UNIPROT Q6IBN9 UNIPROT Q9BTF7 PDB 2MXP PDB 3VVV PDB 3VVW PDB 4GXL PDB 4HAN PDB 4XKL PDB 5AAQ PDB 5Z7A PDB 5Z7L PDB 7EAA Pfam PF17751 PROSITE PS51905 OMIM 604587 DisGeNET 10241 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}. O75604 EBI-24334992 0.56 O75716 EBI-10189253 0.56 P29991 EBI-8829245 0.37 P50613 EBI-21835901 0.35 Q02821 EBI-11534474 0.56 Q06787 EBI-6115370 0.55 Q9Y3C5 EBI-7220121 0.37 Q96S44 EBI-752485 0.74 O00214 EBI-752575 0.85 Q53FD0 EBI-752725 0.37 Q8N715 EBI-752740 0.37 Q8TBB1 EBI-753001 0.55 Q8N2W9 EBI-753673 0.37 Q8N5R6 EBI-753856 0.37 P25786 EBI-753919 0.67 P26599 EBI-754081 0.37 Q3YEC7 EBI-754117 0.37 Q9UBL6 EBI-24292126 0.56 Q96F93 EBI-754906 0.37 Q9Y4Z0 EBI-754981 0.78 P29353 EBI-755236 0.55 P60520 EBI-755311 0.78 Q15906 EBI-755386 0.37 Q9Y4E5 EBI-755704 0.37 Q9BQY9 EBI-755827 0.37 Q14966 EBI-755848 0.37 Q96D16 EBI-755989 0.67 O95201 EBI-756364 0.37 P51116 EBI-756460 0.37 Q7L590 EBI-756649 0.37 Q9UNA4 EBI-756718 0.37 Q9UKA9 EBI-756841 0.37 O95251 EBI-757276 0.37 Q9BSM1 EBI-757711 0.37 P56279 EBI-757792 0.87 Q96GM5 EBI-757918 0.67 Q8IYF1 EBI-757939 0.55 O14639 EBI-757951 0.37 Q13137 EBI-758068 0.37 Q9H0I2 EBI-758104 0.67 Q9BUY5 EBI-758131 0.37 Q9BVV2 EBI-758146 0.67 P30626 EBI-758236 0.74 Q9BWD7 EBI-758320 0.37 Q12933 EBI-758476 0.37 Q9H9D4 EBI-758947 0.67 Q15038 EBI-759250 0.67 Q8TCX5 EBI-759364 0.37 Q9UBV8 EBI-759700 0.67 Q9UBZ4 EBI-759748 0.37 Q9H0R8 EBI-759847 0.78 O95990 EBI-760045 0.37 Q7Z3B3 EBI-760072 0.74 Q5NEX4 EBI-2808427 0.00 A0A3N4B896 EBI-2840104 0.00 Q9UNI6 EBI-8633706 0.74 Q15884 EBI-8636634 0.37 Q13671 EBI-8641704 0.67 Q8WUI4 EBI-10276459 0.56 Q99471 EBI-8644653 0.67 Q6PF05 EBI-8656859 0.37 Q86YD7 EBI-8656891 0.78 P01106 EBI-3962281 0.35 O43913 EBI-3935022 0.37 P15927 EBI-3935032 0.37 Q9Y4K3 EBI-3935052 0.37 Q9Y6K9 EBI-3935062 0.37 Q14161 EBI-3935072 0.37 Q8TDY2 EBI-3935082 0.37 Q15051 EBI-4286917 0.35 Q7Z434 EBI-6115370 0.58 Q8NCU4 EBI-6115370 0.35 Q9UHD2 EBI-6115370 0.75 P48634 EBI-6115370 0.35 A7MCY6 EBI-6115370 0.53 Q9H6S1 EBI-6115370 0.53 Q9NVV4 EBI-6115370 0.50 Q9QYP6 EBI-6115837 0.35 Q99IB8 EBI-6928172 0.37 Q9WMX2 EBI-9081202 0.57 O41947 EBI-9640332 0.37 A8KA13 EBI-10174899 0.56 Q2TBE0 EBI-10175027 0.56 B2R9Y1 EBI-10175744 0.56 Q8WWY3 EBI-10177378 0.72 O00560 EBI-10180081 0.56 O43189 EBI-10183509 0.56 O43324 EBI-10183831 0.56 O43602 EBI-10184475 0.56 O95363 EBI-10191564 0.78 P00540 EBI-10193294 0.78 P14678 EBI-10198485 0.56 P17482 EBI-10199927 0.56 P25791 EBI-10202872 0.56 P26196 EBI-10203823 0.72 P26640 EBI-10204357 0.56 P32969 EBI-10206135 0.56 P41227 EBI-10208549 0.78 P49901 EBI-10211623 0.56 P50539 EBI-10212007 0.72 P51946 EBI-10212597 0.56 P61968 EBI-10218982 0.56 P62979 EBI-10220080 0.56 Q02040 EBI-10222670 0.56 Q05CH4 EBI-10223754 0.56 Q08117 EBI-10224979 0.56 Q12774 EBI-10227037 0.56 Q14997 EBI-10234580 0.56 Q14D33 EBI-10234924 0.72 Q17RB8 EBI-10238780 0.56 Q3B820 EBI-10240301 0.72 Q5U5U6 EBI-10247590 0.56 Q6NYC8 EBI-10251814 0.56 Q6P4J0 EBI-10252829 0.56 Q6PIY7 EBI-10253897 0.56 Q7Z4I7 EBI-10257703 0.56 Q86TG7 EBI-10258559 0.67 Q86W54 EBI-10259956 0.56 Q8IVS8 EBI-10261677 0.56 Q8IYX8 EBI-10264302 0.56 Q8N4T4 EBI-10265711 0.67 Q8NBM4 EBI-10269199 0.56 Q8TBE0 EBI-10273199 0.56 Q8TBZ8 EBI-10273829 0.56 Q8TES7 EBI-10275340 0.56 Q8WU02 EBI-10276217 0.56 Q8WXI9 EBI-10278009 0.56 Q92567 EBI-10278631 0.56 Q92608 EBI-10278809 0.56 Q969Z0 EBI-10281521 0.56 Q96A72 EBI-10281716 0.72 Q96BZ8 EBI-10282682 0.56 Q96C32 EBI-10283082 0.56 Q96D03 EBI-10284252 0.56 Q96T37 EBI-10293900 0.56 Q99732 EBI-10294748 0.72 Q9BU23 EBI-10298573 0.56 Q9BV47 EBI-10299234 0.56 Q9BXF9 EBI-10301058 0.67 Q9BXY8 EBI-10301594 0.56 Q9H7H0 EBI-10308833 0.78 Q9HC52 EBI-10310384 0.72 Q9NQT4 EBI-10312366 0.56 Q9NU19 EBI-10313689 0.56 Q9NX63 EBI-10316161 0.56 Q9P0T4 EBI-10317870 0.56 Q9P2K6 EBI-10318921 0.56 Q9UIM3 EBI-10322118 0.56 Q9UJV3 EBI-10322427 0.56 Q9UJW0 EBI-10322497 0.56 Q9UMS0 EBI-10324153 0.56 Q9Y3M9 EBI-10327900 0.56 Q9Y4X0 EBI-10328456 0.67 P30566 EBI-21246927 0.37 Q9HBZ2 EBI-21247102 0.37 X5DP31 EBI-21247566 0.37 X5D7R7 EBI-21250303 0.37 X5DP17 EBI-21250609 0.37 Q99608 EBI-21250960 0.37 O43741 EBI-21251734 0.37 P03182 EBI-11721938 0.35 P30119 EBI-11736591 0.37 P05759 EBI-11522944 0.56 P0CH08 EBI-11523121 0.56 P32902 EBI-11526925 0.56 P38815 EBI-11529521 0.56 P39518 EBI-11529902 0.56 P40302 EBI-11530551 0.56 P40325 EBI-11530725 0.56 P41911 EBI-11531747 0.56 Q06630 EBI-11535826 0.56 Q06707 EBI-11535920 0.56 Q07821 EBI-11536127 0.56 Q12342 EBI-11537295 0.56 P28702 EBI-16433077 0.56 A0A0S2Z4M1 EBI-16433037 0.56 O15169 EBI-16433027 0.56 A0A0S2Z5X4 EBI-16433137 0.56 Q3SY00 EBI-24288555 0.56 P57086 EBI-24289178 0.56 P47897 EBI-24292527 0.56 Q7L5A3 EBI-24308054 0.56 Q5JVL4 EBI-24316916 0.56 P56524 EBI-24325092 0.56 Q9P1Z0 EBI-24331244 0.56 Q96HB5 EBI-24332120 0.56 P54646 EBI-24338182 0.56 Q9BSH4 EBI-24338552 0.56 Q96FJ0 EBI-25243983 0.56 P51504 EBI-24480415 0.56 Q8NE01 EBI-24488458 0.56 Q8NA54 EBI-24496225 0.56 Q14005 EBI-24503792 0.56 Q96IQ9 EBI-24507508 0.56 Q494U1 EBI-24374123 0.56 Q9BWG6 EBI-24383955 0.56 Q6NX45 EBI-24388156 0.56 Q6VB84 EBI-24390683 0.56 Q9C0A6 EBI-24391757 0.56 O00311 EBI-24403310 0.56 P08218 EBI-24406407 0.56 P09067 EBI-24427120 0.56 Q5T619 EBI-24430220 0.56 Q9H7X3 EBI-24432271 0.56 Q6PF15 EBI-24453693 0.56 Q9BXW4 EBI-24455075 0.56 Q99633 EBI-24456947 0.56 P28676 EBI-24461986 0.56 Q6IQ23 EBI-16398399 0.35 Q53EZ4 EBI-21572102 0.35 P0CG47 EBI-21572102 0.35 Q3KP66 EBI-21617875 0.35 Q9H7C4 EBI-21702482 0.35 Q9BU40 EBI-21739567 0.35 Q96DB2 EBI-21787335 0.35 E9PKR8 EBI-21872066 0.35 Q9UHQ4 EBI-21883433 0.40 P29972 EBI-21268671 0.37 Q9H788 EBI-21268710 0.37 P15622 EBI-21268658 0.37 Q96HA8 EBI-21268697 0.37 P61417 EBI-20817146 0.37 Q83DE4 EBI-21285435 0.37 P21580 EBI-20737339 0.35 Q9UKE5 EBI-28946906 0.55 Q14296 EBI-22127120 0.37 P0CG48 EBI-22146758 0.37 Q92574 EBI-26515497 0.37 Q8N612 EBI-34574737 0.27 GO:0005776 GO:0000421 GO:0005737 GO:0031410 GO:0005856 GO:0005829 GO:0043231 GO:0016020 GO:0005634 GO:0048471 GO:0016605 GO:0046872 GO:0042803 GO:1901098 GO:0034341 GO:0016032 GO:0098792 Peripheral UniProt Curator Inference {ECO:0000305} MEETIKDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPIDLNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGARQNPGLAYGNPYSGIQESSSPSPLSIKKCPICKADDICDHTLEQQQMQPLCFNCPICDKIFPATEKQIFEDHVFCHSL 446 Q4R914 Calcium-binding CALCOCO2 9541 None SL-0198 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}. UNIPROT Q4R914 Pfam PF17751 PROSITE PS51905 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}. GO:0005776 GO:0000421 GO:0031410 GO:0005856 GO:0048471 GO:0046872 GO:1901098 GO:0098792 Peripheral UniProt Curator Inference {ECO:0000305} MEKTIEDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDVTCRYTFTQNFIPRQKDWIGIFRVGWKTVREYYTFMWVTLPIDLNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDQDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCVSLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETEQLEHLKKENGHLFLSLTEQRKDQKKLEQTVEEMKQNETTAMKKQQELMDENFDLSRRLSEKKMIYNALQREKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGAGQNPGLVYGNPYSGIQESSSPSQLSIKKCPICKADDICDHTLEQQQMQALCLNCPICDKIFPATEKQIFEDHVFCHSL 398 A2A6M5 Calcium-binding Calcoco2 10090 None SL-0198 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}. UNIPROT A2A6M5 UNIPROT Q3TK36 UNIPROT Q3TKZ6 UNIPROT Q3TL30 UNIPROT Q9CWE3 Pfam PF17751 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}. GO:0005776 GO:0000421 GO:0005737 GO:0031410 GO:0005856 GO:0005829 GO:0043231 GO:0048471 GO:0016605 GO:0042803 GO:1901098 GO:0034341 GO:0098792 Peripheral UniProt Curator Inference {ECO:0000305} MDQCPIPTLLEHGNFSQVLFNNVEKFYAPRGDIMCYYTLTEKFIPRRKDWIGIFKVGWKTTQEYYTFMWAPLPKDQNKDSATQQEIQFKAYYLPKDVERYQFCYVDEDGLVRGTSVPFQFCPDPDEDIMVVINKEKVEEMEQLSEELYQQNQELKDKYADLHEQLQRKQVALEATQRVNKTLEHKVEEKASWEKEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEKEKASWEEEKASWEKEKAPWEVEKAPWKEVKAYWWNDLHR 331 Q5R7H1 Calcium-binding CALCOCO2 9601 None SL-0198 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}. UNIPROT Q5R7H1 Pfam PF17751 PROSITE PS51905 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}. GO:0005776 GO:0000421 GO:0031410 GO:0005856 GO:0048471 GO:0046872 GO:1901098 GO:0098792 Peripheral UniProt Curator Inference {ECO:0000305} MEETIEDPPTSAVLLDHCHFSQVIFSSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPIDLNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDQDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDNCVSLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENKIICNALQREKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGAGQNPGLVYGNPYSGIQESSSPSPLSIKKCPICKADDICDHILEQQQMQPLCLNCPICDKIFPATEKQIFEDHVFCHSL 446 Q6DF48 Calcium-binding calcoco2 8364 None SL-0198 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}. UNIPROT Q6DF48 Pfam PF17751 PROSITE PS51905 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}. GO:0005776 GO:0000421 GO:0031410 GO:0005856 GO:0048471 GO:0046872 GO:1901098 GO:0098792 Peripheral UniProt Curator Inference {ECO:0000305} MASDAPPTSMLQPEERNYSQVVFSRVEQSYVPGIDIICYFTYTSGFHPAKKDWVGIFKVSWKTTREYYTWVSADCEEQGLEKRVTFKAYYLPKESDDYYQFCYVDQKGEVRGVSIPFQLCRKIQDEGEEDILLVTTEEEAQGMKEKQRVLEEKVAALEKDKCTLQDECTQLALEQKNKAALIESLQAQQLECAKKNEELDQQNQELERQLEEEKCKNGSLHLKVVSAEEERERVQNDIRSLQLEQNQLKEENMELHKHTNDMEFSLKKYSEEAKNQEEEVQELKDKLWDAEAKHHLLQVQLQDIQMEKKKDKYSIELLTKEAEKVADLRQNLEKKDKTMETMEKQLAQLQRENATVLRQMEDLSYTLELRKAEISDMQQQRVRDGAEIEHLNRLLTEQSSSTPRNQGLFFQNPYESESLISFANEPQPGEAPGGSSVRHVQMQCPECGSEFENFQVFQDHIFCHDLESTE 470 A8XA40 Calnexin cnx 6238 None SL-0198 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}. UNIPROT A8XA40 Pfam PF00262 PROSITE PS00803 PROSITE PS00804 PROSITE PS00805 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}. GO:0031410 GO:0005789 GO:0016021 GO:0048471 GO:0005509 GO:0051082 GO:0030968 GO:0006457 GO:0009408 GO:0030433 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLNRKWSFVFLTFLLVISVNANDDVFEDEDEASESGVEKDEFVPSNFVAPKLADTSKPNFFDYFPVGSKIGQTWIKSLAKKDDVDSEIAKYNGEWSIGAPTKVSIEGDYGLIVKTKARHHAIAAKLETPFVFGSNKFIAQYDVKFEEGQECGGGYLKLLSEGAEKDLASFQDKTPYTIMFGPDKCGASGQVHLIFRYKNPVNGTVSEYHAKQPASIGTAYWDDHNTHLFTLVVKPTGEYSVSVDGKSLYYGNMLSDISPSLTPPKEIFDETDLKPEDWDEREQIEDETASKPDDWDENEPQNVVDESATKPYDWNEEENELIPDPEAQKPQDWDEDMDGSWEAPLIDNPACKGLSGCGTWKPPTIKNPKYRGKWVRPKIANPAYKGKWSPRLIDNPNYFEPKPFDGLAPISAVGIELWTMSENILFDNILITSSEQDASEIAKQTFYIKQQEEYRLAAATGSSNGIFQQIVDATNEKPWLWAVYILCILLPLIAIGVFCFGKGSKPAPNFAKKSDTYSPDDDRVPNLVDDQEEEIIAEDEEDNQPGPSGTQNQPPIDEDEQDEVEQQPSSSKTASSESSSAAEEEDNDHVVHENEPVQPTEEVAKKSPRVTGGAKRRTARRGD 623 P34652 Calnexin cnx 6239 None SL-0198 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. UNIPROT P34652 Pfam PF00262 PROSITE PS00803 PROSITE PS00804 PROSITE PS00805 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}. Q18953 EBI-335408 0.00 Q9NH52 EBI-343937 0.00 GO:0031410 GO:0005789 GO:0030176 GO:0048471 GO:0005509 GO:0030246 GO:0051082 GO:0030968 GO:0006457 GO:0009408 GO:0030433 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVNRKWMYIFIQFLLVSSIRSDDDVFEDDEEEVTKGSDDKEEFVPSLFVAPKLSDKSTPNFFDYFPVGSKIGLTWIKSLAKKDDVDSDIAKYNGEWSIGAPTKVSIEGDLGLIVKTKARHHAIAAKLNTPFAFDANTFVVQYDIKFEEGQECGGGYLKLLSEGAEKDLANFQDKTAYTIMFGPDKCGATGKVHLIFRYKNPINGTISEYHANQPTTIGSTYWDDHNTHLFTLVVKPTGEYSVSVDGKSLYYGNMMSDVTPALTPPKQIFDETDLKPVDWDERENIEDESAVKPDDWDENEPQSVVDEAATKPYDWNEEENELIADPEAKKPQDWDEDMDGSWEAPLIDNPACKGLSGCGTWKAPTIKNPKYKGKWIRPKISNPAFKGKWTARLIDNPNYFEPKPFAGLAPITAVGIEMWTMSENILFDNILITSSEEDSSDVAKQTFYVKQKEEYRLAAATGNGNGFFQQIIDATNEKPWLWAVYILCVLLPLVAIGVFCFGKQSKPTPNFAKKSDAYSADDDRVPNLVDDDEEEIIGDEEDDVNQPGPSGSQSNPEPQDEEENAEQQSANSSQSSAAEEEDDEHVVPENEPVKPTEEFAKKSPKNTGGAKRRTARRGD 619 Q9Y6Q1 Calpain-6 CAPN6 9606 None SL-0198 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. UNIPROT Q9Y6Q1 UNIPROT D3DUY7 UNIPROT Q9UEQ1 UNIPROT Q9UJA8 Pfam PF00168 Pfam PF01067 Pfam PF00648 PROSITE PS50004 PROSITE PS50203 OMIM 300146 DisGeNET 827 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}. O94901 EBI-21501330 0.35 Q8TD16 EBI-21501330 0.35 Q8WXH0 EBI-21501330 0.35 O14745 EBI-7814911 0.40 P15311 EBI-7814930 0.40 P01023 EBI-7183126 0.35 O43829 EBI-24469714 0.56 Q6PJG9 EBI-21501330 0.35 P21333 EBI-21501330 0.35 Q9ULT8 EBI-21501330 0.35 Q9NRL2 EBI-21501330 0.35 Q9NRG0 EBI-21501330 0.35 Q8N5W9 EBI-21501330 0.35 Q5TB80 EBI-21501330 0.35 P23378 EBI-21501330 0.35 A0AVT1 EBI-21501330 0.35 P19338 EBI-20905504 0.40 P16403 EBI-20920500 0.40 GO:0005737 GO:0048471 GO:0005876 GO:0004198 GO:0008017 GO:0001578 GO:0051493 Unknown UniProt Sequence Analysis MGPPLKLFKNQKYQELKQECIKDSRLFCDPTFLPENDSLFYNRLLPGKVVWKRPQDICDDPHLIVGNISNHQLTQGRLGHKPMVSAFSCLAVQESHWTKTIPNHKEQEWDPQKTEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLGCYEALDGLTITDIIVDFTGTLAETVDMQKGRYTELVEEKYKLFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGHTYTMTDIRKIRLGERLVEVFSAEKVYMVRLRNPLGRQEWSGPWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCRNFHKLNVCRNVNNPIFGRKELESVLGCWTVDDDPLMNRSGGCYNNRDTFLQNPQYIFTVPEDGHKVIMSLQQKDLRTYRRMGRPDNYIIGFELFKVEMNRKFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLRELTLDMPKMSCWNLARGYPKVVTQITVHSAEDLEKKYANETVNPYLVIKCGKEEVRSPVQKNTVHAIFDTQAIFYRRTTDIPIIVQVWNSRKFCDQFLGQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLTEL 641 O35646 Calpain-6 Capn6 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:20814968}. UNIPROT O35646 UNIPROT Q3UM55 Pfam PF00168 Pfam PF01067 Pfam PF00648 PROSITE PS50004 PROSITE PS50203 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}. GO:0005737 GO:0005874 GO:0048471 GO:0005876 GO:0008017 GO:0001578 GO:0051493 Unknown UniProt Sequence Analysis MGPPLKLFKNQKYQELKQECMKDGRLFCDPTFLPENDSLFFNRLLPGKVVWKRPQDISDDPHLIVGNISNHQLIQGRLGNKAMISAFSCLAVQESHWTKAIPNHKDQEWDPRKPEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLGCYEALDGLTITDIIMDFTGTLAEIIDMQKGRYTDLVEEKYKLFGELYKTFTKGGLICCSIESPSQEEQEVETDWGLLKGYTYTMTDIRKLRLGERLVEVFSTEKLYMVRLRNPLGRQEWSGPWSEISEEWQQLTVTDRKNLGLVMSDDGEFWMSLEDFCHNFHKLNVCRNVNNPVFGRKELESVVGCWTVDDDPLMNRSGGCYNNRDTFLQNPQYIFTVPEDGHKVIMSLQQKDLRTYRRMGRPDNYIIGFELFKVEMNRRFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGSYVLVPTMFQHGRTSEFLLRIFSEVPVQLRELTLDMPKMSCWNLARGYPKVVTQITVHSAEGLEKKYANETVNPYLIIKCGKEEVRSPVQKNTVHAIFDTQAIFYRRTTDIPIIIQVWNSRKFCDQFLGQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLTEL 641 O88501 Calpain-6 Capn6 10116 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. UNIPROT O88501 Pfam PF00168 Pfam PF01067 Pfam PF00648 PROSITE PS50004 PROSITE PS50203 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}. GO:0005737 GO:0005874 GO:0048471 GO:0005876 GO:0008017 GO:0001578 GO:0051493 Unknown UniProt Sequence Analysis MGPPLKLFKNQKYQELKQDCMKDGRLFCDPTFLPENDSLFFNRLLPGKVVWKRPQDISDDPHLIVGNISNHQLIQGRLGNKAMISAFSCLAVQESHWTKAIPNHKEQEWDPRKPEKYAGIFRFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLGCYEALDGLTITDIIMDFTGTLAEIIDMQKGRYTDLVEEKYKLFGELYKTFTKGGLISCSIESPSQEEQEVETDWGLLKGYTYTMTDIRKLRLGERLVEVFSTEKLYMVRLRNPLGRQEWSGPWSEISEEWQQLTVTDRKNLGLVMSDDGEFWMSLEDFCHNFHKLNVCRNVNNPVFGRKELESVVGCWTVDDDPLMNRSGGCYNNRDTFLQNPQYIFTVPEDGHKVIMSLQQKDLRTYRRMGRPDNYIIGFELFKVEMNRRFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLRELTLDMPKMSCWNLARGYPKVVTQITVHSAEGLEKKYANETVNPYLTIKCGKEEVRSPVQKNTVHAIFDTQAIFYRRTTDIPIIIQVWNSRKFCDQFLGQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLTEL 641 A5D7H5 Protein CASC3 9913 None SL-0198 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}. UNIPROT A5D7H5 Pfam PF09405 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}. GO:0010494 GO:0030425 GO:0035145 GO:0016607 GO:0005634 GO:0048471 GO:0071006 GO:0003729 GO:0000398 GO:0051028 GO:0000184 GO:0006417 Unknown UniProt Sequence Analysis MADRRRQRASQDTEDEESGASGSDSGGSPARGGGSCSGSVGGGGSGSLPSQRGGRAGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGDDGEYSEEENSKVELKSEANDAANSSAKDEKGEEKPDTKGTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRFGSPPQRDPSWIGERPNKSHRHQGPGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFKEGRTGFRPAEAGGQHAGRSGETVKHETSYRSRHLEQTPVRDPSPEADAQVLGSPEKEEVAPEIPNPAPDTAPPVPDRPVEKKSYSRARRTRIKAGDAGKVAEEVPPPPEGLTPAPPVPEATPPTPAKTGNWEAPVDSTTGGLEQDVAQLNITEQNWSPGQPAFLQSRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMIVQPEMHLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS 703 Q1ECZ4 Protein casc3 7955 None SL-0198 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}. UNIPROT Q1ECZ4 UNIPROT Q7T1P0 Pfam PF09405 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}. GO:0010494 GO:0030425 GO:0035145 GO:0016607 GO:0005634 GO:0048471 GO:0071006 GO:0003729 GO:0000398 GO:0051028 GO:0000184 GO:0006417 Unknown UniProt Sequence Analysis MADRRRRRRRASQDSEEEDESASGSESGRSFSASRKTRGREPEPVESPAERVAAKSDDESECVSEDGVGEAVLSDYDSADLEENGSHTEGGEEEEEAEHFSEEEASRPAAESKPVADAPTEELVEGEERDESVKEVKADEKGNLAGERQSGDGQESTEDPENKGSKGQKLDDDEDRKNPAYIPRKGLFFEHDVRGQATEEERPKGRNRKLWKDEGRWEHDKFREEEQAPKSRDELIAFYGYDIRNGTGPSDGRSYRSRKPRHAGSPSREPRRYREGDKSVRSSWQGPPPGHRNAPQSVTVQSGQPLAPLSAPKPSGRPSTQPPQRSFQGSRAPSAPHRTEGRGPSKPSLDGAPLRGPRSQPVEGERGPRLRGRSSHAVHADRSPSLVVEDICSEEEEEEGEIPTATTTYTAHHYKTEKERVPSPRKQDSGMVMEGGSAAGQVRELSPPQERQVEKKSYSRARRATRTRPSDLSKQASLDDSSSAVQQAPVAAKSESWQEQSEAGTQSGLTGLDQDLARLSLTGQNWAQNPPSYLQAEMRGIRGSMHMAGGPPQYGNMEDMGVGGGRAKRYSSQRQRPVPEPAPMHIGVMEGHYYEPMTFQGPIYTHGESPAALPPQGMLVQPEMHLPHPTHPGLHPHQSGGPLPNPAIYAAPPVSLSPGQPPPQQLLPPPFYPPPGVMTFGNTNYPYPAGGTLPPMYPNPQAQSQVYGGVTYYDTIQQQAQPKRSPPRRSSNPVTVRPPPPEDQSRKAAEEIRS 754 O15234 Protein CASC3 9606 None SL-0198 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}. UNIPROT O15234 UNIPROT A8K8R0 PDB 2HYI PDB 2J0Q PDB 2J0S PDB 2J0U PDB 2XB2 PDB 3EX7 PDB 5XJC PDB 5YZG PDB 6ICZ Pfam PF09405 OMIM 606504 DisGeNET 22794 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}. P38919 EBI-299122 0.98 P61326 EBI-299142 0.96 O95793 EBI-536629 0.35 Q9Y5S9 EBI-15556968 0.86 Q9BZI7 EBI-15674292 0.79 Q9H1J1 EBI-3869363 0.35 P62993 EBI-3937731 0.37 Q00534 EBI-5292877 0.44 P04578 EBI-6176374 0.35 Q9Y2W1 EBI-6464350 0.40 Q86VP6 EBI-21322532 0.35 P31749 EBI-9065079 0.37 P25054 EBI-9065274 0.37 Q14790 EBI-9066600 0.37 P42771 EBI-9067082 0.37 Q92731 EBI-9067732 0.37 P22455 EBI-9068122 0.37 O60934 EBI-9068798 0.37 P35232 EBI-9069474 0.37 P18031 EBI-9069851 0.37 Q12913 EBI-9070007 0.37 P67809 EBI-9985228 0.35 P41218 EBI-9996028 0.35 Q6P1M3 EBI-11024291 0.35 Q9CWZ3 EBI-11033143 0.35 Q93074 EBI-11039728 0.35 Q9D902 EBI-11096128 0.35 Q8NB78 EBI-11101709 0.35 Q7LFX5 EBI-11123526 0.35 Q6P5F9 EBI-11603310 0.35 Q3LI66 EBI-24633422 0.56 Q9UEU0 EBI-21525256 0.35 P47902 EBI-21581572 0.35 Q12926 EBI-21666158 0.35 Q8IYD1 EBI-21666681 0.35 Q96AK3 EBI-21666867 0.35 Q13595 EBI-21690239 0.35 P26368 EBI-21718427 0.35 P49760 EBI-21726948 0.35 Q6ZUT1 EBI-21727187 0.35 Q8N6W0 EBI-21727590 0.35 Q8TAD8 EBI-21727669 0.35 Q9H307 EBI-21728050 0.35 Q9NQ29 EBI-21728243 0.35 Q9BRP8 EBI-21727928 0.35 Q9NQX1 EBI-21728580 0.35 Q9Y383 EBI-21728858 0.35 Q9UBU9 EBI-21728803 0.35 Q92900 EBI-15784788 0.70 Q9HAU5 EBI-15855293 0.70 Q9UPY3 EBI-20621391 0.35 P03372 EBI-21302175 0.35 Q92574 EBI-26515506 0.37 O60306 EBI-26901687 0.32 P35226 EBI-27109494 0.35 GO:0010494 GO:0005829 GO:0030425 GO:0035145 GO:0031965 GO:0016607 GO:0005654 GO:0005634 GO:0048471 GO:0071006 GO:0019899 GO:0042802 GO:0003729 GO:0003723 GO:0031625 GO:0008298 GO:0006406 GO:0000398 GO:0000184 GO:2000622 GO:0006417 Unknown UniProt Sequence Analysis MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFKEGRAGFRPVEAGGQHGGRSGETVKHEISYRSRRLEQTSVRDPSPEADAPVLGSPEKEEAASEPPAAAPDAAPPPPDRPIEKKSYSRARRTRTKVGDAVKLAEEVPPPPEGLIPAPPVPETTPTPPTKTGTWEAPVDSSTSGLEQDVAQLNIAEQNWSPGQPSFLQPRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMLVQPGMNLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS 703 Q8K3W3 Protein Casc3 10090 None SL-0198 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}. UNIPROT Q8K3W3 UNIPROT A3KFP7 UNIPROT Q3UT99 UNIPROT Q8K219 UNIPROT Q99NF0 Pfam PF09405 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}. P35922 EBI-16728828 0.35 GO:0005737 GO:0010494 GO:0030425 GO:0035145 GO:0031965 GO:0016607 GO:0005634 GO:0048471 GO:1990904 GO:0071006 GO:0019899 GO:0042802 GO:0003729 GO:0031625 GO:0008298 GO:0006406 GO:0000398 GO:0000184 GO:2000622 GO:0006417 Unknown UniProt Sequence Analysis MADRRRQRASQDTEDEESGASGSDSGSPARGGGSCSGSVGGGGSGSLPSQRGGRGGGLHLRRVESGGAKSAEESECESEDGMEGDAVLSDYESAEDSEGEEDYSEEENSKVELKSEANDAADSSAKEKGEEKPESKGTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRFGSSPQRDPNWIGDRSSKSHRHQGPGGNLPPRTFINRNTAGTGRMSASRNYSRSGGFKDGRTSFRPVEVAGQHGGRSAETLKHEASYRSRRLEQTPVRDPSPEPDAPLLGSPEKEEVASETPAAVPDITPPAPDRPIEKKSYSRARRTRTKVGDAVKAAEEVPPPSEGLASTATVPETTPAAKTGNWEAPVDSTTGGLEQDVAQLNIAEQSWSPSQPSFLQPRELRGVPNHIHMGAGPPPQFNRMEEMGVQSGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMIVQPEMHLPHPGLHPHQSPGPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPNYPYAPGALPPPPPPHLYPNTQAPPQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVSIKPPPPEVVSRGSS 698 Q8K3X0 Protein Casc3 10116 None SL-0198 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}. UNIPROT Q8K3X0 Pfam PF09405 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}. GO:0005737 GO:0010494 GO:0030425 GO:0035145 GO:0016607 GO:0005634 GO:0048471 GO:1990904 GO:0071006 GO:0019899 GO:0042802 GO:0003729 GO:0031625 GO:0008298 GO:0000398 GO:0051028 GO:0000184 GO:2000622 GO:0006417 Unknown UniProt Sequence Analysis MADRRRQRASQDTEDEESGASGSDSGSPARGGGSCSGSAGGGGSGSLPSQRGGRGGGLHLRRVESGGAKSAEESECESEDGMEGDAVLSDYESAEDSEGEEEYSEEENSKVELKSEANDAADSSAKEKGEEKPESKGTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRFGSPPQRDPNWIGDRSSKSHRHQGPGGNLPPRTFINRNAAGTGRMSTSRNYSRSGGFKEGRTSFRPVEVGGQHGARSGETLKHEANYRSRRLEQTPMRDPSPEPDAPLLGSPEKEEVASETPAAVPDITPPAPDRPIEKKSYSRARRTRTKVGDAVKAAEEVPPPSEGLTSAATVPESTPPAAKTGNWEAPVDSTTGGLEQDVAQLNIAEQNWSPGQPSFLQPRELRGMPNHIHMGAGPPPQFNRMEEMGVQSGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMIVQPEMHLPHPGLHPHQSPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVSIKPPPSEVVSRGSS 699 A0JMU8 Protein casc3 8355 None SL-0198 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}. UNIPROT A0JMU8 UNIPROT B7ZRY2 Pfam PF09405 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}. GO:0010494 GO:0030425 GO:0035145 GO:0016607 GO:0005634 GO:0048471 GO:0071006 GO:0003729 GO:0000398 GO:0051028 GO:0000184 GO:0006417 Unknown UniProt Sequence Analysis MADRRRRRRRASQDSEGEEEEEESGSDSVGSGGESGAPVRQERSEQGNRKAEPPREGKESECESEDGIEGDAVLSDYESADESEIVPTKEVEEAHYNEEEPLKATLKQENNVEEAPAARDQKPKSKGTVTGERQSGDGQESNEPEEDKTIQKSQKQLDDDEDRKNPAYIPRKGLFFEHDLRGHVNDEEVRPKGRHPRKLWKDEGRWVHDRFHEDEQAPKSREELISIYGYDIRSSKNPEEIRPRRPRKPRFSSPSRREENNEKASWPLNRYQDSGDAQPLRPYTNRSAPPSNKVVPSRTYSRQGGYKENRASYQSEEEASLHTYERRQVYGGHRARSSEQGPPPPREFSPEADPIVKEEAVIEKQAAEPSPPPPDRPVEKKSYSRARRSRIKVGDTGKSMEDTTAAELPPPPLMPPAVAAEFTPAPLNVKQGNWEPPAEGGMSGIDEELSQMNLTEQSWNQGQPAYISPRGIPNPMHMGNGPPQYSRMEGMAVQGGRVKRYSSQRQRPVPDPAAMHISLMESHYYDPLQFQGPIYTHGDSSSSMPPQGMIVPPEMHLSHPGMHPHPSPATMSTPNLYPAPVSLPPGQQPPQQLLPPPYFPAPPNVMNFGNPTYPYPPGALPPPPAHLYPNAQAQSQVYGGVTYYNPVQQQVQPKPSPPRRTSQPVTIKPPPPEENRHLKMNEKINS 686 Q5CZI8 Protein casc3 8364 None SL-0198 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}. UNIPROT Q5CZI8 Pfam PF09405 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}. GO:0010494 GO:0030425 GO:0035145 GO:0016607 GO:0005634 GO:0048471 GO:0071006 GO:0003729 GO:0000398 GO:0051028 GO:0000184 GO:0006417 Unknown UniProt Sequence Analysis MADRRRRRRRAFQDSEEEEDEESGSESAGSGGQPAAPSRQESREPGTKRAEPPREGKESECESEDGIEGDAVLSDYESAESEEEEAHLSEEEPLKTTLKQENNVEEAPATREQKPKSKGAVTGERQSGDGQESTEPEENKTSKKSQKQLDDDEDRKNPAYIPRKGLFFEHDLRGHVNDEEVRPKGRHPRKLWKDEGRWEHDRFREDEQAPKSREELISIYGYDIRSSKNSEEIRPRRPRKPRFGSPTRREEISEKPSRPSNRYQDSGISQPLRPYTNRNAPPSNKVGPSRTYSRQGGYKENRSSYQSEEEAPPHPSERRQDYGGHRARSTEQGPAPPREFSPEADPIIKEEPVIEKQAAEPSPPPPDRPVEKKSYSRVRRSRIKVGDTGKSMEDTTVTELPPPPPVPPAVAAEFTPAPLNVKQGNWEPPSEGGMSGIEEELSQMNLSEQSWNPGQPAYISPRGIPNPMHMGGGPPQYNRMEGMAVQGGRVKRYSTQRQRPVPDPAAMHISLMESHYYDPLQFQGPIYAHGDSPSSMPPQGMIVQPEMHLSHPGIHPHQPPATISTPNLYPAPVSLPPGQPPPQQLLPPPYFTAPPNVMNFGNPTYPYPPGALPPPPAHLYPNAQAQSQVYGGVTYYNPVQQQVQPKPSPPRRTSQPVTIKPPPPEENRHVKMKEKSNS 678 Q5H8A6 Ion CASTOR 34305 None SL-0178 SL-0182 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. UNIPROT Q5H8A6 PDB 6O6J PDB 6O7A PDB 6O7C Pfam PF06241 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}. GO:0016021 GO:0031965 GO:0006811 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSLDSEVSVSSSSGRDWFFPSPSFFRSSPSQYGRRFHTNSNTHSAPSSTYPSGIRHRRRVKFSRTPTTSSNEKPQISIVSDKPSAISKNNLNWLSQFGLQFALVTLTIVFLLLLLLRNTHLESQVNKLQGEILRLHACHQLDTLNVSSSTAHKSQDTHPCSCENFKRNLALFLSFMLLLIPLIIFKYIDYVSRSRLSENISEQVSLNKQIAYRVDVFLSVYPYAKPLVLLVATLLLIFLGGLTLFGVTTEDLGHCLWLSWTYVADSGNHASSEGIGPRLVAVSISFGGMLIFAMMLGLVSDAISEKFDSLRKGKSEVVEQNHTLILGWSDKLGSLLNQLAIANESLGGGTIAVMAERDKEDMELDIGKMEFDFKGTSVICRSGSPLILADLKKVSVSKARTIIVLAEDGNADQSDARALRTVLSLTGVKEGLRGHIVVEMSDLDNEVLVKLVGGDLVETVVAHDVIGRLMIQCARQPGLAQIWEDILGFENCEFYIKRWPQLDGMLFEDVLISFPAAIPCGIKVASYGGKIILNPDDSYVLQEGDEVLVIAEDDDTYAPAPLPMVRRGSLPKDFVYPKSPERILFCGWRRDMEDMITVLDASLAPDSELWMFNDVPEKEREKKLIDGGLDISRLENISLVNREGNAVIRRHLESLPLESFDSILILADESVEDSAIQADSRSLATLLLIRDIQARRLPYVAMASQTQGGNFSKGSWIGEMKQASDKTVIISEILDPRTKNLLSMSKISDYVLSNELVSMALAMVAEDRQINDVLEELFAEEGNEMHIRQADIYLREGEEMSFYEIMLRARQRREILIGYRLANAERAVINPPAKTGRRKWSLKDVFVVITEKE 853 Q75LD5 Probable OSJNBa0032G11 39947 None SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q75LD5 UNIPROT Q10AR8 Pfam PF06241 Required for mycorrhizal symbiosis. {ECO:0000269|PubMed:18852152, ECO:0000269|PubMed:18978069}. GO:0016021 GO:0031965 GO:0006811 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPLDPDSSPAPPHRDWFFPPAPPFLPSSRARTPRAPFPSTSRSSNPYSFPDRRPPPTPRSRSRSPLPPPEQQKQQQPPPTTPPPAPRRRDPRYAGVRRGDVRTLTAEKAAAAAAVPTAAQVHGSKSAASATTLRWSGMVSVAAIVLCFSSLVRSNSSLHDQVHHLKAQLAEATTKLQSCITESSMDMSSILSYQSNNSTSQNRGLKNFSLLLSLSTLYAPLLILKYMDLFLKLRSSQDSEEEVPINKRLAYRVDIFLSLQPYAKPLVLLVATLLLIGLGGLALYGVNDDSLLDCLWLSWTFVADSGNHANAEGFGPKLVSVSISIGGMLVFAMMLGLVTDSISEKFDSLRKGRSEVIEQSHTLVLGWSDKLGSLLNQIAIANESLGGGTIVVMAEKDKEEMEADIAKMEFDLKGTAIICRSGSPLILADLKKVSVSKARAIVVLAEEGNADQSDARALRTVLSLTGVKEGLRGHIVVELSDLDNEVLVKLVGGDLVETVVAHDVIGRLMIQCARQPGLAQIWEDILGFENCEFYIKRWPQLDGMQFEDVLISFPDAIPCGIKVASYGGKIILNPDDFYVLQEGDEVLVIAEDDDTYAPAPLPKVMRGYLPKDFVVPKSPERILFCGWRRDMEDMIMVLDAFLAPGSELWMFNDVPEMDRERKLIDGGLDFSRLENITLVHREGNAVIRRHLESLPLESFDSILILADESVEDSAIQADSRSLATLLLIRDIQAKRLPFREAMVSHVTRGSFCEGSWIGEMQQASDKSVIISEILDPRTKNLLSVSKISDYVLSNELVSMALAMVAEDRQINDVLEELFAEQGNEMQIRPADLYLREDEELNFFEVMLRGRQRKEIVIGYRLVDAERAIINPPDKVSRRRWSAKDVFVVITEKE 893 Q91ZF2 Cathepsin Cts7 10090 None SL-0198 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}. UNIPROT Q91ZF2 UNIPROT Q9JI84 Pfam PF08246 Pfam PF00112 PROSITE PS00139 PROSITE PS00639 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}. GO:0005768 GO:0005576 GO:0005615 GO:0005794 GO:0005764 GO:0005634 GO:0048471 GO:0004197 GO:0008233 GO:0051301 GO:0006955 GO:0000278 GO:0045930 GO:0006508 GO:0051603 GO:0060707 Unknown UniProt Sequence Analysis MTPTVFLSILCLGVALAAPAPDYNLDAEWEEWKRSNDRTYSPEEEKQRRAVWEGNVKWIKQHIMENGLWMNNFTIEMNEFGDMTGEEMKMLTESSSYPLRNGKHIQKRNPKIPPTLDWRKEGYVTPVRRQGSCGACWAFSVTACIEGQLFKKTGKLIPLSVQNLMDCSVSYGTKGCDGGRPYDAFQYVKNNGGLEAEATYPYEAKAKHCRYRPERSVVKVNRFFVVPRNEEALLQALVTHGPIAVAIDGSHASFHSYRGGIYHEPKCRKDTLDHGLLLVGYGYEGHESENRKYWLLKNSHGERWGENGYMKLPRGQNNYCGIASYAMYPAL 331 D3ZZ07 Cathepsin Cts7 10116 None SL-0198 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}. UNIPROT D3ZZ07 Pfam PF08246 Pfam PF00112 PROSITE PS00139 PROSITE PS00639 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}. GO:0005768 GO:0005615 GO:0005794 GO:0005764 GO:0005634 GO:0048471 GO:0004197 GO:0051301 GO:0006955 GO:0000278 GO:0045930 GO:0051603 GO:0060707 Unknown UniProt Sequence Analysis MTVAVFLAILCLRAALAAPRPDYSLDAEWEEWKRNNAKTYSPEEEKQRRAVWEENVKMIKWHTMQNGLWMNNFTIEMNEFGDMTGEEMRMMTDSSALTLRNGKHIQKRNVKIPKTLDWRDTGCVAPVRSQGGCGACWAFSVAASIESQLFKKTGKLIPLSVQNLIDCTVTYGNNDCSGGKPYTAFQYVKNNGGLEAEATYPYEAKLRHCRYRPERSVVKIARFFVVPRNEEALMQALVTYGPIAVAIDGSHASFKRYRGGIYHEPKCRRDTLDHGLLLVGYGYEGHESENRKYWLLKNSHGEQWGERGYMKLPRDQNNYCGIASYAMYPLL 331 Q8IX12 Cell CCAR1 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:12816952}. UNIPROT Q8IX12 UNIPROT A0JLT7 UNIPROT A1L4P7 UNIPROT A8K9D4 UNIPROT B4DNP8 UNIPROT B4DRK8 UNIPROT Q32NE3 UNIPROT Q5EBM3 UNIPROT Q5VUP6 UNIPROT Q6PIZ0 UNIPROT Q6X935 UNIPROT Q9H8N4 UNIPROT Q9NVA7 UNIPROT Q9NVQ0 UNIPROT Q9NWM6 Pfam PF19257 Pfam PF14443 Pfam PF19256 Pfam PF14444 Pfam PF02037 PROSITE PS50800 OMIM 612569 DisGeNET 55749 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}. K9N7C7 EBI-26374923 0.35 O43542 EBI-11129266 0.35 P07948 EBI-25379971 0.35 Q8IWX8 EBI-7721515 0.37 Q9Y6K9 EBI-21708976 0.35 Q9BTT4 EBI-394793 0.35 Q920D3 EBI-394916 0.35 Q15428 EBI-7292802 0.40 Q969Q1 EBI-7745325 0.51 Q9BYV6 EBI-7745490 0.40 Q9HAU4 EBI-7746831 0.37 E9Q5G3 EBI-2561306 0.40 P29692 EBI-2688113 0.00 A0A6L7HJW4 EBI-2813341 0.00 A0A6L8PAG8 EBI-2836932 0.00 Q92731 EBI-2880601 0.35 Q9GZV5 EBI-2927886 0.40 Q9EPK5 EBI-2928071 0.46 P05131 EBI-2931831 0.35 Q9BQS8 EBI-3242919 0.35 P26368 EBI-7718617 0.37 P98175 EBI-7723515 0.37 P61978 EBI-7723565 0.37 O15541 EBI-7723603 0.37 P19320 EBI-6189915 0.35 Q08379 EBI-10262415 0.72 Q9NQM4 EBI-10262427 0.56 E9PUA5 EBI-10999661 0.35 Q7TSY8 EBI-11011396 0.35 Q9EP53 EBI-11016226 0.35 O00159 EBI-11030803 0.35 Q1H9T6 EBI-11104278 0.35 A0A286YCX6 EBI-11119288 0.35 P09450 EBI-11127973 0.35 Q15006 EBI-11130215 0.35 Q8N4V1 EBI-11130635 0.35 Q9Y2D8 EBI-11363757 0.35 Q5JR59 EBI-24372606 0.56 Q13643 EBI-21785384 0.35 Q15942 EBI-21889175 0.35 Q92609 EBI-20919940 0.40 Q7Z422 EBI-20924474 0.40 Q9BY12 EBI-20929648 0.40 Q96HF1 EBI-20930680 0.40 Q8TCG1 EBI-20933820 0.40 Q9NPJ6 EBI-25472377 0.35 Q5S007 EBI-21360986 0.35 P03372 EBI-21301141 0.35 P09429 EBI-21461848 0.37 P05771 EBI-25379671 0.35 Q5SSL4 EBI-25409695 0.35 Q6B0I6 EBI-25480104 0.35 P69479 EBI-25568051 0.35 P52298 EBI-26398473 0.35 Q53F19 EBI-26398788 0.35 Q13363 EBI-27046166 0.35 P78362 EBI-28948274 0.35 O15178 EBI-29014443 0.27 P15976 EBI-29016000 0.27 P23771 EBI-29016184 0.27 Q8TDD2 EBI-29740517 0.27 GO:0005641 GO:0005654 GO:0005634 GO:0048471 GO:0030374 GO:0003723 GO:0000978 GO:0003713 GO:0003714 GO:0006915 GO:0007049 GO:0043065 GO:0030335 GO:0008284 GO:0006355 Unknown UniProt Sequence Analysis MAQFGGQKNPPWATQFTATAVSQPAALGVQQPSLLGASPTIYTQQTALAAAGLTTQTPANYQLTQTAALQQQAAAAAAALQQQYSQPQQALYSVQQQLQQPQQTLLTQPAVALPTSLSLSTPQPTAQITVSYPTPRSSQQQTQPQKQRVFTGVVTKLHDTFGFVDEDVFFQLSAVKGKTPQVGDRVLVEATYNPNMPFKWNAQRIQTLPNQNQSQTQPLLKTPPAVLQPIAPQTTFGVQTQPQPQSLLQAQISAASITPLLQTQPQPLLQQPQQKAGLLQPPVRIVSQPQPARRLDPPSRFSGRNDRGDQVPNRKDDRSRERERERRRSRERSPQRKRSRERSPRRERERSPRRVRRVVPRYTVQFSKFSLDCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKNMAILDPPDADHLYSAKVMLMASPSMEDLYHKSCALAEDPQELRDGFQHPARLVKFLVGMKGKDEAMAIGGHWSPSLDGPDPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRPEETHKGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGERKEADGEQDEEEKDDGEAKEISTPTHWSKLDPKTMKVNDLRKELESRALSSKGLKSQLIARLTKQLKVEEQKEEQKELEKSEKEEDEDDDRKSEDDKEEEERKRQEEIERQRRERRYILPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSLLSLPEKEDKKEKDKKSKKDERKDKKEERDDETDEPKPKRRKSGDDKDKKEDRDERKKEDKRKDDSKDDDETEEDNNQDEYDPMEAEEAEDEEDDRDEEEMTKRDDKRDINRYCKERPSKDKEKEKTQMITINRDLLMAFVYFDQSHCGYLLEKDLEEILYTLGLHLSRAQVKKLLNKVVLRESCFYRKLTDTSKDEENHEESESLQEDMLGNRLLLPTPTVKQESKDVEENVGLIVYNGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVKKDLSQLQENLKISENMNLQFENQMNKTIRNLSTVMDEIHTVLKKDNVKNEDKDQKSKENGASV 1150 Q8CH18 Cell Ccar1 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q8CH18 UNIPROT Q05BR1 UNIPROT Q05DK6 UNIPROT Q6AXC9 UNIPROT Q6PAR2 UNIPROT Q80XE4 UNIPROT Q8BJY0 UNIPROT Q8BVN2 UNIPROT Q8CGG1 UNIPROT Q9CSR5 Pfam PF19257 Pfam PF14443 Pfam PF19256 Pfam PF14444 Pfam PF02037 PROSITE PS50800 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}. P47811 EBI-654069 0.37 P59240 EBI-4287460 0.35 P70326 EBI-16360068 0.35 Q61584 EBI-16729686 0.35 Q7TPH6 EBI-16731507 0.35 Q14B62 EBI-27105988 0.35 GO:0005641 GO:0005634 GO:0048471 GO:0030374 GO:0000978 GO:0003713 GO:0003714 GO:0006915 GO:0007049 GO:0043065 GO:0030335 GO:0008284 GO:0006355 Unknown UniProt Sequence Analysis MAQFGGQKNPPWATQFTATAVSQPAALGVQQPSLLGASPTIYTQQTALAAAGLTTQTPANYQLTQTAALQQQAAAVLQQQYSQPQQALYSVQQQLQQPQQTILTQPAVALPTSLSLSTPQPAAQITVSYPTPRSSQQQTQPQKQRVFTGVVTKLHDTFGFVDEDVFFQLGAVKGKTPQVGDRVLVEATYNPNMPFKWNAQRIQTLPNQNQSQTQPLLKTPTAVIQPIVPQTTFGVQAQPQPQSLLQAQISAASITPLLQTQPQPLLQQPQQKAGLLQPPVRIVSQPQPARRLDPPSRFSGRNDRGDQVPNRKDDRSRERDRERRRSRERSPQRKRSRERSPRRERERSPRRVRRVVPRYTVQFSKFSLDCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKNMAVLDPPDADHLYSAKVMLMASPSMEDLYHKSCALAEDPQDLRDGFQHPARLVKFLVGMKGKDEAMAIGGHWSPSLDGPNPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRPEETHKGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGERKKADGEQDEEEKDDGEVKEIATPTHWSKLDPKAMKVNDLRKELESRALSSKGLKSQLIARLTKQLKIEEQKEEQKELEKSEKEEEDEDDKKSEDDKEEEERKRQEEVERQRQERRYILPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSLLSLPEKEDKKDKEKKSKKEERKDKKEEREDDIDEPKPKRRKSGDDKDKKEDRDERKKEEKRKDDSKDDDETEEDNNQDEYDPMEAEEAEDEDDDREEEEVKRDDKRDVSRYCKDRPAKDKEKEKPQMVTVNRDLLMAFVYFDQSHCGYLLEKDLEEILYTLGLHLSRAQVKKLLNKVVLRESCFYRKLTDTSKDDENHEESEALQEDMLGNRLLLPTPTIKQESKDGEENVGLIVYNGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDGKTILNLENSNKSLSGELREVKKDLGQLQENLEVSENMNLQFENQLNKTLRNLSTVMDDIHTVLKKDNVKSEDRDEKSKENGSGV 1146 Q641G3 Cell ccar1 8355 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IX12}. UNIPROT Q641G3 Pfam PF19257 Pfam PF14443 Pfam PF19256 Pfam PF14444 Pfam PF02037 PROSITE PS50800 Transcriptional coactivator for nuclear receptors which may play an important role in regulating cell growth and apoptosis. {ECO:0000250|UniProtKB:Q8IX12}. Q6P5F9 EBI-11606853 0.35 GO:0048471 GO:0007049 GO:0006355 GO:0006417 Unknown UniProt Sequence Analysis MAQFGGQKNPPPWATQFTATAVSQPGPLAVQQSSLLGASPTIYTQQSALAAAGLASPSPANYQLSQTAALQQQAAAAAAAAAAALQQQYTQPQQTIYSVQQQLQPPPQAILTQPAVALPTSLALSTPQQAAQITVSYPTPRSNQQQTQPQKQRVFTGVVTKLHETFGFVDEDVFFQLTAVKGKSPQAGDRVLVEATYNPNMPFKWNAQRIQTLPNQNPASAQSLIKNPAAVMQPVAQPTAYAVQTQPPPQAQTLLQAQISAATLTPLLQTQTSPLLQQPQQKAGLLQTPVRIVSQPQPVRRIEPPSRFSVRNDRGDSILSRKDDRNRERERERRRSRDRSPQRKRSRERSPRRERERSPRRPRRVVPRYTVQISKFCLDCPGCDTMELRRRYQNLYIPSDFFDAQFTWVDAFPISRPFQLGNYSNFYIMHKEVDPLEKNTAIVDPPDADHTYSAKVMLLASPSLEELYHKSCALAEDPIEVREGFQHPARLIKFLVGMKGKDEAMAIGGHWSPSLDGPNPDKDPSVLIRTAVRCCKALTGIELSLCTQWYRFAEIRYHRPEETHKGRTVPAHVETVVLFFPDVWHCLPTRSEWENLCHGYKQQLVDKLQGDRKEADGEQEEEDKEDGDAKEISTPTHWSKLDPKIMKVNDLRKELESRTLSSKGLKSQLIARLTKQLRIEEQKEEQKELEKCEKEEEEEEERKSEDDKEEEERKRQEELERQRREKRYMLPDEPAIIVHPNWSAKNGKFDCSIMSLSVLLDYRIEDNKEHSFEVSLFAELFNEMLQRDFGVRIYRELLALPEKEEKKDKEKKCKKEDKRERKEDKDDDDEPKPKRRKSSDDKIKLEEKEERKRDDRRKEDYREEDDPDYENQDDYEPIAAEEDDGDYDDREDDDDDSSSKDKREDKRDGNRYSKERQSKDKEKDKKQMVTVNRDLLMAFVYFDQSHCGYLLEKDLEEILYTLGLHLSRAQVKKLFTKILLKESLLYRKLTDTATEDGSHEETDPLHNDILGNCSLLPSKAVRTGLSTVEDKGGLIVYKGAMVDVGSLLQKLEKSEKTRTELEHRLQTLESKTEEDEKTISQLEASNRNLSEELKQTKDDVGHLKDSLKAAEDTRSLYEDQLTNTIKNLSAAMGEIQVVLNKNPSTTEDQKSKENGSS 1157 A2IDD5 Coiled-coil CCDC78 9606 None SL-0198 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. UNIPROT A2IDD5 UNIPROT B4DNY4 UNIPROT B4E1U6 UNIPROT Q05BY7 UNIPROT Q05CA0 UNIPROT Q6T2V5 UNIPROT Q6ZR33 UNIPROT Q8IUR3 UNIPROT Q8NAY7 UNIPROT Q96S12 Pfam PF14739 OMIM 614666 OMIM 614807 DisGeNET 124093 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}. 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. Q8D194 EBI-2874016 0.00 Q0VD86 EBI-24727262 0.56 Q9NQ75 EBI-21371981 0.00 GO:0005814 GO:0005737 GO:0098536 GO:0048471 GO:0042383 GO:0016529 GO:0030030 GO:0098535 GO:0003009 Unknown UniProt Sequence Analysis MEHAATTGPRPGPPSRRVENVVLRAKDWLPGAPGGTAVWATSLEAEVPPDLALNKEQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQHRLGSGLQGEVKWALEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKLKDEYVLRLQHCAWQAVEHADGAGQAPATTALRTFLEATLEDIRAAHRSREQQLARAARSYHKRLVDLSRRHEELLVAYRAPGNPQAIFDIASLDLEPLPVPLVTDFSHREDQHGGPGALLSSPKKRPGGASQGGTSEPQGLDAASWAQIHQKLRDFSRSTQSWNGSGHSCWSGPRWLKSNFLSYRSTWTSTWAGTSTKS 438 D3Z5T1 Coiled-coil Ccdc78 10090 None SL-0198 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}. UNIPROT D3Z5T1 Pfam PF14739 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}. GO:0005814 GO:0005737 GO:0098536 GO:0048471 GO:0042383 GO:0016529 GO:0030030 GO:0098535 GO:0003009 Unknown UniProt Sequence Analysis MDQRPELLSSMEYVASPDPKPGVPLRVAENVAPGAEDWLPSASGHLAWATSLETEHQTHLELSEEQRLQISKELVDLQIATHHLREQHEAEVFELRREILRLESRVLELELHGNGACQGHKVQPMANLGQHQVPPLEPPGGQQKLQEELKWLLEHHRARQQALETQVGVLSQQLQGAREEARTTGQQLASQAMVLASCKGQLRQAEAENTQLQLQLKKMNEEYAVRLQHYARETVENASSTNQAALQAFLESTLQDIRAAHRTREQQLAQAARTYRKRLADLNQRQELLLTTCRATFATAINLEPLPMHWATELSHPRENEYGRHRTLLLYPEKGSGETSKENKSQPLALDTASWAQIQQRLQDFSQDTQAELERERAQLMVRATMAEQQLSELQEYVDQHLGRYKQEILKLRKLVNIGDPQGVEAVSSPGSGGARL 437 Q2KI22 G1/S-specific CCND1 9913 None SL-0178 SL-0182 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}. UNIPROT Q2KI22 Pfam PF02984 Pfam PF00134 PROSITE PS00292 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}. GO:0000307 GO:0005737 GO:0031965 GO:0005634 GO:0017053 GO:0016538 GO:0003714 GO:0051301 GO:0006974 GO:0000082 GO:0044772 GO:0031571 GO:0000122 GO:0045737 GO:1900087 GO:0010971 GO:0001934 GO:0000079 GO:0070141 Unknown UniProt Sequence Analysis MAHQLLCCEMETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEILPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPDELLHMELVLVNKLKWNLAAMTPHDFIEHFLSKMPVAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVAAAAQGLHLGSANGFLSYHRLTRFLSKVIRCDPDCLRACQEQIEALLESSLRQAQQQNLDPKAAEEEEEEEEVDLACTPTDVRDVNI 295 Q64HP0 G1/S-specific CCND1 9615 None SL-0178 SL-0182 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}. UNIPROT Q64HP0 Pfam PF02984 Pfam PF00134 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}. GO:0000307 GO:0005737 GO:0031965 GO:0005634 GO:0017053 GO:0016538 GO:0003714 GO:0051301 GO:0006974 GO:0000082 GO:0044772 GO:0031571 GO:0000122 GO:0045737 GO:1900087 GO:0010971 GO:0001934 GO:0000079 GO:0070141 Unknown UniProt Sequence Analysis MAHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEILPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLNRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPDELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPVAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLHLGSSNSFLSYHRLTRFLSKVIKCDADCLRACQEQIEALLESSLRQAQQQSLDPKAAEEEEEEEEADLACTPTDVRDVNI 295 P24385 G1/S-specific CCND1 9606 None SL-0178 SL-0182 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}. UNIPROT P24385 UNIPROT Q6LEF0 PDB 2W96 PDB 2W99 PDB 2W9F PDB 2W9Z PDB 5VZU PDB 6P8E PDB 6P8F PDB 6P8G PDB 6P8H Pfam PF02984 Pfam PF00134 PROSITE PS00292 OMIM 168461 OMIM 254500 DisGeNET 595 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}. 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. P11802 EBI-375341 0.98 O43929 EBI-375191 0.44 Q7L590 EBI-375236 0.44 P38936 EBI-375359 0.96 Q00534 EBI-375368 0.73 P46527 EBI-519440 0.86 P36873 EBI-1207106 0.00 P62140 EBI-1207225 0.00 P24941 EBI-1245713 0.74 P38398 EBI-1381572 0.46 P30285 EBI-6988572 0.40 Q9BQA1 EBI-2940933 0.35 O60477 EBI-3904862 0.37 P06858 EBI-3905646 0.37 Q9H9Y6 EBI-3912891 0.37 Q15276 EBI-3927352 0.37 Q61193 EBI-3956268 0.40 P11233 EBI-3956368 0.27 Q62796 EBI-3958451 0.40 O15211 EBI-3970188 0.44 P06400 EBI-4479659 0.73 Q96PU4 EBI-6051700 0.60 P51668 EBI-6051865 0.44 Q29504 EBI-6051865 0.44 O95273 EBI-7803086 0.40 P11142 EBI-6557805 0.40 P49841 EBI-6594575 0.27 Q13761 EBI-8874899 0.46 Q9BU70 EBI-8996209 0.37 Q5T7W7 EBI-8996222 0.37 O60729 EBI-8996235 0.37 P49336 EBI-8996248 0.37 P17936 EBI-8996274 0.37 Q00597 EBI-8996261 0.37 Q15797 EBI-8996300 0.37 Q96LZ3 EBI-8996287 0.37 Q9BYX2 EBI-8996313 0.37 Q8NHU6 EBI-8996326 0.37 Q9Y2H8 EBI-8996339 0.37 Q9H6U6 EBI-9066887 0.37 P55290 EBI-9066900 0.37 P49862 EBI-9066913 0.37 Q9UKQ9 EBI-9066926 0.37 P42771 EBI-9691857 0.49 Q96TE0 EBI-10201598 0.56 P20020 EBI-11132222 0.35 P05141 EBI-11132222 0.35 P43251 EBI-11132222 0.35 P06493 EBI-11132222 0.53 O60673 EBI-11132222 0.35 Q5VK71 EBI-11602009 0.40 O43823 EBI-11602073 0.40 P49815 EBI-11687054 0.40 Q9UJK0 EBI-21832810 0.35 Q07283 EBI-21832810 0.35 Q00535 EBI-21832810 0.35 P49918 EBI-21832810 0.35 P42773 EBI-21832810 0.35 P10275 EBI-15566960 0.54 O15379 EBI-15567015 0.54 Q16656 EBI-15593340 0.51 Q5XUX0 EBI-15777409 0.58 P30260 EBI-15851991 0.50 P12830 EBI-15852068 0.40 Q02224 EBI-16716754 0.35 O95239 EBI-16716754 0.35 O94880 EBI-16716754 0.35 Q9UH17 EBI-25296686 0.27 P59595 EBI-25746873 0.58 P12004 EBI-26956397 0.44 GO:0005923 GO:0097128 GO:0000307 GO:0005737 GO:0005829 GO:0031965 GO:0005654 GO:0005634 GO:0017053 GO:0016538 GO:0019899 GO:0042826 GO:0070064 GO:0004672 GO:0019901 GO:0044877 GO:0003714 GO:0051301 GO:0006974 GO:0030968 GO:0045444 GO:0000082 GO:0007595 GO:0033327 GO:0097421 GO:0060749 GO:0033598 GO:0044772 GO:0031571 GO:0030857 GO:0043524 GO:0000122 GO:0030182 GO:0045737 GO:1900087 GO:0010971 GO:0033601 GO:0001934 GO:0006468 GO:0000320 GO:0000079 GO:0051592 GO:0051412 GO:0032355 GO:0043627 GO:0045471 GO:0010039 GO:0044321 GO:0032026 GO:0010243 GO:0070141 GO:0033197 GO:0010165 GO:0009410 GO:0016055 Unknown UniProt Sequence Analysis MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI 295 P25322 G1/S-specific Ccnd1 10090 None SL-0178 SL-0182 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}. UNIPROT P25322 Pfam PF02984 Pfam PF00134 PROSITE PS00292 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}. P30285 EBI-1005778 0.94 Q64261 EBI-1005805 0.35 P46414 EBI-1005805 0.35 P97377 EBI-1005805 0.35 P63087 EBI-1202844 0.00 Q99J09 EBI-2939789 0.35 Q8CIG8 EBI-2939789 0.61 O14744 EBI-2941110 0.35 Q9BQA1 EBI-2941649 0.40 P63321 EBI-3956288 0.46 P11234 EBI-3956307 0.40 Q6KAR6 EBI-3956307 0.46 Q9JIW9 EBI-3956328 0.27 P11233 EBI-3956335 0.27 P09055 EBI-3956355 0.27 Q62796 EBI-3956408 0.40 Q01101 EBI-9253124 0.35 O88895 EBI-9253173 0.40 P13405 EBI-11508299 0.40 Q9DBR0 EBI-11602084 0.40 Q9WU00 EBI-15593322 0.35 P11440 EBI-15652518 0.40 GO:0005923 GO:0097128 GO:0000307 GO:0005737 GO:0005829 GO:0031965 GO:0005654 GO:0005634 GO:0017053 GO:0016538 GO:0019899 GO:0042826 GO:0016301 GO:0070064 GO:0004672 GO:0019901 GO:0044877 GO:0003714 GO:0051301 GO:0008283 GO:0006974 GO:0071310 GO:0030968 GO:0045444 GO:0000082 GO:0007595 GO:0033327 GO:0097421 GO:0060749 GO:0033598 GO:0044772 GO:0031571 GO:0030857 GO:0043524 GO:0000122 GO:0030182 GO:0008284 GO:0045737 GO:1900087 GO:0010971 GO:0033601 GO:0001934 GO:0006468 GO:0000320 GO:0051726 GO:0000079 GO:2000045 GO:0051592 GO:0051412 GO:0032355 GO:0043627 GO:0045471 GO:0010039 GO:0044321 GO:0032026 GO:0010243 GO:0070141 GO:0033197 GO:0010165 GO:0009410 GO:0016055 Unknown UniProt Sequence Analysis MEHQLLCCEVETIRRAYPDTNLLNDRVLRAMLKTEETCAPSVSYFKCVQKEIVPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPLKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEADENKQTIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAMQGLNLGSPNNFLSCYRTTHFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNVDPKATEEEGEVEEEAGLACTPTDVRDVDI 295 Q5R6J5 G1/S-specific CCND1 9601 None SL-0178 SL-0182 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}. UNIPROT Q5R6J5 Pfam PF02984 Pfam PF00134 PROSITE PS00292 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}. GO:0005923 GO:0097128 GO:0000307 GO:0005737 GO:0031965 GO:0005654 GO:0005634 GO:0017053 GO:0016538 GO:0042826 GO:0070064 GO:0004672 GO:0019901 GO:0003714 GO:0051301 GO:0006974 GO:0030968 GO:0045444 GO:0000082 GO:0007595 GO:0097421 GO:0060749 GO:0033598 GO:0031571 GO:0030857 GO:0043524 GO:0000122 GO:0030182 GO:0045737 GO:0010971 GO:0033601 GO:0001934 GO:0006468 GO:0000320 GO:0044321 GO:0070141 GO:0009410 GO:0016055 Unknown UniProt Sequence Analysis MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAALTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNSFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI 295 P39948 G1/S-specific Ccnd1 10116 None SL-0178 SL-0182 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}. UNIPROT P39948 Pfam PF02984 Pfam PF00134 PROSITE PS00292 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}. P63322 EBI-3956381 0.27 GO:0005923 GO:0097128 GO:0000307 GO:0005737 GO:0031965 GO:0005654 GO:0005634 GO:0017053 GO:0016538 GO:0019899 GO:0042826 GO:0016301 GO:0070064 GO:0004672 GO:0019901 GO:0044877 GO:0003714 GO:0031100 GO:0051301 GO:0008283 GO:0006974 GO:0071310 GO:0030968 GO:0045444 GO:0000082 GO:0007595 GO:0033327 GO:0001889 GO:0097421 GO:0060749 GO:0033598 GO:0044772 GO:0031571 GO:0030857 GO:0043524 GO:0000122 GO:0030182 GO:0008284 GO:0045737 GO:1900087 GO:0010971 GO:0033601 GO:0001934 GO:0006468 GO:0000320 GO:0050790 GO:0051726 GO:0000079 GO:2000045 GO:0051592 GO:0051412 GO:0032355 GO:0043627 GO:0045471 GO:0051384 GO:0010039 GO:0044321 GO:0032026 GO:0014070 GO:0010033 GO:0010243 GO:0048545 GO:0070141 GO:0033197 GO:0010165 GO:0009410 GO:0016055 Unknown UniProt Sequence Analysis MEHQLLCCEVETIRRAYPDTNLLNDRVLRAMLKTEETCAPSVSYFKCVQREIVPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPLKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEADENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAMQGLNLGSPNNFLSCYRTTHFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNIDPKATEEEGEVEEEAGLACTPTDVRDVDI 295 Q0P5D3 G1/S-specific CCND2 9913 None SL-0178 SL-0182 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}. UNIPROT Q0P5D3 Pfam PF02984 Pfam PF00134 PROSITE PS00292 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}. GO:0000785 GO:0097129 GO:0000307 GO:0005737 GO:0005829 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0016538 GO:0019901 GO:0008344 GO:0051301 GO:0071481 GO:0007616 GO:0044772 GO:0043066 GO:0008284 GO:0045737 GO:1900087 GO:0000079 Unknown UniProt Sequence Analysis MELLCGEVEPVRRAVPDANLLHDDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAINYLDRFLAGVPTPKTHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPQPSEKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEDVSSLTGDALVDLLAKITNTDVDCLKACQEQIEVVLLNSLQQYRQDQGDGSKSEDELDQASTPTDVRDIDL 289 P49706 G1/S-specific CCND2 9031 None SL-0178 SL-0182 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}. UNIPROT P49706 Pfam PF02984 Pfam PF00134 PROSITE PS00292 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}. GO:0000307 GO:0005737 GO:0031965 GO:0005634 GO:0016538 GO:0051301 GO:0044772 GO:1900087 GO:0000079 Unknown UniProt Sequence Analysis MELLCCEVDPMRRALPDPNLLYDDRVLHNLLTIEERYLPQCSYFKCVQKDIQPFMRRMVATWMLEVCEEQKCEEEVFPLAMNYLDRFLAVVPTRKCHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPLPKDKLVLIRKHAQTFIALCATDFNFAMYPPSMIATGSVGAAICGLQLDDGDRSLSGDSLTDFLAKITSTDVDCLKACQEQIESVLVSNLRQVRQQQQQSNPSKTIEELDQASTPTDVRDINL 291 P30279 G1/S-specific CCND2 9606 None SL-0178 SL-0182 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}. UNIPROT P30279 UNIPROT A8K531 UNIPROT Q13955 UNIPROT Q5U035 PDB 6EI2 Pfam PF02984 Pfam PF00134 PROSITE PS00292 OMIM 123833 OMIM 615938 DisGeNET 894 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}. 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. P11802 EBI-768365 0.93 P35227 EBI-7823662 0.59 P38936 EBI-756799 0.95 P46527 EBI-758509 0.77 P24941 EBI-1245720 0.55 Q00535 EBI-6256270 0.96 Q00534 EBI-6380828 0.35 Q5VK71 EBI-11601998 0.40 Q8IWL3 EBI-13943458 0.35 Q08999 EBI-21848702 0.35 P49918 EBI-21848702 0.35 P07550 EBI-20801651 0.37 GO:0000785 GO:0097129 GO:0000307 GO:0005737 GO:0005829 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0016538 GO:0019901 GO:0008344 GO:0051301 GO:0071481 GO:0000082 GO:0007616 GO:0044772 GO:0043066 GO:0008284 GO:0045737 GO:1900087 GO:0001934 GO:0000079 Unknown UniProt Sequence Analysis MELLCHEVDPVRRAVRDRNLLRDDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAMNYLDRFLAGVPTPKSHLQLLGAVCMFLASKLKETSPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPQQREKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEEVSSLTCDALTELLAKITNTDVDCLKACQEQIEAVLLNSLQQYRQDQRDGSKSEDELDQASTPTDVRDIDL 289 P30280 G1/S-specific Ccnd2 10090 None SL-0178 SL-0182 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}. UNIPROT P30280 Pfam PF02984 Pfam PF00134 PROSITE PS00292 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}. P30285 EBI-1005844 0.53 Q01105 EBI-1371868 0.35 Q64261 EBI-6932163 0.46 P11440 EBI-15652535 0.40 GO:0000785 GO:0097129 GO:0000307 GO:0005737 GO:0005829 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0016538 GO:0019901 GO:0008344 GO:0051301 GO:0071481 GO:0000082 GO:0007616 GO:0044772 GO:0043066 GO:2000726 GO:0060045 GO:0008284 GO:0045737 GO:0050679 GO:1900087 GO:0001934 GO:0051726 GO:0000079 Unknown UniProt Sequence Analysis MELLCCEVDPVRRAVPDRNLLEDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAMNYLDRFLAGVPTPKTHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSVKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPQQKEKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDDEVNTLTCDALTELLAKITHTDVDCLKACQEQIEALLLNSLQQFRQEQHNAGSKSVEDPDQATTPTDVRDVDL 289 Q8WNW2 G1/S-specific CCND2 9823 None SL-0178 SL-0182 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}. UNIPROT Q8WNW2 Pfam PF02984 Pfam PF00134 PROSITE PS00292 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}. GO:0000785 GO:0097129 GO:0000307 GO:0005737 GO:0005829 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0016538 GO:0019901 GO:0008344 GO:0051301 GO:0071481 GO:0007616 GO:0044772 GO:0043066 GO:0008284 GO:0045737 GO:1900087 GO:0000079 Unknown UniProt Sequence Analysis MELLCCEVDPVRRAVPDANLLHDDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAINYLDRFLAGVPTPKTHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPQPNEKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEDVSSLTGDALVDLLARITNTDVDCLKACQEQIEVVLLNSLQQYRQDQDGSKSEDELDQASTPTDVRDIDL 288 Q04827 G1/S-specific Ccnd2 10116 None SL-0178 SL-0182 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}. UNIPROT Q04827 Pfam PF02984 Pfam PF00134 PROSITE PS00292 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}. GO:0000785 GO:0097129 GO:0000307 GO:0005737 GO:0005829 GO:0031965 GO:0005730 GO:0005634 GO:0016538 GO:0019901 GO:0008344 GO:0051301 GO:0071549 GO:0071372 GO:0071378 GO:0032869 GO:0071394 GO:0071481 GO:0000082 GO:0001889 GO:0007616 GO:0044772 GO:0043066 GO:2000726 GO:0001541 GO:0060045 GO:0008284 GO:0045737 GO:0050679 GO:1900087 GO:0001934 GO:0051726 GO:0000079 GO:0045664 GO:0051591 GO:0032355 GO:0043627 GO:0045471 GO:0032354 GO:0044752 GO:0014070 GO:0043434 GO:0033574 GO:0007283 Unknown UniProt Sequence Analysis MELLCCEVDPVRRAVPDRNLLEDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAMNYLDRFLAGVPTPKTHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSVKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPQQKEKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEEVNALTCDALTELLTKITHTDVDCLKACQEQIEAVLLNSLQQFRQEQHNGSKSVEDPDQATTPTDVRDVDL 288 P53782 G1/S-specific ccnd2 8355 None SL-0178 SL-0182 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}. UNIPROT P53782 Pfam PF02984 Pfam PF00134 PROSITE PS00292 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}. GO:0005737 GO:0031965 GO:0007049 GO:0051301 Unknown UniProt Sequence Analysis MELLCCEGDTVRRAQPDPALLLDDRVLHNLLTVEERYLPQCSYFKCVQKDIQPFMRRMVATWMLEVCEEQRCEEEVFPMAMNYLDRFLAVIPTRKCHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPLPKDKLLLIRKHAQTFIALCATDFNFAMYPPSMIATGSVGAAICGLQLDVGETSLSGDSLTEHLAKITSTDVDCLKACQEQIESVLVSSLRQTRQQTQQRNSSKSVDELDQASTPTDVQDINL 291 A5PK16 Cyclin-F CCNF 9913 None SL-0198 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}. UNIPROT A5PK16 Pfam PF02984 Pfam PF00134 Pfam PF00646 PROSITE PS00292 PROSITE PS50181 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}. GO:0005814 GO:0005634 GO:0048471 GO:0019005 GO:0007049 GO:0051301 GO:0010826 GO:0016567 GO:0051726 GO:0031146 Unknown UniProt Sequence Analysis MGSGGVIHCRCAKCFCYPSKRRIRRRPRNLTILNLPEDALFHILKWLSVGDILAVRAVHSHLKYLVDNHASVWACASFQELWPSPGNLKLFERAAEKGNFEAAVKLGIAYLYNEGLSVSDEARAEVNGLRASRYFSLAERLNVGAAPFIWLFIRPPWSVSGSCCKAVVHESLRAECQLQKTHRASILHCLGRVLSLFEDEEKQKQARKLFEESANQGCLTSSYLLWESDRRMDMLDPGRCLHSFRKLRDFAAKGCWEAQLSLAKACAHGHQLGLEAKASSEIVCQLFQASHAVNKQRVFSVQKGLNDTMRYILIDWLVEVATMKDFSSLCLHLTVECVDRYLRRRLVPRYRLQLLGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRMMGEVVSALDGKIRVPTVVDYKDVLLTLVPMAPRTQHLCSFLCELSLLHTSLAAYAPAHLAAAALLLARLTHGQTQPWTTQLWDLTGFSCEDLIPCVLSLHQKCFHDDAPKDYRQVSLTAVKQRFEDKRYEEISLEEVLSYGQLCAALGVKQESLEPAPFLSAGDIHAFLSSPSARRTKRKRENSLQEDRGSFVTTPTAELSSQEETLLGSFLDWSLDYCSGYEGDQESEGEKEGDVTAPSGVLDVTVVYLSPEEHCCQESSDEEACPEEACGAQDTQALVPGHQALRTPGPEPPLCSRWGLGKDVTTSGYSSVNSASPTDSGRTSGGPPRSTSELPTGSSLNTQPCHHHARKSCLQCRPPSPPESCAPQQQVKRKNLSAHSEEEEEDMNLGFLKL 788 Q6NYX6 Cyclin-F ccnf 7955 None SL-0198 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}. UNIPROT Q6NYX6 Pfam PF02984 Pfam PF00134 Pfam PF12937 PROSITE PS00292 PROSITE PS50181 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}. GO:0005814 GO:0005813 GO:0000307 GO:0005737 GO:0005634 GO:0048471 GO:0019005 GO:0016538 GO:0051301 GO:0044772 GO:0010826 GO:0016567 GO:0000079 GO:0031146 Unknown UniProt Sequence Analysis MKAGALHCRCAKCFSLPVRKRVRKRASAVSLLSLPEELLVFVLQCLSAEDLLSVRAVHSHLCDIIDTNASIWARVSFKDRWPAPDTVWLFERAAEKGNFEAAVKLGIAYLYNEGPLLSEEGRADLCGRMASRYLSLSESLRSPQAEPFIWLFIRPPWSVSGSCCKAVVFDRLQAECQTSPGRKGTLLYCLARVLQLFDDEEKRDEAELMLKESSRCGSLQSSYLLWAISRASSTADPGRYLQCMRTLRDYAARGCWEAQLAFVKSCGSANPLGLEPRACSELVSQFFQTGPSALRYQPHLQGQDITTKRYILVDWLVEVTTTKDFSSQVLHVTISCVDRYLHLRSVPKAQLQLLGIACMVICTRFISKEILTIREAVWLTDNTYQYEDLVHMMGEVISVLDGKIRTPTVLDYGEVLLSLLPVERRTAHLFSYICELSLLCSPATVPGPARLASAILLLTRALHNYVPVWPVQLEENTGFSKQDLVSCALTLYIKCFGQDVPKDYRHVSLTGVKQRFEDDSYQQISKDTVMGFKELCHVLEVPEVEPQVEVSSTSGQITEMHTFLSSPTSSSKRRRADSMQAHRGAFVATPTAELSNQEETLLGDFLDWSLDTSCSGYEGDRESEGEKDGEISTMEVQMELPLDCADRQTHCCLLSSDDTSLCEEDEQEPPTGGSKPWTRHLSSSSTSSSSSSCGFCTDRHSSGYSSIQSFPSPTGSSALVSPQNPPGVPSQRIRRQVKRKNTAAHSAGEAEQEDDAANLAFLSF 764 P41002 Cyclin-F CCNF 9606 None SL-0198 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}. UNIPROT P41002 UNIPROT B2R8H3 UNIPROT Q96EG9 Pfam PF02984 Pfam PF00134 Pfam PF00646 PROSITE PS00292 PROSITE PS50181 OMIM 600227 OMIM 619141 DisGeNET 899 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}. 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. P52286 EBI-907638 0.40 Q8D0D4 EBI-2848359 0.00 P63208 EBI-15862670 0.64 P31350 EBI-6162528 0.63 Q13616 EBI-6162332 0.66 O43303 EBI-6163027 0.79 GO:0030054 GO:0005814 GO:0005813 GO:0000307 GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0019005 GO:0010997 GO:0016538 GO:0051301 GO:0044772 GO:0010826 GO:0001890 GO:0016567 GO:0000320 GO:0051726 GO:0000079 GO:0031146 Unknown UniProt Sequence Analysis MGSGGVVHCRCAKCFCYPTKRRIRRRPRNLTILSLPEDVLFHILKWLSVEDILAVRAVHSQLKDLVDNHASVWACASFQELWPSPGNLKLFERAAEKGNFEAAVKLGIAYLYNEGLSVSDEARAEVNGLKASRFFSLAERLNVGAAPFIWLFIRPPWSVSGSCCKAVVHESLRAECQLQRTHKASILHCLGRVLSLFEDEEKQQQAHDLFEEAAHQGCLTSSYLLWESDRRTDVSDPGRCLHSFRKLRDYAAKGCWEAQLSLAKACANANQLGLEVRASSEIVCQLFQASQAVSKQQVFSVQKGLNDTMRYILIDWLVEVATMKDFTSLCLHLTVECVDRYLRRRLVPRYRLQLLGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRMMGEIVSALEGKIRVPTVVDYKEVLLTLVPVELRTQHLCSFLCELSLLHTSLSAYAPARLAAAALLLARLTHGQTQPWTTQLWDLTGFSYEDLIPCVLSLHKKCFHDDAPKDYRQVSLTAVKQRFEDKRYGEISQEEVLSYSQLCAALGVTQDSPDPPTFLSTGEIHAFLSSPSGRRTKRKRENSLQEDRGSFVTTPTAELSSQEETLLGSFLDWSLDCCSGYEGDQESEGEKEGDVTAPSGILDVTVVYLNPEQHCCQESSDEEACPEDKGPQDPQALALDTQIPATPGPKPLVRTSREPGKDVTTSGYSSVSTASPTSSVDGGLGALPQPTSVLSLDSDSHTQPCHHQARKSCLQCRPPSPPESSVPQQQVKRINLCIHSEEEDMNLGLVRL 786 P51944 Cyclin-F Ccnf 10090 None SL-0198 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}. UNIPROT P51944 UNIPROT Q3TF73 UNIPROT Q60797 UNIPROT Q60799 UNIPROT Q8BSX9 UNIPROT Q8C4D9 UNIPROT Q8CI26 Pfam PF02984 Pfam PF00134 Pfam PF00646 PROSITE PS00292 PROSITE PS50181 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}. GO:0030054 GO:0005814 GO:0005813 GO:0000307 GO:0005737 GO:0005634 GO:0048471 GO:0019005 GO:0010997 GO:0016538 GO:0051301 GO:0044772 GO:0010826 GO:0001890 GO:0016567 GO:0000320 GO:0051726 GO:0000079 GO:0031146 Unknown UniProt Sequence Analysis MGSGGVIHCRCAKCFCYPTKRRIKRRPRNLTILSLPEDVLFHILKWLSVGDILAVRAVHSHLKYLVDNHASVWASASFQELWPSPQNLKLFERAAEKGNFEAAVKLGIAYLYNEGLSVSDEACAEVNGLKASRFFSMAERLNTGSEPFIWLFIRPPWSVSGSCCKAVVHDSLRAECQLQRSHKASILHCLGRVLNLFEDEEKRKQARSLLEESSRQGCLISSYLLWESDRKVDMSDPGRCLHSFRKLRDYAAKGCWEAQLALAKACAGGSQLGLEGKACSESVCQLFQASQAVNKQQIFSVQKGLSDTMRYILIDWLVEVATMKDFTSLCLHLTVECVDRYLRRRLVPRYKLQLLGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRVMGEIISALEGKIRIPTVVDYKEVLLTLVPVAPRTQHLCSFLCELTLLHTSLSIYAPARLASAALLLARLMHGQTQPWTTHLWDLTGFSYSDLVPCVLSLHKKCFHDDAPKDYRQVSLTAVKQRFEDKCYEEISREEVLSYADLCSTIGVKQESPEPPSFPSSGEIHTFLSSPSGRRSKRKRENSLQEDRGSFVTTPTAELSNQEETLLGSLLDWSLECCSGYEGDQESEGEKEGDVTAPSRLLDVTVVYLNPEEHCCQESSDEEAWPEDKIHPAPGTQAPPASAPRPLLCNRGDRAKDITTSGYSSVSSSSPISSLDGGMGGSPQSTSVLSVGSHSSTKPCHHQAKKSCLQCRPPNSPESGVHQQPVKRQNLSVHSDKDMHLAS 777 Q8K4F8 Cyclin-F Ccnf 10116 None SL-0198 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}. UNIPROT Q8K4F8 UNIPROT D3ZCW7 Pfam PF02984 Pfam PF00134 Pfam PF00646 PROSITE PS00292 PROSITE PS50181 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}. GO:0030054 GO:0005814 GO:0005813 GO:0000307 GO:0005737 GO:0005634 GO:0048471 GO:0019005 GO:0010997 GO:0016538 GO:0019901 GO:0051301 GO:0044772 GO:0010826 GO:0001890 GO:0016567 GO:0000320 GO:0051726 GO:0000079 GO:0010033 GO:0031146 Unknown UniProt Sequence Analysis MGSGGVIHCRCAKCFCYPTKRRIKRRPRNLTILSLPEDVLFHILKWLSVGDILAVRAVHSHLKYLVDNHASVWASASFQELWPSPQNLKLFERAAEKGNFEAAVKLGIAYLYNEGLSVSDEACAEVNGLKASRFFSMAERLNTGSDPFIWLFIRPPWSVSGSCCKAVVHDSLRAECQLQRSHKASILHCLGRVLNLFEDEEKRKQAHNLFEESAHQGCLASSYLLWESDRKVDMSDPGRCLHSFRKLRDYAAKGCWEAQLALAKACAGGSQLGLEGKACSESVCQLFQASQAVNKQQIFSVQKGLSDTMRYILIDWLVEVATMKDFTSLCLHLTVECVDRYLRRRLVPRYKLQLLGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRVMGEIISALEGKIRIPTVVDYKEVLLTLVPVAPRTQHLCSFLCELTLLHTSLSVYAPARLASAALLLARLMHGHTQPWTTQLWDLTGFSYSDLTPCVLSLHKKCFHDDAPKDYRQVSLTAVKQRFEDKCYEEISQEEVLSYAELCSALGVKQESPEPPSFPSSGEIHTFLSSPSGRRSKRKRENSLQEDRGSFVTTPTAELSNQEETLLGSLLDWSLDCCSGYEGDQESEGEKEGDVTAPSGLLDVTVVYLNPEEHCCQESSDEEVWPEDKSHPTPGTQAPPASAPWPLPCNRGDPGKDVTTSGYSSVSSSSPISSLDGGMVGSPRSTSVLSVGSHSSTKPCYHQAKKSCLQCRPPNPPESGAHQQPVKRQNLSVHSDEDTNLGFLKL 780 Q7T0L6 Cyclin-F ccnf 8355 None SL-0198 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}. UNIPROT Q7T0L6 Pfam PF02984 Pfam PF00134 Pfam PF00646 PROSITE PS00292 PROSITE PS50181 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}. GO:0005814 GO:0005634 GO:0048471 GO:0019005 GO:0007049 GO:0051301 GO:0010826 GO:0016567 GO:0031146 Unknown UniProt Sequence Analysis MKGGGLHCRCSKCFAAPPRRRIKRRPRVLTLLSLPEDVLLYVLECLPAVDILSMREVHPHLRSLVDSHSSVWARASFQDVWPSSENLNLFERAAECGNFEACVKLGIAYLYNEGLSVSDDGRAEVNGLKASRFFSLTERLNAGADPFVWLFIRPPWSSSGSCCKAVVFDSLNEECGTVTSGEGATGALKGSIQYCLAKVLSLFEDDDKKREALGMLESSASNGCLHSAYLLWETKQKAALSDPGRYLQSFRQLRDYAARGCWDAQISLAKACGHKNPLNQEQRSAGELVNQVFQSSLPINKSSIFTTQKGMNDTMRYILIDWLVEVATMKDFSSLCLHMTVGLVDRYLKLRSVPRAKLQLVGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRMMGEIISALEGKIRMPTVVDYKDVLSHLIPLDRNTLHLCSYISELSLLYTELSMYSPAQLAAGALLLARILHRQARPWPAQLAETTGFTLEHLTPCVVLLHKKCFHDDAPRDYRQVSLTAVKQRFQDDLYDQISKEKVMDHTHLCELLGVPCHDSESPATCPNAADFHQFLCSPSGNKTKRRREESIQEDRGSFVTTPTAELSNQEEDLLGDFLDWSLETSCSGYEGDRESEGEREGEVTAPSGVLDLSLLLTEHPQCQDSTTDDDSITLHPIPLLSKAENGTDSIEGCVEKSSGYSSVSSGGSPTSSSSPGLPFTPTPGLNHSKLTPIPFPQPCSPLLKASRRQVKRKNQAQHSEDNLSDEL 761 Q5XGG5 Cyclin-F ccnf 8364 None SL-0198 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}. UNIPROT Q5XGG5 Pfam PF02984 Pfam PF00134 Pfam PF00646 PROSITE PS00292 PROSITE PS50181 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}. GO:0005814 GO:0005813 GO:0000307 GO:0005737 GO:0005634 GO:0048471 GO:0019005 GO:0016538 GO:0051301 GO:0044772 GO:0010826 GO:0016567 GO:0000079 GO:0031146 Unknown UniProt Sequence Analysis MKGGALHCRCSKCFAAPPKRRVKRRPRVLTLLSLPEDVLLYVLECLPAVDILSMREVHPHLRSLVDSHSSVWARASFQDVWPSPENLNLFERAAECGNFEACVKLGIAYLYNEGLSLSDDGRAEVNGLKASRFFSLTERLNSGADPFVWLFIRPPWSSSGSCCKAVVFDSLKEECGTVTSEEGATGALKGSIQYCLAKVLSLFEDDDKKREALGMLESSASHGCLHSSYLLWETKQKTALSDPGRYLQSFRQLRDYAARGCWDAQISLAKACGHKNQLSQEQRSASELVNQVFQSSLPINKTSIFTTQKGMNDTMRYILIDWLVEVATMKDFSSLCLHMTVGLVDRYLKLRSVPRAKLQLVGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRMMGEIISALEGKIRMPTVVDYKDVLSHLIPLDRSTLHLCSYISELSLLYTELSTYSPAQLAAGALLLARILHKQARPWPAQLAETTGFTLEHLTPCVVLLHKKCFHDDAPKDYRQVSLTAVKQRFQDDLYDQISKEKVMDHSHLCELLGVPCRDSESPASCPNAADFHQFLCSPSGSKTKRRREDSIQEDRGSFVTTPTAELSNQEEDLLGDFLDWSLETSCSGYEGDRESEGEREGEVTAPSGVLDLSLLITEHQQCQDTTSDDDSLVPLHPIPLLSKLENGTHSTEGCAEKSSGYSSVSSGGSPTSSSSPPGLPFTPTPGLNHSKLMPIPFPQPCSPLFKASRRQVKRKNQAQHSEDNLSDEL 763 Q14094 Cyclin-I CCNI 9606 None SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:28860486}. UNIPROT Q14094 UNIPROT B2R6M0 UNIPROT B7Z6X4 Pfam PF00134 OMIM 618783 DisGeNET 10983 P05783 EBI-3915486 0.37 Q96MT8 EBI-1105510 0.00 P40127 EBI-2873918 0.00 P30304 EBI-3907148 0.37 Q9NPH3 EBI-3915476 0.37 P31749 EBI-9063688 0.37 Q00535 EBI-10103156 0.67 Q00536 EBI-11615332 0.37 Q00534 EBI-24620488 0.56 Q00526 EBI-23812995 0.56 Q96E35 EBI-24558458 0.56 GO:0000307 GO:0005737 GO:0031965 GO:0005634 GO:0016538 GO:0044772 GO:0000079 GO:0007283 Unknown UniProt Sequence Analysis MKFPGPLENQRLSFLLEKAITREAQMWKVNVRKMPSNQNVSPSQRDEVIQWLAKLKYQFNLYPETFALASSLLDRFLATVKAHPKYLSCIAISCFFLAAKTVEEDERIPVLKVLARDSFCGCSSSEILRMERIILDKLNWDLHTATPLDFLHIFHAIAVSTRPQLLFSLPKLSPSQHLAVLTKQLLHCMACNQLLQFRGSMLALAMVSLEMEKLIPDWLSLTIELLQKAQMDSSQLIHCRELVAHHLSTLQSSLPLNSVYVYRPLKHTLVTCDKGVFRLHPSSVPGPDFSKDNSKPEVPVRGTAAFYHHLPAASGCKQTSTKRKVEEMEVDDFYDGIKRLYNEDNVSENVGSVCGTDLSRQEGHASPCPPLQPVSVM 377 O60583 Cyclin-T2 CCNT2 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TQK0}. Nucleus {ECO:0000250|UniProtKB:Q7TQK0}. Note=Nucleus in differentiating cells. {ECO:0000250|UniProtKB:Q7TQK0}. UNIPROT O60583 UNIPROT A8KA48 UNIPROT D3DP73 UNIPROT D3DP74 UNIPROT O60582 UNIPROT Q29R66 UNIPROT Q53SR4 UNIPROT Q5I1Y0 PDB 2IVX Pfam PF00134 OMIM 603862 DisGeNET 905 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}. A0A3Q0PRD7 EBI-2836754 0.00 O95402 EBI-4324040 0.35 Q9UHB7 EBI-4324092 0.35 O00472 EBI-4324079 0.35 P42568 EBI-4324106 0.35 P50750 EBI-4324121 0.85 O60885 EBI-9077135 0.35 Q6NYC1 EBI-9077105 0.40 Q16659 EBI-12502733 0.35 A3KMF4 EBI-11085933 0.35 Q9ERL0 EBI-11086053 0.35 Q9HB65 EBI-21631556 0.35 Q9P0M6 EBI-21731516 0.35 Q96MH2 EBI-21764590 0.35 O94992 EBI-21776048 0.35 Q00534 EBI-21776141 0.35 P14404 EBI-21026252 0.35 Q12802 EBI-25409729 0.35 Q07139 EBI-25410964 0.35 P83105 EBI-25745135 0.35 O60583 EBI-25684887 0.35 A0A0F6B063 EBI-27033283 0.35 D0ZRB2 EBI-27033344 0.35 GO:0008024 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0097322 GO:0003682 GO:0061575 GO:0016538 GO:0019901 GO:0070063 GO:0001223 GO:0007049 GO:0051301 GO:0019085 GO:0019086 GO:0032786 GO:0045944 GO:0032968 GO:0006468 GO:0000079 GO:0051147 GO:0006357 GO:0007519 GO:0006366 Unknown UniProt Sequence Analysis MASGRGASSRWFFTREQLENTPSRRCGVEADKELSCRQQAANLIQEMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNKNIISSTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVILETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPNRLKKIRNWRANQAARKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNISVQDSHTSDNLSMLATGMPSTSYGLSSHQEWPQHQDSARTEQLYSQKQETSLSGSQYNINFQQGPSISLHSGLHHRPDKISDHSSVKQEYTHKAGSSKHHGPISTTPGIIPQKMSLDKYREKRKLETLDLDVRDHYIAAQVEQQHKQGQSQAASSSSVTSPIKMKIPIANTEKYMADKKEKSGSLKLRIPIPPTDKSASKEELKMKIKVSSSERHSSSDEGSGKSKHSSPHISRDHKEKHKEHPSSRHHTSSHKHSHSHSGSSSGGSKHSADGIPPTVLRSPVGLSSDGISSSSSSSRKRLHVNDASHNHHSKMSKSSKSSGSSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVETNGPDANHEYSTSSQHMDYKDTFDMLDSLLSAQGMNM 730 Q7TQK0 Cyclin-T2 Ccnt2 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:23060074}. Nucleus {ECO:0000269|PubMed:23060074}. Note=Nucleus in differentiating cells. {ECO:0000269|PubMed:23060074}. UNIPROT Q7TQK0 UNIPROT K4N0L9 UNIPROT K4N2S3 Pfam PF00134 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}. Q99J95 EBI-6260872 0.35 GO:0008024 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0097322 GO:0003682 GO:0061575 GO:0016538 GO:0019901 GO:0070063 GO:0001223 GO:0007049 GO:0051301 GO:0006351 GO:0019085 GO:0019086 GO:1903655 GO:1903654 GO:0032786 GO:0045944 GO:0032968 GO:0006468 GO:0051147 GO:0006357 GO:0007519 Unknown UniProt Sequence Analysis MASGRGASSRWFFTREQLENTPSRRCGVEADEELSHRQQAANLIQDMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNRNIISPTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVLLETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPSRLKRIRNWRAMAKKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPANPSFQKPSTSTFPAPIPLNSGSTSVQDSRASDNLSVLAAGMPSTSYSLSSHQEWPQHPDSARTDPVYTQKQEATLSGSQYISFQQGPSMALHSGLHHRPDKVADHSSAKQEYTHKAGSSKHHGPIPATPGMLPQKMSLDKYREKRKLETLDVDTRDHYLAAHAEQQHKHGPAQAVTGTSVTSPIKMKLPLTNSDRPEKHVAEKKERSGSLKLRIPIPPPDKGPSKEELKMKIKVASSERHSSSDEGSGKSKHSSPHISRDHKEKHKEHPANRHHSSHKYLHMHSGGSKHTADGMPPTVLRSPVGLGPEGVSSASSARKKLHSSEASHNHHSKMSKSSKSAGSSSSSSSVKQYLSSHSSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVEPHGPEANHEYSTSSQHMDYKDTFDMLDSLLSAQGMNM 723 P46892 Cyclin-dependent Cdk11b 10116 None SL-0178 SL-0182 SL-0198 Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Cytoplasm, perinuclear region. UNIPROT P46892 Pfam PF00069 PROSITE PS50011 PROSITE PS00108 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}. GO:0031965 GO:0005634 GO:0048471 GO:0005524 GO:0004693 GO:0106310 GO:0004674 GO:0001824 GO:0007049 GO:2001234 GO:0006468 GO:0001558 GO:0007346 GO:0007088 GO:0050684 Peripheral UniProt Sequence Analysis MKSEKSRTTSWLFQSHEVTEILGRVKKNRKKLVKGLHRAGPPPEKNYLPDSPALSPIELKQELPKYLPALQGCRSVEEFQCLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPLTSIREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYVEHDLKSLMETMKQPFLPGEVKTLMIQLLSGVKHLHDNWILHRDLKTSNLLLTHAGILKVGDFGLAREYGSPLKAYTPVVVTLWYRAPELLLGAKEYSTACDMWSVGCIFGELLTQKPLFPGKSDIDQINKIFKDIGTPSEKIWPGYSELPAVKKMTFSELPYNNLRKRFGALLSDQGFDLMNKFLTYYPGRRINAEDGLKHEYFRETPLPIDPSMFPTWPAKSEQQCVKRGTSPKPPEGGLGYSQLGDDDLKETGFHLTTTNDGAVSCRPWCSLLF 436 Q28199 Cyclin-dependent CDK5R1 9913 None SL-0198 [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}. UNIPROT Q28199 UNIPROT Q0II69 UNIPROT Q28865 UNIPROT Q29462 Pfam PF03261 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}. Q9JLH6 EBI-307828 0.48 Q9JLH5 EBI-307840 0.48 Q9JLH7 EBI-307855 0.48 P15882 EBI-7146023 0.54 GO:0030424 GO:0043292 GO:0000307 GO:0005737 GO:0030425 GO:0043197 GO:0030426 GO:0016020 GO:0031594 GO:0043005 GO:0043025 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005886 GO:0014069 GO:0016533 GO:0051015 GO:0043014 GO:0048487 GO:0045296 GO:0005509 GO:0061575 GO:0035255 GO:0016301 GO:0002020 GO:0019901 GO:0043539 GO:0007411 GO:0007413 GO:0007420 GO:0021549 GO:0009792 GO:0048013 GO:0007213 GO:0070315 GO:0021766 GO:0035235 GO:0021819 GO:0045892 GO:0007158 GO:0030182 GO:0001764 GO:0031175 GO:0018107 GO:0031116 GO:0043525 GO:0090314 GO:0032956 GO:0061001 GO:0048511 GO:0042501 GO:0021722 Lipid-Anchored UniProt By Similarity {ECO:0000250} MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKVQPNSSYQNNITHLNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGVSSSVKKAPHPAVSSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR 307 Q15078 Cyclin-dependent CDK5R1 9606 None SL-0198 [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}. UNIPROT Q15078 UNIPROT E1P664 UNIPROT Q5U0G3 PDB 1H4L PDB 1UNG PDB 1UNH PDB 1UNL PDB 3O0G PDB 6LDP PDB 7CNG PDB 7VDP PDB 7VDQ PDB 7VDR PDB 7VDS Pfam PF03261 OMIM 603460 DisGeNET 8851 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}. Q9Y3Q8 EBI-754939 0.37 Q00535 EBI-1041602 0.93 P46527 EBI-1226546 0.40 P38936 EBI-1226667 0.40 Q6ZMQ8 EBI-2008413 0.59 Q9HAV2 EBI-9370611 0.40 Q53FC7 EBI-9370589 0.40 Q96BE0 EBI-9370633 0.40 Q01097 EBI-9634890 0.35 P11798 EBI-9634890 0.35 P49615 EBI-9634890 0.35 O35350 EBI-9634890 0.35 Q5JR59 EBI-10235827 0.56 O89053 EBI-11600074 0.44 Q96EY8 EBI-21756327 0.35 Q9NPD8 EBI-21756327 0.35 Q96EY5 EBI-21756327 0.35 Q96DX4 EBI-21756327 0.35 Q04323 EBI-21756327 0.35 Q01581 EBI-21756327 0.35 P24941 EBI-21756327 0.35 P07951 EBI-21756327 0.35 O94903 EBI-21756327 0.35 O43583 EBI-21756327 0.35 Q7Z3S9 EBI-22139521 0.37 A2RUH7 EBI-25906782 0.56 Q8NCR3 EBI-25906774 0.56 Q96E17 EBI-25906766 0.56 Q96QH2 EBI-25906758 0.56 Q9BT49 EBI-25906750 0.56 Q6UXH1 EBI-25906742 0.56 Q9NPC7 EBI-25906734 0.56 Q8N2W9 EBI-25906724 0.56 Q9BQ29 EBI-25906716 0.56 O94983 EBI-25906706 0.56 Q9ULW0 EBI-25906698 0.56 Q9HC98 EBI-25906688 0.56 Q02978 EBI-25906680 0.56 P43356 EBI-25906672 0.56 P16422 EBI-25906664 0.56 P26715 EBI-25906656 0.56 P49184 EBI-25906648 0.56 GO:0030424 GO:0043292 GO:0000307 GO:0005737 GO:0005829 GO:0030425 GO:0043197 GO:0030426 GO:0043231 GO:0016020 GO:0031594 GO:0043005 GO:0043025 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005886 GO:0014069 GO:0098793 GO:0016533 GO:0051015 GO:0043014 GO:0048487 GO:0045296 GO:0005509 GO:0061575 GO:0046875 GO:0035255 GO:0016301 GO:0002020 GO:0030295 GO:0004672 GO:0019901 GO:0043539 GO:0007411 GO:0007413 GO:0007420 GO:0021549 GO:0009792 GO:0048013 GO:0007213 GO:0070315 GO:0021766 GO:0035235 GO:0021819 GO:0000226 GO:0045892 GO:0007158 GO:0030182 GO:0001764 GO:0031175 GO:0018105 GO:0018107 GO:0045348 GO:0031116 GO:0043525 GO:0090314 GO:2000273 GO:0032956 GO:0000079 GO:0061001 GO:0016241 GO:0045664 GO:0098693 GO:0048511 GO:0042501 GO:0021722 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:20213681} MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKVQPNSSYQNNITHLNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGGSSSVKKAPHPAVTSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR 307 P61809 Cyclin-dependent Cdk5r1 10090 None SL-0198 [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}. UNIPROT P61809 UNIPROT Q62938 Pfam PF03261 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}. P15209 EBI-15624695 0.35 P09803 EBI-7840493 0.40 P49615 EBI-7840587 0.56 Q8CFH6 EBI-16094166 0.54 O43164 EBI-16094147 0.40 P62991 EBI-16094258 0.40 Q80U04 EBI-16094239 0.52 GO:0030424 GO:0043292 GO:0000307 GO:0005737 GO:0005829 GO:0030425 GO:0043197 GO:0030426 GO:0043231 GO:0016020 GO:0031594 GO:0043025 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005886 GO:0014069 GO:0098793 GO:0016533 GO:0003779 GO:0051015 GO:0045296 GO:0005509 GO:0061575 GO:0008092 GO:0046875 GO:0051879 GO:0035255 GO:0016301 GO:0002020 GO:0019901 GO:0043539 GO:0007411 GO:0007413 GO:0007420 GO:0021549 GO:0021799 GO:0009792 GO:0048013 GO:0007213 GO:0070315 GO:0021766 GO:0035235 GO:0021819 GO:0045892 GO:0007158 GO:0030182 GO:0001764 GO:0031175 GO:0018105 GO:0018107 GO:0045348 GO:0043525 GO:0045860 GO:0090314 GO:2000273 GO:0032956 GO:0061001 GO:0070507 GO:0098693 GO:0048511 GO:0042501 GO:0021722 Lipid-Anchored UniProt By Similarity {ECO:0000250} MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKAQPNSSYQSNIAHLNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGVSSSVKKAPHPAITSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR 307 P61810 Cyclin-dependent Cdk5r1 10116 None SL-0198 [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}. UNIPROT P61810 UNIPROT Q62938 Pfam PF03261 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}. Q03114 EBI-7038493 0.56 P21263 EBI-7038472 0.46 P62989 EBI-7038532 0.40 Q6ZMQ8 EBI-2008524 0.40 B1WCA1 EBI-8078736 0.54 Q63604 EBI-15624622 0.35 Q03351 EBI-15624585 0.35 P35739 EBI-15624585 0.35 GO:0030424 GO:0043292 GO:0000307 GO:0005737 GO:0030425 GO:0043197 GO:0030426 GO:0016020 GO:0031594 GO:0043025 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005886 GO:0014069 GO:0098793 GO:0016533 GO:0003779 GO:0051015 GO:0045296 GO:0005509 GO:0061575 GO:0046875 GO:0035255 GO:0016301 GO:0002020 GO:0019901 GO:0043539 GO:0048675 GO:0007411 GO:0007413 GO:0007420 GO:0021549 GO:0021799 GO:0009792 GO:0048013 GO:0007213 GO:0070315 GO:0021766 GO:0035235 GO:0021819 GO:0030517 GO:0045892 GO:0007158 GO:0030182 GO:0001764 GO:0031175 GO:0018105 GO:0018107 GO:0043525 GO:0045860 GO:0090314 GO:2000273 GO:0032956 GO:0061001 GO:0070507 GO:0098693 GO:0048511 GO:0042501 GO:0021722 Lipid-Anchored UniProt By Similarity {ECO:0000250} MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKAQPNSSYQSNIAHLNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGVSSSVKKAPHPAITSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR 307 Q4KYY2 Cyclin-dependent CDK5R1 9997 None SL-0198 [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}. UNIPROT Q4KYY2 Pfam PF03261 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}. GO:0043005 GO:0005634 GO:0043204 GO:0048471 GO:0005886 GO:0014069 GO:0016533 GO:0061575 GO:0048013 GO:0061001 GO:0048511 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:Q15078} MGTGLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKGQPNSSYQNNITHLNNENLKKSLSCANLSTFAQPPPAQPPAPPANQLSGSQTGVSSSVKKAPHPSVTSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYVGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQAFSDLKNESGQEDKKRLLLGLDR 307 P06704 Cell CDC31 559292 None SL-0178 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}. UNIPROT P06704 UNIPROT D6W2V8 PDB 2DOQ PDB 2GV5 PDB 3FWB PDB 3FWC PDB 4MBE Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. P38305 EBI-761900 0.40 Q99181 EBI-857104 0.00 P00927 EBI-7366294 0.40 P41940 EBI-7560454 0.44 P47116 EBI-7562977 0.44 P10659 EBI-7668648 0.40 P34730 EBI-7930447 0.40 O94742 EBI-7945620 0.40 P46674 EBI-7945717 0.77 P39015 EBI-7945762 0.40 P11353 EBI-8031674 0.40 Q02959 EBI-8051544 0.59 P53164 EBI-8463661 0.40 P53030 EBI-8221748 0.22 Q6WNK7 EBI-1370393 0.76 Q02336 EBI-1370467 0.35 P53040 EBI-1370499 0.35 Q08231 EBI-1370592 0.76 P11927 EBI-2212825 0.40 P47069 EBI-2212835 0.59 P40457 EBI-2212931 0.40 Q12369 EBI-2213075 0.56 P06704 EBI-2213075 0.52 P54199 EBI-2612619 0.35 P38590 EBI-2612691 0.35 P32944 EBI-2613930 0.35 Q08921 EBI-2613976 0.35 P32447 EBI-2881789 0.00 Q07457 EBI-2882228 0.00 P26448 EBI-2882390 0.00 Q00684 EBI-2882792 0.00 P14832 EBI-2882919 0.00 P32472 EBI-2883301 0.00 P02293 EBI-2884858 0.00 Q02796 EBI-2885546 0.00 Q02206 EBI-2886536 0.00 P38890 EBI-2887466 0.00 P39723 EBI-2887969 0.00 Q04477 EBI-2887856 0.00 P46675 EBI-2888241 0.00 P25302 EBI-2888465 0.00 Q06677 EBI-3651969 0.35 P10591 EBI-3668305 0.35 P11484 EBI-3686264 0.35 P38915 EBI-4375569 0.35 Q12060 EBI-4376704 0.35 P50102 EBI-4380099 0.35 GO:0005737 GO:0005825 GO:0005815 GO:0044732 GO:0005635 GO:0070390 GO:0005509 GO:0042802 GO:0008017 GO:0051301 GO:0048193 GO:0006406 GO:0045944 GO:0043161 GO:0043549 GO:0030474 Unknown UniProt Sequence Analysis MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKREILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS 161 Q9BWU1 Cyclin-dependent CDK19 9606 None SL-0198 Cytoplasm {ECO:0000269|PubMed:32330417}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32330417}. Nucleus {ECO:0000269|PubMed:32330417}. UNIPROT Q9BWU1 UNIPROT Q5JQZ7 UNIPROT Q5JR00 UNIPROT Q8TC78 UNIPROT Q9UPX2 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 614720 OMIM 618916 DisGeNET 23097 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. P10909 EBI-6381327 0.35 P50613 EBI-15560892 0.44 A0JLT2 EBI-394580 0.62 Q9BTT4 EBI-394793 0.62 Q9NWA0 EBI-394834 0.71 Q9NX70 EBI-394875 0.71 Q920D3 EBI-394916 0.35 O95402 EBI-394957 0.71 P49336 EBI-395095 0.40 Q71F56 EBI-395095 0.67 Q9P086 EBI-395095 0.56 Q93074 EBI-395095 0.85 Q9UHV7 EBI-395095 0.74 O60244 EBI-395095 0.67 Q96RN5 EBI-395095 0.67 Q9Y2X0 EBI-395095 0.67 Q9NVC6 EBI-395095 0.67 Q9BUE0 EBI-395095 0.56 Q15648 EBI-395095 0.67 Q9H944 EBI-395095 0.67 Q13503 EBI-395095 0.67 Q15528 EBI-395095 0.67 Q9ULK4 EBI-395095 0.67 O75448 EBI-395095 0.67 Q6P2C8 EBI-395095 0.67 Q9H204 EBI-395095 0.56 Q96HR3 EBI-395095 0.67 Q9Y3C7 EBI-395095 0.74 Q9NPJ6 EBI-395095 0.67 O75586 EBI-395095 0.67 O43513 EBI-395095 0.74 Q96G25 EBI-395095 0.67 Q8TDY2 EBI-1068461 0.00 Q8TBZ2 EBI-1074027 0.00 P0DOE9 EBI-6138583 0.35 P05090 EBI-6381327 0.35 P12273 EBI-6381327 0.35 P25311 EBI-6381327 0.35 Q8IUD2 EBI-6381327 0.53 P24863 EBI-6381327 0.80 P50750 EBI-8765229 0.35 Q12888 EBI-20207896 0.27 Q83B01 EBI-21286333 0.37 Q96DY7 EBI-28945018 0.35 Q8ND56 EBI-28945018 0.35 Q86YW9 EBI-28945018 0.35 Q71SY5 EBI-28945018 0.35 Q16543 EBI-28945018 0.35 Q15021 EBI-28945018 0.35 P49736 EBI-28945018 0.35 P45983 EBI-28945018 0.35 P33991 EBI-28945018 0.35 P25205 EBI-28945018 0.35 Q99816 EBI-30840175 0.44 GO:0005829 GO:0016592 GO:0005654 GO:0005634 GO:0048471 GO:0005524 GO:0004693 GO:0106310 GO:0008353 GO:0071222 GO:0043065 GO:0050729 GO:0006468 Unknown UniProt Sequence Analysis MDYDFKAKLAAERERVEDLFEYEGCKVGRGTYGHVYKARRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQEDPLPTLDVFAGCQIPYPKREFLNEDDPEEKGDKNQQQQQNQHQQPTAPPQQAAAPPQAPPPQQNSTQTNGTAGGAGAGVGGTGAGLQHSQDSSLNQVPPNKKPRLGPSGANSGGPVMPSDYQHSSSRLNYQSSVQGSSQSQSTLGYSSSSQQSSQYHPSHQAHRY 502 Q8BWD8 Cyclin-dependent Cdk19 10090 None SL-0198 Cytoplasm {ECO:0000250|UniProtKB:Q9BWU1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9BWU1}. Nucleus {ECO:0000250|UniProtKB:Q9BWU1}. UNIPROT Q8BWD8 UNIPROT Q80TM1 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 Q83FA5 EBI-21286775 0.37 GO:0005829 GO:0016592 GO:0005654 GO:0005634 GO:0048471 GO:0005524 GO:0004693 GO:0106310 GO:0008353 GO:0071222 GO:0043065 GO:0050729 GO:0006468 Unknown UniProt Sequence Analysis MDYDFKAKLAAERERVEDLFEYEGCKVGRGTYGHVYKARRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQEDPLPTLDVFAGCQIPYPKREFLNEDEPEEKGDKNQPQQQNPHQQPAAPAQQTAAPPQAPPPQQSSAQTNGTAGGATAGGGGAGAGLQHSQDPGLNQVPPNKKPRIGPSGANSGGPVMPSDYQHSSSRLNYQSSVQGSSQSQSTLGYSSSQQSTQYHSSHQTHRY 501 Q32KY4 Cyclin-dependent CDK4 9913 None SL-0178 SL-0182 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}. UNIPROT Q32KY4 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0005737 GO:0016592 GO:0031965 GO:0005634 GO:0005524 GO:0004693 GO:0106310 GO:0008353 GO:0007049 GO:0051301 GO:0010971 GO:0006468 GO:0051726 Unknown UniProt Sequence Analysis MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFSPRGPRPVQSVVPELEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGDAE 303 P11802 Cyclin-dependent CDK4 9606 None SL-0178 SL-0182 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}. UNIPROT P11802 UNIPROT B2R9A0 UNIPROT B4DNF9 UNIPROT O00576 UNIPROT Q6FG61 PDB 2W96 PDB 2W99 PDB 2W9F PDB 2W9Z PDB 3G33 PDB 5FWK PDB 5FWL PDB 5FWM PDB 5FWP PDB 6P8E PDB 6P8F PDB 6P8G PDB 6P8H Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 123829 OMIM 609048 DisGeNET 1019 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}. 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. O75694 EBI-1065754 0.00 P01112 EBI-27045317 0.27 P07948 EBI-1063758 0.00 P0DTD1 EBI-26495747 0.35 Q24158 EBI-8620418 0.37 Q16543 EBI-295633 0.93 P42771 EBI-375269 0.96 P30281 EBI-375326 0.98 P49736 EBI-375329 0.44 P24385 EBI-375341 0.98 P38936 EBI-375404 0.92 O00311 EBI-375437 0.44 P49918 EBI-519276 0.40 P46527 EBI-519297 0.93 Q8N720 EBI-625679 0.71 P42772 EBI-760282 0.97 P04632 EBI-728826 0.00 P46379 EBI-729744 0.00 Q15047 EBI-7118776 0.55 Q9UGY1 EBI-737135 0.00 P55273 EBI-754729 0.96 Q9NP79 EBI-758428 0.37 P30279 EBI-768365 0.93 Q1EHW4 EBI-922367 0.35 Q9UJU6 EBI-1063375 0.00 Q9NS64 EBI-1063663 0.00 Q8IZT6 EBI-11132267 0.56 P23508 EBI-1065583 0.00 Q12996 EBI-1066306 0.00 P42773 EBI-3906668 0.97 Q04323 EBI-1068290 0.00 P57678 EBI-1068996 0.00 Q96T76 EBI-1069744 0.00 Q9UQE7 EBI-1071705 0.00 P35606 EBI-1072884 0.00 Q14683 EBI-1073208 0.00 Q9UDX5 EBI-1074355 0.00 Q9P1U1 EBI-1075412 0.00 P62136 EBI-1206902 0.00 P36873 EBI-1207334 0.00 P30154 EBI-1266474 0.35 P30153 EBI-1266485 0.35 P32121 EBI-1642843 0.35 Q9BQA1 EBI-2940933 0.35 Q9H0R8 EBI-3048562 0.35 P01106 EBI-3906703 0.59 Q99956 EBI-3906683 0.37 Q13261 EBI-3906693 0.37 P63208 EBI-3906713 0.37 Q99828 EBI-3914485 0.37 Q15555 EBI-3914495 0.37 P52209 EBI-3927622 0.37 P20073 EBI-7096705 0.37 P51693 EBI-7117963 0.37 P06576 EBI-7118041 0.37 O95865 EBI-7118309 0.37 Q12766 EBI-7118436 0.37 Q9Y383 EBI-7118499 0.37 P14618 EBI-7118577 0.37 P47897 EBI-7118684 0.37 Q8IZ69 EBI-7118859 0.37 Q05516 EBI-7118939 0.37 Q15038 EBI-7139218 0.37 P37840 EBI-7391065 0.37 P04183 EBI-7396108 0.37 Q8IZC7 EBI-5283871 0.44 Q9H165 EBI-5283535 0.44 Q08050 EBI-5283631 0.44 P32243 EBI-5278204 0.44 P28698 EBI-5283775 0.44 O60902 EBI-5282940 0.44 Q9P2Y4 EBI-5282927 0.44 Q99741 EBI-5283967 0.44 P28749 EBI-5278658 0.44 Q14493 EBI-5284015 0.44 Q9H4L4 EBI-5283823 0.44 Q08999 EBI-5283583 0.44 Q9H4Z2 EBI-5284063 0.44 Q6UB98 EBI-5283727 0.44 Q9C0J8 EBI-5282970 0.44 P08151 EBI-5282953 0.44 Q96PU4 EBI-6051398 0.40 Q02556 EBI-6115692 0.35 P08238 EBI-6255377 0.78 P07900 EBI-6255377 0.53 Q00534 EBI-6255377 0.35 Q12931 EBI-6255377 0.35 Q14004 EBI-6380178 0.53 Q13616 EBI-21323857 0.35 Q92905 EBI-21325777 0.35 Q13620 EBI-21327757 0.35 Q7L5N1 EBI-21328549 0.35 Q13618 EBI-21329068 0.35 P84022 EBI-6593176 0.27 Q77Q36 EBI-9082540 0.40 Q13451 EBI-9393873 0.64 Q9UJC3 EBI-10197685 0.86 P53671 EBI-10103591 0.35 P03129 EBI-11721568 0.35 Q9BX66 EBI-11132267 0.35 P53814 EBI-11132267 0.35 Q9P2E3 EBI-11132267 0.35 Q6PJT7 EBI-11132267 0.35 Q9H061 EBI-11132267 0.35 Q8WUM0 EBI-11132267 0.35 P46940 EBI-11132927 0.35 Q66GS9 EBI-11386281 0.27 Q8N448 EBI-11766518 0.49 Q16254 EBI-12449950 0.53 P49815 EBI-11687060 0.40 Q9UKT9 EBI-24394070 0.56 Q0VD86 EBI-24622275 0.56 Q9ULD0 EBI-24764997 0.56 Q8WXX5 EBI-11925475 0.00 Q8IVT5 EBI-14035152 0.35 P04004 EBI-21709311 0.35 Q9UKA8 EBI-21786597 0.35 Q58FG0 EBI-21835664 0.35 Q5TC84 EBI-21835664 0.35 Q58FF7 EBI-21835664 0.35 Q58FF6 EBI-21835664 0.35 P55789 EBI-21835664 0.35 P52333 EBI-21835664 0.35 P08236 EBI-21835664 0.35 Q9NZT2 EBI-21848776 0.40 P50613 EBI-15560841 0.44 P46414 EBI-15763467 0.40 Q92830 EBI-16107564 0.40 Q9JHD2 EBI-16107581 0.40 Q9Y6K9 EBI-20737021 0.35 Q5S007 EBI-21360986 0.35 Q9UH17 EBI-25296426 0.64 P82930 EBI-25477405 0.35 P53007 EBI-25477405 0.35 P43307 EBI-25477405 0.35 P28482 EBI-25477405 0.35 P54819 EBI-25477405 0.35 Q8TB24 EBI-26518569 0.35 Q9H9E1 EBI-26656693 0.35 P01116 EBI-27041844 0.27 P01111 EBI-27042293 0.27 P09936 EBI-27121923 0.59 P00441 EBI-28996885 0.40 Q13619 EBI-30863570 0.35 GO:0005923 GO:0000785 GO:0097128 GO:0097129 GO:0097130 GO:0000307 GO:0005829 GO:0016592 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0005667 GO:0005524 GO:0030332 GO:0004693 GO:0016538 GO:0106310 GO:0008353 GO:0060612 GO:0051301 GO:0032869 GO:0071353 GO:1904637 GO:0071222 GO:1904628 GO:0000082 GO:0008284 GO:0048146 GO:0010971 GO:0006468 GO:0051726 GO:0010468 GO:0046626 GO:0046890 GO:0050994 GO:0040014 GO:0060260 GO:0061469 GO:0009410 GO:0007165 Unknown UniProt Sequence Analysis MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE 303 P30285 Cyclin-dependent Cdk4 10090 None SL-0178 SL-0182 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}. UNIPROT P30285 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. P24385 EBI-6988572 0.40 P25322 EBI-1005778 0.94 P30280 EBI-1005844 0.53 P46414 EBI-1005778 0.56 P30282 EBI-1005844 0.53 P06400 EBI-1182824 0.62 P63087 EBI-1202851 0.00 Q01105 EBI-1371868 0.35 Q8CIG8 EBI-2941146 0.50 Q99J09 EBI-3401852 0.35 O15211 EBI-3956301 0.40 P46527 EBI-12737659 0.35 P51480 EBI-15653801 0.35 Q60772 EBI-15653801 0.35 P55271 EBI-15653855 0.35 P09936 EBI-27097896 0.40 Q9R0P9 EBI-27121708 0.35 GO:0005923 GO:0000785 GO:0097128 GO:0097129 GO:0097130 GO:0000307 GO:0005737 GO:0005829 GO:0016592 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0032991 GO:0005667 GO:0005524 GO:0030332 GO:0004693 GO:0016301 GO:0004672 GO:0106310 GO:0004674 GO:0044877 GO:0008353 GO:0060612 GO:0051301 GO:0032869 GO:0071353 GO:1904637 GO:0071222 GO:1904628 GO:0000082 GO:0043065 GO:0008284 GO:0045793 GO:0050679 GO:0048146 GO:0010971 GO:0045727 GO:0006468 GO:0051726 GO:0010468 GO:0046626 GO:0046890 GO:0050994 GO:0040014 GO:0061469 GO:0010288 GO:0010033 GO:0033574 GO:0009410 GO:0007165 Unknown UniProt Sequence Analysis MAATRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGAAGGGLPVSTVREVALLRRLEAFEHPNVVRLMDVCATSRTDRDIKVTLVFEHIDQDLRTYLDKAPPPGLPVETIKDLMRQFLSGLDFLHANCIVHRDLKPENILVTSNGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPREVSLPRGAFAPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKEESDAE 303 P79432 Cyclin-dependent CDK4 9823 None SL-0178 SL-0182 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}. UNIPROT P79432 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0005923 GO:0000785 GO:0097128 GO:0097129 GO:0097130 GO:0005737 GO:0005829 GO:0016592 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0005667 GO:0005524 GO:0030332 GO:0004693 GO:0106310 GO:0008353 GO:0060612 GO:0051301 GO:0032869 GO:0071353 GO:1904637 GO:0071222 GO:1904628 GO:0000082 GO:0048146 GO:0010971 GO:0006468 GO:0051726 GO:0010468 GO:0046626 GO:0046890 GO:0050994 GO:0040014 GO:0061469 GO:0009410 GO:0007165 Unknown UniProt Sequence Analysis MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFSPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGNPE 303 P35426 Cyclin-dependent Cdk4 10116 None SL-0178 SL-0182 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}. UNIPROT P35426 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0005923 GO:0000785 GO:0097128 GO:0097129 GO:0097130 GO:0000307 GO:0005737 GO:0016592 GO:0031965 GO:0005634 GO:0048471 GO:0032991 GO:0005667 GO:0005524 GO:0030332 GO:0004693 GO:0016301 GO:0004672 GO:0106310 GO:0004674 GO:0044877 GO:0008353 GO:0060612 GO:0031100 GO:0051301 GO:0032869 GO:0071353 GO:1904637 GO:0071222 GO:1904628 GO:1904584 GO:0007623 GO:0000082 GO:0002088 GO:0043065 GO:0008284 GO:0045793 GO:0050679 GO:0048146 GO:0010971 GO:0045727 GO:0006468 GO:0051726 GO:0042127 GO:0010468 GO:0046626 GO:0046890 GO:0050994 GO:0040014 GO:0061469 GO:0055093 GO:0010288 GO:0010033 GO:0033574 GO:0009636 GO:0009410 GO:0007165 Unknown UniProt Sequence Analysis MATTRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGAAGGGLPVSTVREVALLRRLEAFEHPNVVRLMDVCATSRTDRDIKVTLVFEHIDQDLRTYLDKAPPPGLPVETIKDLMRQFLSGLDFLHANCIVHRDLKPENILVTSNGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPREVSLPRGAFSPRGPRPVQSVVPEMEESGAQLLLEMLTFNPLKRISAFRALQHSYLHKEESDPE 303 B2MVY4 Cyclin-dependent CDK4 9940 None SL-0178 SL-0182 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}. UNIPROT B2MVY4 UNIPROT B2CL06 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0005923 GO:0000785 GO:0097128 GO:0097129 GO:0097130 GO:0005829 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0005667 GO:0005524 GO:0030332 GO:0004693 GO:0106310 GO:0060612 GO:0051301 GO:0032869 GO:0071353 GO:1904637 GO:0071222 GO:1904628 GO:0000082 GO:0048146 GO:0010971 GO:0006468 GO:0010468 GO:0046626 GO:0046890 GO:0050994 GO:0040014 GO:0061469 GO:0009410 GO:0007165 Unknown UniProt Sequence Analysis MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFSPRGPRPVQSVVPELEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGDAE 303 P50613 Cyclin-dependent CDK7 9606 None SL-0198 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}. UNIPROT P50613 UNIPROT Q9BS60 UNIPROT Q9UE19 PDB 1UA2 PDB 6O9L PDB 6XBZ PDB 6XD3 PDB 7B5O PDB 7B5Q PDB 7EGB PDB 7EGC PDB 7ENA PDB 7ENC PDB 7LBM PDB 7NVR Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 601955 DisGeNET 1022 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}. O15027 EBI-16790014 0.35 P11802 EBI-15560841 0.44 P12270 EBI-16790014 0.35 P51948 EBI-1245984 0.82 P51946 EBI-1245984 0.93 P32121 EBI-1642567 0.35 A0A380PKN3 EBI-2873645 0.00 P31016 EBI-7960638 0.44 P51659 EBI-3906748 0.37 P01909 EBI-3906738 0.37 P24941 EBI-6255891 0.71 P01023 EBI-6380434 0.35 P32780 EBI-6380434 0.76 P48740 EBI-6380434 0.35 P19447 EBI-6380434 0.74 P18074 EBI-6380434 0.74 Q92759 EBI-6380434 0.67 Q13888 EBI-6380434 0.67 P23634 EBI-6380434 0.35 P28715 EBI-6380434 0.67 Q13889 EBI-6380434 0.67 Q6ZYL4 EBI-6380434 0.74 P78362 EBI-6657590 0.59 Q96SB4 EBI-6659767 0.59 P08238 EBI-6424069 0.56 Q01094 EBI-6599707 0.27 Q6P1K8 EBI-21622006 0.53 O96006 EBI-21692488 0.35 P14635 EBI-21835901 0.35 Q58FG0 EBI-21835901 0.35 Q9UBF8 EBI-21835901 0.35 Q96NH3 EBI-21835901 0.35 Q8IZL9 EBI-21835901 0.35 Q58FG1 EBI-21835901 0.35 Q58FF7 EBI-21835901 0.35 Q58FF6 EBI-21835901 0.35 Q13451 EBI-21835901 0.35 Q13137 EBI-21835901 0.35 P46527 EBI-21835901 0.35 P24864 EBI-21835901 0.35 P20248 EBI-21835901 0.35 P07900 EBI-21835901 0.35 P06493 EBI-15560801 0.44 P24928 EBI-15560781 0.44 Q6IAW3 EBI-15560872 0.44 Q9BWU1 EBI-15560892 0.44 O00267 EBI-15560912 0.44 P21127 EBI-15560932 0.44 Q9NXF1 EBI-16789709 0.27 Q96PZ0 EBI-16789709 0.27 Q8WUA4 EBI-16789709 0.27 Q7Z4V5 EBI-16789709 0.27 O15355 EBI-16789709 0.27 Q13042 EBI-16789709 0.27 Q8N1G0 EBI-16789709 0.27 P30260 EBI-16789709 0.27 Q96ME7 EBI-16789709 0.27 Q8TDI0 EBI-16789709 0.27 Q7Z5K2 EBI-16789709 0.27 Q9NW82 EBI-16789709 0.27 Q9Y3C7 EBI-16789709 0.27 Q9Y2R4 EBI-16789709 0.27 Q9UK58 EBI-16789709 0.27 Q9NY93 EBI-16789709 0.27 Q9NX58 EBI-16789709 0.27 Q9NW13 EBI-16789709 0.27 Q9NVC6 EBI-16789709 0.27 Q9H0A0 EBI-16789709 0.27 Q9BZE4 EBI-16789709 0.27 Q96S94 EBI-16789709 0.27 Q92621 EBI-16789709 0.27 Q8TF01 EBI-16789709 0.27 Q8IY81 EBI-16789709 0.27 Q8IX01 EBI-16789709 0.27 Q6PD62 EBI-16789709 0.27 Q16543 EBI-16789709 0.42 Q14684 EBI-16789709 0.27 Q14241 EBI-16789709 0.27 Q13823 EBI-16789709 0.27 Q13610 EBI-16789709 0.27 Q13011 EBI-16789709 0.27 P55199 EBI-16789709 0.27 P46013 EBI-16789709 0.48 P29083 EBI-16789709 0.27 O75683 EBI-16789709 0.27 O00541 EBI-16789709 0.27 Q9Y5Q9 EBI-16789709 0.27 Q9Y5Q8 EBI-16789709 0.27 Q9Y4W2 EBI-16789709 0.27 Q9Y2X9 EBI-16789709 0.27 Q9Y2G7 EBI-16789709 0.27 Q9H9Y6 EBI-16789709 0.27 Q9H9B1 EBI-16789709 0.27 Q9BYE7 EBI-16789709 0.27 Q9BTC8 EBI-16789709 0.27 Q8IWI9 EBI-16789709 0.27 Q6P1X5 EBI-16789709 0.27 Q5UIP0 EBI-16789709 0.27 Q15542 EBI-16789709 0.27 Q13206 EBI-16789709 0.27 Q12789 EBI-16789709 0.27 P62891 EBI-16789709 0.27 P49848 EBI-16789709 0.27 P49642 EBI-16789709 0.27 P38432 EBI-16789709 0.27 P29084 EBI-16789709 0.27 P21675 EBI-16789709 0.27 O95602 EBI-16789709 0.27 O00268 EBI-16789709 0.27 P15927 EBI-16790014 0.35 P56270 EBI-16790014 0.35 P0DMV8 EBI-16790014 0.35 Q7Z739 EBI-16790014 0.35 Q709F0 EBI-16790014 0.35 P62633 EBI-16790014 0.35 O15235 EBI-16790014 0.35 Q02539 EBI-20913302 0.40 P03372 EBI-21301141 0.35 Q9Y2W1 EBI-28935791 0.35 Q9UPE1 EBI-28935791 0.35 Q9UHB6 EBI-28935791 0.35 Q9NYF8 EBI-28935791 0.35 Q96SB3 EBI-28935791 0.35 Q8ND56 EBI-28935791 0.35 Q8IUD2 EBI-28935791 0.35 Q86X55 EBI-28935791 0.35 Q16891 EBI-28935791 0.35 Q16643 EBI-28935791 0.35 Q01082 EBI-28935791 0.35 P54886 EBI-28935791 0.35 P11388 EBI-28935791 0.35 P0C0S5 EBI-28935791 0.35 P04637 EBI-28935791 0.35 O00763 EBI-28935791 0.35 GO:0070516 GO:0019907 GO:0005737 GO:0005829 GO:0001650 GO:0001673 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0000439 GO:0005675 GO:0070985 GO:0005524 GO:0008094 GO:0004693 GO:0008022 GO:0004672 GO:0106310 GO:0004674 GO:0008353 GO:0007049 GO:0051301 GO:0006281 GO:0070816 GO:0045944 GO:0006468 GO:0050821 GO:0051726 GO:0000079 GO:2000045 GO:0042795 GO:0006366 GO:0006367 Unknown UniProt Sequence Analysis MALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSNRPGPTPGCQLPRPNCPVETLKEQSNPALAIKRKRTEALEQGGLPKKLIF 346 Q03147 Cyclin-dependent Cdk7 10090 None SL-0198 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}. UNIPROT Q03147 UNIPROT Q99KK3 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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. Q99J95 EBI-6260872 0.35 GO:0070516 GO:0019907 GO:0005737 GO:0005856 GO:0005829 GO:0001650 GO:0001673 GO:0016020 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0000439 GO:0005675 GO:0070985 GO:0005524 GO:0008094 GO:0004693 GO:0016301 GO:0008022 GO:0004672 GO:0106310 GO:0044877 GO:0008353 GO:0007049 GO:0051301 GO:0006281 GO:0070816 GO:0045944 GO:0006468 GO:0050821 GO:2000045 GO:0006366 GO:0006367 Unknown UniProt Sequence Analysis MAVDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGVPLQHIFIAAGDDLLELIQGLFLFNPCTRTTASQALKTKYFSNRPGPTPGCQLPRPNCPVEALKEPANPTVATKRKRAEALEQGILPKKLIF 346 P51952 Cyclin-dependent Cdk7 10116 None SL-0198 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}. UNIPROT P51952 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0070516 GO:0019907 GO:0000307 GO:0005737 GO:0005856 GO:0005829 GO:0001673 GO:0016020 GO:0005634 GO:0048471 GO:0000439 GO:0005675 GO:0070985 GO:0005524 GO:0008094 GO:0004693 GO:0016301 GO:0008022 GO:0004672 GO:0106310 GO:0044877 GO:0008353 GO:0051301 GO:0006281 GO:0051321 GO:0070816 GO:0045944 GO:0006468 GO:0050821 GO:2000045 GO:0006366 GO:0006367 Unknown UniProt Sequence Analysis ANRNEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNWAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGIPLQHIFIAAGDDLLELIQGLFLFNPCTRITASQALRTKYFSNRPGPTPGCQLPRPNCPVEALKEQSNPAMATKRKRAEALEQ 329 Q16667 Cyclin-dependent CDKN3 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:10669749}. UNIPROT Q16667 UNIPROT Q53ZU6 UNIPROT Q5U0M4 UNIPROT Q6P1N8 UNIPROT Q99585 UNIPROT Q9BPW7 UNIPROT Q9BY36 UNIPROT Q9C042 UNIPROT Q9C046 UNIPROT Q9C047 UNIPROT Q9C049 UNIPROT Q9C051 UNIPROT Q9C053 PDB 1FPZ PDB 1FQ1 Pfam PF05706 PROSITE PS50056 PROSITE PS50054 OMIM 114550 OMIM 123832 DisGeNET 1033 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}. 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. Q00526 EBI-8650121 0.55 P00546 EBI-8650104 0.37 P24941 EBI-8650171 0.89 P06493 EBI-8650137 0.55 Q86YZ3 EBI-14026618 0.35 P16949 EBI-14026618 0.35 Q66LE6 EBI-14026618 0.35 P54829 EBI-14026618 0.35 P50747 EBI-14026618 0.35 P38646 EBI-20906264 0.40 GO:0005737 GO:0005829 GO:0048471 GO:0017018 GO:0004722 GO:0004725 GO:0008138 GO:0000082 GO:0008285 GO:0006470 GO:0051726 GO:0000079 Unknown UniProt Sequence Analysis MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGSGAIQTIKQYNYLHEFRDKLAAHLSSRDSQSRSVSR 212 Q810P3 Cyclin-dependent Cdkn3 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q16667}. UNIPROT Q810P3 UNIPROT Q9CWS3 Pfam PF05706 PROSITE PS50056 PROSITE PS50054 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}. GO:0005737 GO:0005829 GO:0048471 GO:0017018 GO:0004722 GO:0004725 GO:0008138 GO:0007049 GO:0006974 GO:0006470 GO:0051726 Unknown UniProt Sequence Analysis MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLAACLLLYLSDSISPQQAIDSLRDVRGSGAIQTIKQYNYLHEFRDKLAAYLSSRDSLSRSVSR 211 Q9MYN5 Cyclin-dependent CDKN3 9823 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q16667}. UNIPROT Q9MYN5 Pfam PF05706 PROSITE PS50056 PROSITE PS50054 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}. GO:0005737 GO:0048471 GO:0017018 GO:0004725 GO:0008138 GO:0007049 GO:0006470 Unknown UniProt Sequence Analysis MKPPSSIQTSEFDSSDEEPIEDEQTPIQISWLPLSRVNYSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDVFVFCTRGELSKYRVPNLLDLYHQYGIITHHHPIPDGGAPDIASCCEIMEELEICLQNNRKTLIHCYGGLGRSCLVAACLLLYLSDTVSPQQAIDSLRDLRGSGAIQTIKQYNYLHEFRDKLAAHLSSRESLSRSVSR 212 B2RZ50 Cyclin-dependent Cdkn3 10116 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q16667}. UNIPROT B2RZ50 Pfam PF05706 PROSITE PS50056 PROSITE PS50054 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}. GO:0005737 GO:0048471 GO:0017018 GO:0004722 GO:0004725 GO:0008138 GO:0007049 GO:0006470 GO:0051726 Unknown UniProt Sequence Analysis MKPPISIQASEFDSSDEEPADDEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSSGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAIDSLRDVRGSGAIQTIKQYNYLHEFRDKLAAYLSSRDSLSRSVSR 212 Q19972 Chromo cec 6239 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:26607792}. Membrane {ECO:0000305|PubMed:26607792}; Peripheral membrane protein {ECO:0000305|PubMed:26607792}. UNIPROT Q19972 Pfam PF00385 PROSITE PS50013 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}. GO:0000793 GO:0005637 GO:0003682 GO:0035064 GO:0097240 GO:0045595 GO:0010468 Peripheral UniProt Curator Inference {ECO:0000305|PubMed:26607792} MAKKTVEGEHGTPKTNFTKKETSKNHDDFKKIIGHKVVEEHYVEYEVELTSGKTITATEFDFKGDDSLLSTYKKKVTKQSDDSSGEYAVERVLAHRKVKGSPLYLVQWKGYPHPVWNSEMWEEDLDNCKDLLAAYKKHQEDLKIAQTPKKTPSKTPKKTPKSLKRRALTPSDDEEEAGPIAPEPKKTPKQSTKKLKRTTSPETNLVEKSKKKAIPDLENHTLDQEKNDVIERVEEIQEDEDDDDEQREEVVTTAPVETKSRWGFGSWKWF 270 P42573 Cell ced 6239 None SL-0178 SL-0182 SL-0198 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}. UNIPROT P42573 UNIPROT P45435 UNIPROT Q9GQQ4 UNIPROT Q9NAQ8 PDB 4M9R PDB 4M9S PDB 4M9X PDB 4M9Y PDB 4M9Z Pfam PF00619 PROSITE PS50209 PROSITE PS01122 PROSITE PS01121 PROSITE PS50207 PROSITE PS50208 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}. P30429 EBI-494268 0.86 Q8STE5 EBI-8001700 0.37 P41958 EBI-494631 0.70 P42573 EBI-2655158 0.75 G5ECW5 EBI-15727540 0.60 Q9XXH8 EBI-16127213 0.44 Q9NAG4 EBI-16587378 0.35 GO:0070161 GO:0008303 GO:0005737 GO:0016020 GO:0005739 GO:0043025 GO:0031965 GO:0043204 GO:0048471 GO:0098793 GO:0008656 GO:0004197 GO:0097153 GO:0097199 GO:0097200 GO:0004175 GO:0042802 GO:0030042 GO:0097202 GO:0006919 GO:0006915 GO:1902742 GO:0050829 GO:0009792 GO:0097194 GO:0046716 GO:1905803 GO:1900118 GO:1904747 GO:1905845 GO:0043525 GO:1901046 GO:0010954 GO:1905808 GO:0012501 GO:0016540 GO:0030163 GO:0006508 GO:0030155 GO:0042659 GO:0040034 GO:0040012 GO:0031647 GO:0050807 GO:0040028 Unknown UniProt Sequence Analysis MMRQDRRSLLERNIMMFSSHLKVDEILEVLIAKQVLNSDNGDMINSCGTVREKRREIVKAVQRRGDVAFDAFYDALRSTGHEGLAEVLEPLARSVDSNAVEFECPMSPASHRRSRALSPAGYTSPTRVHRDSVSSVSSFTSYQDIYSRARSRSRSRALHSSDRHNYSSPPVNAFPSQPSSANSSFTGCSSLGYSSSRNRSFSKASGPTQYIFHEEDMNFVDAPTISRVFDEKTMYRNFSSPRGMCLIINNEHFEQMPTRNGTKADKDNLTNLFRCMGYTVICKDNLTGRGMLLTIRDFAKHESHGDSAILVILSHGEENVIIGVDDIPISTHEIYDLLNAANAPRLANKPKIVFVQACRGERRDNGFPVLDSVDGVPAFLRRGWDNRDGPLFNFLGCVRPQVQQVWRKKPSQADILIAYATTAQYVSWRNSARGSWFIQAVCEVFSTHAKDMDVVELLTEVNKKVACGFQTSQGSNILKQMPEMTSRLLKKFYFWPEARNSAV 503 P45436 Cell ced 31234 None SL-0178 SL-0182 SL-0198 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}. UNIPROT P45436 UNIPROT E3M6B9 Pfam PF00619 PROSITE PS50209 PROSITE PS01122 PROSITE PS01121 PROSITE PS50207 PROSITE PS50208 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}. GO:0070161 GO:0008303 GO:0005739 GO:0031965 GO:0043204 GO:0048471 GO:0098793 GO:0008656 GO:0097200 GO:0042802 GO:0030042 GO:0097202 GO:1902742 GO:0050829 GO:0009792 GO:0046716 GO:1905803 GO:1900118 GO:1904747 GO:1905845 GO:0043525 GO:1901046 GO:0010954 GO:1905808 GO:0016540 GO:0030163 GO:0030155 GO:0042659 GO:0040034 GO:0040012 GO:0031647 GO:0040028 Unknown UniProt Sequence Analysis MMRQDRRNLLERNILVFSNKLQSEQILEVLIAKQILNADNGDVINSCRTERDKRKEIVKAVQRRGDVAFDAFYDALRDTGHHELAAVLEPLARTIDFITPRDLECPMSPASHRRSRALSPSTFSSPTRVHRDSVSSVSSFTSTYQDVYTRARSTSRSSRPLHASDRHNYVSPSNSFQSQPSSANSSFTGCSSLGYSSSRTRSYSKASAHSQYIFHEEDMNYVDAPTIHRVFDEKTMYRNFSTPRGLCLIINNEHFEQMPTRNGTKADKDNISNLFRCMGYIVHCKDNLTGRAMMLTIRDFAKNETHGDSAILVILSHGEENVIIGVDDVSVNVHEIYDLLNAANAPRLANKPKLVFVQACRGERRDNGFPVLDSVDGVPALIRPRGWDKGDGPLFNFLGCVRPQAQQVWRKKPSQADILIAYATTAQYVSWRNSARGSWFIQAVCEVFSLHAKDMDVVELLTEVNKKVACGFQTSQGANILKQMPELTSRLLKKFYFWPEDRNRSSAV 508 Q60Z52 Cell ced 6238 None SL-0198 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}. UNIPROT Q60Z52 UNIPROT A8XSP2 Pfam PF00619 Pfam PF00931 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}. GO:0008303 GO:0005829 GO:0016020 GO:0005739 GO:0005634 GO:0048471 GO:0043531 GO:0005524 GO:0051432 GO:0051434 GO:0089720 GO:0008656 GO:0061133 GO:0042802 GO:0000287 GO:0030042 GO:0097202 GO:0006915 GO:1902742 GO:0050829 GO:0009792 GO:0048598 GO:0046716 GO:0043066 GO:1900118 GO:0043065 GO:1904747 GO:0010954 GO:1905808 GO:0030155 GO:0008361 GO:0040034 GO:0031647 Unknown UniProt Sequence Analysis MLCEIECRALNAAHTMLIQDFEPRDALTYLEGEKIFTEDHSDLISNMPTRLERIANFLRAYRRQASELAPLIDFFEYNNQNHLKDFLDEYLWFATHQPDKLRPVVLVPKFSRQMLDRKLLLGNVPKQMNCFSREFHVDRVIEKLDEMCDLESFFLFLHGRSGSGKSVIASQALSKSDQLIGINYDSVVWLKDSGTTPKATFDLFTDLLLMLKRARVVSDTDDSHNMPDFINRVLSRSEDDLLNFPSVEHVTSVVLKRMIANALIDRPNTLFVLDDVVQEDTIRWAQELRLRCLITTRDVEISNAASPECEFIEVTPLESYECFELLESYGMPVPAIERDEDILHKTIDLTSGNPAALMMIFKSCEPKTFEKMAQLNSKLETRGLSAIECITPYCYKSLSSSLQRCVEVLSDEDRSALAFAVIMPPGIDIPVKIWSCVIPVDICSNEEDQLDDEVADRLKRLSKRGALLSGKRSPVLTYKIDHVIHLFLKHVVDVQTIANGISILEQRLHELGNNNTPTPERHMPSKFRRTSAGDMFPKVEDSVIRPEDYSKFMQIHRTFYDSLKKFTSQ 569 P30429 Cell ced 6239 None SL-0198 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}. UNIPROT P30429 UNIPROT Q5BHI5 PDB 2A5Y PDB 3LQQ PDB 3LQR PDB 4M9S PDB 4M9X PDB 4M9Y PDB 4M9Z Pfam PF00619 Pfam PF00931 PROSITE PS50209 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}. P41958 EBI-494126 0.84 Q07817 EBI-494146 0.40 P42573 EBI-494268 0.86 O61667 EBI-11688070 0.35 P30429 EBI-2655126 0.44 Q20924 EBI-15599089 0.56 Q14790 EBI-16211709 0.40 Q9NAG4 EBI-16587288 0.57 GO:0008303 GO:0005829 GO:0016020 GO:0005739 GO:0005634 GO:0048471 GO:0032991 GO:0043531 GO:0005524 GO:0051432 GO:0051434 GO:0089720 GO:0008656 GO:0061133 GO:0042802 GO:0000287 GO:0016505 GO:0030042 GO:0097202 GO:0006919 GO:0006915 GO:1902742 GO:0050829 GO:0009792 GO:0048598 GO:0046716 GO:0043066 GO:1900118 GO:0043065 GO:1904747 GO:2001056 GO:0010954 GO:1905808 GO:0030155 GO:0008361 GO:0043281 GO:0040034 GO:0031647 Unknown UniProt Sequence Analysis MLCEIECRALSTAHTRLIHDFEPRDALTYLEGKNIFTEDHSELISKMSTRLERIANFLRIYRRQASELGPLIDFFNYNNQSHLADFLEDYIDFAINEPDLLRPVVIAPQFSRQMLDRKLLLGNVPKQMTCYIREYHVDRVIKKLDEMCDLDSFFLFLHGRAGSGKSVIASQALSKSDQLIGINYDSIVWLKDSGTAPKSTFDLFTDILLMLARVVSDTDDSHSITDFINRVLSRSEDDLLNFPSVEHVTSVVLKRMICNALIDRPNTLFVFDDVVQEETIRWAQELRLRCLVTTRDVEISNAASQTCEFIEVTSLEIDECYDFLEAYGMPMPVGEKEEDVLNKTIELSSGNPATLMMFFKSCEPKTFEKMAQLNNKLESRGLVGVECITPYSYKSLAMALQRCVEVLSDEDRSALAFAVVMPPGVDIPVKLWSCVIPVDICSNEEEQLDDEVADRLKRLSKRGALLSGKRMPVLTFKIDHIIHMFLKHVVDAQTIANGISILEQRLLEIGNNNVSVPERHIPSHFQKFRRSSASEMYPKTTEETVIRPEDFPKFMQLHQKFYDSLKNFACC 571 P49454 Centromere CENPF 9606 None SL-0198 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. UNIPROT P49454 UNIPROT Q13171 UNIPROT Q13246 UNIPROT Q5VVM7 Pfam PF10490 Pfam PF10473 Pfam PF10481 OMIM 243605 OMIM 600236 DisGeNET 1063 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}. 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. K9N7C7 EBI-26374676 0.35 P0DTD1 EBI-25490757 0.53 P43034 EBI-2298103 0.35 Q15714 EBI-1083967 0.00 Q9GZM8 EBI-2295215 0.75 Q8WUM0 EBI-7328986 0.48 P57740 EBI-7329356 0.35 Q02224 EBI-1375056 0.37 P32121 EBI-1642843 0.35 Q9NXR1 EBI-2298075 0.40 A2AUM9 EBI-2563733 0.40 O46385 EBI-7872444 0.37 O00257 EBI-3951698 0.35 Q7L5N1 EBI-21328549 0.35 Q5S007 EBI-6515052 0.35 P05412 EBI-11323169 0.35 Q7TSY8 EBI-11011396 0.35 Q8BZQ7 EBI-11026803 0.35 Q96FF9 EBI-11027063 0.35 P63005 EBI-11041417 0.35 P70399 EBI-11051507 0.35 Q9QYY8 EBI-11090422 0.35 Q99PT9 EBI-11092405 0.35 P01106 EBI-11105437 0.35 Q13283 EBI-11106283 0.35 Q08AG7 EBI-11108327 0.35 Q8CI51 EBI-11124806 0.35 P25963 EBI-11133856 0.35 Q9Y253 EBI-11141689 0.35 Q71F23 EBI-11156542 0.35 Q9UQN3 EBI-11510767 0.37 P49356 EBI-21502393 0.35 Q96KS9 EBI-21503766 0.35 Q8TDR4 EBI-21617027 0.35 Q96A37 EBI-21627270 0.35 Q9Y2V7 EBI-21673529 0.35 Q8N5R6 EBI-21699069 0.35 Q9H2F9 EBI-21702403 0.35 Q9Y6K9 EBI-21708976 0.35 Q9HD26 EBI-21720201 0.35 Q96T17 EBI-21796065 0.35 Q9UKA1 EBI-21796233 0.35 Q96EY4 EBI-21806027 0.35 Q96AP7 EBI-21848470 0.35 Q9UPY6 EBI-21852540 0.35 Q96JN8 EBI-16814395 0.35 P46013 EBI-20562326 0.35 P30040 EBI-20902848 0.40 Q9BYW2 EBI-20911906 0.40 Q02539 EBI-20938636 0.40 P14404 EBI-21028244 0.35 Q9NRI5 EBI-21370473 0.00 Q8NCK7 EBI-27103180 0.35 Q9UM73 EBI-32719830 0.27 Q8N612 EBI-34574737 0.27 GO:0005930 GO:0005813 GO:0000775 GO:0036064 GO:0097539 GO:0005737 GO:0005829 GO:0000776 GO:0030496 GO:0005635 GO:0016363 GO:0005654 GO:0005634 GO:0000940 GO:0048471 GO:0045120 GO:0005819 GO:0000922 GO:0003682 GO:0140297 GO:0070840 GO:0008017 GO:0008022 GO:0042803 GO:0030154 GO:0051301 GO:0007059 GO:0071897 GO:0001822 GO:0051382 GO:0051310 GO:0000278 GO:0007094 GO:0007517 GO:0045892 GO:0015031 GO:0010389 GO:0016202 GO:0009410 GO:0021591 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:10852915} MSWALEEWKEGLPTRALQKIQELEGQLDKLKKEKQQRQFQLDSLEAALQKQKQKVENEKTEGTNLKRENQRLMEICESLEKTKQKISHELQVKESQVNFQEGQLNSGKKQIEKLEQELKRCKSELERSQQAAQSADVSLNPCNTPQKIFTTPLTPSQYYSGSKYEDLKEKYNKEVEERKRLEAEVKALQAKKASQTLPQATMNHRDIARHQASSSVFSWQQEKTPSHLSSNSQRTPIRRDFSASYFSGEQEVTPSRSTLQIGKRDANSSFFDNSSSPHLLDQLKAQNQELRNKINELELRLQGHEKEMKGQVNKFQELQLQLEKAKVELIEKEKVLNKCRDELVRTTAQYDQASTKYTALEQKLKKLTEDLSCQRQNAESARCSLEQKIKEKEKEFQEELSRQQRSFQTLDQECIQMKARLTQELQQAKNMHNVLQAELDKLTSVKQQLENNLEEFKQKLCRAEQAFQASQIKENELRRSMEEMKKENNLLKSHSEQKAREVCHLEAELKNIKQCLNQSQNFAEEMKAKNTSQETMLRDLQEKINQQENSLTLEKLKLAVADLEKQRDCSQDLLKKREHHIEQLNDKLSKTEKESKALLSALELKKKEYEELKEEKTLFSCWKSENEKLLTQMESEKENLQSKINHLETCLKTQQIKSHEYNERVRTLEMDRENLSVEIRNLHNVLDSKSVEVETQKLAYMELQQKAEFSDQKHQKEIENMCLKTSQLTGQVEDLEHKLQLLSNEIMDKDRCYQDLHAEYESLRDLLKSKDASLVTNEDHQRSLLAFDQQPAMHHSFANIIGEQGSMPSERSECRLEADQSPKNSAILQNRVDSLEFSLESQKQMNSDLQKQCEELVQIKGEIEENLMKAEQMHQSFVAETSQRISKLQEDTSAHQNVVAETLSALENKEKELQLLNDKVETEQAEIQELKKSNHLLEDSLKELQLLSETLSLEKKEMSSIISLNKREIEELTQENGTLKEINASLNQEKMNLIQKSESFANYIDEREKSISELSDQYKQEKLILLQRCEETGNAYEDLSQKYKAAQEKNSKLECLLNECTSLCENRKNELEQLKEAFAKEHQEFLTKLAFAEERNQNLMLELETVQQALRSEMTDNQNNSKSEAGGLKQEIMTLKEEQNKMQKEVNDLLQENEQLMKVMKTKHECQNLESEPIRNSVKERESERNQCNFKPQMDLEVKEISLDSYNAQLVQLEAMLRNKELKLQESEKEKECLQHELQTIRGDLETSNLQDMQSQEISGLKDCEIDAEEKYISGPHELSTSQNDNAHLQCSLQTTMNKLNELEKICEILQAEKYELVTELNDSRSECITATRKMAEEVGKLLNEVKILNDDSGLLHGELVEDIPGGEFGEQPNEQHPVSLAPLDESNSYEHLTLSDKEVQMHFAELQEKFLSLQSEHKILHDQHCQMSSKMSELQTYVDSLKAENLVLSTNLRNFQGDLVKEMQLGLEEGLVPSLSSSCVPDSSSLSSLGDSSFYRALLEQTGDMSLLSNLEGAVSANQCSVDEVFCSSLQEENLTRKETPSAPAKGVEELESLCEVYRQSLEKLEEKMESQGIMKNKEIQELEQLLSSERQELDCLRKQYLSENEQWQQKLTSVTLEMESKLAAEKKQTEQLSLELEVARLQLQGLDLSSRSLLGIDTEDAIQGRNESCDISKEHTSETTERTPKHDVHQICDKDAQQDLNLDIEKITETGAVKPTGECSGEQSPDTNYEPPGEDKTQGSSECISELSFSGPNALVPMDFLGNQEDIHNLQLRVKETSNENLRLLHVIEDRDRKVESLLNEMKELDSKLHLQEVQLMTKIEACIELEKIVGELKKENSDLSEKLEYFSCDHQELLQRVETSEGLNSDLEMHADKSSREDIGDNVAKVNDSWKERFLDVENELSRIRSEKASIEHEALYLEADLEVVQTEKLCLEKDNENKQKVIVCLEEELSVVTSERNQLRGELDTMSKKTTALDQLSEKMKEKTQELESHQSECLHCIQVAEAEVKEKTELLQTLSSDVSELLKDKTHLQEKLQSLEKDSQALSLTKCELENQIAQLNKEKELLVKESESLQARLSESDYEKLNVSKALEAALVEKGEFALRLSSTQEEVHQLRRGIEKLRVRIEADEKKQLHIAEKLKERERENDSLKDKVENLERELQMSEENQELVILDAENSKAEVETLKTQIEEMARSLKVFELDLVTLRSEKENLTKQIQEKQGQLSELDKLLSSFKSLLEEKEQAEIQIKEESKTAVEMLQNQLKELNEAVAALCGDQEIMKATEQSLDPPIEEEHQLRNSIEKLRARLEADEKKQLCVLQQLKESEHHADLLKGRVENLERELEIARTNQEHAALEAENSKGEVETLKAKIEGMTQSLRGLELDVVTIRSEKENLTNELQKEQERISELEIINSSFENILQEKEQEKVQMKEKSSTAMEMLQTQLKELNERVAALHNDQEACKAKEQNLSSQVECLELEKAQLLQGLDEAKNNYIVLQSSVNGLIQEVEDGKQKLEKKDEEISRLKNQIQDQEQLVSKLSQVEGEHQLWKEQNLELRNLTVELEQKIQVLQSKNASLQDTLEVLQSSYKNLENELELTKMDKMSFVEKVNKMTAKETELQREMHEMAQKTAELQEELSGEKNRLAGELQLLLEEIKSSKDQLKELTLENSELKKSLDCMHKDQVEKEGKVREEIAEYQLRLHEAEKKHQALLLDTNKQYEVEIQTYREKLTSKEECLSSQKLEIDLLKSSKEELNNSLKATTQILEELKKTKMDNLKYVNQLKKENERAQGKMKLLIKSCKQLEEEKEILQKELSQLQAAQEKQKTGTVMDTKVDELTTEIKELKETLEEKTKEADEYLDKYCSLLISHEKLEKAKEMLETQVAHLCSQQSKQDSRGSPLLGPVVPGPSPIPSVTEKRLSSGQNKASGKRQRSSGIWENGRGPTPATPESFSKKSKKAVMSGIHPAEDTEGTEFEPEGLPEVVKKGFADIPTGKTSPYILRRTTMATRTSPRLAAQKLALSPLSLGKENLAESSKPTAGGSRSQKVKVAQRSPVDSGTILREPTTKSVPVNNLPERSPTDSPREGLRVKRGRLVPSPKAGLESNGSENCKVQ 3114 Q5ZKD1 Choline/ethanolaminephosphotransferase CEPT1 9031 None SL-0178 SL-0182 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}. UNIPROT Q5ZKD1 Pfam PF01066 PROSITE PS00379 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}. GO:0005789 GO:0005794 GO:0016021 GO:0031965 GO:0047359 GO:0004142 GO:0004307 GO:0046872 GO:0006646 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSGHRNLKRRCGESHLESPAGCAHGPAAACVLSKLVQLPTPPLSKHQLKRLEEHKYQSAGRSLLEPLMQGYWEWLVGKVPAWIAPNLITIIGLLINIFTTLLLVYYCPTATEQAPPWAYIACACGLFIYQSLDTIDGKQARRTNSSTPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSLIPILNIQVKIFPALCTVAGTIFSCTNYFGVIFTGGVGKNGSTIAGTSVLSPFLHIGSVIALAAMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALIFSLFDLLRYCVSVCNQIAAHLHIHVFRIKSSSTHSNHH 416 Q9Y6K0 Choline/ethanolaminephosphotransferase CEPT1 9606 None SL-0178 SL-0182 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}. UNIPROT Q9Y6K0 UNIPROT Q69YJ9 UNIPROT Q9P0Y8 Pfam PF01066 PROSITE PS00379 OMIM 616751 DisGeNET 10390 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}. A0A142I5B9 EBI-20626314 0.35 O43542 EBI-11129266 0.35 P04626 EBI-32718334 0.35 Q6ZRP7 EBI-11127397 0.35 Q921T2 EBI-10996616 0.35 Q9P0L0 EBI-11120309 0.35 P01106 EBI-1237540 0.35 A0A384KHP8 EBI-2873575 0.00 Q77M19 EBI-6270503 0.35 Q16659 EBI-12502733 0.35 P03182 EBI-11721938 0.35 P06460 EBI-11723082 0.35 P06792 EBI-11724527 0.35 E9PUA5 EBI-10999661 0.35 P60953 EBI-11002356 0.35 P19784 EBI-11002671 0.35 Q99JP4 EBI-11005491 0.35 Q96SB8 EBI-11007096 0.35 Q14807 EBI-11033337 0.35 Q7Z406 EBI-11033498 0.35 O88441 EBI-11096794 0.35 O96008 EBI-11113522 0.35 Q9D7F7 EBI-11116442 0.35 Q6NZB1 EBI-11119708 0.35 P62191 EBI-11123102 0.35 P54368 EBI-11123446 0.35 Q7LFX5 EBI-11123526 0.35 P70335 EBI-11124658 0.35 O43379 EBI-11127003 0.35 Q969M3 EBI-11127233 0.35 Q9NYU2 EBI-11127729 0.35 P46940 EBI-11132927 0.35 O00400 EBI-11135399 0.35 Q9NZD8 EBI-24511333 0.56 Q9NUH8 EBI-25231884 0.56 Q8N6H7 EBI-21875078 0.35 P78332 EBI-21875078 0.35 P55196 EBI-21875078 0.35 P03372 EBI-21301141 0.35 P19419 EBI-25378580 0.35 P0DOF2 EBI-25603126 0.35 Q96T52 EBI-27049069 0.27 Q9H5K3 EBI-28948637 0.35 Q06418 EBI-32719716 0.35 GO:0005789 GO:0005794 GO:0016021 GO:0031965 GO:0047359 GO:0004142 GO:0004307 GO:0046872 GO:0006629 GO:0006646 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVRRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIPVLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAAMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH 416 Q8BGS7 Choline/ethanolaminephosphotransferase Cept1 10090 None SL-0178 SL-0182 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}. UNIPROT Q8BGS7 UNIPROT Q8VC64 Pfam PF01066 PROSITE PS00379 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}. GO:0005789 GO:0005794 GO:0016021 GO:0031965 GO:0047359 GO:0004142 GO:0004307 GO:0046872 GO:0016780 GO:0006656 GO:0006646 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVGRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIPVLNIQMKLLPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAVMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALIFSFFDLIRYCVSVCNQIASHLHIHVFRIKASTAHSNHH 416 Q6AXM5 Choline/ethanolaminephosphotransferase Cept1 10116 None SL-0178 SL-0182 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}. UNIPROT Q6AXM5 Pfam PF01066 PROSITE PS00379 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}. GO:0005789 GO:0005794 GO:0016021 GO:0031965 GO:0047359 GO:0004142 GO:0004307 GO:0046872 GO:0016780 GO:0006656 GO:0006646 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSGHRSTRKRCGDSHPESPVGFGHMSTTGCILNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVGRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIPVLNIQMKLFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAVMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKTSTAHSNHH 416 Q7ZYQ3 Choline/ethanolaminephosphotransferase cept1 8355 None SL-0178 SL-0182 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}. UNIPROT Q7ZYQ3 Pfam PF01066 PROSITE PS00379 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}. GO:0005789 GO:0016021 GO:0031965 GO:0047359 GO:0004142 GO:0004307 GO:0046872 GO:0006646 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSAQRAAKRRTGDFHSEFPSSCGNPYQTACLLSKFIELPNPPLSRHQLKRLEEHRYQSCGKSLLEPLMQGFWEWLVIQVPQWIAPNLITIIGLLINIVTTVVLIYYCPTATEKAPTWTYLSCAIGLFMYQSLDAIDGKQARRTNSSTPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGMFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAAIGGPTLWLSMIPVLNVPMKLFPALCTVAGTVFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPMLHIGSVIVLATMIYKKSSVQLFEKHPCLYILTFGFVSAKVTNKLVVAHMTKSEMHLHDSAFIGPALLFLNQYFNSFIDEYLVLWIALVLSLIDLIRYSVSVCNQIASHLHIEVFRIKTKMARFNHH 416 Q28H54 Choline/ethanolaminephosphotransferase cept1 8364 None SL-0178 SL-0182 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}. UNIPROT Q28H54 Pfam PF01066 PROSITE PS00379 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}. GO:0005789 GO:0005794 GO:0016021 GO:0031965 GO:0047359 GO:0004142 GO:0004307 GO:0046872 GO:0006646 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSGQRAAKRRTGDLHTEFPTSCGNPYQTACLLSKFIELPTPPLTRHQLKRLEEHRYQSCGKSLLEPIMQGFWEWLVEQVPQWIAPNLITIIGLLINIITTVVLVYYCPTATEKAPTWTYLSCAIGLFIYQSLDAIDGKQARRTNSSTPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGMFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAAIGGPTLWLSMIPVLNVPMKLFPALCTVAGTVFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPMLHIGSVIVLATMIYKKSSVQLFEKHPCLYILTFGFVSAKVTNKLVVAHMTKSEMHLHDSAFIGPALLFLNQYFNSFIDEHLVLWIALVLSFIDLIRYSVSICNQIASHLHIEVFRIKTKVARFNHH 416 Q2TBN3 Centrin-2 CETN2 9913 None SL-0178 SL-0185 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}. UNIPROT Q2TBN3 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0097729 GO:0045177 GO:0005814 GO:0005813 GO:0036064 GO:0005737 GO:0044615 GO:0032391 GO:0070390 GO:0071942 GO:0005509 GO:0031683 GO:0032795 GO:0008017 GO:0051301 GO:0007099 GO:0000278 GO:0051028 GO:0006289 GO:0015031 GO:0032465 GO:0007283 Unknown UniProt Sequence Analysis MASNFKKANMASTTQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFSDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLSDEELQEMIDEADRDGDGEVNEQEFLRIMKKTSLY 172 P41208 Centrin-2 CETN2 9606 None SL-0178 SL-0185 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}. UNIPROT P41208 UNIPROT B2R4T4 UNIPROT Q53XW1 PDB 1M39 PDB 1ZMZ PDB 2A4J PDB 2GGM PDB 2K2I PDB 2OBH Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 300006 DisGeNET 1069 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}. O43303 EBI-1789852 0.52 Q70CQ1 EBI-2512828 0.40 Q9H0E7 EBI-2513724 0.59 Q9R1K9 EBI-2561097 0.40 A8K8P3 EBI-2659498 0.65 P15289 EBI-3904577 0.37 Q96LA8 EBI-3915269 0.37 P54727 EBI-4567671 0.57 Q01831 EBI-4567671 0.78 Q2NKQ1 EBI-10208385 0.72 Q8NA72 EBI-10208397 0.80 Q96PV4 EBI-10208407 0.56 Q6P5D4 EBI-10991106 0.35 P52732 EBI-11007621 0.35 Q6PD62 EBI-11013551 0.35 Q99598 EBI-11044893 0.35 P48754 EBI-11097282 0.35 O88286 EBI-11104133 0.35 Q3V6T2 EBI-11141559 0.35 P29341 EBI-11149873 0.35 Q14103 EBI-11152836 0.35 O14640 EBI-11382084 0.27 Q8N0X7 EBI-11382084 0.27 P53680 EBI-11382084 0.27 P50991 EBI-11382084 0.27 P49368 EBI-11382084 0.27 P20290 EBI-11382084 0.27 Q99832 EBI-11382084 0.27 Q9UNY4 EBI-11382084 0.27 Q16513 EBI-11382084 0.27 Q9BYS8 EBI-11382084 0.27 P78371 EBI-11382084 0.27 P48643 EBI-11382084 0.27 P17987 EBI-11382084 0.27 Q8WUY9 EBI-11382084 0.27 Q9NYP9 EBI-11382084 0.27 P40227 EBI-11382084 0.27 P35606 EBI-11382084 0.27 O14737 EBI-11382084 0.27 Q8WU90 EBI-11382084 0.27 P56945 EBI-15099687 0.35 Q12798 EBI-21576600 0.35 P16104 EBI-21578956 0.35 Q96A08 EBI-21579454 0.35 O14874 EBI-21725538 0.53 Q5VW00 EBI-21725806 0.35 P08887 EBI-21731028 0.35 Q8IW19 EBI-21791365 0.35 Q6ZNE5 EBI-21819923 0.35 Q9BQ69 EBI-21827171 0.35 Q96DD0 EBI-21832541 0.35 Q9NTX7 EBI-21839807 0.35 P15927 EBI-21839521 0.35 Q0VDD8 EBI-21849985 0.35 Q8NEE6 EBI-21867658 0.40 P42858 EBI-21132926 0.67 P03372 EBI-21301141 0.35 Q16526 EBI-21981854 0.35 Q8N488 EBI-27110926 0.35 GO:0097729 GO:0045177 GO:0005814 GO:0005813 GO:0036064 GO:0005829 GO:0044615 GO:0005654 GO:0032391 GO:0070390 GO:0071942 GO:0005509 GO:0031683 GO:0032795 GO:0008017 GO:0051301 GO:0007099 GO:0000278 GO:0051028 GO:0006289 GO:0015031 GO:0032465 GO:0007283 Unknown UniProt Sequence Analysis MASNFKKANMASSSQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFGDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVSEQEFLRIMKKTSLY 172 Q9R1K9 Centrin-2 Cetn2 10090 None SL-0178 SL-0185 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}. UNIPROT Q9R1K9 UNIPROT B1AUQ6 UNIPROT B1AUQ8 UNIPROT Q3UBB4 UNIPROT Q9CWM0 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. O15182 EBI-2561097 0.40 O60318 EBI-11111151 0.35 P41208 EBI-2561097 0.40 Q14974 EBI-11111151 0.35 Q8NA72 EBI-2561097 0.56 P54727 EBI-2561097 0.40 Q01831 EBI-2561097 0.56 P54728 EBI-4567934 0.35 P20263 EBI-5240764 0.35 Q92738 EBI-11111151 0.35 Q15154 EBI-11111151 0.35 P20226 EBI-11111151 0.35 P35221 EBI-11111151 0.35 O75340 EBI-11111151 0.35 Q9UPN4 EBI-11111151 0.35 E5RK82 EBI-11111151 0.35 P28289 EBI-11111151 0.35 Q6P597 EBI-11111151 0.35 P30044 EBI-11111151 0.35 F5H4F1 EBI-11111151 0.35 A8K8P3 EBI-11111151 0.35 O60879 EBI-11112667 0.35 Q92917 EBI-11112667 0.35 Q8IXQ4 EBI-11112667 0.35 O75923 EBI-11112667 0.35 Q3V6T2 EBI-11112667 0.35 Q04837 EBI-11112667 0.35 Q9BYT8 EBI-11112667 0.35 P31948 EBI-11112667 0.35 Q8IWJ2 EBI-11112667 0.35 Q08AD1 EBI-11112667 0.35 Q6NZM9 EBI-26473140 0.35 GO:0097729 GO:0045177 GO:0005814 GO:0005813 GO:0036064 GO:0005929 GO:0005737 GO:0044615 GO:0032391 GO:0070390 GO:0071942 GO:0005509 GO:0031683 GO:0032795 GO:0008017 GO:0051301 GO:0007099 GO:0000278 GO:0051028 GO:0006289 GO:0015031 GO:0032465 GO:0007283 Unknown UniProt Sequence Analysis MASNFKKTTMASSAQRKRMSPKPELTEDQKQEIREAFDLFDADGTGTIDIKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFSDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVNEQEFLRIMKKTSLY 172 O15182 Centrin-3 CETN3 9606 None SL-0178 SL-0185 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}. UNIPROT O15182 UNIPROT Q53YD2 UNIPROT Q9BS23 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 602907 DisGeNET 1070 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}. O43924 EBI-729774 0.00 Q5UIP0 EBI-729777 0.00 Q13432 EBI-729780 0.00 O95229 EBI-1001131 0.35 Q6UVJ0 EBI-1570168 0.27 Q70CQ1 EBI-2512828 0.40 Q9R1K9 EBI-2561097 0.40 Q9H0K1 EBI-2910196 0.27 Q9Y6K9 EBI-5772724 0.00 P04792 EBI-6872539 0.37 Q2NKQ1 EBI-10182468 0.72 Q8NA72 EBI-10182480 0.80 Q15293 EBI-24265783 0.56 O95994 EBI-24269242 0.56 P19237 EBI-24271146 0.56 P17540 EBI-24678114 0.56 O00141 EBI-24728013 0.56 O43679 EBI-24793336 0.56 Q12798 EBI-21576600 0.35 Q8N490 EBI-21596986 0.35 Q96EV8 EBI-21651992 0.35 O00212 EBI-21717184 0.35 O14874 EBI-21725538 0.53 O95976 EBI-21725569 0.35 Q01831 EBI-21725721 0.53 P18509 EBI-21725612 0.35 Q5VW00 EBI-21725806 0.35 O15273 EBI-21729416 0.40 Q5S007 EBI-20587935 0.44 Q9Y4C4 EBI-20589725 0.44 Q92844 EBI-20737201 0.35 Q9UQ80 EBI-20904872 0.40 Q5T7N2 EBI-20993270 0.35 P13473 EBI-25872710 0.56 Q9Y371 EBI-25921828 0.56 P0C6X7 EBI-26376977 0.35 GO:0005814 GO:0005813 GO:0036064 GO:0005737 GO:0005815 GO:0044615 GO:0005730 GO:0032391 GO:0070390 GO:0005509 GO:0031683 GO:0008017 GO:0051301 GO:0007098 GO:0051028 GO:0015031 Unknown UniProt Sequence Analysis MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFIAIMTGDI 167 O35648 Centrin-3 Cetn3 10090 None SL-0178 SL-0185 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}. UNIPROT O35648 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0005814 GO:0005813 GO:0036064 GO:0035869 GO:0005737 GO:0005815 GO:0044615 GO:0005730 GO:0032391 GO:0070390 GO:0005509 GO:0031683 GO:0008017 GO:0007049 GO:0051301 GO:0051028 GO:0015031 Unknown UniProt Sequence Analysis MSLALRGELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDQAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFIAIMTGDI 167 P30922 Chitinase-3-like CHI3L1 9913 None SL-0198 Secreted, extracellular space. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. UNIPROT P30922 UNIPROT O18949 UNIPROT Q58CW2 UNIPROT Q7YSE8 PDB 1OWQ PDB 2ESC Pfam PF00704 PROSITE PS51910 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}. GO:0005737 GO:0005783 GO:0005576 GO:0005615 GO:0048471 GO:0030246 GO:0008061 GO:0007250 GO:0006915 GO:0005975 GO:0071356 GO:0006032 GO:0006954 GO:0030324 GO:0045766 GO:0070374 GO:0032757 GO:0010800 GO:0051897 GO:0070555 GO:0070741 GO:0009612 GO:0034612 Unknown UniProt Sequence Analysis MGLRAAHTGFVVLVLLQSCAAYKLICYYTSWSQYREGDGSCFPDAIDPFLCTHVIYSFANISNNEIDTWEWNDVTLYDTLNTLKNRNPNLKTLLSVGGWNFGSQRFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGWRDKRHLTTLVKEMKAEFVREAQAGTEQLLLSAAVPAGKIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFRGQEDASSDRFSNADYAVSYMLRLGAPANKLVMGIPTFGRSYTLASSKTDVGAPISGPGIPGQFTKEKGILAYYEICDFLHGATTHRFRDQQVPYATKGNQWVAYDDQESVKNKARYLKNRQLAGAMVWALDLDDFRGTFCGQNLTFPLTSAIKDVLARV 383 Q7YS85 Chitinase-3-like CHI3L1 89462 None SL-0198 Secreted, extracellular space. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. UNIPROT Q7YS85 UNIPROT I6YIV5 PDB 1TFV PDB 2O9O PDB 2QF8 PDB 4MAV PDB 4ML4 PDB 4MPK PDB 4MTV PDB 4NSB PDB 4Q7N PDB 5Z05 PDB 5Z3S PDB 5Z4W Pfam PF00704 PROSITE PS51910 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}. GO:0005737 GO:0005783 GO:0005615 GO:0048471 GO:0030246 GO:0008061 GO:0007250 GO:0006915 GO:0005975 GO:0071356 GO:0006954 GO:0030324 GO:0045766 GO:0070374 GO:0032757 GO:0010800 GO:0051897 GO:0070555 GO:0070741 GO:0009612 GO:0034612 Unknown UniProt Sequence Analysis MGLRVAQTGFVVLVLLQSCAAYKLICYYTSWSQYREGDGSCFPDAIDPFLCTHVIYSFANISNNEIDTWEWNDVTLYDTLNTLKNRNPKLKTLLSVGGWNFGSQRFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGWRDKRHLTTLVKEMKAEFVREAQAGTEQLLLSAAVPAGKIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFRGQEDASSDRFSNADYAVSYMLRLGAPANKLVMGIPTFGKSYTLASSKTDVGAPISGPGIPGQFTKEKGILAYYEICDFLHGATTHRFRDQQVPYATKGNQWVAYDDQESVKNKARYLKNRQLAGAMVWALDLDDFRGTFCGQNLAFPLTNAIKDVLAGV 383 Q8SPQ0 Chitinase-3-like CHI3L1 9925 None SL-0198 Secreted, extracellular space. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. UNIPROT Q8SPQ0 PDB 1LJY PDB 1SYT PDB 1ZBV PDB 1ZBW PDB 1ZU8 PDB 2AOS PDB 2B31 PDB 2DSZ PDB 2DT0 PDB 2DT1 PDB 2DT2 PDB 2DT3 PDB 2O92 PDB 2OLH Pfam PF00704 PROSITE PS51910 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}. GO:0005737 GO:0005783 GO:0005615 GO:0048471 GO:0030246 GO:0008061 GO:0007250 GO:0006915 GO:0005975 GO:0071356 GO:0006954 GO:0030324 GO:0045766 GO:0070374 GO:0032757 GO:0010800 GO:0051897 GO:0070555 GO:0070741 GO:0009612 GO:0034612 Unknown UniProt Sequence Analysis MGLRASGTGFVVLVLLQSCAAYKLICYYTSWSQYREGDGSCFPDAIDPFLCTHIIYSFANISNNEIDTWEWNDVTLYDTLNTLKNRNPKLKTLLSVGGWNFGPERFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKRHLTGLVKEMKAEFAREAQAGTERLLLSAAVSAGKIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFRGQEDASSDRFSNADYAVSYMLRLGAPANKLVMGIPTFGRSFTLASSKTDVGAPISGPGIPGRFTKEKGILAYYEICDFLHGATTHRFRDQQVPYATKGNQWVAYDDQESVKNKARYLKNRQLAGAMVWALDLDDFRGTFCGQNLTFPLTSAVKDVLAEV 383 P36222 Chitinase-3-like CHI3L1 9606 None SL-0198 Secreted, extracellular space {ECO:0000269|PubMed:9492324}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. UNIPROT P36222 UNIPROT B2R7B0 UNIPROT P30923 UNIPROT Q8IVA4 UNIPROT Q96HI7 PDB 1HJV PDB 1HJW PDB 1HJX PDB 1NWR PDB 1NWS PDB 1NWT PDB 1NWU PDB 7CJ2 Pfam PF00704 PROSITE PS51910 OMIM 181500 OMIM 601525 OMIM 611960 DisGeNET 1116 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}. 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. Q14627 EBI-15187745 0.80 P27797 EBI-21846148 0.35 P11142 EBI-21846148 0.35 Q9NXR7 EBI-21865463 0.35 O94830 EBI-21866416 0.35 P08174 EBI-21866441 0.40 Q9UGC7 EBI-21866460 0.35 P17931 EBI-20260956 0.52 Q86XT9 EBI-20559520 0.40 O88786 EBI-21257604 0.35 GO:0005737 GO:0005783 GO:0070062 GO:0031012 GO:0005576 GO:0005615 GO:0048471 GO:0035580 GO:0030246 GO:0008061 GO:0005201 GO:0007250 GO:0006915 GO:0005975 GO:0051216 GO:0071356 GO:0006032 GO:0006954 GO:0030324 GO:0045766 GO:0070374 GO:0032757 GO:0010800 GO:0051897 GO:0070555 GO:0070741 GO:0009612 GO:0034612 Unknown UniProt Sequence Analysis MGVKASQTGFVVLVLLQCCSAYKLVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANISNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNFGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKQHFTTLIKEMKAEFIKEAQPGKKQLLLSAALSAGKVTIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSPLFRGQEDASPDRFSNTDYAVGYMLRLGAPASKLVMGIPTFGRSFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICDFLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKDRQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALAAT 383 Q29411 Chitinase-3-like CHI3L1 9823 None SL-0198 Secreted, extracellular space {ECO:0000269|PubMed:3086326, ECO:0000269|PubMed:7768902}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. UNIPROT Q29411 UNIPROT Q5UC99 PDB 1XHG PDB 1XRV PDB 1ZB5 PDB 1ZBC Pfam PF00704 PROSITE PS51910 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}. GO:0005737 GO:0005783 GO:0005576 GO:0005615 GO:0048471 GO:0030246 GO:0008061 GO:0007250 GO:0006915 GO:0005975 GO:0071356 GO:0006032 GO:0006954 GO:0030324 GO:0045766 GO:0070374 GO:0032757 GO:0010800 GO:0051897 GO:0070555 GO:0070741 GO:0009612 GO:0034612 Unknown UniProt Sequence Analysis MGLRVAQTGFVALVLLQSCAAYKLVCYYTSWSQYREGDGSCFPDAIDPFLCTHIIYSFANISNNEIDTWEWNDVTLYDTLNTLKNRNPNLKTLLSVGGWNFGSQRFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKRHLTTLVKEMKAEFIREAQAGTEQLLLSAAVSAGKVAIDRGYDIAQISQHLDFISLLTYDFHGAWRQTTGHHSPLFRGQEDASSDRFSNADYAVSYVLRLGAPANKLVMGIPTFGRSFTLASSKTDVGAPVSGPGIPGRFTKEKGILAYYEICDFLQGATTHRFRDQQVPYATKGNQWVGYDDQESVKNKAKYLKSRQLAGAMVWALDLDDFRGNFCGQNLRFPLTSAIKDVLAAA 383 Q5RBP6 Chitinase-3-like CHI3L1 9601 None SL-0198 Secreted, extracellular space {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. UNIPROT Q5RBP6 Pfam PF00704 PROSITE PS51910 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}. GO:0005737 GO:0005783 GO:0005615 GO:0048471 GO:0030246 GO:0008061 GO:0007250 GO:0006915 GO:0005975 GO:0071356 GO:0006954 GO:0030324 GO:0045766 GO:0070374 GO:0032757 GO:0010800 GO:0051897 GO:0070555 GO:0070741 GO:0009612 GO:0034612 Unknown UniProt Sequence Analysis MGVKAAQTGIWASQGQSIRVVGFQAQTAHRAICLLGFVVLVLLQCCSAYKLVCYYTSWSQYREGDGSCFPDAIDRFLCTHIIYSFANISNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNFGSQRFSNIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGQRDKQHFTTLIKEMRAEFIKEAQPGKKQLLLSAAVSAGKVTIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSPLFRGQEDASPDRFSNTDYAVGYMLRLEAPASKLVMGIPTFGRSFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICDFLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKERQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALAAT 410 Q9WTV1 Chitinase-3-like Chi3l1 10116 None SL-0198 Secreted, extracellular space {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. UNIPROT Q9WTV1 UNIPROT Q5BJR6 Pfam PF00704 PROSITE PS51910 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}. GO:0005737 GO:0005783 GO:0005576 GO:0005615 GO:0048471 GO:0030246 GO:0008061 GO:0007250 GO:0006915 GO:0005975 GO:0071347 GO:0071356 GO:0006032 GO:0006954 GO:0030324 GO:0045766 GO:0070374 GO:0032757 GO:0010800 GO:0051897 GO:0070555 GO:0070741 GO:0009612 GO:0034612 Unknown UniProt Sequence Analysis MTLQLPGFAVLMLLQSCSAYKLVCYYTNWSQYREGNGSCFPDALDHSLCTHIIYSFANISNNKLSTSEWNDVTLYGMLNTLKTRNPRLKTLLSVGGWSFGSERFSRIVSNAKSRKTFVQSVAPFLRTYGFDGLDLAWLYPGPKDKQHFTTLIKELKAEFTKEVQPGTEKLLLSAAVSAGKVTLDSGYDVAQIAQHLDFINLMTYDFHGTWRHTTGHHSPLFRGQQDTGPDRFSNVDYGVGYMLRLGAPTNKLVMGIPTFGKSFTLASSENQVGAPITGSGLPGRYTKEKGTLAYYEICDFLRGAEVHRILGQQVPFATKGNQWVGYDDPESVKNKVKYLKNKQLAGAMVWAVDLDDFRGSFCGHNVHFPLTNAIKEALAVA 381 Q6TMG6 Chitinase-3-like CHI3L1 9940 None SL-0198 Secreted, extracellular space {ECO:0000269|PubMed:17188513}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. UNIPROT Q6TMG6 PDB 1SR0 PDB 1ZBK PDB 1ZL1 PDB 2DPE PDB 2DSU PDB 2DSV PDB 2DSW PDB 2FDM PDB 2G41 PDB 2G8Z PDB 2PI6 PDB 5Z4V Pfam PF00704 PROSITE PS51910 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}. GO:0005737 GO:0005783 GO:0005615 GO:0048471 GO:0030246 GO:0008061 GO:0007250 GO:0006915 GO:0005975 GO:0071356 GO:0006954 GO:0030324 GO:0045766 GO:0070374 GO:0032757 GO:0010800 GO:0051897 GO:0070555 GO:0070741 GO:0009612 GO:0034612 Unknown UniProt Sequence Analysis YKLICYYTSWSQYREGDGSCFPDAIDPFLCTHVIYSFANISNNEIDTWEWNDVTLYDTLNTLKNRNPKLKTLLSVGGWNFGPERFSAIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKRHLTTLVKEMKAEFIREAQAGTEQLLLSAAVSAGKIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFAGNEDASSRFSNADYAVSYMLRLGAPANKLVMGIPTFGRSFTLASSKTDVGAPVSGPGVPGRFTKEKGILAYYEICDFLHGATTHRFRDQQVPYATKGNQWVAYDDQESVKNKARYLKNRQLAGAMVWALDLDDFRGTFCGQNLTFPLTSAVKDVLAEV 361 Q8IWX8 Calcium CHERP 9606 None SL-0198 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}. UNIPROT Q8IWX8 UNIPROT O00302 UNIPROT Q4G0Y5 UNIPROT Q8WU30 UNIPROT Q99492 Pfam PF04818 Pfam PF01585 Pfam PF01805 PROSITE PS51391 PROSITE PS50174 PROSITE PS50128 OMIM 618539 DisGeNET 10523 Involved in calcium homeostasis, growth and proliferation. {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674}. O43542 EBI-11129266 0.35 O75716 EBI-28931389 0.35 P07948 EBI-25390944 0.35 P63244 EBI-7723227 0.37 O75554 EBI-7722318 0.40 Q8K4Z5 EBI-2555364 0.40 Q13573 EBI-7950968 0.35 Q99459 EBI-7954144 0.35 P31016 EBI-7958999 0.44 Q01844 EBI-3935753 0.37 P26368 EBI-7704096 0.51 Q14562 EBI-7704116 0.51 Q8WVK2 EBI-7704173 0.51 Q70Z53 EBI-7704153 0.51 Q9NQ29 EBI-7704193 0.51 P08621 EBI-7708765 0.37 O75400 EBI-7711561 0.37 Q15427 EBI-7716078 0.37 Q01081 EBI-7719282 0.37 Q8IX12 EBI-7721515 0.37 Q86U06 EBI-7721614 0.37 Q14498 EBI-7721713 0.37 O43290 EBI-7721793 0.37 Q8NAV1 EBI-7721925 0.37 Q8TAD8 EBI-7722081 0.37 Q15287 EBI-7722240 0.37 Q9Y580 EBI-7722477 0.37 Q9NWB6 EBI-7722538 0.37 Q8N302 EBI-7722635 0.37 Q8WUA2 EBI-7722733 0.37 P31942 EBI-7722992 0.37 Q96N46 EBI-7723120 0.37 P78362 EBI-6658253 0.44 Q96SB4 EBI-6660503 0.44 O43143 EBI-9246997 0.53 Q5S007 EBI-9660150 0.44 Q15637 EBI-11297492 0.58 E9PUA5 EBI-10999661 0.35 O00159 EBI-11030803 0.35 Q9ULU4 EBI-11059997 0.35 P09450 EBI-11127973 0.35 Q15006 EBI-11130215 0.35 Q12899 EBI-11135299 0.35 P16070 EBI-11137406 0.35 Q9UJV9 EBI-11473486 0.35 Q5HY92 EBI-24281098 0.56 Q14847 EBI-24325847 0.56 Q04726 EBI-24332621 0.56 Q8IYX7 EBI-24335366 0.56 Q6P1W5 EBI-24340482 0.56 Q6UY14 EBI-24343283 0.56 O43251 EBI-24345250 0.56 Q8IUC1 EBI-24616416 0.56 Q9Y5V3 EBI-24375990 0.56 O60504 EBI-24405530 0.56 Q70EL1 EBI-25260374 0.56 Q14296 EBI-24435404 0.56 P49761 EBI-25179685 0.56 P36817 EBI-26508164 0.37 P06423 EBI-16046574 0.49 P06921 EBI-16047171 0.00 P06422 EBI-16048319 0.00 P36780 EBI-16049196 0.00 P62136 EBI-14025896 0.42 P22492 EBI-21580683 0.35 Q02809 EBI-21585081 0.35 Q96P53 EBI-21607501 0.35 P55075 EBI-21635166 0.35 P15880 EBI-21677299 0.35 P62304 EBI-21697668 0.35 P21802 EBI-21718282 0.35 Q15696 EBI-21718626 0.35 Q6NYC1 EBI-21718825 0.35 Q96I25 EBI-21719204 0.35 P62241 EBI-21741627 0.35 Q6ZNJ1 EBI-16749633 0.35 O15042 EBI-20925834 0.40 P07947 EBI-25390545 0.35 Q09161 EBI-26396507 0.35 Q53F19 EBI-26396827 0.35 P52298 EBI-26398473 0.35 P14240 EBI-26968430 0.35 Q13363 EBI-27046166 0.35 P27361 EBI-28934804 0.35 Q15208 EBI-28941263 0.35 Q96BR1 EBI-28944277 0.35 Q9Y2H9 EBI-28948459 0.35 GO:0005737 GO:0016020 GO:0005654 GO:0048471 GO:0033017 GO:0003723 GO:0044325 GO:0006874 GO:0008285 GO:0007399 GO:0070886 GO:0051209 GO:0006396 Unknown UniProt Sequence Analysis MEMPLPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKLALEQQQLICKQQTPELEPAATMPPLPQPPLAPAAPIPPAQGAPSMDELIQQSQWNLQQQEQHLLALRQEQVTAAVAHAVEQQMQKLLEETQLDMNEFDNLLQPIIDTCTKDAISAGKNWMFSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKVVVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYSSVVQPVQLAFQQQIQTLKTQHEEFVTSLAQQQQQQQQQQQQLQMPQMEAEVKATPPPPAPPPAPAPAPAIPPTTQPDDSKPPIQMPGSSEYEAPGGVQDPAAAGPRGPGPHDQIPPNKPPWFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPGWNGQRDAPWNNQPDAAWNSQFEGPWNSQHEQPPWGGGQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPHPHNFNRFPPRFMQDDFPPRHPFERPPYPHRFDYPQGDFPAEMGPPHHHPGHRMPHPGINEHPPWAGPQHPDFGPPPHGFNGQPPHMRRQGPPHINHDDPSLVPNVPYFDLPAGLMAPLVKLEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQNGLYEFFRAKMRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSNSRSSKSSGSYSRSRSRSCSRSYSRSRSRSRSRSRSSRSRSRSQSRSRSKSYSPGRRRRSRSRSPTPPSSAGLGSNSAPPIPDSRLGEENKGHQMLVKMGWSGSGGLGAKEQGIQDPIKGGDVRDKWDQYKGVGVALDDPYENYRRNKSYSFIARMKARDECK 916 Q8CGZ0 Calcium Cherp 10090 None SL-0198 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}. UNIPROT Q8CGZ0 UNIPROT Q8K291 UNIPROT Q8VCD2 Pfam PF04818 Pfam PF01585 Pfam PF01805 PROSITE PS51391 PROSITE PS50174 PROSITE PS50128 Involved in calcium homeostasis, growth and proliferation. {ECO:0000250|UniProtKB:Q8IWX8}. Q13131 EBI-2362860 0.37 Q15637 EBI-11298622 0.00 Q3UL36 EBI-26888124 0.35 GO:0005737 GO:0048471 GO:0033017 GO:0003723 GO:0044325 GO:0006874 GO:0008285 GO:0070886 GO:0051209 GO:0006396 Unknown UniProt Sequence Analysis MEMPMPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKLALEQQQLICKQQAPELEPTSAMPPLPQPPLAPTASLTPAQGTPSMDELIQQSQWSLQQQEQHLLALRQEQVTTAVAHAVEQQMQKLLEETQLDMSEFDNLLQPIIDTCTKDAISAGKNWMFSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKVVVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYSSVVQPVQLAFQQQIQSLKTQHEEFVSSLAQQQQQQQQQQQQQPQPQPQPQIQLPQMEADVKATPPPPAPPPASAPAPTIPPTTQPDDNKPPIQMPGSSEYDTSAGVQDPAAAGPRGPGPHEQIPPNKPPWFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPGWNGQRDAPWNNQPDPNWNNQFEGPWNNQHEPPPWGGAQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPHPHNFNRFPPRFMQDDFPPRHPFERPPYPHRFDYPQGDFPADMGPPHHHPGHRMPHPGINEHPPWAGPQHPDFGPPPHGFNGQPPHMRRQGPPHINHDDPSLVPNVPYFDLPAGLMAPLVKLEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQNGLYEFFRAKMRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSSSRSSKSSRSSSRSHSRSRSRSSSRSRSRSRSRSRSSRSRSRSRSRSRSKSYSPGRRRRSRSRSPTPPSAAGLGSNSAPPIPDSRLGEENKGHQMLVKMGWSGSGGLGAKEQGIQDPIKGGDVRDKWDQYKGVGVALDDPYENYRRNKSYSFIARMKARDEFSTFGTRKEEKED 936 O35744 Chitinase-like Chil3 10090 None SL-0178 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. UNIPROT O35744 UNIPROT P70201 UNIPROT Q3U462 UNIPROT Q3UV87 UNIPROT Q61201 PDB 1E9L PDB 1VF8 Pfam PF00704 PROSITE PS51910 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}. GO:0005737 GO:0031410 GO:0005576 GO:0005615 GO:0005635 GO:0048237 GO:0004563 GO:0030246 GO:0008061 GO:0019900 GO:0102148 GO:0006032 GO:0006954 GO:0000272 GO:0032722 GO:0002532 Unknown UniProt Sequence Analysis MAKLILVTGLAILLNVQLGSSYQLMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQNNEITYTHEQDLRDYEALNGLKDKNTELKTLLAIGGWKFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVKEMRKAFEEESVEKDIPRLLLTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSADLNVDSIISYWKDHGAASEKLIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDAPQEVPYAYQGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDDFSGSFCHQRHFPLTSTLKGDLNIHSASCKGPY 398 Q9N3Z3 Serine/threonine-protein chk 6239 None SL-0198 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}. UNIPROT Q9N3Z3 UNIPROT Q17375 UNIPROT Q86FM7 Pfam PF00069 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. Q9XTY9 EBI-344141 0.37 Q9N4A9 EBI-344144 0.37 GO:0005634 GO:0048471 GO:0005524 GO:0106310 GO:0004674 GO:0000077 GO:0009792 GO:0035556 GO:0033314 GO:0006468 Unknown UniProt Sequence Analysis MSAASTTSTPAAAAVAPQQPESLYRVVQTLGEGAFGEVLLIVNTKNPEVAAAMKKINIANKSKDFIDNIRKEYLLQKRVSAVGHDNVIRMIGMRNDPQFYYLFLEYADGGELFDKIEPDCGMSPVFAQFYFKQLICGLKFIHDNDVVHRDIKPENLLLTGTHVLKISDFGMATLYRNKGEERLLDLSCGTIPYAAPELCAGKKYRGPPVDVWSSGIVLIAMLTGELPWDRASDASQSYMGWISNTSLDERPWKKIDVRALCMLRKIVTDKTDKRATIEQIQADPWYQHNFGQVETPNGRPLKRARNNDENITCTQQAECSAKRRHLETPNEKSTLAERQNASFSQPTKTEDLLLTQHIDMSQTNSNLLQRMVCRMTRFCVVTDIRSTYQKVARASEHAGFGVRETDDYRLLVTWREVSMMVSLYTMGDIPDKPRVMVDFRRSRGDGIQFKKMFMDVRNRMHEWICTDGNNWLANLGYVPRNPQIVNGGGVNVEHSASSINVDV 503 O43633 Charged CHMP2A 9606 None SL-0178 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}. UNIPROT O43633 UNIPROT B2R4W6 UNIPROT Q3ZTT0 Pfam PF03357 OMIM 610893 DisGeNET 27243 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}. P40818 EBI-8601078 0.44 Q70EL1 EBI-8601283 0.44 P61457 EBI-2692786 0.00 Q16254 EBI-3916764 0.37 P10600 EBI-3918280 0.37 P19320 EBI-6189915 0.35 Q8NF50 EBI-10184717 0.56 Q9ERU9 EBI-10999306 0.35 P35278 EBI-11012136 0.35 Q8BT07 EBI-11014656 0.35 Q92734 EBI-11029015 0.35 Q9JLQ0 EBI-11033702 0.35 O75787 EBI-11037152 0.35 P51148 EBI-11046231 0.35 P51149 EBI-11050319 0.35 Q9D8B3 EBI-11052854 0.35 Q9WUM4 EBI-11065690 0.35 Q9QYY8 EBI-11090422 0.35 Q6PB44 EBI-11097749 0.35 P46467 EBI-11115954 0.35 P61019 EBI-11127113 0.35 Q9H444 EBI-11148324 0.59 O35730 EBI-11162936 0.35 Q6P5F9 EBI-11603310 0.35 Q9Y3E7 EBI-11509057 0.67 Q9UN37 EBI-11510032 0.37 O43633 EBI-11510376 0.37 Q13144 EBI-11510746 0.37 Q8WV92 EBI-11510750 0.73 O94818 EBI-11511236 0.37 O95630 EBI-11511994 0.55 P62491 EBI-11512003 0.37 Q9Y5L0 EBI-11512013 0.37 Q8TEL6 EBI-11512033 0.37 Q6DKK2 EBI-11512041 0.37 Q92882 EBI-21519358 0.35 Q9NPC8 EBI-21617697 0.35 O00161 EBI-21756983 0.40 Q8IWF9 EBI-21757002 0.35 Q9UBP0 EBI-21757061 0.35 Q9UPQ4 EBI-21888198 0.35 Q9NZZ3 EBI-21888198 0.35 Q9NP79 EBI-21888198 0.35 Q16698 EBI-21888198 0.35 P36957 EBI-20305285 0.35 O14979 EBI-20937156 0.40 P0DTD2 EBI-25491493 0.53 P42858 EBI-25958665 0.56 Q8N488 EBI-27110926 0.35 GO:1904930 GO:0000421 GO:0005829 GO:0000815 GO:0070062 GO:0000776 GO:0005828 GO:0005765 GO:0016020 GO:0030117 GO:0030496 GO:0005771 GO:0032585 GO:0005635 GO:0005643 GO:0005886 GO:0031210 GO:0019904 GO:0097352 GO:0006914 GO:0032509 GO:1904903 GO:0045184 GO:0010458 GO:1902774 GO:0045324 GO:0016236 GO:0090148 GO:0010324 GO:0061952 GO:0007080 GO:0036258 GO:0071985 GO:0061763 GO:0060548 GO:1903723 GO:0031468 GO:0006997 GO:0001778 GO:1903543 GO:0051260 GO:0051258 GO:0015031 GO:0010824 GO:1901673 GO:0043162 GO:0051469 GO:0046761 GO:0039702 GO:0019076 Peripheral UniProt Sequence Analysis MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEAAASALADADADLEERLKNLRRD 222 Q9DB34 Charged Chmp2a 10090 None SL-0178 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}. UNIPROT Q9DB34 Pfam PF03357 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}. P10909 EBI-11115096 0.35 P68510 EBI-8586548 0.35 Q9Y3E7 EBI-11090637 0.35 Q9HD42 EBI-11090637 0.35 Q9H444 EBI-11090637 0.35 O60684 EBI-11115096 0.35 Q5T8P6 EBI-11115096 0.35 O00255 EBI-11115096 0.35 P48681 EBI-11115096 0.35 Q6NZM9 EBI-26473528 0.35 GO:1904930 GO:0000421 GO:0000785 GO:0005829 GO:0000815 GO:0000776 GO:0005828 GO:0005765 GO:0030117 GO:0030496 GO:0005771 GO:0032585 GO:0005635 GO:0005643 GO:0005886 GO:0031210 GO:0019904 GO:0097352 GO:0006914 GO:0032509 GO:0045184 GO:0010458 GO:1902774 GO:0045324 GO:0090148 GO:0010324 GO:0061952 GO:0007080 GO:0036258 GO:0071985 GO:0061763 GO:0060548 GO:1903723 GO:0031468 GO:0006997 GO:0001778 GO:1903543 GO:0051260 GO:0051258 GO:0015031 GO:0010824 GO:1901673 GO:0043162 GO:0051469 GO:0046761 GO:0039702 GO:0019076 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:O43633} MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEATASALADADADLEERLKNLRRD 222 Q9H444 Charged CHMP4B 9606 None SL-0178 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}. UNIPROT Q9H444 UNIPROT E1P5N4 UNIPROT Q53ZD6 PDB 3C3Q PDB 3UM3 PDB 4ABM PDB 5MK2 Pfam PF03357 OMIM 605387 OMIM 610897 DisGeNET 128866 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}. 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. O43633 EBI-11148324 0.59 P02545 EBI-16796036 0.27 P19525 EBI-11151252 0.35 P52948 EBI-11148324 0.35 P53990 EBI-11148324 0.35 P63279 EBI-757456 0.55 Q8WUX9 EBI-11513083 0.54 Q9DB34 EBI-11090637 0.35 Q9ERU9 EBI-10999306 0.35 O95630 EBI-2118145 0.55 P40818 EBI-8601147 0.44 Q70EL1 EBI-8601371 0.44 Q9CQ10 EBI-2563199 0.40 P10644 EBI-2691105 0.00 P38606 EBI-4324466 0.53 Q9H3S7 EBI-7178748 0.66 P19320 EBI-6189915 0.35 P42858 EBI-9052823 0.67 O14862 EBI-9995694 0.35 P36895 EBI-11008521 0.35 Q8BT07 EBI-11014656 0.35 Q9QWF0 EBI-11015136 0.35 A2AUY4 EBI-11016281 0.35 P60122 EBI-11023741 0.35 Q92734 EBI-11029015 0.35 Q96H55 EBI-11031416 0.35 Q9JLQ0 EBI-11033702 0.35 P21333 EBI-11038784 0.35 P60710 EBI-11045267 0.35 P51148 EBI-11046231 0.35 P51149 EBI-11050319 0.35 Q9JHJ0 EBI-11063313 0.35 P58771 EBI-11063826 0.35 Q9WUM4 EBI-11065690 0.35 Q6ZQ29 EBI-11075869 0.35 Q16643 EBI-11080402 0.35 Q00610 EBI-11082478 0.35 P55072 EBI-11084314 0.35 Q8R5L1 EBI-11085290 0.35 Q9UER7 EBI-11088574 0.35 Q9QYY8 EBI-11090422 0.35 Q61187 EBI-11090666 0.35 Q6PB44 EBI-11097749 0.35 P46467 EBI-11115954 0.35 P47755 EBI-11117728 0.35 Q9UQE7 EBI-11147323 0.35 Q9Y3E7 EBI-11148324 0.69 Q6P1N0 EBI-11148324 0.55 Q5T0F9 EBI-11148324 0.35 Q99816 EBI-11148324 0.35 Q96SN8 EBI-11148324 0.35 O95714 EBI-11148324 0.35 Q6ZS30 EBI-11148324 0.35 O60684 EBI-11148324 0.35 Q13395 EBI-11148324 0.35 Q02878 EBI-11148324 0.35 Q93050 EBI-11148324 0.35 P11717 EBI-11148324 0.35 P51608 EBI-11148324 0.35 Q9Y2X9 EBI-11148324 0.35 Q8N6N3 EBI-11148324 0.35 H0Y9L7 EBI-11148324 0.35 Q9ULT0 EBI-11148324 0.35 Q641Q3 EBI-11148324 0.35 Q9NZZ3 EBI-11148324 0.55 P21281 EBI-11148324 0.35 P49711 EBI-11148324 0.35 O60447 EBI-11148324 0.35 Q5SVZ6 EBI-11148324 0.35 Q86Y56 EBI-11148324 0.35 Q8WV92 EBI-11148324 0.35 Q96K19 EBI-11148324 0.35 P26641 EBI-11148324 0.35 Q9Y4G6 EBI-11148324 0.35 Q96SU4 EBI-11148324 0.35 Q6NUK1 EBI-11148324 0.35 E9PSI1 EBI-11148324 0.35 Q9NVX2 EBI-11148324 0.35 Q7LBR1 EBI-11151252 0.55 Q9H773 EBI-11151252 0.35 Q9UKT4 EBI-11151252 0.35 Q8WUM4 EBI-11151252 0.86 Q9Y6W3 EBI-11151252 0.35 Q9UQN3 EBI-11151252 0.59 Q14254 EBI-11151252 0.35 Q9Y2B5 EBI-11151252 0.35 P27824 EBI-11151252 0.35 Q10589 EBI-11151252 0.35 Q9NQS3 EBI-11151252 0.35 Q5T3F8 EBI-11151252 0.35 Q96BY9 EBI-11151252 0.35 Q9UBP0 EBI-11151252 0.35 Q9HD42 EBI-11151252 0.35 P61421 EBI-11151252 0.35 Q96EY5 EBI-11151252 0.35 Q16739 EBI-11151252 0.35 E5RHG8 EBI-11151252 0.35 O75955 EBI-11151252 0.35 Q7LBC6 EBI-11151252 0.35 Q96QD8 EBI-11151252 0.35 P36543 EBI-11151252 0.35 Q9Y3E0 EBI-11161387 0.35 Q9BY43 EBI-24635622 0.56 Q9H444 EBI-11510097 0.64 Q96FZ7 EBI-11510183 0.37 Q9UN37 EBI-11510230 0.37 Q96CF2 EBI-11510324 0.37 O75928 EBI-11510785 0.37 Q06265 EBI-11510789 0.37 Q9H2X6 EBI-11510793 0.37 Q12873 EBI-11511252 0.37 O60664 EBI-24515780 0.56 Q7KZS0 EBI-25218607 0.56 Q6IQ23 EBI-16398399 0.35 Q9WU78 EBI-15788562 0.52 Q5VW32 EBI-15979635 0.61 Q96H96 EBI-20304156 0.35 Q7KZN9 EBI-20304305 0.35 P36957 EBI-20305285 0.35 P35610 EBI-20307233 0.35 P21796 EBI-20307902 0.35 P05067 EBI-20821761 0.35 P62807 EBI-25471348 0.27 P55040 EBI-21260056 0.35 P14316 EBI-21260627 0.35 P54920 EBI-21261831 0.35 P03372 EBI-21301141 0.35 F1PAA9 EBI-27079701 0.27 P35226 EBI-27108918 0.35 Q8TEA7 EBI-28943849 0.35 P48431 EBI-29373058 0.35 P31314 EBI-29607649 0.35 P22455 EBI-32722168 0.27 P07949 EBI-32725031 0.27 GO:1904930 GO:0000421 GO:0005737 GO:0009898 GO:0005829 GO:0005768 GO:0000815 GO:0070062 GO:0000776 GO:0005828 GO:0005765 GO:0030117 GO:0030496 GO:0005771 GO:0032585 GO:0005635 GO:0005643 GO:0005634 GO:0005886 GO:0031982 GO:0045296 GO:0042802 GO:0042803 GO:0097352 GO:0006914 GO:0010458 GO:1902774 GO:0032511 GO:0016236 GO:0036438 GO:0090148 GO:0061952 GO:0000281 GO:0007080 GO:0036258 GO:0071985 GO:0061763 GO:1902902 GO:0060548 GO:1901215 GO:0031468 GO:0006997 GO:0001778 GO:0006620 GO:0051258 GO:0010824 GO:1901673 GO:0043162 GO:0090611 GO:0006900 GO:0051469 GO:0046755 GO:0046761 GO:0039702 Peripheral UniProt Curator Inference {ECO:0000305} MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSIALPSKPAKKKEEEDDDMKELENWAGSM 224 Q9D8B3 Charged Chmp4b 10090 None SL-0178 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}. UNIPROT Q9D8B3 UNIPROT A2AVM1 UNIPROT Q3TXM7 UNIPROT Q91VM7 UNIPROT Q922P1 Pfam PF03357 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}. O43633 EBI-11052854 0.35 P53990 EBI-11052854 0.35 Q07065 EBI-11052854 0.35 Q14244 EBI-11052854 0.35 Q14764 EBI-11052854 0.35 Q6P5Z2 EBI-11052854 0.35 Q6P9B9 EBI-11113387 0.35 P68510 EBI-8586548 0.35 Q7LBR1 EBI-11052854 0.35 Q9Y3E7 EBI-11052854 0.35 Q6P1N0 EBI-11052854 0.35 Q53TN4 EBI-11052854 0.35 Q10589 EBI-11052854 0.35 Q9NZZ3 EBI-11052854 0.35 Q9BY43 EBI-11052854 0.35 Q9UI12 EBI-11052854 0.35 P28288 EBI-11052854 0.35 Q9Y5K6 EBI-11052854 0.35 O75477 EBI-11052854 0.35 Q9UJZ1 EBI-11052854 0.35 Q9UNQ0 EBI-11052854 0.35 Q9UHR4 EBI-11052854 0.35 P21281 EBI-11052854 0.35 Q9NRL2 EBI-11052854 0.35 Q9H0H5 EBI-11052854 0.35 O00560 EBI-11052854 0.35 Q969G5 EBI-11052854 0.35 Q8WUM4 EBI-11052854 0.56 P02786 EBI-11052854 0.35 P14923 EBI-11052854 0.35 Q13111 EBI-11052854 0.35 Q96NT0 EBI-11052854 0.35 Q4KMQ1 EBI-11052854 0.35 Q9UIF8 EBI-11052854 0.35 O75351 EBI-11052854 0.35 Q9HD42 EBI-11052854 0.35 P08754 EBI-11052854 0.35 Q9UKS6 EBI-11052854 0.35 P40818 EBI-11052854 0.35 Q9UBH6 EBI-11052854 0.35 P61421 EBI-11052854 0.35 Q96EY5 EBI-11052854 0.35 Q86UP2 EBI-11052854 0.35 Q14126 EBI-11052854 0.35 Q15904 EBI-11052854 0.35 B4E2V5 EBI-11052854 0.35 Q6NZI2 EBI-11052854 0.35 P36543 EBI-11052854 0.35 Q9UQN3 EBI-11052854 0.35 Q9H3S7 EBI-11052854 0.35 O75955 EBI-11052854 0.35 Q03135 EBI-11052854 0.35 P35610 EBI-11052854 0.35 Q8WV92 EBI-11052854 0.35 P14384 EBI-11052854 0.35 Q96QD8 EBI-11052854 0.35 Q99623 EBI-11052854 0.35 Q5T0F9 EBI-11052854 0.35 E9PSI1 EBI-11052854 0.35 Q13112 EBI-11052854 0.35 Q9ULH0 EBI-11052854 0.35 Q8NFJ5 EBI-11052854 0.35 Q14254 EBI-11052854 0.35 Q96CM3 EBI-11113387 0.35 Q86TX2 EBI-11113387 0.35 Q9Y573 EBI-11113387 0.35 J3QR07 EBI-11113387 0.35 Q96QC4 EBI-11113387 0.35 Q13838 EBI-11113387 0.35 Q5VTR2 EBI-11113387 0.35 Q9BTV6 EBI-11113387 0.35 Q16222 EBI-11113387 0.35 Q7Z6E9 EBI-11113387 0.35 A6H8Y1 EBI-11113387 0.35 Q9H3P2 EBI-11113387 0.35 Q8NI27 EBI-11113387 0.35 Q9NU22 EBI-11113387 0.35 H0YBU6 EBI-11113387 0.35 G3V4T2 EBI-11113387 0.35 Q7Z2Z2 EBI-11113387 0.35 Q5SYE7 EBI-11113387 0.35 O75340 EBI-11113387 0.35 Q9BY77 EBI-11113387 0.35 Q5VST9 EBI-11113387 0.35 Q6UUV7 EBI-11113387 0.35 Q8TEU7 EBI-11113387 0.35 Q9D8B3 EBI-15613912 0.40 Q8VI24 EBI-26885104 0.35 GO:1904930 GO:0000421 GO:0005737 GO:0009898 GO:0005829 GO:0005768 GO:0000815 GO:0098978 GO:0000776 GO:0005828 GO:0005765 GO:0016020 GO:0030117 GO:0030496 GO:0005771 GO:0032585 GO:0005635 GO:0005643 GO:0005634 GO:0005886 GO:0014069 GO:0031982 GO:0042802 GO:0042803 GO:0097352 GO:0006914 GO:0010458 GO:1902774 GO:0032511 GO:0036438 GO:0090148 GO:0061952 GO:0000281 GO:0007080 GO:0036258 GO:0071985 GO:0061763 GO:1902902 GO:0060548 GO:1901215 GO:0031468 GO:0006997 GO:0001778 GO:0006620 GO:0051258 GO:0010506 GO:0010824 GO:1901673 GO:0043162 GO:0090611 GO:0006900 GO:0051469 GO:0046755 GO:0046761 GO:0039702 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q9H444} MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSVALPSKPAKKKEEEDDDMKELENWAGSM 224 Q5ZJB7 Charged CHMP7 9031 None SL-0178 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}. UNIPROT Q5ZJB7 Pfam PF03357 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}. GO:0000815 GO:0005771 GO:0005635 GO:0010458 GO:0045324 GO:0032511 GO:0031468 GO:0015031 GO:0006900 Unknown UniProt Sequence Analysis MCSPGRAPPGPAPAGDLPPEWETDDERMAFLFSAFKQSREVNSTEWDSKMAFWVGLVLARGRRRGVVRTCLRELQNGFERRGSVPLGLGTVLRELLRRGKMQRESDFMASVDSSWISWGVGVFILKPLKWTLSSVLGDSKVPEEEEVLIYVELLQEKAEEVYRLYQNSVLSSHPVVALSELRSLCAGVCPDERTFYLLLLQLQKEKKVTILEQNGEKIVKFARGLHAKVSPMNDVDIGVYQLMQSEQLLSQKVESLSQEAEKCKDDARSACRAGKKQLALRCLKSKRRTERRIEELHSKLDAVQGILDRIYASQTDQMVFNAYQAGVGALKLSMKDVTVEKAENLVDQIQELCDTQDEVAQTLAGAGVNGLEMDSEELEKELDSLLQDSAKEPVHLHPVPQKDSGFAGAISDAELEAELEKLSVCDGDLAQKTPSASSEPQTALGLNL 448 Q6PBQ2 Charged chmp7 7955 None SL-0178 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}. UNIPROT Q6PBQ2 UNIPROT Q6NYA6 Pfam PF03357 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}. GO:0000815 GO:0005771 GO:0005635 GO:0010458 GO:0045324 GO:0032511 GO:0031468 GO:0015031 GO:0006900 Unknown UniProt Sequence Analysis MSVSVEKRSAWFPPDWDDDERMSFLFSAFKENRDVDCTDWDGKIDFWSPLIIEHCRRCGSVCVNLQDLNENFRRKGSVPLGLSTVIQSMIRSGKVQKESDFAANVDSGWLSWGVGLLLVRPLKWTLSALLGSGRVPLEESFVVIELVKEKAAELLAAYRGSALSARSLLSFQELRSLSSHICPDESTLCMALLQLQREKHVTVSLHEGEKLVKFSQAGQGRVSPVSEVDLGIYQLQCSEKLLEERVEALGHEAEKCKQQAKSLLKEGKKSQALRCLRGSKRVEKKADRLFAQLETVKGILDRIANSQTDRLVMQAYQAGVAALRISLKGVTVERAENLVDQIQELCDTQDEVNQTLASGAPDAGEDSEDLEEELKSLMEKSVPENDLFPAVPTHPITPPRKTDLPDAAFVQFLPSVPNPGMNITDEELDRELRRLTVSDKGLPRESVSPQRRLEPAQ 457 Q8WUX9 Charged CHMP7 9606 None SL-0178 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}. UNIPROT Q8WUX9 UNIPROT B2RDT3 UNIPROT B4DKJ6 UNIPROT D3DSS1 UNIPROT Q8NDM1 UNIPROT Q9BT50 Pfam PF03357 OMIM 611130 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}. P01112 EBI-25869447 0.66 P62826 EBI-25890253 0.56 Q15102 EBI-757165 0.55 Q96GX1 EBI-11394923 0.27 Q6P5F9 EBI-11603310 0.35 Q9H444 EBI-11513083 0.54 Q9BY43 EBI-11513112 0.37 Q96CF2 EBI-11513134 0.37 P27824 EBI-16788621 0.27 Q9BYV6 EBI-22022524 0.00 P55212 EBI-25835897 0.56 P06307 EBI-25837149 0.56 P28329 EBI-25838258 0.56 G5E9A7 EBI-25843392 0.56 P22607 EBI-25855156 0.56 Q0VDC6 EBI-25856156 0.56 Q14957 EBI-25863073 0.56 P06396 EBI-25864746 0.56 P54652 EBI-25870109 0.56 P13473 EBI-25874252 0.56 D3DTS7 EBI-25883702 0.56 O14645 EBI-25903256 0.56 O14901 EBI-25906055 0.56 Q9BVL2 EBI-25908519 0.56 Q9UMX0 EBI-25921437 0.56 Q7Z699 EBI-25933071 0.56 P01116 EBI-27041844 0.27 P01111 EBI-27042293 0.27 P07949 EBI-32725031 0.27 GO:1904930 GO:0000421 GO:0005829 GO:0000815 GO:0000776 GO:0005828 GO:0005765 GO:0030496 GO:0005771 GO:0032585 GO:0005635 GO:0005643 GO:0005654 GO:0005886 GO:0097352 GO:0006914 GO:1904903 GO:0010458 GO:1902774 GO:0045324 GO:0032511 GO:0090148 GO:0061952 GO:0007080 GO:0036258 GO:0071985 GO:0061763 GO:0060548 GO:0031468 GO:0006997 GO:0001778 GO:0071168 GO:0015031 GO:1901673 GO:0043162 GO:0006900 GO:0051469 GO:0046761 GO:0039702 Unknown UniProt Sequence Analysis MWSPEREAEAPAGGDPAGLLPPEWEEDEERMSFLFSAFKRSREVNSTDWDSKMGFWAPLVLSHSRRQGVVRLRLRDLQEAFQRKGSVPLGLATVLQDLLRRGELQRESDFMASVDSSWISWGVGVFLLKPLKWTLSNMLGDNKVPAEEVLVAVELLKEKAEEVYRLYQNSPLSSHPVVALSELSTLCANSCPDERTFYLVLLQLQKEKRVTVLEQNGEKIVKFARGPRAKVSPVNDVDVGVYQLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKEPLDLPDNPRNRHFTNSVPNPRISDAELEAELEKLSLSEGGLVPSSKSPKRQLEPTLKPL 453 Q8R1T1 Charged Chmp7 10090 None SL-0178 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}. UNIPROT Q8R1T1 UNIPROT Q8CFW4 Pfam PF03357 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}. GO:1904930 GO:0000421 GO:0000785 GO:0005829 GO:0000815 GO:0000776 GO:0005828 GO:0005765 GO:0030496 GO:0005771 GO:0032585 GO:0005635 GO:0005643 GO:0005654 GO:0005886 GO:0097352 GO:0006914 GO:0010458 GO:1902774 GO:0045324 GO:0032511 GO:0090148 GO:0061952 GO:0007080 GO:0036258 GO:0071985 GO:0061763 GO:0060548 GO:0031468 GO:0006997 GO:0001778 GO:0071168 GO:0015031 GO:1901673 GO:0043162 GO:0006900 GO:0051469 GO:0046761 GO:0039702 Unknown UniProt Sequence Analysis MWSPEREAQAPTGGDPAGLLPPEWEEDEERMSFLFSAFKRSREVNSTDWDSKMGFWAPLVLSHSRRQGVVRLRLRDLQEAFQRKGSVPLGLATVLQDLLRRGELQRESDFMASVDSSWISWGVGVFLLKPLKWTLSNMLGDHKVPAEEVLVAVELLKEKAEEVYRLYQNSPLSSHPVVALSELSALCANSCPDERTFYLVLLQLQKEKRVTVLEQNGEKIVKFARGPHAKVSPVNDVDVGVYQLMQSEQLLSRKVESLSQESERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTTEPLSLLETPQETTLYTNSVPKPRILDAELEAELEKLSLSEGGLIPSSKSPKRQLEPTL 451 Q5R812 Charged CHMP7 9601 None SL-0178 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}. UNIPROT Q5R812 Pfam PF03357 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}. GO:1904930 GO:0000815 GO:0000776 GO:0005828 GO:0005765 GO:0030496 GO:0032585 GO:0005635 GO:0005643 GO:0097352 GO:0010458 GO:1902774 GO:0045324 GO:0061952 GO:0007080 GO:0071985 GO:0060548 GO:0031468 GO:0001778 GO:0015031 GO:1901673 GO:0043162 GO:0046761 GO:0039702 Unknown UniProt Sequence Analysis MWSPEREAEAPAGGDPAGLLPPEWEEDEERMSFLFSAFKRSREVNSTDWDSKMGFWAPLVLSHSRRQGVVRLRLRDLQEAFQRKGSVPLGLATVLQDLLRRGELQRESDFMASVDSSWISWGVGVFLLKPLKWTLSNMLGDNKVPAEEVLVAVELLKEKAEEVYRLYQSSPLSSHPVVALSELSTLCANSCPDERTFYLVLLQLQKEKRVTVLEQNGEKIVKFARGPHAKVSPVNDVDVGVYQLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKEPLDLPDNPRDRHFTNSVPNPRISDAGLEAELEKLSLSEGGLVPSGKSPKRQLEPTLKPL 453 Q7T0X5 Charged chmp7 8355 None SL-0178 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}. UNIPROT Q7T0X5 Pfam PF03357 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}. Q6P5F9 EBI-11606853 0.35 GO:0000815 GO:0005635 GO:0010458 GO:0045324 GO:0031468 GO:0015031 Unknown UniProt Sequence Analysis MAPLSCNPPEWEDDERMSFLFSAFKRTRDVNTCDWDGKMKFWIPLILTHARAQGLLSITLSQLENDFRRKGCAPMGLRTVIQEMIRQGTLRKETDFVSGVSSGWLSWGMRQLVIRPLRWTIGTMLGSQVGPDEPLVIPEVIKERAALVLQRYQSSTFRSFPLLCEEEVHTLCAEICPNPSALNLVLLQLQGDKKICVLERAGQKLVKFVRVSVGQVEPISESDLGIYQLQQGEKLLSERLQSAGEESNRLTEEARTYNRAGNKNQALRCLRKRKLVERRITELQNKQDNIQGILERISAAETDRKVVSAYQMGVSALKQALKDVTLEKAESIVDQIQEYCDLQDDLSQTLSSVTDADVDSDDLERELNEILQNEEMIIDLPDVPSGPVIISPKRPTEWKMDQAAHSPADGSFLRSVPEPMLQ 422 Q5FW14 Charged chmp7 8364 None SL-0178 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}. UNIPROT Q5FW14 Pfam PF03357 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}. GO:0000815 GO:0005771 GO:0005635 GO:0010458 GO:0045324 GO:0032511 GO:0031468 GO:0015031 GO:0006900 Unknown UniProt Sequence Analysis MAALSCYPPEWDDDERMSFLFSAFKQTRDVNTSDWDGKMKFWIPLILKHARAQGLLSISLSQLERDFRRKGFAPLGLRIVIQEMMRQGTLRKESDYVSNVSSGWLSWGMRQLVIRPLRWTIGTVLGSQMGPDEPLVIPEIIKERAALVLQRYQSSPLRALPLLSEEEVRTLCAEICPNPSALNLVLLQLQGDKKICVLERAGKKLVKFVRVSVGQVDPISESDLGIYELQQSEKLLSERLQSAGEESDRLTEEARTYNRAGNKHQALRCLRKRKLLERRITELQNKQDTVQGILERIAAAETDRKVVSAYQMGVSALKLALKDVTMEKAESIVDQIQEYCDLQDDLSQTLASVSDADIDSEDLEKELNDILQNKEMIVDLPDVPSGPVVISPQRPTEWETDQDIDSEDLEKELNDILQKEEMIVDLPDVPSGPVVISPQRPTEWKTDQASRSPADGSFSRSVPEPVLQ 468 Q96LT7 Guanine C9orf72 9606 None SL-0178 SL-0182 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}. UNIPROT Q96LT7 UNIPROT A8K5W0 UNIPROT D3DRK6 UNIPROT G8I0B6 UNIPROT Q6NUS9 PDB 6LT0 PDB 6V4U PDB 7MGE PDB 7O2W Pfam PF15019 PROSITE PS51835 OMIM 105550 OMIM 614260 DisGeNET 203228 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}. 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}. O08788 EBI-26613562 0.35 P04626 EBI-20938756 0.35 Q8TDY2 EBI-16693641 0.71 P49770 EBI-8634732 0.67 Q96SB4 EBI-6660776 0.44 O43186 EBI-10290948 0.56 Q04864 EBI-10290958 0.56 Q13287 EBI-10290968 0.56 Q53XC2 EBI-10290978 0.56 Q9BPX4 EBI-10290998 0.56 Q61539 EBI-11143365 0.35 Q8TEV9 EBI-11773551 0.81 P38432 EBI-24341833 0.56 Q9H8Y1 EBI-24620575 0.60 Q9NP66 EBI-23775639 0.56 Q86UV6 EBI-24752111 0.56 O75817 EBI-23856758 0.56 Q17R54 EBI-24600914 0.56 O75385 EBI-16693788 0.67 O75143 EBI-16693805 0.69 P62820 EBI-16697556 0.58 P27824 EBI-16788621 0.27 Q96I36 EBI-16791250 0.27 Q9HBL7 EBI-16797780 0.27 P51151 EBI-16798325 0.27 O43493 EBI-16800265 0.27 Q15388 EBI-16801791 0.27 Q9NS69 EBI-16802054 0.27 Q9HAD4 EBI-26618111 0.56 Q86VY4 EBI-20938756 0.35 Q8WXF1 EBI-20938756 0.35 Q9BSF8 EBI-20938756 0.35 O15015 EBI-20938756 0.35 Q13610 EBI-20938756 0.35 P20290 EBI-20938756 0.35 O15235 EBI-20938756 0.35 Q9P086 EBI-20938756 0.35 P62891 EBI-20938756 0.35 O75935 EBI-20938756 0.35 P62314 EBI-20938756 0.35 Q9BWH6 EBI-20938756 0.35 Q9H6T0 EBI-20938756 0.35 P26038 EBI-20938756 0.35 Q14137 EBI-20938756 0.35 P63208 EBI-20938756 0.35 Q9BPZ7 EBI-20938756 0.35 Q9Y4Y9 EBI-20938756 0.35 P31942 EBI-20938756 0.35 O14647 EBI-20938756 0.35 Q06455 EBI-20938756 0.35 P62273 EBI-20938756 0.35 Q8N184 EBI-20938756 0.35 Q96RE9 EBI-20938756 0.35 Q9P0L1 EBI-20938756 0.35 P09496 EBI-20938756 0.35 P05388 EBI-20938756 0.35 P62987 EBI-20938756 0.35 P35637 EBI-20938756 0.35 Q9Y446 EBI-20938756 0.35 Q8IWZ3 EBI-20938756 0.35 Q9Y2P7 EBI-20938756 0.35 Q9Z2X2 EBI-26613562 0.35 Q5EG47 EBI-26613562 0.35 O08547 EBI-26613562 0.35 Q6P8X1 EBI-26613562 0.35 P46467 EBI-26613562 0.35 Q6PA06 EBI-26613562 0.35 Q8BGH2 EBI-26613562 0.35 Q8R5A6 EBI-26613562 0.35 Q91YL2 EBI-26613562 0.35 Q9R1P0 EBI-26613562 0.35 O35963 EBI-26613562 0.35 Q9ESK9 EBI-26613562 0.35 Q8BHC1 EBI-26613562 0.35 Q921F2 EBI-26613562 0.35 Q64337 EBI-26613562 0.35 A2AH22 EBI-26613562 0.35 Q9JKF1 EBI-26613562 0.35 P07901 EBI-26613562 0.35 Q9JHU4 EBI-26613562 0.35 P63017 EBI-26613562 0.35 Q7TMY8 EBI-26613562 0.35 Q8BND3 EBI-26613562 0.35 Q9JIS5 EBI-26613562 0.35 Q8CFD4 EBI-26613562 0.35 Q9WTV7 EBI-26613562 0.35 Q99KJ8 EBI-26613562 0.35 O35226 EBI-26613562 0.35 P35279 EBI-26613562 0.35 Q9WUN2 EBI-26613562 0.35 Q9D0I4 EBI-26613562 0.35 Q504M8 EBI-26613562 0.35 Q9CX56 EBI-26613562 0.35 Q920Q4 EBI-26613562 0.35 Q8K4Q0 EBI-26613562 0.35 P55258 EBI-26613562 0.35 Q9WUD1 EBI-26613562 0.35 P46460 EBI-26613562 0.35 Q3UDP0 EBI-26613562 0.35 Q3UMB5 EBI-26613562 0.35 Q9JLV1 EBI-26613562 0.35 A2AN08 EBI-26613562 0.35 P52332 EBI-26613562 0.35 A2AKX3 EBI-26613562 0.35 P61006 EBI-26618111 0.44 Q96DA2 EBI-26618130 0.44 Q9UHD2 EBI-26618650 0.44 Q86YD7 EBI-28997307 0.35 P29322 EBI-32721175 0.27 P07949 EBI-32725031 0.27 GO:0070161 GO:0005776 GO:0044295 GO:0005737 GO:0010494 GO:0005829 GO:0030425 GO:0005768 GO:0005615 GO:0090543 GO:0032045 GO:0043231 GO:0005764 GO:0044304 GO:0031965 GO:0005634 GO:0000932 GO:0043204 GO:0098794 GO:0098793 GO:0005085 GO:0031267 GO:0006914 GO:0048675 GO:0006897 GO:1902774 GO:0045920 GO:1904425 GO:0050777 GO:0001933 GO:0043547 GO:0016239 GO:0110053 GO:2000785 GO:0010506 GO:0032880 GO:1903432 GO:0034063 Peripheral UniProt Curator Inference {ECO:0000305} MSTLCPPPSPAVAKTEIALSGKSPLLAATFAYWDNILGPRVRHIWAPKTEQVLLSDGEITFLANHTLNGEILRNAESGAIDVKFFVLSEKGVIIVSLIFDGNWNGDRSTYGLSIILPQTELSFYLPLHRVCVDRLTHIIRKGRIWMHKERQENVQKIILEGTERMEDQGQSIIPMLTGEVIPVMELLSSMKSHSVPEEIDIADTVLNDDDIGDSCHEGFLLNAISSHLQTCGCSVVVGSSAEKVNKIVRTLCLFLTPAERKCSRLCEAESSFKYESGLFVQGLLKDSTGSFVLPFRQVMYAPYPTTHIDVDVNTVKQMPPCHEHIYNQRRYMRSELTAFWRATSEEDMAQDTIIYTDESFTPDLNIFQDVLHRDTLVKAFLDQVFQLKPGLSLRSTFLAQFLLVLHRKALTLIKYIEDDTQKGKKPFKSLRNLKIDLDLTAEGDLNIIMALAEKIKPGLHSFIFGRPFYTSVQERDVLMTF 481 Q17QE5 Calcium CIB1 9913 None SL-0198 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}. UNIPROT Q17QE5 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0016324 GO:0030424 GO:0071944 GO:0005813 GO:0005737 GO:0032433 GO:0030426 GO:0030027 GO:0043005 GO:0043025 GO:0005634 GO:0043204 GO:0048471 GO:0005886 GO:0032587 GO:0042383 GO:0005509 GO:0000287 GO:0043495 GO:0001525 GO:0006915 GO:0007155 GO:0051301 GO:0071363 GO:1990090 GO:0071356 GO:0031122 GO:0007113 GO:0043066 GO:0008285 GO:0045653 GO:0007026 GO:0010977 GO:0051898 GO:0001933 GO:0030220 GO:0070886 GO:0043085 GO:0033630 GO:0030307 GO:0030335 GO:0090050 GO:0008284 GO:0001954 GO:0070374 GO:2000256 GO:0051092 GO:1903078 GO:0001934 GO:0071902 GO:0090314 GO:1900026 GO:0051302 GO:0042127 GO:0002931 GO:0007286 GO:0038163 Lipid-Anchored UniProt By Similarity {ECO:0000250} MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEHRSVEESLQARVSLEQILSLPELKANPFKERICKVFSTSPSRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSQLVNCLTGESEDTRLSASEMKQLIDNILEESDIDRDGTINLSEFQHVISRSPDFASSFKIVL 191 Q99828 Calcium CIB1 9606 None SL-0198 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}. UNIPROT Q99828 UNIPROT B5BU40 UNIPROT H6WJF3 UNIPROT O00693 UNIPROT O00735 UNIPROT Q6IB49 UNIPROT Q96J54 UNIPROT Q99971 PDB 1DGU PDB 1DGV PDB 1XO5 PDB 1Y1A PDB 2L4H PDB 2L4I PDB 2LM5 PDB 6OCX PDB 6OD0 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 OMIM 602293 OMIM 618267 DisGeNET 10519 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}. 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. P11802 EBI-3914485 0.37 Q92993 EBI-25912340 0.56 P49810 EBI-7017541 0.56 Q01780 EBI-373746 0.00 O00401 EBI-8290175 0.63 P17301 EBI-8290662 0.40 Q5NHQ1 EBI-2799151 0.00 A0A6L8PDF7 EBI-2810599 0.00 Q81Y46 EBI-2813274 0.00 A0A6H3ACH2 EBI-2817511 0.00 A0A6L7HLB1 EBI-2817492 0.00 A0A6L8PAR8 EBI-2817518 0.00 Q74RZ6 EBI-2843481 0.00 A0A0H2W7X9 EBI-2848345 0.00 Q96GD4 EBI-3935743 0.37 Q13153 EBI-9074151 0.40 Q8IUH5 EBI-9091611 0.37 Q04637 EBI-24338171 0.56 Q3KNT9 EBI-24519662 0.56 P40199 EBI-25265860 0.56 P10092 EBI-24613829 0.56 O43639 EBI-23674636 0.56 Q8NEA6 EBI-24536125 0.56 P26842 EBI-24432861 0.56 Q9H7N4 EBI-24557755 0.56 Q3SY00 EBI-24793494 0.56 O00746 EBI-24538334 0.56 O60422 EBI-24540023 0.56 P48449 EBI-24540975 0.56 P23759 EBI-24553159 0.56 Q7RTT5 EBI-24583715 0.56 Q6ZSB9 EBI-24594105 0.56 Q6UXG2 EBI-24635958 0.56 P04066 EBI-24638052 0.56 O00322 EBI-21504674 0.35 Q7Z402 EBI-21657108 0.35 Q99683 EBI-15804106 0.66 P05362 EBI-25872248 0.56 P61981 EBI-25902198 0.56 Q15047 EBI-25909149 0.56 Q8TAP4 EBI-25926078 0.56 Q7Z699 EBI-25931600 0.56 GO:0016324 GO:0030424 GO:0071944 GO:0005813 GO:0005737 GO:0005783 GO:0070062 GO:0032433 GO:0005794 GO:0030426 GO:0030027 GO:0016020 GO:0043005 GO:0043025 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005886 GO:0032587 GO:0042383 GO:0031982 GO:0005509 GO:0008427 GO:0000287 GO:0030291 GO:0043495 GO:0031267 GO:0044325 GO:0001525 GO:0006915 GO:0007155 GO:0051301 GO:0006974 GO:0071363 GO:1990090 GO:0071356 GO:0031122 GO:0006302 GO:0007113 GO:0097191 GO:0043066 GO:0008285 GO:0045653 GO:0007026 GO:0010977 GO:0051898 GO:0001933 GO:0030220 GO:0070886 GO:0043085 GO:0033630 GO:0030307 GO:0030335 GO:0090050 GO:0008284 GO:0001954 GO:0070374 GO:2000256 GO:0051092 GO:1903078 GO:0001934 GO:0071902 GO:0090314 GO:1900026 GO:0051302 GO:0042127 GO:0002931 GO:0007286 GO:0038163 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:10366599} MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEQRSVESSLRAQVPFEQILSLPELKANPFKERICRVFSTSPAKDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSRLVNCLTGEGEDTRLSASEMKQLIDNILEESDIDRDGTINLSEFQHVISRSPDFASSFKIVL 191 Q9Z0F4 Calcium Cib1 10090 None SL-0198 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}. UNIPROT Q9Z0F4 UNIPROT Q3TN80 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0016324 GO:0030424 GO:0071944 GO:0005813 GO:0005737 GO:0030425 GO:0005783 GO:0032433 GO:0030426 GO:0030027 GO:0016020 GO:0043005 GO:0043025 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005886 GO:0032587 GO:0042383 GO:0005509 GO:0008427 GO:0000287 GO:0008022 GO:0019901 GO:0030291 GO:0043495 GO:0031267 GO:0044325 GO:0001525 GO:0006915 GO:0007155 GO:0051301 GO:0006974 GO:0071363 GO:1990090 GO:0071356 GO:0031122 GO:0007113 GO:0043066 GO:0008285 GO:0045653 GO:0007026 GO:0010977 GO:0051898 GO:0001933 GO:0030220 GO:0070886 GO:0043085 GO:0033630 GO:0030307 GO:0030335 GO:0090050 GO:0008284 GO:0001954 GO:0070374 GO:2000256 GO:0051092 GO:1903078 GO:0001934 GO:0071902 GO:0090314 GO:1900026 GO:0051302 GO:0042127 GO:0002931 GO:0007286 GO:0038163 Lipid-Anchored UniProt By Similarity {ECO:0000250} MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPPEQRTVEESLHTRVSFEQILSLPELKANPFKERICMVFSTSPTRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLDREDLSQLVNCLTGEGEDTRLSASEMKQLIDNILEESDIDRDGTINLSEFQHVISRSPDFASSFKIVL 191 Q9R010 Calcium Cib1 10116 None SL-0198 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}. UNIPROT Q9R010 UNIPROT Q5BKA8 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. P35465 EBI-9230038 0.40 GO:0016324 GO:0030424 GO:0071944 GO:0005813 GO:0005737 GO:0030425 GO:0005783 GO:0032433 GO:0030426 GO:0030027 GO:0016020 GO:0043005 GO:0043025 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005886 GO:0032587 GO:0042383 GO:0005509 GO:0008427 GO:0000287 GO:0008022 GO:0019901 GO:0030291 GO:0043495 GO:0031267 GO:0044325 GO:0001525 GO:0006915 GO:0007155 GO:0051301 GO:0006974 GO:0071363 GO:1990090 GO:0071356 GO:0031122 GO:0007113 GO:0043066 GO:0008285 GO:0045653 GO:0007026 GO:0010977 GO:0051898 GO:0001933 GO:0030220 GO:0070886 GO:0043085 GO:0033630 GO:0030307 GO:0030335 GO:0090050 GO:0008284 GO:0001954 GO:0070374 GO:2000256 GO:0051092 GO:1903078 GO:0001934 GO:0071902 GO:0090314 GO:1900026 GO:0051302 GO:0042127 GO:0002931 GO:0007286 GO:0038163 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:18627437} MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPPEHRTVEESLHTRVSFEQILSLPELKANPFKERICMVFSTSPTRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLDREDLSRLVNCLTGEGEDTRLSASEMKQLIDNILEESDIDRDGTINLSEFQHVISRSPDFASSFKIVL 191 B1A8Z2 Calcium CIB1 9940 None SL-0198 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}. UNIPROT B1A8Z2 Pfam PF13499 PROSITE PS00018 PROSITE PS50222 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}. GO:0016324 GO:0005813 GO:0005783 GO:0032433 GO:0030426 GO:0030027 GO:0005654 GO:0043204 GO:0048471 GO:0032587 GO:0042383 GO:0005509 GO:0008427 GO:0030291 GO:0043495 GO:0031267 GO:0044325 GO:0001525 GO:0006915 GO:0007155 GO:0051301 GO:0006974 GO:1990090 GO:0071356 GO:0031122 GO:0007113 GO:0007229 GO:0043066 GO:0008285 GO:0045653 GO:0007026 GO:0010977 GO:0051898 GO:0001933 GO:0030220 GO:0070886 GO:0033630 GO:0030307 GO:0090050 GO:0001954 GO:0070374 GO:2000256 GO:0051092 GO:1903078 GO:0071902 GO:0090314 GO:1900026 GO:0051302 GO:0002931 GO:0007286 GO:0038163 Lipid-Anchored UniProt Sequence Analysis {ECO:0000255} MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEHRSVEESLQARVSLEQILSLPELKANPFKERICKVFSTSPSRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSQLVNCLTGESEDTRLSASEMKQLIDNILEESDIDRDGTINLSEFQHVISRSPDFASSFKIVL 191 Q15642 Cdc42-interacting TRIP10 9606 None SL-0198 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. UNIPROT Q15642 UNIPROT B2R8A6 UNIPROT B7WP22 UNIPROT D6W645 UNIPROT O15184 UNIPROT Q53G22 UNIPROT Q5TZN1 UNIPROT Q6FI24 UNIPROT Q8NFL1 UNIPROT Q8TCY1 UNIPROT Q8TDX3 UNIPROT Q96RJ1 PDB 2CT4 PDB 2EFK PDB 2KE4 Pfam PF00611 Pfam PF00018 PROSITE PS51741 PROSITE PS51860 PROSITE PS50002 OMIM 604504 DisGeNET 9322 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}. P07948 EBI-8565817 0.51 Q14974 EBI-30827298 0.44 P60953 EBI-7213336 0.61 Q9Y2W2 EBI-752548 0.37 Q15642 EBI-1268134 0.74 Q96RU3 EBI-1647547 0.27 P48023 EBI-7908855 0.59 A0A384KSJ5 EBI-2817480 0.00 A0A5P8YEZ8 EBI-2873377 0.00 Q9Y4D1 EBI-6550032 0.52 Q9Z207 EBI-6550121 0.40 O08808 EBI-6550199 0.40 O00401 EBI-24407610 0.56 Q8IUH5 EBI-9090827 0.37 Q92558 EBI-10236688 0.56 Q17R89 EBI-10238339 0.56 Q1RLN5 EBI-10239195 0.56 Q68EM7 EBI-10249175 0.56 Q969G3 EBI-10280647 0.56 Q9H4E5 EBI-10306633 0.56 Q9Y3L3 EBI-10327866 0.56 P46379 EBI-11154173 0.35 Q6SPF0 EBI-11160311 0.35 P54274 EBI-11308271 0.37 Q9BSI4 EBI-11308281 0.51 Q9NUX5 EBI-11308291 0.37 P53933 EBI-11533915 0.56 O15156 EBI-24294257 0.56 Q8IZP0 EBI-24302596 0.56 P26367 EBI-24333764 0.56 Q8IWW6 EBI-24337375 0.56 P50221 EBI-25244628 0.56 P42684 EBI-25250506 0.56 Q13671 EBI-24484923 0.56 Q15428 EBI-24624817 0.56 O75564 EBI-24780027 0.56 Q6FHY5 EBI-24376152 0.56 Q5T230 EBI-24395781 0.56 Q9NVV9 EBI-24455319 0.56 O43248 EBI-24560095 0.56 Q8N9I9 EBI-25196090 0.56 P52952 EBI-24792337 0.56 P81408 EBI-21535449 0.35 O15389 EBI-21881508 0.35 Q6UY01 EBI-21887518 0.40 Q6IN36 EBI-16191410 0.35 Q5BJU7 EBI-16191410 0.35 P97573 EBI-16191410 0.50 E9PT20 EBI-16191410 0.35 O08816 EBI-16191410 0.35 P39052 EBI-16191410 0.35 P18484 EBI-16191410 0.35 P17096 EBI-20935428 0.40 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 P78325 EBI-21225631 0.56 P42858 EBI-25944092 0.56 Q9BYB0 EBI-26515065 0.37 GO:0005938 GO:0042995 GO:0005737 GO:0005856 GO:0005829 GO:0070062 GO:0005794 GO:0043231 GO:0005764 GO:0005654 GO:0048471 GO:0001891 GO:0042802 GO:0008289 GO:0030036 GO:0007154 GO:0006897 GO:0007165 Unknown UniProt Sequence Analysis MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN 601 Q07065 Cytoskeleton-associated CKAP4 9606 None SL-0198 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. UNIPROT Q07065 UNIPROT Q504S5 UNIPROT Q53ES6 OMIM 618595 DisGeNET 10970 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}. A0A142I5B9 EBI-20626314 0.35 O43542 EBI-11129266 0.35 O76050 EBI-20901648 0.40 P00519 EBI-10101379 0.35 P00533 EBI-702075 0.35 P01112 EBI-27045317 0.27 Q9H1I8 EBI-733925 0.00 P49407 EBI-1642094 0.35 Q70EL3 EBI-2512984 0.40 P40692 EBI-2932395 0.37 Q8IYT8 EBI-2984710 0.35 P60520 EBI-3046676 0.35 P01106 EBI-3893169 0.35 P18848 EBI-3927782 0.37 P17568 EBI-3936336 0.37 Q99598 EBI-3936346 0.37 Q14764 EBI-3936356 0.37 Q07065 EBI-3942157 0.37 Q9Y3C0 EBI-3942167 0.37 P81172 EBI-3942177 0.37 Q6I9Y2 EBI-3942193 0.37 P04578 EBI-6174316 0.46 Q92905 EBI-21325777 0.35 Q13618 EBI-21329068 0.35 P63208 EBI-8835658 0.35 O75807 EBI-9976880 0.35 O60307 EBI-10103761 0.35 Q96FW1 EBI-10770198 0.35 P05412 EBI-11323169 0.35 P36895 EBI-11008521 0.35 P35278 EBI-11012136 0.35 Q3UJU9 EBI-11021410 0.35 O75787 EBI-11037152 0.35 P51148 EBI-11046231 0.35 P51149 EBI-11050319 0.35 Q9D8B3 EBI-11052854 0.35 Q16513 EBI-11070511 0.35 F8VQC7 EBI-11104527 0.35 Q9R0Q3 EBI-11111571 0.35 Q9P0L0 EBI-11120309 0.35 P09450 EBI-11127973 0.35 Q15006 EBI-11130215 0.35 Q8N4V1 EBI-11130635 0.35 O00400 EBI-11135399 0.35 Q5T3F8 EBI-11155257 0.35 Q9Y3E0 EBI-11161387 0.35 Q2MV58 EBI-11366929 0.27 Q5HYA8 EBI-11367583 0.27 Q6NUS6 EBI-11368748 0.27 Q86UK5 EBI-11372136 0.27 Q86X19 EBI-11372615 0.27 Q96GX1 EBI-11375285 0.27 Q96Q45 EBI-11377173 0.27 Q9P0N5 EBI-11378021 0.27 Q99IB8 EBI-11613941 0.35 Q6IQ23 EBI-16398399 0.35 Q13503 EBI-21501670 0.35 P30825 EBI-21505748 0.35 Q92633 EBI-21508694 0.35 Q9H8X2 EBI-21509881 0.35 Q16581 EBI-21515265 0.35 Q6P5W5 EBI-21515976 0.35 Q9UGM1 EBI-21517134 0.35 A2A2Y4 EBI-21527504 0.35 O75326 EBI-21558128 0.35 O95274 EBI-21607810 0.35 Q99689 EBI-21638763 0.35 O94766 EBI-21668731 0.35 Q99871 EBI-21670231 0.35 Q9NVF7 EBI-21671334 0.35 Q7LGA3 EBI-21675787 0.35 Q16322 EBI-21690666 0.35 P49796 EBI-21716735 0.35 Q86Y78 EBI-21717654 0.35 O14763 EBI-21722795 0.35 Q8WWF3 EBI-21811588 0.35 P08842 EBI-21852400 0.35 P51888 EBI-21852864 0.35 Q9Y6Z7 EBI-21859525 0.35 Q9BZR6 EBI-21865956 0.35 Q5BJH7 EBI-21881931 0.35 P50876 EBI-21881918 0.40 O60858 EBI-21881893 0.35 O15155 EBI-16788067 0.27 P27824 EBI-16788621 0.42 Q96I36 EBI-16791250 0.27 P13073 EBI-16791533 0.27 P11279 EBI-16794808 0.27 Q9HBL7 EBI-16797780 0.27 P51151 EBI-16798325 0.27 Q9NS69 EBI-16802054 0.27 O43493 EBI-16800982 0.42 P36957 EBI-20305285 0.35 P08559 EBI-20306509 0.35 P31040 EBI-20306992 0.35 Q9UKU6 EBI-20901800 0.40 Q8WXX0 EBI-20901792 0.40 P04275 EBI-20903352 0.40 P29475 EBI-20905832 0.40 Q6NUK1 EBI-20909712 0.40 Q8IVJ8 EBI-20910272 0.40 Q96NB3 EBI-20910632 0.40 P21675 EBI-20917908 0.40 P16403 EBI-20926338 0.40 A6NNW6 EBI-20932560 0.40 Q9ULG1 EBI-20935724 0.40 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 P62079 EBI-20977847 0.35 O95858 EBI-20977902 0.35 Q15077 EBI-21262943 0.35 Q9H1C4 EBI-21266770 0.35 P25100 EBI-21277437 0.35 Q00059 EBI-21980665 0.35 O84793 EBI-22302936 0.35 Q640N3 EBI-25409042 0.35 Q5FWK3 EBI-25409394 0.35 P0DOF2 EBI-25603126 0.35 P23497 EBI-25485215 0.35 Q9C0B5 EBI-25636144 0.35 P0DTD8 EBI-25687199 0.35 Q7TFA1 EBI-25688644 0.35 P02452 EBI-26366205 0.35 Q53F19 EBI-26396827 0.35 P52298 EBI-26398473 0.35 Q9NRI5 EBI-26610886 0.35 Q8NDZ4 EBI-26597064 0.35 P01116 EBI-27041844 0.27 P01111 EBI-27042293 0.27 Q13363 EBI-27044482 0.35 A0A0H3NFP4 EBI-27055788 0.27 A0A0H3NG92 EBI-27055968 0.27 A0A0H3NF08 EBI-27055973 0.27 A0A0H3NB75 EBI-27055983 0.27 P35226 EBI-27108918 0.35 Q99592 EBI-27093179 0.35 Q92630 EBI-28952196 0.27 Q8NCK7 EBI-27105115 0.35 P56180 EBI-27116883 0.27 P0DTC4 EBI-28955127 0.35 P08069 EBI-32718669 0.35 P08922 EBI-32719572 0.35 Q5JZY3 EBI-32720634 0.27 P29322 EBI-32721175 0.27 P54760 EBI-32721396 0.27 P21860 EBI-32721529 0.27 P06213 EBI-32723092 0.27 P14616 EBI-32723232 0.27 O15146 EBI-32724025 0.27 P04629 EBI-32724282 0.27 P16234 EBI-32724889 0.27 P09619 EBI-32724964 0.27 P07949 EBI-32725031 0.27 Q04912 EBI-32725158 0.27 Q6J9G0 EBI-32731895 0.27 Q8TCJ2 EBI-32732289 0.27 GO:0035577 GO:0005856 GO:0005783 GO:0005788 GO:0005789 GO:0070062 GO:0016021 GO:0042599 GO:0005811 GO:0016020 GO:0048471 GO:0005886 GO:0005791 GO:0035579 GO:0003723 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPSAKQRGSKGGHGAASPSEKGAHPSGGADDVAKKPPPAPQQPPPPPAPHPQQHPQQHPQNQAHGKGGHRGGGGGGGKSSSSSSASAAAAAAAASSSASCSRRLGRALNFLFYLALVAAAAFSGWCVHHVLEEVQQVRRSHQDFSRQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASLEESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKSDSHGPKEDGGFRHSEAFEALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQRLAALQGRLEGLGSSEADQDGLASTVRSLGETQLVLYGDVEELKRSVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPPQDFLDRLSSLDNLKASVSQVEADLKMLRTAVDSLVAYSVKIETNENNLESAKGLLDDLRNDLDRLFVKVEKIHEKV 602 Q8BMK4 Cytoskeleton-associated Ckap4 10090 None SL-0198 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}. UNIPROT Q8BMK4 UNIPROT B2RRB4 UNIPROT Q8BTK8 UNIPROT Q8R3F2 High-affinity epithelial cell surface receptor for APF. {ECO:0000250}. Mediates the anchoring of the endoplasmic reticulum to microtubules. {ECO:0000250}. P68510 EBI-8586548 0.35 P14094 EBI-20566937 0.35 Q8BRE0 EBI-20718973 0.35 P07602 EBI-21347829 0.35 GO:0009986 GO:0005856 GO:0005783 GO:0005789 GO:0016021 GO:0005811 GO:0048471 GO:0005886 GO:0005791 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPSAKQRGSKGGHGAASPSDKGAHPSGGADDVAKKPPAAPQQPQPPAPHPPQHPQNQAHRGGHRGRSSAATANASSASCSRRLGRVLNFLFYLSLVAAAAFSGWYVHHVLEEVQQVRRGHQDFSRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEGAVFKDSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQEHVGNLGSSSDLASTVRSLGETQLALSSDLKELKQSLGELPGTVESLQEQVLSLLSQDQAQAEGLPPQDFLDRLSSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNLESAKGLLDDLRNDLDRLFLKVEKIHEKI 575 Q9LEX1 Calcium-dependent CLB 3702 None SL-0178 SL-0182 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}. UNIPROT Q9LEX1 UNIPROT P92940 Pfam PF00168 Pfam PF17047 PROSITE PS50004 PROSITE PS51847 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}. GO:0005783 GO:0016021 GO:0031965 GO:0005886 GO:0097001 GO:0008289 GO:0046872 GO:0043565 GO:0006869 GO:0045892 GO:0009958 GO:0009651 GO:0009414 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGLISGILFGIIFGVALMAGWSRMMTHRSSKRVAKAVDMKLLGSLSRDDLKKICGDNFPQWISFPAFEQVKWLNKLLSKMWPYIAEAATMVIRDSVEPLLEDYRPPGITSLKFSKLTLGNVAPKIEGIRVQSFKEGQVTMDVDLRWGGDPNIVLGVTALVASIPIQLKDLQVFTVARVIFQLADEIPCISAVVVALLAEPKPRIDYTLKAVGGSLTAIPGLSDMIDDTVDTIVKDMLQWPHRIVVPIGGIPVDLSDLELKPQGKLIVTVVKATNLKNKELIGKSDPYATIYIRPVFKYKTKAIENNLNPVWDQTFELIAEDKETQSLTVEVFDKDVGQDERLGLVKLPLSSLEAGVTKELELNLLSSLDTLKVKDKKDRGSITLKVHYHEFNKEEQMAALEDEKKIMEERKRLKEAGVIGSTMDAVGMVGSGLGAGVGMVGTGIGTGVGLVGSGVSSGVGMVGSGFGAVGSGLSKAGRFMGRTITGQSSKRSGSSTPVNTVPENDGAKQQ 510 Q1LZF8 Chloride CLCC1 9913 None SL-0178 SL-0182 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}. UNIPROT Q1LZF8 Pfam PF05934 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}. GO:0034707 GO:0005783 GO:0005789 GO:0000139 GO:0044233 GO:0031965 GO:0005254 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLYSLLLCECLWLITAYAHDDEWIDPTDMLNYDAASGRMRKSQVKYGISEKEEVNPDLSCANELSECYNRLDSLTYKIDECEKQKRKDYESQSNPVFRRYLNKILIETKKLGLPDENKHDMHYDAEIILKRQTLLEIQKFLSGEDWKPGALDDALSDILINFKFHDFETWKWRFEEFFGVDPYNVFMVLLCLLCIVALVATELWTYVRWYTQLKRVFFISFLISLGWNWMYLYKLAFAQHQAEVAKMEPLNNVCAEKMNWSGSLWEWLRSSWTYKDDPCQKYYELLLVNPIWLVPPTKALAVTFTNFVTEPLKHVGKGAGEFIKALMKEIPVLLHIPVLIIMALAVLSFCYGAGKSVNMLRHVGGPEREAPQALQAGERRRQQKIDYRPHGGAGDADFYYRGQISPIEQGPNDNTYEGRRDVLRERDVGLRFQTGNKSPEVLRPFDLQEAEAREHPKVVPGLKSPNLESKPREMGEIPGESTPTESSTESSQPAKPVSGQKVSEGVEGCPAVEKAQLRTDAAGGPEEGSTCSPASTAVEVCG 542 A0A2R8Q3S9 Chloride clcc1 7955 None SL-0178 SL-0182 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}. UNIPROT A0A2R8Q3S9 Pfam PF05934 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}. GO:0034707 GO:0005783 GO:0005789 GO:0000139 GO:0031965 GO:0005254 Transmembrane UniProt Sequence Analysis {ECO:0000255} MKLSSSSSFGLCILVVFFCFVVIESAKIRIDGYNDEAWIDPYDMLNYDPTTKRMRKSTESESYQNVPTKRREFNSESCDVPKCPDEHECIKKLHILQKEFDEQKSKSTATLSKPVCLPVFKRFLSKLLKETSKLGLPDDGITAMHYDAEVKLSKQSLAEIQKLLNDEDGWTTGAMDEALSQILVQFKLHDYEAWKWRFEDTFHVDVDTVLKVSLIVLIIVAIICTQLWSVVSWFVQFRRMFAVSFFISLIWNWFHLYMLAFAEHKKNIVQVESFNAKCTGLKQLNWQDSLSEWYRRTWTLQDDPCKKYYEVLVVNPILLVPPTKAITITITNFITDPLKHIGEGISEFLRALLKDLPVTLQIPVLIIIILAILIFVYGSAQAAIHQVARFPRLGWRQEQPPPAVGQRQNPQLRAHEEPWEGGDARQPLPMRQDNRGNHVGNRGDQGFRDANAPENREEDRSMDIRQEFSTKRTPVETLQATGNTFPDDETDSQQRTQELDSGANVEEEVKVEEKEKKESFSVDNKEQKETKSPDRSEPITSEPPSSIDVKTVGADQGNEHLMCTKRKWAAQNGFKLQVILCEINSEASADLPEEEECFSFKHPVQETQS 609 Q96S66 Chloride CLCC1 9606 None SL-0178 SL-0182 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}. UNIPROT Q96S66 UNIPROT O94861 UNIPROT Q8WYP8 UNIPROT Q8WYP9 UNIPROT Q9BU25 Pfam PF05934 OMIM 609913 OMIM 617539 DisGeNET 23155 Seems to act as a chloride ion channel (PubMed:30157172). Plays a role in retina development (PubMed:30157172). {ECO:0000269|PubMed:30157172}. 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. O15162 EBI-21724762 0.35 P00533 EBI-32720286 0.27 P01112 EBI-27045317 0.27 P04626 EBI-32721465 0.27 A0A6H3AJ02 EBI-2836117 0.00 P0DOE9 EBI-6138583 0.35 Q13618 EBI-21329068 0.35 P06460 EBI-11723082 0.35 P06927 EBI-11724813 0.35 Q99JN2 EBI-11026090 0.35 Q6NUS6 EBI-11368748 0.27 Q86X19 EBI-11372615 0.27 Q96GX1 EBI-11375285 0.27 Q9P0N5 EBI-11378021 0.27 Q2MV58 EBI-11384104 0.27 Q86UK5 EBI-11389870 0.27 O75326 EBI-21558128 0.35 O95858 EBI-21724762 0.35 Q96IK5 EBI-21724762 0.35 Q8IWV7 EBI-21724762 0.35 Q15813 EBI-21724762 0.35 Q15038 EBI-21724762 0.35 P55061 EBI-21724762 0.35 P23470 EBI-21724762 0.35 Q6ZMD2 EBI-21898749 0.40 P27824 EBI-16788621 0.27 P11279 EBI-16794808 0.27 Q9HBL7 EBI-16797780 0.27 P51151 EBI-16798325 0.27 Q7KZN9 EBI-20304305 0.35 P21796 EBI-20307902 0.35 P13693 EBI-20992046 0.35 F5H1C8 EBI-21264930 0.35 Q9H1C4 EBI-21266770 0.35 Q9UKW4 EBI-25410543 0.35 Q92888 EBI-25411420 0.35 P0DTC3 EBI-25491278 0.84 P19739 EBI-25685423 0.35 P59632 EBI-25688265 0.53 K9N7D2 EBI-26375184 0.35 Q2TAZ0 EBI-26443127 0.35 A0A0B4J2F0 EBI-26657494 0.63 P01116 EBI-27041844 0.27 P01111 EBI-27042293 0.27 A0A0H3NG92 EBI-27055968 0.27 A0A0H3NF08 EBI-27055973 0.27 A0A0H3NB75 EBI-27055983 0.27 Q86YV6 EBI-28942265 0.35 Q92932 EBI-27116679 0.27 P56180 EBI-27116883 0.27 P08922 EBI-32719572 0.35 Q9UM73 EBI-32719830 0.27 P54756 EBI-32720907 0.27 P29322 EBI-32721175 0.27 P11362 EBI-32721578 0.27 P35916 EBI-32722728 0.27 P08069 EBI-32722947 0.27 P06213 EBI-32723092 0.27 P14616 EBI-32723232 0.27 O15146 EBI-32724025 0.27 P04629 EBI-32724282 0.27 Q16288 EBI-32724526 0.27 P16234 EBI-32724889 0.27 P07949 EBI-32725031 0.27 Q01974 EBI-32725367 0.27 Q6J9G0 EBI-32731895 0.27 Q8TCJ2 EBI-32732289 0.27 GO:0034707 GO:0005783 GO:0005789 GO:0000139 GO:0043231 GO:0016020 GO:0044233 GO:0031965 GO:0005254 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLCSLLLCECLLLVAGYAHDDDWIDPTDMLNYDAASGTMRKSQAKYGISGEKDVSPDLSCADEISECYHKLDSLTYKIDECEKKKREDYESQSNPVFRRYLNKILIEAGKLGLPDENKGDMHYDAEIILKRETLLEIQKFLNGEDWKPGALDDALSDILINFKFHDFETWKWRFEDSFGVDPYNVLMVLLCLLCIVVLVATELWTYVRWYTQLRRVLIISFLFSLGWNWMYLYKLAFAQHQAEVAKMEPLNNVCAKKMDWTGSIWEWFRSSWTYKDDPCQKYYELLLVNPIWLVPPTKALAVTFTTFVTEPLKHIGKGTGEFIKALMKEIPALLHLPVLIIMALAILSFCYGAGKSVHVLRHIGGPESEPPQALRPRDRRRQEEIDYRPDGGAGDADFHYRGQMGPTEQGPYAKTYEGRREILRERDVDLRFQTGNKSPEVLRAFDVPDAEAREHPTVVPSHKSPVLDTKPKETGGILGEGTPKESSTESSQSAKPVSGQDTSGNTEGSPAAEKAQLKSEAAGSPDQGSTYSPARGVAGPRGQDPVSSPCG 551 Q99LI2 Chloride Clcc1 10090 None SL-0178 SL-0182 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}. UNIPROT Q99LI2 UNIPROT A2AEK9 Pfam PF05934 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}. Q9CZE3 EBI-11570876 0.35 Q9D0P8 EBI-11571153 0.35 Q8BIZ1 EBI-26595802 0.35 GO:0034707 GO:0005737 GO:0005783 GO:0005789 GO:0005794 GO:0000139 GO:0043231 GO:0044233 GO:0031965 GO:0005634 GO:0005254 GO:0006821 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLCRLLLCECLLLITGYAHDDDWIDPTDMLNYDAASGTMRKSQVRSGTSEKKEVSPDSSEAEELSDCLHRLDSLTHKVDSCEKKKMKDYESQSNPVFRRYLNKILIEAGKLGLPDENKVEMRYDAEILLSRQTLLEIQKFLSGEEWKPGALDDALSDILINFKCHDSEAWKWQFEDYFGVDPYNVFMVLLCLLCLVVLVATELWTYVRWYTQMKRIFIISFLLSLAWNWIYLYKMAFAQHQANIAGMEPFDNLCAKKMDWTGSLWEWFTSSWTYKDDPCQKYYELLIVNPIWLVPPTKALAITFTNFVTEPLKHIGKGAGEFIKALMKEIPVLLQIPVLAILALAVLSFCYGAGRSVPMLRHFGGPDREPPRALEPDDRRRQKGLDYRLHGGAGDADFSYRGPAGSIEQGPYDKMHASKRDALRQRFHSGNKSPEVLRAFDLPDTEAQEHPEVVPSHKSPIMNTNLETGELPGESTPTEYSQSAKDVSGQVPSAGKSSPTVDKAQLKTDSECSPPGGCPPSKEAAVAAHGTEPVSSPCG 539 Q9WU61 Chloride Clcc1 10116 None SL-0178 SL-0182 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}. UNIPROT Q9WU61 UNIPROT Q66HQ5 UNIPROT Q8VIE8 UNIPROT Q8VIE9 UNIPROT Q8VIF0 UNIPROT Q8VIF1 Pfam PF05934 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}. GO:0034707 GO:0005737 GO:0005783 GO:0005789 GO:0005794 GO:0000139 GO:0044233 GO:0031965 GO:0005634 GO:0005254 GO:0006821 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLCSLLLCGCLLLITGYAHDDDWIDPTDMLNYDAASGTMRKSQAKYGTSEKKEVNPGLSDAQELSDCLQRLDSLTHKVDDCEKKKMKDYESQSNPVFRRYLNKILIEAGKLGLPDEDRVDVRYDAEILLTRQTLLEIQKFLSGEEWKPGALDDALSDILTNFKSHDAEAWKWQFEDYFGVDPYNVFMVLLCLLCIVALVATELWTYVRWHTQLKRVCIISFLVSLGWNWIYLYKVAFAQHQANVAKMAPLNDVCAKKMDWTENLWEWFRISWTYKDDPCQKYYELLIVNPIWLVPPTKALAVTFTNFVTEPLKYIGKGTGEFIKALMKEIPVLLQIPVLVILALAVLGFCYGAGQSVPMLRHFRGPEREPPRALEPDDRRRQKELDYRFHGGAGDADFSYRGPAGSIEQGPYDKMHVCERDVLRQRQVNMRFPSGNKSPEVLRAFDLPDTEAQEHPEVVPSHKPSIVNTSLKETSELPRESTLAECSQCAKDGSGQVPSTAESSPIVEKAQLKTDSECRPHSTEAAAAAARGTDPVSSPCG 541 Q91892 Chloride clcc1 8355 None SL-0178 SL-0182 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}. UNIPROT Q91892 Pfam PF05934 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}. GO:0034707 GO:0005789 GO:0000139 GO:0044233 GO:0031965 GO:0005254 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRLFLLVALYLSPVYGDYTDEWIDPSDMLNYDAASGKMKNKPQVESTQSYYSVENTVSQDATQQPAQKANELHQNPDMTCSAEYQEYKTKLENLKGQLEETKRMEKSKSKSQAIFKRYLNKILIEAGRIGLPDESYPKAHYDAEVVFTMEMLQEIQSFLNNGDWNVGALDDALSSTLVQFKHHNEEEWKWKFEDSFGVDVYTLFMLILCVLCLVKLIATEIWTHIGWFTQLKRLLILSTVISFGWNWMYLYKVAFAERQAELAKLQDFDKCSQKISWSESLFDWMKGAATFQNDPCEDYFKALIVSPTLMVPPTKALALTFTNFITEPLKHIGKGIGEFLNALLSEIPLFFQVPVLIFIAVLLLAFFYGAGTAVMNPVNLYRRLTGPEREKPLPVEPTRSNRKRFIEDVRVPPALGQLPRDNDVVNIPKQQPLDDIDGSNNPPVTAPADPSDTGQVKSNNTGEPLVQEDHSIKKSIKESRNDERPNTESPEAKPQRPEEPVVETLRST 508 Q5E9B7 Chloride CLIC1 9913 None SL-0178 SL-0182 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}. UNIPROT Q5E9B7 Pfam PF13409 PROSITE PS50405 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}. GO:0034707 GO:0005737 GO:0070062 GO:0016020 GO:0005739 GO:0031965 GO:0048471 GO:0005886 GO:0005254 GO:0005244 GO:0006821 GO:0045669 GO:0051726 GO:0034765 GO:0051881 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPDEVDETSAEDEGISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFSIPDVFRGVHRYLRNAYAREEFASTCPDDEEIELAYEQVAKALK 241 O00299 Chloride CLIC1 9606 None SL-0178 SL-0182 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}. UNIPROT O00299 UNIPROT Q15089 UNIPROT Q502X1 PDB 1K0M PDB 1K0N PDB 1K0O PDB 1RK4 PDB 3O3T PDB 3P8W PDB 3P90 PDB 3QR6 PDB 3SWL PDB 3TGZ PDB 3UVH PDB 4IQA PDB 4JZQ PDB 4K0G PDB 4K0N PDB 7F8R Pfam PF13409 PROSITE PS50405 OMIM 602872 DisGeNET 1192 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}. O15116 EBI-23757154 0.67 P23508 EBI-1063923 0.00 P62330 EBI-1068310 0.00 P11171 EBI-1078375 0.00 P01889 EBI-1081273 0.00 Q14164 EBI-1083332 0.00 P32121 EBI-1642567 0.35 Q5NID2 EBI-2799144 0.00 A0A3P1U0S6 EBI-2811954 0.00 Q81U22 EBI-2836081 0.00 A0A6L8P1I7 EBI-2836088 0.00 A0A0F7REA8 EBI-2836074 0.00 Q8CZM8 EBI-2848306 0.00 A0A3N4BEU0 EBI-2873204 0.00 P40692 EBI-2932395 0.37 Q9H0R8 EBI-3048562 0.35 P20292 EBI-3904626 0.37 P24539 EBI-3904636 0.37 P27449 EBI-3904646 0.37 Q93050 EBI-3904656 0.37 P34130 EBI-3907454 0.37 P50416 EBI-3907444 0.37 Q99676 EBI-3907496 0.37 P05386 EBI-3907469 0.37 P10827 EBI-3907479 0.37 Q9Y6K9 EBI-3907506 0.37 P37198 EBI-3916132 0.37 Q9NR11 EBI-3916149 0.37 Q13162 EBI-3935813 0.37 P15336 EBI-5529812 0.35 P19320 EBI-6189915 0.35 Q96FW1 EBI-10770198 0.35 P05412 EBI-11324725 0.35 Q9NQW6 EBI-11009421 0.35 Q61879 EBI-11041929 0.35 P60710 EBI-11045267 0.35 Q9D6P8 EBI-11062262 0.35 Q9WUM4 EBI-11065690 0.35 Q8N3V7 EBI-11086992 0.35 Q9NQX4 EBI-11100755 0.35 P47755 EBI-11117728 0.35 P36873 EBI-11128681 0.35 P46940 EBI-11132927 0.35 O00400 EBI-11135399 0.35 H9XIJ5 EBI-11514200 0.37 Q6FHY5 EBI-24478573 0.56 Q4KMQ1 EBI-24491483 0.67 Q5HYW2 EBI-25156542 0.56 P56945 EBI-15099538 0.35 Q9HCN8 EBI-21660533 0.35 Q86WR7 EBI-21889242 0.35 O75832 EBI-16718696 0.65 Q9Y2H1 EBI-20624829 0.27 Q83D60 EBI-21285616 0.37 Q5S007 EBI-21360986 0.35 P04156 EBI-21014477 0.35 Q9Y251 EBI-21260107 0.35 P03372 EBI-21301141 0.35 P13569 EBI-25416349 0.53 Q8N5H7 EBI-25387159 0.35 Q15139 EBI-25395029 0.35 Q01995 EBI-26878675 0.35 P05154 EBI-27038496 0.35 F1PAA9 EBI-27079701 0.27 P35226 EBI-27108918 0.35 O43318 EBI-28931001 0.35 Q96Q04 EBI-32723651 0.27 GO:0072562 GO:0005903 GO:0034707 GO:0005737 GO:0070062 GO:0005615 GO:0016020 GO:0005739 GO:0005635 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:0031982 GO:0045296 GO:0005254 GO:0005244 GO:0006821 GO:0070527 GO:0045669 GO:0051726 GO:0034765 GO:0051881 GO:0007165 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK 241 Q9Z1Q5 Chloride Clic1 10090 None SL-0178 SL-0182 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}. UNIPROT Q9Z1Q5 Pfam PF13409 PROSITE PS50405 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}. P70181 EBI-653938 0.37 GO:0034707 GO:0005737 GO:0070062 GO:0016020 GO:0005739 GO:0005635 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:0005254 GO:0005244 GO:0006821 GO:0045669 GO:0051726 GO:0034765 GO:0051881 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAMLCPPRYPKLAALNPESNTSGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVARALK 241 Q29238 Chloride CLIC1 9823 None SL-0178 SL-0182 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}. UNIPROT Q29238 Pfam PF13409 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}. GO:0034707 GO:0005737 GO:0016020 GO:0031965 GO:0005886 GO:0005254 GO:0005244 GO:0006821 GO:0051726 GO:0034765 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDI 110 Q95MF9 Chloride CLIC1 9986 None SL-0178 SL-0182 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}. UNIPROT Q95MF9 Pfam PF13409 PROSITE PS50405 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}. GO:0034707 GO:0005737 GO:0031965 GO:0005886 GO:0005254 GO:0005244 GO:0051726 GO:0034765 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVHKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGVDIFAKFSAYIKNSNPALNDNLEKGLLKALKILDNYLTSPLPEEVDETSAEDEGISQRKFLDGNELTLADCNLLPKLHIVQVVCKKNRGFTIPEVFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK 241 Q6MG61 Chloride Clic1 10116 None SL-0178 SL-0182 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}. UNIPROT Q6MG61 Pfam PF13409 PROSITE PS50405 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}. GO:0034707 GO:0005737 GO:0070062 GO:0016020 GO:0005739 GO:0005635 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:0005254 GO:0005247 GO:0006821 GO:0045669 GO:0051726 GO:0034765 GO:0051881 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTSGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVARALK 241 P17697 Clusterin CLU 9913 None SL-0198 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}. UNIPROT P17697 UNIPROT A5D983 UNIPROT Q148K1 Pfam PF01093 PROSITE PS00492 PROSITE PS00493 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}. GO:0042583 GO:0005737 GO:0005829 GO:0005615 GO:0043231 GO:0005743 GO:0005739 GO:0005634 GO:0099020 GO:0048471 GO:0034366 GO:0051787 GO:0031625 GO:0051082 GO:0061077 GO:0002434 GO:0097193 GO:1905907 GO:1902230 GO:0031333 GO:0043065 GO:2001244 GO:0051092 GO:0032436 GO:0048260 GO:2000060 GO:0050821 GO:0042981 GO:0042127 GO:0051788 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P10909} MKTLLLLMGLLLSWESGWAISDKELQEMSTEGSKYVNKEIKNALKEVKQIKTQIEQTNEERKLLLSSLEEAKKKKEDALNDTRDSENKLKASQGVCNETMTALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWINGDRIDSLMENDREQSHVMDVMEDSFTRASSIMDELFQDRFFLRRPQDTQYYSPFSSFPRGSLFFNPKSRFARNVMPFPLLEPFNFHDVFQPFYDMIHQAQQAMDAHLQRTPYHFPTMEFTENNDRTVCKEIRHNSTGCLRMKDQCEKCQEILEVDCSASNPTQTLLRQQLNASLQLAEKFSRLYDQLLQSYQQKMLNTSALLKQLNEQFTWVSQLANLTQSDDQHYLQVFTVNSHNSDPSIPSGLTKVIVKLFNSFPITVTVPQEVSSPNFMENVAEKALQQYRRKSQEE 439 P25473 Clusterin CLU 9615 None SL-0198 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}. UNIPROT P25473 Pfam PF01093 PROSITE PS00492 PROSITE PS00493 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}. GO:0042583 GO:0005829 GO:0005788 GO:0005615 GO:0005794 GO:0005743 GO:0005739 GO:0005634 GO:0099020 GO:0048471 GO:0034366 GO:0051087 GO:0051787 GO:0031625 GO:0051082 GO:0061077 GO:0002434 GO:0097193 GO:1905907 GO:1902230 GO:0031333 GO:0043065 GO:2001244 GO:0051092 GO:0032436 GO:0048260 GO:2000060 GO:0050821 GO:0042981 GO:0042127 GO:0051788 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P10909} MMKTLLLLVGLLLTWDNGRVLGDQAVSDTELQEMSTEGSKYINKEIKNALKGVKQIKTLIEQTNEERKSLLSNLEEAKKKKEDALNDTKDSETKLKASQGVCNDTMMALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHALDVMQDSFNRASSIMDELFQDRFFTREPQDTYHYSPFSLFQRRPFFNPKFRIARNIIPFPRFQPLNFHDMFQPFFDMIHQAQQAMDVNLHRIPYHFPIEFPEEDNRTVCKEIRHNSTGCLKMKDQCEKCQEILSVDCSSNNPAQVQLRQELSNSLQIAEKFTKLYDELLQSYQEKMFNTSSLLKQLNEQFSWVSQLANLTQSEDPFYLQVTTVGSQTSDSNVPVGFTKVVVKLFDSDPITVMIPEAVSRNNPKFMETVAEKALQEYRQKHREE 445 Q29482 Clusterin CLU 9796 None SL-0198 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}. UNIPROT Q29482 Pfam PF01093 PROSITE PS00492 PROSITE PS00493 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}. GO:0042583 GO:0005737 GO:0005829 GO:0005615 GO:0043231 GO:0005743 GO:0005739 GO:0005634 GO:0099020 GO:0048471 GO:0034366 GO:0051787 GO:0031625 GO:0051082 GO:0061077 GO:0002434 GO:0097193 GO:1905907 GO:1902230 GO:0031333 GO:0043065 GO:2001244 GO:0051092 GO:0032436 GO:0048260 GO:2000060 GO:0050821 GO:0042981 GO:0042127 GO:0051788 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P10909} MKTLLLLVGLLLTLENGQVLGDKAVSDRELQEMSTQGSNYINKEIKNALKGVKQIKNLIEQTNEERKSLLGTLEEAKKKKEGALNDTKDSEMKLKESQGVCNETMTALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWINGDRIDSLLENDRQQTHVLDVMQDSFDRASSIMDELFQDRFFTREPQDTYYYSPFSSPHRRSSLLFNPKSRFARNIMHFPMYRHLNFNDMFQPFFDMIHQAQQAMNLHLHRLPDQLPMTEFSEGDNHDRTVCKEIRHNSTGCLKMKDQCEKCQEILSVDCSTNNPSQMQLRQELNNSLQLAEKFTKLYDELLQSYQEKMLNTSSLLKQLNEQFSWVSQLANLTQGEDQYYLQVTTVSSHNSDSEVPSGLTRVVVKLFDSYPITVTVPEVVSRNNPKFMETVAEKALQEYRQKNREE 449 P10909 Clusterin CLU 9606 None SL-0198 [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}. UNIPROT P10909 UNIPROT B2R9Q1 UNIPROT B3KSE6 UNIPROT P11380 UNIPROT P11381 UNIPROT Q2TU75 UNIPROT Q5HYC1 UNIPROT Q7Z5B9 Pfam PF01093 PROSITE PS00492 PROSITE PS00493 OMIM 185430 DisGeNET 1191 [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}. O14656 EBI-21693789 0.35 Q9NRI5 EBI-1105564 0.00 Q9UKE5 EBI-1105584 0.00 P30101 EBI-7172377 0.59 P02647 EBI-1220621 0.35 P01876 EBI-1221175 0.35 P01857 EBI-1222317 0.35 P62993 EBI-2115936 0.00 O35638 EBI-2559549 0.40 P16104 EBI-2564373 0.35 P22736 EBI-2681480 0.00 P01100 EBI-2694247 0.52 Q00987 EBI-2682977 0.00 P04150 EBI-2684198 0.00 P37231 EBI-2793955 0.52 P17028 EBI-2691450 0.00 A0A6L7HEE9 EBI-2836046 0.00 P02866 EBI-2906001 0.35 O15160 EBI-3907424 0.37 P05181 EBI-3907394 0.37 Q99708 EBI-3907404 0.37 O14901 EBI-3907414 0.37 Q14145 EBI-3907434 0.37 Q9Y3Q8 EBI-3916122 0.37 P45984 EBI-3927894 0.37 P62829 EBI-3927914 0.37 P46379 EBI-3927904 0.37 Q07817 EBI-4322676 0.61 Q9BWU1 EBI-6381327 0.35 P18509 EBI-10129061 0.54 P06460 EBI-11723082 0.35 P06792 EBI-11724527 0.35 P0C739 EBI-11725101 0.35 P0CK56 EBI-11725466 0.35 P69901 EBI-11733364 0.35 Q8AZK7 EBI-11734159 0.35 Q6P5D4 EBI-10991106 0.35 A2APR8 EBI-11001201 0.35 P14625 EBI-11044830 0.35 Q9Z0X1 EBI-11065573 0.35 Q9D3R3 EBI-11075393 0.35 Q6ZQ29 EBI-11075869 0.35 Q6NXE6 EBI-11080193 0.35 Q96RT8 EBI-11083232 0.35 Q9DB34 EBI-11115096 0.35 P51114 EBI-11117520 0.35 Q96HP0 EBI-11117520 0.35 Q7Z333 EBI-11117520 0.35 Q5VW52 EBI-11117520 0.35 P27824 EBI-11117520 0.35 P16234 EBI-11134723 0.35 P03428 EBI-12580574 0.35 Q6IQ23 EBI-16398399 0.35 P20036 EBI-21511890 0.35 Q01814 EBI-21599092 0.35 Q9H8H2 EBI-21616235 0.35 Q8NI29 EBI-21693789 0.35 Q6P9B9 EBI-21693789 0.35 Q9UHG3 EBI-21693789 0.35 Q9UBQ6 EBI-21693789 0.35 Q9P273 EBI-21693789 0.35 Q9NYQ6 EBI-21693789 0.35 Q9NX40 EBI-21693789 0.35 Q9H0V9 EBI-21693789 0.35 Q9BV94 EBI-21693789 0.35 Q8NFZ4 EBI-21693789 0.35 Q8NBM8 EBI-21693789 0.35 Q6V0I7 EBI-21693789 0.35 Q6PKC3 EBI-21693789 0.35 Q5SRI9 EBI-21693789 0.35 Q5JTY5 EBI-21693789 0.35 Q58EX2 EBI-21693789 0.35 Q13332 EBI-21693789 0.35 P62879 EBI-21693789 0.35 P53708 EBI-21693789 0.35 P41273 EBI-21693789 0.35 P33908 EBI-21693789 0.35 P10586 EBI-21693789 0.35 O60476 EBI-21693789 0.35 Q6ZRI8 EBI-21744920 0.35 O15063 EBI-21830964 0.35 Q6P158 EBI-21831097 0.35 Q96AT9 EBI-21831245 0.35 Q96QG7 EBI-21831285 0.35 P05067 EBI-15960333 0.68 Q9H4B6 EBI-16425156 0.37 Q96RS6 EBI-20723339 0.35 Q9HCE5 EBI-20595531 0.35 Q9NZV6 EBI-20976398 0.67 Q5S007 EBI-21360986 0.35 Q9NRD1 EBI-21259874 0.35 Q14108 EBI-21264396 0.35 Q9Y275 EBI-21266480 0.35 Q16799 EBI-21368794 0.37 Q9Y6D5 EBI-21370252 0.00 Q15185 EBI-21370704 0.00 Q9UBU8 EBI-21370901 0.00 Q96PY5 EBI-21371604 0.00 Q06787 EBI-21371844 0.00 P10909 EBI-21371813 0.00 P11766 EBI-21372154 0.00 Q7Z699 EBI-21372907 0.00 P14868 EBI-21372879 0.00 P36957 EBI-21373212 0.00 Q7Z698 EBI-21373545 0.00 Q9UL68 EBI-21374623 0.00 O75592 EBI-21374795 0.00 Q86TG7 EBI-21374847 0.00 P02794 EBI-21376448 0.00 Q6AI39 EBI-21376290 0.00 Q6GYQ0 EBI-21376644 0.00 Q96EK5 EBI-21377229 0.00 Q00994 EBI-21377480 0.00 F8VWT9 EBI-21378210 0.00 Q13439 EBI-21378008 0.00 P08238 EBI-21379316 0.00 P07900 EBI-21379300 0.00 Q6ZMI3 EBI-21379522 0.00 Q5SZL2 EBI-21380088 0.00 P26367 EBI-21381283 0.00 Q9NR80 EBI-21381216 0.00 Q9UBW8 EBI-21381443 0.00 Q9Y575 EBI-21381570 0.00 P48426 EBI-21382180 0.00 Q9BZ95 EBI-21382818 0.00 Q9NVR2 EBI-21383211 0.00 Q9NWB6 EBI-21383120 0.00 Q5VTB9 EBI-21383239 0.00 P53041 EBI-21383361 0.00 P31321 EBI-21383806 0.00 Q9NPF5 EBI-21384190 0.00 Q58WW2 EBI-21383966 0.00 Q6NUQ1 EBI-21385792 0.00 Q9BXM7 EBI-21386538 0.00 Q07890 EBI-21387074 0.00 Q99615 EBI-21387981 0.00 P26640 EBI-21388258 0.00 Q15059 EBI-21389314 0.00 Q9C093 EBI-21389142 0.00 Q9H974 EBI-21389084 0.00 Q96MT8 EBI-21389423 0.00 Q14515 EBI-21390086 0.00 Q96K75 EBI-21390447 0.00 Q92610 EBI-21392680 0.00 Q9Y2B5 EBI-21392543 0.00 P27918 EBI-21995211 0.35 P37840 EBI-25295611 0.66 P0DOF2 EBI-25603126 0.35 O96028 EBI-25486814 0.35 Q9BY14 EBI-25505396 0.35 P0DTC3 EBI-25686340 0.35 P0DTC8 EBI-25687968 0.35 Q5EP34 EBI-25773054 0.35 Q15672 EBI-25824698 0.37 P78352 EBI-26509146 0.37 Q9BYB0 EBI-26513929 0.37 Q8N488 EBI-27111302 0.35 P20794 EBI-28934658 0.35 Q8NI60 EBI-28943519 0.35 Q9H5K3 EBI-28948637 0.35 Q16832 EBI-32717626 0.42 P11362 EBI-32718427 0.35 Q16288 EBI-32719212 0.35 P09619 EBI-32719373 0.35 P07949 EBI-32719411 0.35 P34925 EBI-32719634 0.35 Q06418 EBI-32719716 0.35 GO:0097440 GO:0072562 GO:0009986 GO:0042583 GO:0062023 GO:0005737 GO:0005829 GO:0070062 GO:0005576 GO:0005615 GO:0005794 GO:0043231 GO:0005743 GO:0005739 GO:0097418 GO:0005634 GO:0099020 GO:0048471 GO:0031093 GO:0032991 GO:0034366 GO:0045202 GO:0001540 GO:0051087 GO:0050750 GO:0051787 GO:0140597 GO:0046982 GO:0044877 GO:0005102 GO:0048156 GO:0031625 GO:0051082 GO:0000902 GO:0032286 GO:0051131 GO:0061077 GO:0006956 GO:0006958 GO:0002434 GO:0045087 GO:0097193 GO:0006629 GO:0001774 GO:0061518 GO:1905907 GO:1902430 GO:0060548 GO:1905892 GO:1905895 GO:1902230 GO:0031333 GO:0090201 GO:1903573 GO:1905908 GO:1902004 GO:0043065 GO:0010628 GO:2001244 GO:1902998 GO:1901216 GO:0051092 GO:0045429 GO:0032436 GO:0031334 GO:0048260 GO:1902949 GO:0032760 GO:2000060 GO:0017038 GO:0050821 GO:0061740 GO:1900221 GO:0042981 GO:0042127 GO:1901214 GO:1902847 GO:0001836 GO:0051788 GO:0009615 GO:0043691 Peripheral UniProt Sequence Analysis MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE 449 P14683 Clusterin CLU 10036 None SL-0198 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}. UNIPROT P14683 Pfam PF01093 PROSITE PS00493 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}. GO:0042583 GO:0005737 GO:0005829 GO:0005576 GO:0043231 GO:0005743 GO:0005739 GO:0005634 GO:0099020 GO:0051082 GO:0030154 GO:0002434 GO:1905907 GO:0043065 GO:0048260 GO:0050821 GO:0042127 GO:0007283 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P10909} NRRPHFLYPKSRLIRSLLPPPHYGPLSFHDMFQPFLEMIHQAQQAMDVQFHSPAFQFPDMDLLREGEDDRAVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSANNPAQAHLRQELNDSLQVAERLTQRYNELLHSLQTKMLNTSSLLEQLNEQFNWVSQLANLTQGEDQYYLRVSTVTTHSSDSEVPSRVT 191 Q06890 Clusterin Clu 10090 None SL-0198 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}. UNIPROT Q06890 Pfam PF01093 PROSITE PS00492 PROSITE PS00493 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}. P04925 EBI-7188678 0.40 Q62108 EBI-16724752 0.53 Q80YT7 EBI-16732484 0.35 P83510 EBI-16734044 0.35 Q9JLC3 EBI-20976809 0.40 P16056 EBI-27112678 0.35 GO:0016235 GO:0097440 GO:0071944 GO:0009986 GO:0042583 GO:0005737 GO:0005856 GO:0005829 GO:0005615 GO:0030426 GO:0043231 GO:0016020 GO:0005743 GO:0005739 GO:0097418 GO:0043005 GO:0005634 GO:0099020 GO:0048471 GO:0032991 GO:0034366 GO:0045202 GO:0001540 GO:0050750 GO:0051787 GO:0140597 GO:0047485 GO:0044877 GO:0005102 GO:0048156 GO:0031625 GO:0051082 GO:0000902 GO:0032286 GO:0051131 GO:0061077 GO:0031018 GO:0002434 GO:0097193 GO:0001774 GO:0061518 GO:1905907 GO:1902430 GO:0043066 GO:0060548 GO:1905892 GO:1905895 GO:1902230 GO:0031333 GO:1903573 GO:0048812 GO:1902004 GO:0043065 GO:0045597 GO:0008284 GO:0010628 GO:2001244 GO:1902998 GO:1901216 GO:0051092 GO:0045429 GO:0032436 GO:0031334 GO:0048260 GO:1902949 GO:0032760 GO:2000060 GO:0017038 GO:0050821 GO:0061740 GO:1900221 GO:0042981 GO:0042127 GO:1901214 GO:1902847 GO:0051788 GO:0009615 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P10909} MKILLLCVALLLIWDNGMVLGEQEVSDNELQELSTQGSRYINKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEDALEDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGQQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFARASGIIDTLFQDRFFARELHDPHYFSPIGFPHKRPHFLYPKSRLVRSLMSPSHYGPPSFHNMFQPFFEMIHQAQQAMDVQLHSPAFQFPDVDFLREGEDDRTVCKEIRRNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTEQYKELLQSFQSKMLNTSSLLEQLNDQFNWVSQLANLTQGEDKYYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRAE 448 Q29549 Clusterin CLU 9823 None SL-0198 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}. UNIPROT Q29549 Pfam PF01093 PROSITE PS00492 PROSITE PS00493 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}. F0QRW4 EBI-13630150 0.37 GO:0042583 GO:0005737 GO:0005829 GO:0005615 GO:0043231 GO:0005743 GO:0005739 GO:0005634 GO:0099020 GO:0048471 GO:0034366 GO:0051787 GO:0031625 GO:0051082 GO:0061077 GO:0002434 GO:0097193 GO:1905907 GO:1902230 GO:0031333 GO:0043065 GO:2001244 GO:0051092 GO:0032436 GO:0048260 GO:2000060 GO:0050821 GO:0042981 GO:0042127 GO:0051788 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P10909} MKTLLLLVGLLLTWENGPWVLGDKAISDKELQEMSTEGSKYVNKEIKNALKEVKQIKTLIEQSNEERKSLLSSLEEAKKKKEDALNDTRDTETKLKGSQGLCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWINGDRIDSLMENDRQQSHVMDIMEDSFNRASNIMDELFQDRFFNREPFDTQFFSPFGSSHRGSLFFNPKSRFARNIMPFPLFTDLNYHDMFQPFFDMIHQAQQAMDAHLHRIPYHFPEAGVPENSNDRAVCKEIRHNSTGCLRMKDQCEKCREILSVDCSASNSSQMQLRQELYTSLQMAEKFSKLYDQLLQSYQQKMLNTSSLLKQLNEQFSWVSQLANLTQNDDRYYLQVTTVNSHGSDPSVPSGLTKVVVKLFDSYPITLIIPQEVSDPKFMETVAEEALQQYRQRSREE 446 Q9XSC5 Clusterin CLU 9986 None SL-0198 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}. UNIPROT Q9XSC5 Pfam PF01093 PROSITE PS00492 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}. GO:0042583 GO:0005737 GO:0005829 GO:0005615 GO:0043231 GO:0005743 GO:0005739 GO:0005634 GO:0099020 GO:0048471 GO:0034366 GO:0051787 GO:0031625 GO:0051082 GO:0061077 GO:0002434 GO:0097193 GO:1905907 GO:1902230 GO:0031333 GO:0043065 GO:2001244 GO:0051092 GO:0032436 GO:0048260 GO:2000060 GO:0050821 GO:0042127 GO:0051788 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P10909} MKTLLLCVGLLLSWERGQVLGDQLVSDNELQEMSTQGSKYIDREIQNAVKGVQEIKTLIEKTNEERKTLLSVLEEAKKNKEDALNETRDSETKLKAFPEVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWINGDRIDSLLENDRQQSHVLDVMQDSFNRATGIMDELFQDRFFTHKPQDTFYHSPFSYFRRPPLHYAKSRLVRNIMPLSLYGPLNFQDMFQPFFEMIHQAQQAMDVHLHSPAYQTPNVEFITGGPDDRAVCKEIRHNSTGCLRMKDQCAKCQEILSVDCSANNPSQNQLRQELNDSLRLAEELTKRYNELLQSYQWKMLNTSSLLDQPNEQFNWVSQLANLTQGPDQYYLRVSTVTSHTSESEAPSRVTEVVVKLFDSDPITITIPEEVSRDNPKFMETVAEKALQEYRKKKRVE 447 P05371 Clusterin Clu 10116 None SL-0198 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}. UNIPROT P05371 Pfam PF01093 PROSITE PS00492 PROSITE PS00493 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}. P21708 EBI-7618770 0.35 GO:0016235 GO:0097440 GO:0009986 GO:0042583 GO:0005737 GO:0005829 GO:0005615 GO:0030426 GO:0043231 GO:0005743 GO:0005739 GO:0097418 GO:0043005 GO:0005634 GO:0099020 GO:0048471 GO:0032991 GO:0034366 GO:0045202 GO:0001540 GO:0050750 GO:0051787 GO:0140597 GO:0047485 GO:0044877 GO:0005102 GO:0048156 GO:0031625 GO:0051082 GO:0007568 GO:0000902 GO:0071363 GO:0032286 GO:0051131 GO:0061077 GO:0031018 GO:0044849 GO:0002434 GO:0097193 GO:0001774 GO:0061518 GO:1905907 GO:1902430 GO:0043066 GO:0060548 GO:1905892 GO:1905895 GO:1902230 GO:0031333 GO:1903573 GO:0048812 GO:1902004 GO:0043065 GO:0045597 GO:0008284 GO:0010628 GO:2001244 GO:1902998 GO:1901216 GO:0051092 GO:0045429 GO:0032436 GO:0031334 GO:0048260 GO:1902949 GO:0032760 GO:2000060 GO:0017038 GO:0050821 GO:0061740 GO:1900221 GO:0042981 GO:0042127 GO:1901214 GO:1902847 GO:0009416 GO:0051788 GO:0035864 GO:0009615 GO:0009611 GO:0007283 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P10909} MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFHNMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTQQYNELLHSLQSKMLNTSSLLEQLNDQFTWVSQLANLTQGDDQYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME 447 P17698 Clusterin CLU 9940 None SL-0198 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}. UNIPROT P17698 Pfam PF01093 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}. GO:0042583 GO:0005737 GO:0005829 GO:0005576 GO:0043231 GO:0005743 GO:0005739 GO:0005634 GO:0099020 GO:0051082 GO:0002434 GO:1905907 GO:0043065 GO:0048260 GO:0050821 GO:0042127 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P10909} ISGKELQEMSTEGSKYVNKEIKNALKEVLQIKLVMEQGREQSSVMNVMPFPLLEPLNFHDVFQPFY 66 Q8N3K9 Cardiomyopathy-associated CMYA5 9606 None SL-0198 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}. UNIPROT Q8N3K9 UNIPROT A0PJB7 UNIPROT Q05CT4 UNIPROT Q2NKX1 UNIPROT Q2T9G9 UNIPROT Q69YQ8 UNIPROT Q69YQ9 UNIPROT Q6P517 UNIPROT Q6P5U3 UNIPROT Q7Z4I1 UNIPROT Q86T34 UNIPROT Q86T49 UNIPROT Q8N3S4 UNIPROT Q8N3S7 UNIPROT Q8NAG8 UNIPROT Q9UK88 Pfam PF00041 PROSITE PS50188 PROSITE PS50853 OMIM 612193 DisGeNET 202333 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}. O95295 EBI-5664244 0.00 P43686 EBI-1060801 0.00 Q7L1Q6 EBI-1074757 0.00 Q96EB6 EBI-2321764 0.40 Q9NTG7 EBI-2322825 0.40 O75923 EBI-5357119 0.50 P20807 EBI-5655093 0.00 Q8N3C7 EBI-5655585 0.00 P40189 EBI-5655920 0.00 Q8N3K9 EBI-5655903 0.00 Q14324 EBI-5660911 0.00 Q96CV9 EBI-5662034 0.00 Q16082 EBI-15487490 0.37 Q01968 EBI-16412116 0.35 Q02539 EBI-20922246 0.40 A2A935 EBI-21024514 0.35 GO:0005737 GO:0005829 GO:0043231 GO:0031430 GO:0016607 GO:0005634 GO:0048471 GO:0005886 GO:0016529 Unknown UniProt Sequence Analysis MASRDSNHAGESFLGSDGDEEATRELETEEESEGEEDETAAESEEEPDSRLSDQDEEGKIKQEYIISDPSFSMVTVQREDSGITWETNSSRSSTPWASEESQTSGVCSREGSTVNSPPGNVSFIVDEVKKVRKRTHKSKHGSPSLRRKGNRKRNSFESQDVPTNKKGSPLTSASQVLTTEKEKSYTGIYDKARKKKTTSNTPPITGAIYKEHKPLVLRPVYIGTVQYKIKMFNSVKEELIPLQFYGTLPKGYVIKEIHYRKGKDASISLEPDLDNSGSNTVSKTRKLVAQSIEDKVKEVFPPWRGALSKGSESLTLMFSHEDQKKIYADSPLNATSALEHTVPSYSSSGRAEQGIQLRHSQSVPQQPEDEAKPHEVEPPSVTPDTPATMFLRTTKEECELASPGTAASENDSSVSPSFANEVKKEDVYSAHHSISLEAASPGLAASTQDGLDPDQEQPDLTSIERAEPVSAKLTPTHPSVKGEKEENMLEPSISLSEPLMLEEPEKEEIETSLPIAITPEPEDSNLVEEEIVELDYPESPLVSEKPFPPHMSPEVEHKEEELILPLLAASSPEHVALSEEEREEIASVSTGSAFVSEYSVPQDLNHELQEQEGEPVPPSNVEAIAEHAVLSEEENEEFEAYSPAAAPTSESSLSPSTTEKTSENQSPLFSTVTPEYMVLSGDEASESGCYTPDSTSASEYSVPSLATKESLKKTIDRKSPLILKGVSEYMIPSEEKEDTGSFTPAVAPASEPSLSPSTTEKTSECQSPLPSTATSEHVVPSEGEDLGSERFTPDSKLISKYAAPLNATQESQKKIINEASQFKPKGISEHTVLSVDGKEVIGPSSPDLVVASEHSFPPHTTEMTSECQAPPLSATPSEYVVLSDEEAVELERYTPSSTSASEFSVPPYATPEAQEEEIVHRSLNLKGASSPMNLSEEDQEDIGPFSPDSAFVSEFSFPPYATQEAEKREFECDSPICLTSPSEHTILSDEDTEEAELFSPDSASQVSIPPFRISETEKNELEPDSLLTAVSASGYSCFSEADEEDIGSTAATPVSEQFSSSQKQKAETFPLMSPLEDLSLPPSTDKSEKAEIKPEIPTTSTSVSEYLILAQKQKTQAYLEPESEDLIPSHLTSEVEKGEREASSSVAAIPAALPAQSSIVKEETKPASPHSVLPDSVPAIKKEQEPTAALTLKAADEQMALSKVRKEEIVPDSQEATAHVSQDQKMEPQPPNVPESEMKYSVLPDMVDEPKKGVKPKLVLNVTSELEQRKLSKNEPEVIKPYSPLKETSLSGPEALSAVKMEMKHDSKITTTPIVLHSASSGVEKQVEHGPPALAFSALSEEIKKEIEPSSSTTTASVTKLDSNLTRAVKEEIPTDSSLITPVDRPVLTKVGKGELGSGLPPLVTSADEHSVLAEEDKVAIKGASPIETSSKHLAWSEAEKEIKFDSLPSVSSIAEHSVLSEVEAKEVKAGLPVIKTSSSQHSDKSEEARVEDKQDLLFSTVCDSERLVSSQKKSLMSTSEVLEPEHELPLSLWGEIKKKETELPSSQNVSPASKHIIPKGKDEETASSSPELENLASGLAPTLLLLSDDKNKPAVEVSSTAQGDFPSEKQDVALAELSLEPEKKDKPHQPLELPNAGSEFSSDLGRQSGSIGTKQAKSPITETEDSVLEKGPAELRSREGKEENRELCASSTMPAISELSSLLREESQNEEIKPFSPKIISLESKEPPASVAEGGNPEEFQPFTFSLKGLSEEVSHPADFKKGGNQEIGPLPPTGNLKAQVMGDILDKLSEETGHPNSSQVLQSITEPSKIAPSDLLVEQKKTEKALHSDQTVKLPDVSTSSEDKQDLGIKQFSLMRENLPLEQSKSFMTTKPADVKETKMEEFFISPKDENWMLGKPENVASQHEQRIAGSVQLDSSSSNELRPGQLKAAVSSKDHTCEVRKQVLPHSAEESHLSSQEAVSALDTSSGNTETLSSKSYSSEEVKLAEEPKSLVLAGNVERNIAEGKEIHSLMESESLLLEKANTELSWPSKEDSQEKIKLPPERFFQKPVSGLSVEQVKSETISSSVKTAHFPAEGVEPALGNEKEAHRSTPPFPEEKPLEESKMVQSKVIDDADEGKKPSPEVKIPTQRKPISSIHAREPQSPESPEVTQNPPTQPKVAKPDLPEEKGKKGISSFKSWMSSLFFGSSTPDNKVAEQEDLETQPSPSVEKAVTVIDPEGTIPTNFNVAEKPADHSLSEVKLKTADEPRGTLVKSGDGQNVKEKSMILSNVEDLQQPKFISEVSREDYGKKEISGDSEEMNINSVVTSADGENLEIQSYSLIGEKLVMEEAKTIVPPHVTDSKRVQKPAIAPPSKWNISIFKEEPRSDQKQKSLLSFDVVDKVPQQPKSASSNFASKNITKESEKPESIILPVEESKGSLIDFSEDRLKKEMQNPTSLKISEEETKLRSVSPTEKKDNLENRSYTLAEKKVLAEKQNSVAPLELRDSNEIGKTQITLGSRSTELKESKADAMPQHFYQNEDYNERPKIIVGSEKEKGEEKENQVYVLSEGKKQQEHQPYSVNVAESMSRESDISLGHSLGETQSFSLVKATSVTEKSEAMLAEAHPEIREAKAVGTQPHPLEESKVLVEKTKTFLPVALSCRDEIENHSLSQEGNLVLEKSSRDMPDHSEEKEQFRESELSKGGSVDITKETVKQGFQEKAVGTQPRPLEESKVLVEKTKTFLPVVLSCHDEIENHSLSQEGNLVLEKSSRDMPDHSEEKEQFKESELWKGGSVDITKESMKEGFPSKESERTLARPFDETKSSETPPYLLSPVKPQTLASGASPEINAVKKKEMPRSELTPERHTVHTIQTSKDDTSDVPKQSVLVSKHHLEAAEDTRVKEPLSSAKSNYAQFISNTSASNADKMVSNKEMPKEPEDTYAKGEDFTVTSKPAGLSEDQKTAFSIISEGCEILNIHAPAFISSIDQEESEQMQDKLEYLEEKASFKTIPLPDDSETVACHKTLKSRLEDEKVTPLKENKQKETHKTKEEISTDSETDLSFIQPTIPSEEDYFEKYTLIDYNISPDPEKQKAPQKLNVEEKLSKEVTEETISFPVSSVESALEHEYDLVKLDESFYGPEKGHNILSHPETQSQNSADRNVSKDTKRDVDSKSPGMPLFEAEEGVLSRTQIFPTTIKVIDPEFLEEPPALAFLYKDLYEEAVGEKKKEEETASEGDSVNSEASFPSRNSDTDDGTGIYFEKYILKDDILHDTSLTQKDQGQGLEEKRVGKDDSYQPIAAEGEIWGKFGTICREKSLEEQKGVYGEGESVDHVETVGNVAMQKKAPITEDVRVATQKISYAVPFEDTHHVLERADEAGSHGNEVGNASPEVNLNVPVQVSFPEEEFASGATHVQETSLEEPKILVPPEPSEERLRNSPVQDEYEFTESLHNEVVPQDILSEELSSESTPEDVLSQGKESFEHISENEFASEAEQSTPAEQKELGSERKEEDQLSSEVVTEKAQKELKKSQIDTYCYTCKCPISATDKVFGTHKDHEVSTLDTAISAVKVQLAEFLENLQEKSLRIEAFVSEIESFFNTIEENCSKNEKRLEEQNEEMMKKVLAQYDEKAQSFEEVKKKKMEFLHEQMVHFLQSMDTAKDTLETIVREAEELDEAVFLTSFEEINERLLSAMESTASLEKMPAAFSLFEHYDDSSARSDQMLKQVAVPQPPRLEPQEPNSATSTTIAVYWSMNKEDVIDSFQVYCMEEPQDDQEVNELVEEYRLTVKESYCIFEDLEPDRCYQVWVMAVNFTGCSLPSERAIFRTAPSTPVIRAEDCTVCWNTATIRWRPTTPEATETYTLEYCRQHSPEGEGLRSFSGIKGLQLKVNLQPNDNYFFYVRAINAFGTSEQSEAALISTRGTRFLLLRETAHPALHISSSGTVISFGERRRLTEIPSVLGEELPSCGQHYWETTVTDCPAYRLGICSSSAVQAGALGQGETSWYMHCSEPQRYTFFYSGIVSDVHVTERPARVGILLDYNNQRLIFINAESEQLLFIIRHRFNEGVHPAFALEKPGKCTLHLGIEPPDSVRHK 4069 Q70KF4 Cardiomyopathy-associated Cmya5 10090 None SL-0198 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}. UNIPROT Q70KF4 UNIPROT Q70X91 UNIPROT Q9CV01 UNIPROT Q9CV02 UNIPROT Q9ER93 UNIPROT Q9ER96 Pfam PF00041 PROSITE PS50188 PROSITE PS50853 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}. Q91WZ8 EBI-782286 0.59 Q70KF4 EBI-782304 0.37 O88609 EBI-13951518 0.35 GO:0043034 GO:0005737 GO:0005829 GO:0043231 GO:0031430 GO:0016607 GO:0005634 GO:0048471 GO:0005886 GO:0016529 GO:0042802 GO:0070885 GO:0032515 GO:0014733 Unknown UniProt Sequence Analysis MESGDSGLAAQGFLGWGADEEVAQELETEEESEGEGEETAAESEEEPDARLSDEDEEGKTKQECIVSDPSFSMVAVQREDSGITWETNSSRSSTPWASGESQTSGICSLEGSALTSPPGSVSFIMDEVKRTRKRTQKSKRGSPSLRRKGSKKRNSLESQDVLTNQEDGPSISESPVLNIENEKSSIGTYDKTRRKKTASNTPPITGAIYKEHKPLVLKPVYIGTVQYKIKMFNSVKEELIPLQFYGTLPKGYVIKEIHYRRGKDSSISLEPDLSNGGSNIVPQRKLAQSPEEDKVRELAPPWRGALSKGSRTSLFSHEEQKKTYADSNLNVPSSTEHAFPSSARNDTADQEENLSLPQMMPQQPADESKTHRMEPPSIPATMVLERAKEELEQNAQGKESSEDDASVLTGSADDVQQEGLVSVNHSMPWEAEKESLETGPPRPAPAIQEKFEPDMEGLEPISTEKTEQASEYVTSSEPIVHREEEHAPEPIVHREEEHAPEPIVHREEEHAPEPESIVHREEEHAPESIVHREEEHAPEPVPIVHREEEHAPEPESIVHREEEHAPEPIVHRDKGHALEPIVHREEEHAPEPIVHRDEGHAPEPIVHREEEHVPEPESIVRKGEEHAPEPIVHREEEQVPEPESIVHREEEHAPEPIVHREEEQVPEPESIVHREEEHAPEPMVLREEHAPEPIVRREEEHAPEPIVHREEEHAPEPMVHRKAQQLERGVETSTPITDITEPEDSSLEEEIIELDYPESPLASKETSPSPLSPEVEHRKEPILPTQMTFTPERITLSEEEREENESVSTDSAFVSEYSVLQDLNHTPEKLEVEAVSVSDVKSSNEPAVFSEDDEERESYSPAMTSVSEQSLSPSTTEKTSAIQSPLFSTVSPVLSGDEASENVCHSPESESAAEYSVPAHAQELLLKTGDHKLPLKSQRVSEPIIQAEDEKEDIGLLPPAALSQAVLSEDESLGSGSFASDSKLPFKPSVSQNATRESPQKTIDDMPQFKPRGLSDPATLLEEEKEAIGVGLSSSNEVSAVECALPPQTTELLSESHAPPPWAISSEQVVQSEEGSRDQQRGSFSSTPELGHTSLLLKGASSPTGLSEQGQEEDNIGPLSPDSAFASEFSFSPYPTQELEKRELGRDSPLCLTSPSEQTVLSEEDTEEADLFSPDSASQVSIPPYRIAETEQNKVEPDELLPTRSAPDYPYFSEADEEEAGSSVVTLVPEHSEPSQEREESSPCRPVFEDLSLPPSADKTGQAETMSDVPTISTSVSEYLILARQAKTQASLEPEAEDLVPPPTSGWEKRDAKSSLPAVTIAASSSALSSVVKEETTSVLPTSQPSVSPESTCVLKPEQEPTAPLTLTSADEQMALPRVGREKAVLDSQEATAHKSQDQTPEPRLPNVPGSGMKYSVLSDLGDEPKADVKLNLAPTVTSELEQRMLSKNEPEVAKPHSPPEETSISGPKVLSAVKTEVKQESKITRELPAASSGRERGAEHSPPVPPALPALTEETGKDTEASSSATTVPVTKLDSNSTKLGRDEVLTDPSLASPVEHPGLKGIGKSELGSGLPLPSMSASEVLRPEPKLPVNSGVEVEREDNEPPPLQVSPTSKPTVPNDKHEEITRSPDSENLVSDDLAPTLLAFRHEMNRQAEETSSPVPGSFLSGEQELIKLPPEPEKHKQLSEVPTAGSELIDSRDRDRSLGIEPVKPIGTEPGPSILEKGPAELQRRGKEQEENRKLPVPASAPLETASFDLPIEQKEPKRTLHEGQAVEVPDESSSSADKPELGVKQLAEKKENLEQPKPFVTTERASVTGSKVKESLISPKDNIWMLEKPDGLVNQHEDRKPGTGQLESSESTDLMSEKLGAASLDTDHTSETRNQETSKAPVSGEKLSQEPRRVQSKAVDDSEEGRKLASGNVEVLTQSKSVPAVKAKATPQPPETPEVTQKPSEKSLVTEQGLPAEKGKKGISSFKSWMSSLLFGSSIPDSKVSDNEDLETRPGPSVEKAVPAIEPKGTVPAEVNIAEKPAVHSLPEVTVKLAEEPKGVSVKSSISQDLKEKLTFLSNEDVLKQPKSNSENYGQKELPGFSEGMGESLATSVGDKHPGIHPCSPMGEKVGMEEAQNMAPLHITESQRRQKPEVSPPSMWNISARKEEPSSDHKETWLSSSDVVDRMPQKPKSAQSAFTRMNSEEPASMILPVESKGSLSDLGEDRLRQEMPKPTSLEHCEEEVERPTEEKDGWETRSFSLAGKRGLAEKQEIMAPLELRENEAVGELQRMPESRPFKLEESKAAERLEQRISPTEKLMEKPSKTLALDRREKEVQEWVFSEGEKQEYPPAAMPVPGASAVSLDKAQPHLLAKPTPVVEKPEHIVTEVYPEIRERKAAETQPHPQEEGKTLVEKTKVSRVESPHGEETDGHSLTQEGNLELEKSGESRVDLKEERRRFVMPELPLGASVAAEDGSVQPRPLSKDAARASDMTDETKHLGTPPTQPSAVEPQTLVLGTSVEHAVKKQETWSDRPTVHTFQTSKDDTEEMLKQSVLISKHHLEAVEDVHRNEPPSSAASNYAQFMLSASEISADGVPPMGGTAQEPEGTSVKDEEFSVTSKPAGLSEDQKSAFSIISEGCEILNIHAPAFIPSVDQEESEQMQDKLQYLEEKASFKSISVHDEKKAAASHKTQKSKLEVPDRKITSLKENKTKETHKTKEEIATDSGMGDFTPIQPTVSGEEDYFEKYTLIDYNLSPGSGKQKSTVEESSEEATKTLTSFPESSAEQALDHEYNLVKLDESFYGPEKDDSKLSHAEMQKSLAIQKPDDRNAPKGISRDVDSRSPGMPLFDVEEGVLSKRQIFPTTPKAVNPELLEEPPALSFFYKDLYEGACGEKNEGETASEGDSVDSETSFPRRHSDTDDGPGMYFEKYILKDDILHDESVTQEDQGQGLEEKPVGEEDSQQLRVAEREIRRKPETSFWEKNLEEQHKVVGREGEPTGHMETLDEAAMQQKAPITEQVRAVTQKMSYAVPFQDTRCVLESEPSSQGNEAGNASPDVNLNVPVQVSFPEEESAAGATYAPEVLQERLVPSVSREERLHNTPVQDEYDFVGSLNQEAASQAILPEEPGSESSPKEVLSQGSESFEHIREQELTSEGEPRMSASQEVWDRTEDQSARESVTAKTQKEPKKTQAESYCYTCKSLVSEMDKALDIHKDHEVSALDTAISAVKVQLGEFLENLQEKSLRIEAFVSEIESFFNTIEEKCSKNEKRLEMQNEEMMKRVLAQYDEKAQSFEEVKKKKMEFLHDQMVHFLQSMDTAKDTLETIVREAEELDETVFLASFEEINERLLSAMESTASLENMPAAFSLFEHYDDSSARSDQMLKQVAVPQPPRLEPQEPSSATSTTIAVYWSVNKEDVVDSFQVYCVEEPQDDQEINELVEEYRLTVKESCCIFEDLEPDRCYQVWVMAVNFTGCSLPSERAIFRTAPSTPVIHVEDCTVCWNTATVRWRPANPEATETYTLEYCRQHSPEGEGLRSFSGIKGHQLKVNLPPNDNYFFYVRATNASGTSEQSEAALISTRGTRFLLLRETAHPALQISANGTVISFSERRRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGETSWYMHCSEPQRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFALEKPGRCTLHLGLEPPDSVRHK 3739 G7IBJ4 Protein CNGC15A 3880 None SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000255}. UNIPROT G7IBJ4 Pfam PF00027 Pfam PF00520 PROSITE PS50042 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}. GO:0016021 GO:0031965 GO:0005262 GO:0044325 GO:0005249 GO:0036377 GO:0009877 Transmembrane UniProt Sequence Analysis {ECO:0000255} MASVISRAVRFHDDLEKEKLQEGEESHMEMRAYEMSSEYKHGKDAINKPSSNGRGLSRVFSEDYDAGEILVFDPRGPRINLWNKIFLAACLISLFVDPLFFYLPVAKKEKCIDMSIGLEVSLTIIRTFVDAFYIIHIYIRFQTAYIAPSSRVSGRGELIIDSSKIASNYMKKELWSDLVAALPLPQVLIWAVIPNIKGSEMIASRHVVRLVSIFQYLLRLYLIYPLSSKITKASGVMMEKAWAGAAYYLTLYMLASHVLGSTWYLLSIERQDECWKKACTLQYPHCQYHYLDCQSLSDPNRNAWLKSSNLSGLCDQNSHFFQFGIFDDAVTLEITSSNFLTKYYYCLWWGLRNLSSSGENLLTSTHVAEINFAVIVAILGLVLFALLIGNMQTYLQSTTIRLEEWRIRRTDTERWMHHRQLPHYLKENVRRHDQFRWVATRGVDEEAILRDLPVDLRRDIKRHLCLNLVRQVPLFDQMDDRMLDAICERLKPTLCTPGTCIVREGDPVDEMLFIVRGRLDSCTTNGGRTGFFNTCRIGSGDFCGEELLPWALDPRPTAVLPSSTRTVRAITEVEAFALIAEDLKFVAAQFRRLHSKQLRQTFRFYSHQWRTWAACFIQAAWFRYKRMKETNEVKEKENLMMMSNVKYYGNDDSQYFSAPLQVPKGSSYSMYSGKLVGSLRRGRSMRYGSELDMLGTLRKPIEPDFNDDGD 710 G7JND3 Protein CNGC15B 3880 None SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000255}. UNIPROT G7JND3 UNIPROT A0A0C3WX45 Pfam PF00027 Pfam PF00520 PROSITE PS50042 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}. GO:0016021 GO:0031965 GO:0005262 GO:0044325 GO:0005249 GO:0036377 GO:0009877 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVTPKFMSDLFEGDHLELAKLTSPNGDNGIKFNEKHVAPRVLSRVFSEDYKRVKRRRRIFDPRGQTIHQWNKIFLVACLISLFVDPLFFYLPIVQDEVCIDIGIAVEVFLIIIRSIADVFYVIHIFMRFHTAYVAPSSRVFGRGELVIDSSKIASRYLHKGFFLDFIAALPLPQVLIWIVIPNLGGSTIANTKNVLRFIIIIQYLPRLFLIFPLSSQIVKATGVVTETAWAGAAYNLMLYMLASHVLGACWYLLSIERQEACWKSVCKLEESSCQFDFFDCNMVKDSLRVSWFVTSNVTNLCSPNSLFYQFGIYGDAVTSKVTTSAFFNKYFFCLWWGLRNLSSLGQGLLTSTFVGEIMFAIVIATLGLVLFALLIGNMQTYLQSTTVRLEEWRVKRTDTEQWMHHRQLPQELRQSVRKYDQYKWIATRGVDEESLLRGLPLDLRRDIKRHLCLELVRRVPLFDAMDERMLDAICERLKPALCTENTYLVREGDPVNEMLFIIRGNLDSYTTDGGRTGFFNSCRIGPGDFCGEELLTWALDPRPTMVIPSSTRTVKAISEVEAFALIAEDLKFVASQFRRLHSKQLRNKLRFHSHQWRTWAACFIQVAWRRTIQEKKGSC 620 A0A072VMJ3 Protein CNGC15C 3880 None SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000255}. UNIPROT A0A072VMJ3 Pfam PF00520 PROSITE PS50042 PROSITE PS50096 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}. GO:0016021 GO:0031965 GO:0044325 GO:0005249 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGFDNPRSERFEDDPEISKIPTTSGVKVKYHIDGTQIPEQSSKKSRKNETRNKFLKTRVLSRVFSEDYERVKKRVLVLDPRGQLIHRWNKIFLVACLVSLFVDPLFFYLPVVREEVCIDIGKTLEVILTVVRSFGDLFYIVQICMKFRTAYVAPSSKVFGRGELVLTYSKIALRYFSKGFWLDFIAALPLPQVLIWIIIPTLRGSTMANTKNVLRFFIIFQYIPRLYLIFPLSSQIVKATGVVTETAWAGAAYNLMLYMLASHILGACWYLLSIERQEACWKSVCNMEKSNCQYGFFNCHSIKDAPRVAWFIASNVTNLCSPNAGFYPFGIYADAMTSKVTSSPFFNKYFYCLWWGLRNLSSLGQGLLTSTFIGEIMVAIVVATLGLVLFALLIGNMQTYLQSITVRLEEWRVKRTDTEQWMHHRQLPPELRESIRKYNQYKWVATRGVEEEDLLKGLPLDLRREIKRHLCLELVRGVPLFDQMDERMLDAICERLKPALCTEGTYLVREGDPVNEMLFIIRGHLDSYTTNGGRDGFFNSCRIGPGDFCGEELLTWALDPRPSVILPSSTRTVKAFSEVEAFALIAEDLKFVASQFRRLHSKQLRHKFRFYSHQWRTWAACFIQAAWRRHKKRKEAAELRAKENLVAASEAENEIAKKYGKGFVVYGTRVARSTRKGVNMHSGTNSGVVSSLQKPTEPDFSDE 703 Q1RMV9 CTD CTDNEP1 9913 None SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT Q1RMV9 Pfam PF03031 PROSITE PS50969 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}. GO:0005737 GO:0005789 GO:0016021 GO:0005811 GO:0071595 GO:0005635 GO:0031965 GO:0017018 GO:0004721 GO:0004722 GO:0060070 GO:0007276 GO:0007498 GO:0006998 GO:0090263 GO:0010867 GO:0006470 GO:0034504 Transmembrane UniProt Sequence Analysis {ECO:0000255} MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPVSRNRLSQVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQHCTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQHRLW 244 Q20432 CTD cnep 6239 None SL-0178 Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:32271860}. UNIPROT Q20432 UNIPROT H1ZUW4 Pfam PF03031 PROSITE PS50969 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}. GO:0005737 GO:0005789 GO:0016021 GO:0071595 GO:0005635 GO:0031965 GO:0017018 GO:0004721 GO:0004722 GO:0006998 GO:0031468 GO:0010867 GO:0006470 GO:0051783 Transmembrane UniProt Sequence Analysis {ECO:0000255} MTTIAQSVFCFLAGFFNFFLLYFRKTSRAYCKYQVVKYHSNIPMSPLTTHRLLTVKRKILVLDLDETLIHSHHDGVLRQTVKPGTPSDFTIRVVIDRHPVKFSVHERPHVDYFLSVVSQWYELVVFTASMEVYGTSVADRLDRGRGILKRRYFRQHCTMEVGGYTKDLSAIHPDLSSICILDNSPGAYRKFPHNAIPIPSWFSDPNDTCLLNLLPFLDALRFTSDVRSVLSRNMQALPETQSVQYY 246 O95476 CTD CTDNEP1 9606 None SL-0178 SL-0182 Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein. UNIPROT O95476 UNIPROT D3DTN7 UNIPROT Q96GQ9 Pfam PF03031 PROSITE PS50969 OMIM 610684 DisGeNET 23399 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}. O00165 EBI-27113178 0.35 O15173 EBI-27115722 0.27 O94901 EBI-27115722 0.27 Q8N9A8 EBI-5323532 0.46 Q91ZP3 EBI-5323701 0.27 Q9WH76 EBI-10823914 0.58 P08563 EBI-11478420 0.40 Q9UHD9 EBI-24288048 0.56 P81408 EBI-21535449 0.35 O95897 EBI-21570405 0.35 Q6UX71 EBI-21588922 0.35 P58658 EBI-21588759 0.35 Q9Y5M8 EBI-21633655 0.35 O00624 EBI-21654627 0.35 P09619 EBI-21694943 0.35 Q8WV48 EBI-21710200 0.35 O60602 EBI-21773313 0.35 P01911 EBI-21815688 0.35 A2ICZ0 EBI-25685386 0.35 P0DTD8 EBI-25687199 0.35 Q7TFA1 EBI-25688644 0.35 Q9BUF5 EBI-27113178 0.35 P16615 EBI-27113178 0.35 Q96A33 EBI-27115722 0.27 Q8N766 EBI-27115722 0.27 P18031 EBI-27115722 0.27 P51648 EBI-27115722 0.27 Q9BTX1 EBI-27115722 0.27 Q8NEN9 EBI-27115722 0.27 Q96CP6 EBI-27115722 0.27 Q9NRG9 EBI-27115722 0.27 Q9HBM0 EBI-27115722 0.27 Q9NXE4 EBI-27115722 0.27 Q9P0I2 EBI-27115722 0.27 Q15904 EBI-27115722 0.27 Q8WXH0 EBI-27115722 0.27 Q9NX40 EBI-27115722 0.27 Q86Y07 EBI-27115722 0.27 P28288 EBI-27115722 0.27 O60858 EBI-27115722 0.27 Q9HC62 EBI-27115722 0.27 Q9Y2U8 EBI-27115722 0.27 Q9UH99 EBI-27115722 0.27 Q96RL7 EBI-27115722 0.27 Q14573 EBI-27115722 0.27 P16435 EBI-27115722 0.27 Q14571 EBI-27115722 0.27 Q14643 EBI-27115722 0.27 Q5T8D3 EBI-27115722 0.27 GO:0005737 GO:0005789 GO:0016021 GO:0005811 GO:0071595 GO:0005635 GO:0031965 GO:0017018 GO:0004721 GO:0004722 GO:0060070 GO:0007276 GO:0007498 GO:0007077 GO:0006998 GO:0090263 GO:0010867 GO:0006470 GO:0034504 Transmembrane UniProt Sequence Analysis {ECO:0000255} MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPVSRNRLAQVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQHCTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQHRLW 244 Q3TP92 CTD Ctdnep1 10090 None SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT Q3TP92 UNIPROT Q5NCW4 UNIPROT Q8VEL4 Pfam PF03031 PROSITE PS50969 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}. GO:0005737 GO:0005789 GO:0016021 GO:0005811 GO:0071595 GO:0005635 GO:0031965 GO:0005634 GO:0017018 GO:0004721 GO:0004722 GO:0060070 GO:0007276 GO:0007498 GO:0006998 GO:0090263 GO:0010867 GO:0006470 GO:0034504 Transmembrane UniProt Sequence Analysis {ECO:0000255} MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPLSRNRLAQVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQHCTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQHRLW 244 Q3B7T6 CTD Ctdnep1 10116 None SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT Q3B7T6 UNIPROT Q5M952 Pfam PF03031 PROSITE PS50969 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}. GO:0005737 GO:0005789 GO:0016021 GO:0071595 GO:0005635 GO:0031965 GO:0005634 GO:0017018 GO:0004721 GO:0004722 GO:0060070 GO:0007276 GO:0007498 GO:0006998 GO:0090263 GO:0010867 GO:0006470 GO:0034504 Transmembrane UniProt Sequence Analysis {ECO:0000255} MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPLSRNRLAQVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQHCTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQHRLW 244 Q8JIL9 CTD ctdnep1 8355 None SL-0198 Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17141153}. UNIPROT Q8JIL9 UNIPROT Q640I6 Pfam PF03031 PROSITE PS50969 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}. GO:0005737 GO:0005789 GO:0016021 GO:0071595 GO:0005635 GO:0031965 GO:0048471 GO:0017018 GO:0004722 GO:0030154 GO:0007399 GO:0006998 GO:0010867 GO:0006470 Transmembrane UniProt Sequence Analysis {ECO:0000255} MMRTPGLLGLRGFVAFAAKLWSFVLYLLRRQFRTIIQYQTVRYDVLPLSPASRNRLSQVKRKVLVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNNKGVLRRRFYRQHCTLELGSYIKDLSVVHSDLSSVVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQHRLW 244 Q28HW9 CTD ctdnep1 8364 None SL-0198 Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q28HW9 Pfam PF03031 PROSITE PS50969 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}. GO:0005737 GO:0005789 GO:0016021 GO:0071595 GO:0005635 GO:0031965 GO:0048471 GO:0017018 GO:0004721 GO:0004722 GO:0030154 GO:0007399 GO:0006998 GO:0010867 GO:0006470 Transmembrane UniProt Sequence Analysis {ECO:0000255} MMRTPGLLGLRGFVAFAAKLWSFVLYLLRRQVRTIIQYQTVRYDVLPLSPASRNRLSQVKRKVLVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNNRGVLRRRFYRQHCTLELGSYIKDLSVVHSDLSSVVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQHRLW 244 Q5U395 CTD ctdnep1a 7955 None SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT Q5U395 Pfam PF03031 PROSITE PS50969 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}. GO:0005737 GO:0005789 GO:0016021 GO:0071595 GO:0005635 GO:0031965 GO:0017018 GO:0004721 GO:0004722 GO:0006998 GO:0010867 GO:0006470 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLKTRQCLLGIRTFLGVTSRIWSFFLYILRKHLRTIIQYQTVRYDILPLSPISRNRLNAVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNNRGILKRRYYRQHCTLDLGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTSDVRSVLSRNLHQHRLW 245 Q5U3T3 CTD ctdnep1b 7955 None SL-0178 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT Q5U3T3 Pfam PF03031 PROSITE PS50969 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}. GO:0005737 GO:0005789 GO:0016021 GO:0071595 GO:0005635 GO:0031965 GO:0017018 GO:0004721 GO:0004722 GO:0060322 GO:0006998 GO:0010867 GO:0006470 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLKTRQCLLGVRTFHGVTSRIWSFFLYILRKHIRTIIQYQTVRYDILSLSPISRNRLNNVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNNKAILKRRYYRQHCTLDSGSYIKDLSVVHDDLSSVVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFPADVRSVLSRNLHQHRLW 245 Q9BV73 Centrosome-associated CEP250 9606 None SL-0198 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. UNIPROT Q9BV73 UNIPROT E1P5Q3 UNIPROT O14812 UNIPROT O60588 UNIPROT Q9H450 PDB 6OQA OMIM 609689 OMIM 618358 DisGeNET 11190 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}. 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. A0A142I5B9 EBI-20626135 0.35 K9N7C7 EBI-26374676 0.35 O08788 EBI-11066549 0.35 P0C6X7 EBI-26377017 0.35 P0DTD1 EBI-26950012 0.56 Q7Z3B4 EBI-21639232 0.35 Q91B85 EBI-11422888 0.37 Q96CV9 EBI-25910879 0.56 Q6VMQ6 EBI-7244323 0.37 Q15008 EBI-1066651 0.00 Q6UVJ0 EBI-1570162 0.27 Q04917 EBI-1644092 0.35 O88566 EBI-7866996 0.46 P63104 EBI-8063698 0.35 Q8ZGW9 EBI-2872616 0.00 Q9H0K1 EBI-2909672 0.62 Q9HAU0 EBI-3447325 0.00 Q9WMX2 EBI-9082134 0.37 P35579 EBI-11144042 0.35 Q9E7P0 EBI-11422880 0.37 Q96KS9 EBI-21503766 0.35 Q5SW79 EBI-21644990 0.35 Q9NV56 EBI-21683633 0.35 Q9H7C4 EBI-21702482 0.35 Q96ES7 EBI-21781962 0.35 Q96GS4 EBI-21795617 0.35 Q15311 EBI-21818654 0.35 Q96JB2 EBI-21879136 0.35 Q9NQ48 EBI-21889038 0.35 O94986 EBI-16171575 0.35 P06576 EBI-20904592 0.40 P27824 EBI-20908048 0.40 Q9UII2 EBI-20933940 0.40 P0DTC6 EBI-26495724 0.35 Q13547 EBI-26367383 0.35 P53355 EBI-28938354 0.35 GO:0005814 GO:0005813 GO:0036064 GO:0005829 GO:0070062 GO:0005815 GO:0048471 GO:0001917 GO:0001750 GO:0032991 GO:0008022 GO:0019904 GO:0019901 GO:0010457 GO:0060271 GO:0050908 GO:0000278 GO:1905515 GO:1904781 GO:0008104 GO:0071539 GO:0033365 GO:0030997 Unknown UniProt Sequence Analysis METRSPGLNNMKPQSLQLVLEEQVLALQQQMAENQAASWRKLKNSQEAQQRQATLVRKLQAKVLQYRSWCQELEKRLEATGGPIPQRWENVEEPNLDELLVRLEEEQQRCESLAEVNTQLRLHMEKADVVNKALREDVEKLTVDWSRARDELMRKESQWQMEQEFFKGYLKGEHGRLLSLWREVVTFRRHFLEMKSATDRDLMELKAEHVRLSGSLLTCCLRLTVGAQSREPNGSGRMDGREPAQLLLLLAKTQELEKEAHERSQELIQLKSQGDLEKAELQDRVTELSALLTQSQKQNEDYEKMIKALRETVEILETNHTELMEHEASLSRNAQEEKLSLQQVIKDITQVMVEEGDNIAQGSGHENSLELDSSIFSQFDYQDADKALTLVRSVLTRRRQAVQDLRQQLAGCQEAVNLLQQQHDQWEEEGKALRQRLQKLTGERDTLAGQTVDLQGEVDSLSKERELLQKAREELRQQLEVLEQEAWRLRRVNVELQLQGDSAQGQKEEQQEELHLAVRERERLQEMLMGLEAKQSESLSELITLREALESSHLEGELLRQEQTEVTAALARAEQSIAELSSSENTLKTEVADLRAAAVKLSALNEALALDKVGLNQQLLQLEEENQSVCSRMEAAEQARNALQVDLAEAEKRREALWEKNTHLEAQLQKAEEAGAELQADLRDIQEEKEEIQKKLSESRHQQEAATTQLEQLHQEAKRQEEVLARAVQEKEALVREKAALEVRLQAVERDRQDLAEQLQGLSSAKELLESSLFEAQQQNSVIEVTKGQLEVQIQTVTQAKEVIQGEVRCLKLELDTERSQAEQERDAAARQLAQAEQEGKTALEQQKAAHEKEVNQLREKWEKERSWHQQELAKALESLEREKMELEMRLKEQQTEMEAIQAQREEERTQAESALCQMQLETEKERVSLLETLLQTQKELADASQQLERLRQDMKVQKLKEQETTGILQTQLQEAQRELKEAARQHRDDLAALQEESSSLLQDKMDLQKQVEDLKSQLVAQDDSQRLVEQEVQEKLRETQEYNRIQKELEREKASLTLSLMEKEQRLLVLQEADSIRQQELSALRQDMQEAQGEQKELSAQMELLRQEVKEKEADFLAQEAQLLEELEASHITEQQLRASLWAQEAKAAQLQLRLRSTESQLEALAAEQQPGNQAQAQAQLASLYSALQQALGSVCESRPELSGGGDSAPSVWGLEPDQNGARSLFKRGPLLTALSAEAVASALHKLHQDLWKTQQTRDVLRDQVQKLEERLTDTEAEKSQVHTELQDLQRQLSQNQEEKSKWEGKQNSLESELMELHETMASLQSRLRRAELQRMEAQGERELLQAAKENLTAQVEHLQAAVVEARAQASAAGILEEDLRTARSALKLKNEEVESERERAQALQEQGELKVAQGKALQENLALLTQTLAEREEEVETLRGQIQELEKQREMQKAALELLSLDLKKRNQEVDLQQEQIQELEKCRSVLEHLPMAVQEREQKLTVQREQIRELEKDRETQRNVLEHQLLELEKKDQMIESQRGQVQDLKKQLVTLECLALELEENHHKMECQQKLIKELEGQRETQRVALTHLTLDLEERSQELQAQSSQIHDLESHSTVLARELQERDQEVKSQREQIEELQRQKEHLTQDLERRDQELMLQKERIQVLEDQRTRQTKILEEDLEQIKLSLRERGRELTTQRQLMQERAEEGKGPSKAQRGSLEHMKLILRDKEKEVECQQEHIHELQELKDQLEQQLQGLHRKVGETSLLLSQREQEIVVLQQQLQEAREQGELKEQSLQSQLDEAQRALAQRDQELEALQQEQQQAQGQEERVKEKADALQGALEQAHMTLKERHGELQDHKEQARRLEEELAVEGRRVQALEEVLGDLRAESREQEKALLALQQQCAEQAQEHEVETRALQDSWLQAQAVLKERDQELEALRAESQSSRHQEEAARARAEALQEALGKAHAALQGKEQHLLEQAELSRSLEASTATLQASLDACQAHSRQLEEALRIQEGEIQDQDLRYQEDVQQLQQALAQRDEELRHQQEREQLLEKSLAQRVQENMIQEKQNLGQEREEEEIRGLHQSVRELQLTLAQKEQEILELRETQQRNNLEALPHSHKTSPMEEQSLKLDSLEPRLQRELERLQAALRQTEAREIEWREKAQDLALSLAQTKASVSSLQEVAMFLQASVLERDSEQQRLQDELELTRRALEKERLHSPGATSTAELGSRGEQGVQLGEVSGVEAEPSPDGMEKQSWRQRLEHLQQAVARLEIDRSRLQRHNVQLRSTLEQVERERRKLKREAMRAAQAGSLEISKATASSPTQQDGRGQKNSDAKCVAELQKEVVLLQAQLTLERKQKQDYITRSAQTSRELAGLHHSLSHSLLAVAQAPEATVLEAETRRLDESLTQSLTSPGPVLLHPSPSTTQAASR 2442 Q60952 Centrosome-associated Cep250 10090 None SL-0198 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. UNIPROT Q60952 UNIPROT E9QMB2 UNIPROT Q2I8G3 UNIPROT Q3UTR4 UNIPROT Q6PFF6 UNIPROT Q8BLC6 May be involved in ciliogenesis. Probably plays an important role in centrosome cohesion during interphase. {ECO:0000250|UniProtKB:Q9BV73}. Q8BH43 EBI-651063 0.37 Q9P2X0 EBI-11075169 0.35 Q8NFH4 EBI-11075169 0.35 Q5JTD0 EBI-11075169 0.35 P53618 EBI-11075169 0.35 P13861 EBI-11075169 0.35 Q8IYS2 EBI-11075169 0.35 Q8BHC1 EBI-11568621 0.35 GO:0005814 GO:0005813 GO:0036064 GO:0048471 GO:0001917 GO:0001750 GO:0032991 GO:0031616 GO:0008022 GO:0019904 GO:0019901 GO:0010457 GO:0060271 GO:0050908 GO:0000278 GO:1905515 GO:1904781 GO:0008104 GO:0033365 GO:0030997 Unknown UniProt Sequence Analysis METGSPGLNMKPQSLQLVLEGQVLALQQQMAENQAASWRKLKNSQEAQKRQATLVRKLQAKVLQYRSWCQDLEKRLEATGGLIPQRWESVEEPNLEQLLIRLEEEQQRCESLVEVNTELRLHMEKADVVNKALQEDVEKLTVDWSRARDELVRKESQWRMEQEFFKGYLRGEHGRLLNLWREVVTFRRHFLKMKSATDRDLTELKAEHARLSGSLLTCCLRLTLRAQSRESSGSGRTEESEPARLLLLVAKTQALEKEAHEKSQELMQLKSHGDLEKAELQDRVTELSALLTQSQKQNEDYEKMVKALRETMEILETNHAELMEHEASLSRNAQEEKLSLQQVIKAITQALASVEEEDTVTQSSGHEDSLQSDCNGLSQFDPQDPDRALTLVQSVLTRRQQAVQDLRQQLSGCQEAMSFLQQQHDQWEEEGRALREKLQKLTGERDALAGQTVGLQGEVDSLSRERELLQKARGELQQQLEVLEQEAWRLRRMNMELQLQGDSAQGEKLEQQEELHLAVRERERLQETLVGLEAKQSESLSELLTLREALESSRLEGELLKQERVEVAAALARAEQSIVELSGSENSLKAEVADLRAAAVKLGALNEALALDKVELNQQLLQLEQENQSLCSRVEAAEQLRSALQVDLAEAERRREALWEKKTQLETQLQKAEEAGAELQAELRGTREEKEELKDKLSEAHHQQETATAHLEQLHQDAERQEETLARAVQEKEALVRERAALEVRLQAVERDRQDLTEHVLGLRSAKEQLESNLFEAQQQNSVIQVTKGQLEVQIQTIIQAKEVIQGEVKCLKLELDAERTRAEQEWDAVARQLAQAEQEGQASLERQKVAHEEEVNRLQEKWEKERSWLQQELDKTLETLERERAELETKLREQQTEMEAIRAQREEERSQADSALYQMQLETEKERVSLLETLLRTQKELADASQQLERLRQDMKIQKLKEQETTGMLQAQLQETQQELKEAAQQHRDDLAAFQKDKLDLQKQVEDLMSQLVAHDDSQRLVKEEIEEKVKVAQECSRIQKELEKENASLALSLVEKEKRLLILQEADSVRQQELSSLRQDIQEAQEGQRELGVQVELLRQEVKEKEADFVAREAQLLEELEASRVAEQQLRASLWAQEAKATQLQLQLRSTESQLEALVAEQQPENQAQAQLASLCSVLQQALGSACESRPELRGGGDSAPTLWGPDPDQNGASRLFKRWSLPTALSPEAVALALQKLHQDVWKARQARDDLRDQVQKLVQRLTDTEAQKSQVHSELQDLQRQLSQSQEEKSKWEGRQNSLESELRDLHETAASLQSRLRQAELQKMEAQNDRELLQASKEKLSAQVEHLQACVAEAQAQADAAAVLEEDLRTARSALKLKNEELESERERAQALQEQGELKVAQGKALQENLALLAQTLSNREREVETLQAEVQELEKQREMQKAALELLSLDLKKRSREVDLQQEQIQELEQCRSVLEHLPMAVQEREQKLSVQRDQIRELENDREAQRSVLEHQLLDLEQKAQVIESQRGQIQDLKKQLGTLECLALELEESHHKVESQQKMITELEGQREMQRVALTHLTLDLEERSQELQAQSSQLHELENHSTHLAKELQERDQEVTSQRQQIDELQKQQEQLAQALERKGQELVLQKERIQVLEDQRTLQTKILEEDLEQIKHSLRERSQELASQWQLVHERADDGKSPSKGQRGSLEHLKLILRDKEKEVECQQERIQELQGHMGQLEQQLQGLHRKVGETSLLLTHREQETATLQQHLQEAKEQGELREQVLQGQLEEAQRDLAQRDHELETLRQEKQQTQDQEESMKLKTSALQAALEQAHATLKERQGELEEHREQVRRLQEELEVEGRQVRALEEVLGDLRAESREHEKAVLALQQRCAEQAQEHEAEARTLQDSWLQAQATLTEQEQELAALRAENQYSRRQEEAAVSQAEALQEALSKAQAALQEKEQSLLEQAELSHTLEASTAALQATLDTCQASARQLEEALRIREGEIQAQALQHHEVTQHLQQELCQKKEELRQLLEKAGARRSQENGIQEKQSLEQERQEETRRLLESLKELQLTVAQREEEILMLREASSPRHRALPAEKPALQPLPAQQELERLQTALRQTEAREIEWREKAQDLALSLAQSKASISSLQEITMFLQASVLERESEQQRLQEELVLSRQALEEQQSGGPHSTSRADQGPKVGQGSQSGEVETEPSPGVEEKERLTQRLERLQQAVAELEVDRSKLQCHNAQLRTALEQVERERRKLKRDSVRASRAGSLEARETMTSSPTQQDGRGSQRGSSDSVLVVELQREVALLRAQLALERKQRQDYIARSVQTSRELAGLHHSLSHSLLTVAQAPEATVLEAETRKLDESLNQSLTSPGPCLLHPSLDTTQNTHR 2414 Q7SXN4 Cytoplasmic cpeb4 7955 None SL-0198 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}. UNIPROT Q7SXN4 Pfam PF16366 Pfam PF16367 PROSITE PS50102 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}. GO:0070161 GO:0005737 GO:0030425 GO:0043197 GO:0005783 GO:0030426 GO:1990124 GO:0043005 GO:0005634 GO:0048471 GO:0014069 GO:0045202 GO:0003730 GO:0000900 GO:0043022 GO:0008135 GO:0071230 GO:0036294 GO:0042149 GO:0035235 GO:2000766 GO:0043524 GO:0002931 Unknown UniProt Sequence Analysis MQDDILESEMSKAPQLQQESQEGQDKQTLSPPGHQEPPGIISELDNALPEENQLEKGTMENANGKETLRLESPVLSGFDYQETTGIGTLAQSSSSSSSSLTGFSSWSTAMPPNPSTLIEEVGFFNQAATTNNAPPPLLFQSFSHHTSTGFGGNFSHQIGPLSQHHPSPHPHFQHPHNQHRRSSASPHPPPFSHRSAAFNQLPHLGNNLSKPPSPWGSYQSPSSTPSSTSWSPGGGYGGWGSSQGREYRRGGVNPLNSISPLKKSFPNNQTQTQKYPRNNSGFNTKPWVEDTINRNESIFPFQERSRSFDGFSMHSLENSLIDIMRAEQDSLKGHSSLFPMEDERSYGEDERSDQSLSGLGSPHSFPHQNGERIERYSRKVFVGGLPPDIDEDEITASFRRFGHLFVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACMEEDGKLYLCVSSPTIKDKPVQIRPWNLNDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN 635 Q17RY0 Cytoplasmic CPEB4 9606 None SL-0198 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}. UNIPROT Q17RY0 UNIPROT B7ZLQ7 UNIPROT Q7Z310 UNIPROT Q8N405 UNIPROT Q9C0J0 PDB 2MKI PDB 2MKJ PDB 5DIF Pfam PF16366 Pfam PF16367 PROSITE PS50102 OMIM 610607 DisGeNET 80315 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}. Q8D052 EBI-2848200 0.00 P50616 EBI-8596337 0.54 Q9H4B6 EBI-8799416 0.27 Q9H6Z9 EBI-12503146 0.35 Q61474 EBI-11474493 0.40 Q17RY0 EBI-11474906 0.40 Q9BZB8 EBI-11474918 0.40 Q6ZNJ1 EBI-16749633 0.35 P69479 EBI-25568044 0.35 GO:0070161 GO:0005737 GO:0030425 GO:0043197 GO:0005783 GO:0030426 GO:1990124 GO:0043005 GO:0005634 GO:0048471 GO:0014069 GO:0045202 GO:0046872 GO:0003730 GO:0000900 GO:0043022 GO:0003723 GO:0008135 GO:0071230 GO:0036294 GO:0042149 GO:0035235 GO:2000766 GO:0043524 GO:0002931 Unknown UniProt Sequence Analysis MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPSPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKAKSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKSEENQGDNSSENGNGKEKIRIESPVLTGFDYQEATGLGTSTQPLTSSASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPAASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQHHHSQHQQQRRSPASPHPPPFTHRNAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGGSQGRDHRRGLNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPDRPRTFDMHSLESSLIDIMRAENDTIKGRLNYSYPGSDSSLLINARTYGRRRGQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFSHQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN 729 Q7TN98 Cytoplasmic Cpeb4 10090 None SL-0198 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}. UNIPROT Q7TN98 UNIPROT A6H6G0 UNIPROT Q69ZD7 Pfam PF16366 Pfam PF16367 PROSITE PS50102 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}. GO:0070161 GO:0005737 GO:0030425 GO:0043197 GO:0005783 GO:0030426 GO:1990124 GO:0043005 GO:0005634 GO:0048471 GO:0098794 GO:0014069 GO:0045202 GO:0046872 GO:0003730 GO:0000900 GO:0043022 GO:0003723 GO:0008135 GO:0071230 GO:0036294 GO:0042149 GO:0035235 GO:2000766 GO:0043524 GO:0002931 Unknown UniProt Sequence Analysis MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPNPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKAKSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKAEENPGDSSSENSNGKEKLRIESPVLTGFDYQEATGLGTSTQPLTSSASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPGASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQHHHSQHQQQRRSPASPHPPPFTHRSAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGASQGRDHRRGLNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPERPRTFDMHSLESSLIDIMRAENDSIKGRLNYSYPGSDSSLLINARTYGRRRGQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFTHQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN 729 Q9LV85 Protein CPR5 3702 None SL-0178 SL-0182 Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:21875893, ECO:0000269|PubMed:25455564}. UNIPROT Q9LV85 UNIPROT Q8W3U8 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}. GO:0005783 GO:0016021 GO:0016020 GO:0005635 GO:0031965 GO:0005634 GO:0007568 GO:0006952 GO:0010150 GO:0048573 GO:0009723 GO:0010182 GO:0009627 GO:0010090 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEALLLPPSPEPQNQITNPANSKPNHQSGDVHKDETMMMKKKKDTNPSNLEKRKLKGKKKEIMDNDEASSSYCSTSSTSNSNSTKRVTRVVHRLRNPMRLGMARRSVGERQAEKLAKPLGFSLAAFANMVIARKNAAGQNVYVDDLVEIFATLVEESLANVYGNKLGSFATNFEQTFSSTLKILKLTNECANPHQSNNNDGGSCNLDRSTIDGCSDTELFERETSSATSAYEVMQGSATATSLMNELALFEETLQLSCVPPRSSAMALTTDERFLKEQTRANDLKTVEIGLQIRELRCKETALGLKFESNNLGKAALELDVSKAAFRAEKFKTELEDTRKEEMVTRIMDWLLVSVFSMLASMVLGVYNFSIKRIEDATSVCDQSEEKSSSWWVPKQVSSINSGFNTFICRVRVWVQIFFGVLMIIVFTYFLNKRSSGTKQTMPISFIVLFLGIFCGVSGKLCVDTLGGDGKLWLIVWEVFCLLQFVANVFTLALYGLMFGPINVTQETRSNRCNSMFPYWARRSVVYVVILFVLPVINGLLPFATFGEWRDFAMYHLHGGSDYA 564 Q0VCQ0 Ceramide-1-phosphate CPTP 9913 None SL-0178 SL-0182 SL-0183 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}. UNIPROT Q0VCQ0 Pfam PF08718 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}. GO:0005829 GO:0010008 GO:0005794 GO:0005640 GO:0005886 GO:1902387 GO:1902388 GO:0005543 GO:1902389 GO:0035627 GO:0120009 GO:0010507 GO:0032691 GO:1900226 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q5TA50} MDDLESEFNLKVVLVSFKQCLNEKEEVLLEYYLAGWRGLVRFLNSLGTIFSFISKDVVTKLQIMDQLRSGPQQEHYSSLQAMVAYEVGNQLVDLERRSRHPDSGCRTVLRLHRALRWLQLFLEGVRTSPEDARTSVLCTDSYNASLATYHPWIIRRAVTVAFCALPTRKVFLESMNVGSSEQAVEMLNEALPFIERVYNISQKLYAEHALLDLP 214 Q6DBQ8 Ceramide-1-phosphate cptp 7955 None SL-0178 SL-0182 SL-0183 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}. UNIPROT Q6DBQ8 Pfam PF08718 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}. GO:0005829 GO:0010008 GO:0005794 GO:0005640 GO:0005886 GO:1902387 GO:1902388 GO:0005543 GO:1902389 GO:0035627 GO:0120009 GO:0010507 GO:0032691 GO:1900226 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q5TA50} MADAFSLQRVLETFRSSLSENKEVYIKYYIAGWQELVSFMNSLGNVFSFISKDVVSKIQILENFLSGENGSNYVTIQSMVKYELENDLVDLTKRGSHPESGCRTLLRLHRALRWLELFLERLRTSTEDSKTSVMCSDAYNESLANHHPWLIRKAVGVAFCALPGRETFFDVMNAGDHTQVVALLGESLPLIAEVYQITEDLYAKNNLLELP 211 Q5TA50 Ceramide-1-phosphate CPTP 9606 None SL-0178 SL-0182 SL-0183 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}. UNIPROT Q5TA50 UNIPROT Q4G0E6 UNIPROT Q7L5A4 PDB 4K80 PDB 4K84 PDB 4K85 PDB 4K8N PDB 4KBS PDB 4KF6 Pfam PF08718 OMIM 615467 DisGeNET 80772 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}. P09564 EBI-3913933 0.37 Q16610 EBI-3916784 0.37 P84022 EBI-3919182 0.37 Q15369 EBI-3921421 0.37 Q9Y4E5 EBI-3924080 0.37 Q9BT40 EBI-3924709 0.37 Q86YI8 EBI-3925466 0.37 Q5S007 EBI-9660046 0.44 GO:0005829 GO:0010008 GO:0005794 GO:0005640 GO:0005886 GO:1902387 GO:1902388 GO:0005543 GO:1902389 GO:0035627 GO:0006687 GO:0120009 GO:0010507 GO:0032691 GO:1900226 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:23863933} MDDSETGFNLKVVLVSFKQCLDEKEEVLLDPYIASWKGLVRFLNSLGTIFSFISKDVVSKLRIMERLRGGPQSEHYRSLQAMVAHELSNRLVDLERRSHHPESGCRTVLRLHRALHWLQLFLEGLRTSPEDARTSALCADSYNASLAAYHPWVVRRAVTVAFCTLPTREVFLEAMNVGPPEQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP 214 Q8BS40 Ceramide-1-phosphate Cptp 10090 None SL-0178 SL-0182 SL-0183 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}. UNIPROT Q8BS40 UNIPROT A2ADA2 UNIPROT Q99LU9 PDB 4KBR Pfam PF08718 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}. GO:0005829 GO:0010008 GO:0005794 GO:0005640 GO:0005886 GO:1902387 GO:1902388 GO:0005543 GO:1902389 GO:0035627 GO:0120009 GO:0010507 GO:0032691 GO:1900226 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q5TA50} MDDSEKDFNLKVVLVSFKQCLTDKGEVLLDHYIAGWKGLVRFLNSLGAVFSFISKDVVAKLQIMERLRSSPQSEHYASLQSMVAYEVSNKLVDMDHRSHPRHPHSGCRTVLRLHRALHWLQLFLDGLRTSSEDARTSTLCSEAYNATLANYHSWIVRQAVTVAFCALPSRKVFLEAMNMESTEQAVEMLGEALPFIEHVYDISQKLYAEHSLLDLP 216 Q5XIS2 Ceramide-1-phosphate Cptp 10116 None SL-0178 SL-0182 SL-0183 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}. UNIPROT Q5XIS2 Pfam PF08718 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}. GO:0005829 GO:0010008 GO:0005794 GO:0005640 GO:0005886 GO:1902387 GO:1902388 GO:0005543 GO:1902389 GO:0035627 GO:0120009 GO:0010507 GO:0032691 GO:1900226 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q5TA50} MDGPERDFNLKVVLISFKKCLTDKGEVLLDHYTASWKGLVRFLNSLGAVFSFISKDVVSKLQIMEHLRSGPQSEHYISLQSMVAYEVSNKLVDRDSRSRPRHPNSGCRTVLRLHRALHWLQLFLEGLRTSSEDARTSTLCSEAYNATLAAYHSWIVRQAVNVAFHALPPRKVFLEAMNMGSSEQAVEMLGEALPFIEQVYDISQKLYAEHSLLDLP 216 Q5HZ92 Ceramide-1-phosphate cptp 8355 None SL-0178 SL-0182 SL-0183 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}. UNIPROT Q5HZ92 Pfam PF08718 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}. GO:0005829 GO:0010008 GO:0005794 GO:0005640 GO:0005886 GO:1902387 GO:1902388 GO:0005543 GO:1902389 GO:0010507 GO:0032691 GO:1900226 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q5TA50} MSSTEEKFSLKEVLVSFKACLIDDDKDVILEHYVNGWKGLVRFMSSLGTIFSFVSKDAVSKIQIMESYLAGPNGERYRTLQSMVEYELSSDLVDLTKRSDHTDSGCRTLLRLHRALRWLQLFLEKLRVSNEDSKTSTLCTEAYNDSLANFHPWIVRKAATVSFIALPYRNTFFEIMNVGTTEEVVAMLGESMPYVTKVYDFTQEVYSQHNLLELP 215 Q66JG2 Ceramide-1-phosphate cptp 8364 None SL-0178 SL-0182 SL-0183 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}. UNIPROT Q66JG2 Pfam PF08718 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}. GO:0005829 GO:0010008 GO:0005794 GO:0005640 GO:0005886 GO:1902387 GO:1902388 GO:0005543 GO:1902389 GO:0035627 GO:0120009 GO:0010507 GO:0032691 GO:1900226 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q5TA50} MSSTEEKFSLKEVLVSFKSCLVDDDQDIIVEQYLNGWKGLVRFMNSLGTIFSFVSKDAVTKIQIMENYLAGTNGERYRTLQSMVEHELSSDLVDLTKRCNNPDSGCRTILRLHRALRWLQLFLEKLRTSNEDSKTSTLCTEAYNDSLANFHPWIIRKTATVAFLALPTRNTFFEVMNVGTTEEVVAMLGESMPYVTKVYDFTHEIYSQHNLLELP 215 F4HRT5 Protein CRWN1 3702 None SL-0178 SL-0180 SL-0182 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}. UNIPROT F4HRT5 UNIPROT Q0WKV7 UNIPROT Q8GZ88 UNIPROT Q9FYH0 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}. GO:0000785 GO:0005739 GO:0005635 GO:0005652 GO:0031965 GO:0034399 GO:0005654 GO:0005634 GO:0006997 GO:0097298 Peripheral UniProt Sequence Analysis MSTPLKVWQRWSTPTKATNPDSNGSSHGTGLDMVTPVSGRVSEIQFDDPRILPEKISELEKELFEYQHSMGLLLIEKKEWSSQYEALQQAFEEVNECLKQERNAHLIAIADVEKREEGLRKALGIEKQCALDLEKALKELRAENAEIKFTADSKLTEANALVRSVEEKSLEVEAKLRAVDAKLAEVSRKSSDVERKAKEVEARESSLQRERFSYIAEREADEATLSKQREDLREWERKLQEGEERVAKSQMIVKQREDRANESDKIIKQKGKELEEAQKKIDAANLAVKKLEDDVSSRIKDLALREQETDVLKKSIETKARELQALQEKLEAREKMAVQQLVDEHQAKLDSTQREFELEMEQKRKSIDDSLKSKVAEVEKREAEWKHMEEKVAKREQALDRKLEKHKEKENDFDLRLKGISGREKALKSEEKALETEKKKLLEDKEIILNLKALVEKVSGENQAQLSEINKEKDELRVTEEERSEYLRLQTELKEQIEKCRSQQELLQKEAEDLKAQRESFEKEWEELDERKAKIGNELKNITDQKEKLERHIHLEEERLKKEKQAANENMERELETLEVAKASFAETMEYERSMLSKKAESERSQLLHDIEMRKRKLESDMQTILEEKERELQAKKKLFEEEREKELSNINYLRDVARREMMDMQNERQRIEKEKLEVDSSKNHLEEQQTEIRKDVDDLVALTKKLKEQREQFISERSRFLSSMESNRNCSRCGELLSELVLPEIDNLEMPNMSKLANILDNEAPRQEMRDISPTAAGLGLPVTGGKVSWFRKCTSKMLKLSPIKMTEPSVTWNLADQEPQSTEQANVGGPSTTVQAATTYSFDVQKAESETGTKEVEVTNVNSDGDQSDINSKAQEVAADSLSNLDVDGQSRMKGKGKARTRRTRSVKDVVDDAKALYGESINLYEPNDSTENVDDSTKASTGETGRSDKAISKNGRKRGRVGSLRTCTTEQDGNESDGKSDSVTGGAHQRKRRQKVASEQQGEVVGQRYNLRRPRRVTGEPALSKKNEDIGGVQQEEGIHCTQATATASVGVAVSDNGVSTNVVQHEATADSEDTDAGSPKRTDESEAMSEDVNKTPLRADSDGEDDESDAEHPGKVSIGKKLWTFLTT 1132 Q9SAF6 Protein CRWN2 3702 None SL-0178 SL-0180 SL-0182 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}. UNIPROT Q9SAF6 UNIPROT F4HP35 UNIPROT Q0WQM6 UNIPROT Q94AW6 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}. GO:0005737 GO:0005652 GO:0031965 GO:0034399 GO:0005654 GO:0006997 GO:0097298 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:17873096} MTPRSETHKIGGVTNPRNADRKGKAVAFSDDLVIPTLPPPPIGTLTGQGVSRGHTDDMDMGDWRRFREVGLLNEASMEKKDQEALLEKISTLEKELYGYQHNMGLLLMENKELVSKHEQLNQAFQEAQEILKREQSSHLYALTTVEQREENLRKALGLEKQCVQELEKALREIQEENSKIRLSSEAKLVEANALVASVNGRSSDVENKIYSAESKLAEATRKSSELKLRLKEVETRESVLQQERLSFTKERESYEGTFQKQREYLNEWEKKLQGKEESITEQKRNLNQREEKVNEIEKKLKLKEKELEEWNRKVDLSMSKSKETEEDITKRLEELTTKEKEAHTLQITLLAKENELRAFEEKLIAREGTEIQKLIDDQKEVLGSKMLEFELECEEIRKSLDKELQRKIEELERQKVEIDHSEEKLEKRNQAMNKKFDRVNEKEMDLEAKLKTIKEREKIIQAEEKRLSLEKQQLLSDKESLEDLQQEIEKIRAEMTKKEEMIEEECKSLEIKKEEREEYLRLQSELKSQIEKSRVHEEFLSKEVENLKQEKERFEKEWEILDEKQAVYNKERIRISEEKEKFERFQLLEGERLKKEESALRVQIMQELDDIRLQRESFEANMEHERSALQEKVKLEQSKVIDDLEMMRRNLEIELQERKEQDEKDLLDRMAQFEDKRMAELSDINHQKQALNREMEEMMSKRSALQKESEEIAKHKDKLKEQQVEMHNDISELSTLSINLKKRREVFGRERSRFLAFVQKLKDCGSCGQLVNDFVLSDLQLPSNDEVAILPPIGVLNDLPGSSNASDSCNIKKSLDGDASGSGGSRRPSMSILQKCTSIIFSPSKRVEHGIDTGKPEQRLSSSVAVGMETKGEKPLPVDLRLRPSSSSIPEEDEEYTDSRVQETSEGSQLSEFQSSRRGRGRPRKAKPALNPTSSVKHASLEESSKDELSGHVSVTSKKTTGGGGRKRQHIDDTATGGKRRRQQTVAVLPQTPGQRHYNLRRKKTVDQVPADVEDNAAAGEDDADIAASAPSKDTVEETVVETLRARRIETNADVVSAENNGDVPVANVEPTVNEDTNEDGDEEEDEAQDDDNEENQDDDDDDDGDDDGSPRPGEGSIRKKLWTFLTT 1128 Q9CA42 Protein CRWN3 3702 None SL-0178 SL-0180 SL-0182 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}. UNIPROT Q9CA42 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}. Q9SB04 EBI-1999431 0.37 Q9ZWS7 EBI-1999571 0.37 GO:0005737 GO:0005652 GO:0031965 GO:0005730 GO:0005654 GO:0009506 GO:0006997 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:F4HRT5} MFTPQRNRWPETDRKGKAIAFSDEIITPPPQRVLLREDDDWQKFKEVGLLDEASLERKDRDALIEKILKLEKELFDYQHNMGLLLIEKKQWTSTNNELQQAYDEAMEMLKREKTSNAITLNEADKREENLRKALIDEKQFVAELENDLKYWQREHSVVKSTSEAKLEEANALVIGMKEKALEVDRERAIAEEKFSVMNRKSSELERKLKEVETREKVHQREHLSLVTEREAHEAVFYKQREDLQEWEKKLTLEEDRLSEVKRSINHREERVMENERTIEKKEKILENLQQKISVAKSELTEKEESIKIKLNDISLKEKDFEAMKAKVDIKEKELHEFEENLIEREQMEIGKLLDDQKAVLDSRRREFEMELEQMRRSLDEELEGKKAEIEQLQVEISHKEEKLAKREAALEKKEEGVKKKEKDLDARLKTVKEKEKALKAEEKKLHMENERLLEDKECLRKLKDEIEEIGTETTKQESRIREEHESLRITKEERVEFLRLQSELKQQIDKVKQEEELLLKEREELKQDKERFEKEWEALDKKRANITREQNEVAEENEKLRNLQISEKHRLKREEMTSRDNLKRELDGVKMQKESFEADMEDLEMQKRNLDMEFQRQEEAGERDFNERARTYEKRSQEELDNINYTKKLAQREMEEMQYEKLALEREREQISVRKKLLKEQEAEMHKDITELDVLRSSLKEKRKEFICERERFLVFLEKLKSCSSCGEITENFVLSDLRLPDVEDGDKRFGKQKLKAEEALNISPSAENSKRTSLLGKIASKLLSISPIGKTDKVTDLGITVKLPESSQPDDSLDRVSGEDHEPSATEQSFTDSRIQEGPEGSLQSEMKSDKPRRGRGRGRGRGKSVRGRSQATKAVSRDSKPSDGETPRKRQREQTSRITESEQAAGDSDEGVDSITTGGRRKKRQIAVPVSQTPGQTRYQLRRHRNVGTEEDKAQASKGATEKQERVNDDIRKVPSPKETRTPPEGENRENGKAEVLVETVTHEEIVTVETETVFKVNNTGKNPVEDPQLEVGGSGEIREHGEEDDENISMIEEENEGEEEEETERQGNDASIGKKIWVFFTT 1085 Q9FLH0 Protein CRWN4 3702 None SL-0178 SL-0180 SL-0182 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}. UNIPROT Q9FLH0 UNIPROT F4JXK1 UNIPROT O49539 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}. GO:0010369 GO:0005737 GO:0005652 GO:0031965 GO:0034399 GO:0005654 GO:0006974 GO:0006997 GO:0097298 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:23396599} MATSSRSERFPITPSTAATNRLTITPNSRVLKSPLTEEIMWKRLKDAGFDEQSIKNRDKAALIAYIAKLESEVYDYQHNMGLLLLEKNELSSQYEEIKASVDESDLTHMREKSAYVSALAEAKKREESLKKDVGIAKECISSLEKTLHEMRAECAETKVSAGSTMSEAHVMIEDALKKLADAEAKMRAAEALQAEANRYHRIAERKLKEVESREDDLTRRLASFKSECETKENEMVIERQTLNERRKSLQQEHERLLDAQVSLNQREDHIFARSQELAELEKGLDTAKTTFEEERKAFEDKKSNLEIALALCAKREEAVSERESSLLKKEQELLVAEEKIASKESELIQNVLANQEVILRKRKSDVEAELECKSKSVEVEIESKRRAWELREVDIKQREDLVGEKEHDLEVQSRALAEKEKDITEKSFNLDEKEKNLVATEEDINRKTTMLEDEKERLRKLDLELQQSLTSLEDKRKRVDSATQKLEALKSETSELSTLEMKLKEELDDLRAQKLEMLAEADRLKVEKAKFEAEWEHIDVKREELRKEAEYITRQREAFSMYLKDERDNIKEERDALRNQHKNDVESLNREREEFMNKMVEEHSEWLSKIQRERADFLLGIEMQKRELEYCIENKREELENSSRDREKAFEQEKKLEEERIQSLKEMAEKELEHVQVELKRLDAERLEIKLDRERREREWAELKDSVEELKVQREKLETQRHMLRAERDEIRHEIEELKKLENLKVALDDMSMAKMQLSNLERSWEKVSALKQKVVSRDDELDLQNGVSTVSNSEDGYNSSMERQNGLTPSSATPFSWIKRCTNLIFKTSPEKSTLMHHYEEEGGVPSEKLKLESSRREEKAYTEGLSIAVERLEAGRKRRGNTSGDETSEPSNNKKRKHDVTQKYSDEADTQSVISSPQNVPEDKHELPSSQTQTPSGMVVISETVKITRVTCETEVTNKVTTLDCSESPSEAGRKMGEETEDGDCNQTGINASETVIHNEAATEDICT 1010 Q17DK5 Cryptochrome-1 cry 7159 None SL-0198 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}. UNIPROT Q17DK5 Pfam PF00875 Pfam PF03441 PROSITE PS00394 PROSITE PS51645 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}. GO:0005737 GO:0005634 GO:0048471 GO:0009882 GO:0050660 GO:0045892 GO:0006139 GO:0042752 GO:0006950 GO:0048511 Unknown UniProt Sequence Analysis MTVNNILWFRHGLRLHDNPSLLEALRNDGTGSESVRLYPIFIFDGESAGTKLVGFNRMKFLLESLADLDRQLREIGGQLYVFKGNAVNVMRRLFEELNIRKLCFEQDCEPIWKARDDAIQNLCRMMDVKCVEKVSHTLWDPQQIIRTNGGIPPLTYQMFLHTVDIIGKPPRPVAAPSFEFVEFGSIPSILAQEVKLQQVRNLSPEDFGIYYEGNPDISHQQWMGGETKALECLGHRLKQEEEAFLGGYFLPTQAKPEFLVPPTSMSAALRFGCLSVRMFYWCVHDLYEKVQANNQYRNPGGQHITGQLIWREYFYTMSVHNPHYAEMEANPICLNIPWYEPKDDSLDRWKEGRTGFPMIDAAMRQLLAEGWLHHILRNITATFLTRGALWISWEAGVQHFLKYLLDADWSVCAGNWMWVSSSAFEKLLDSSSCTSPIALARRLDPKGEYVRRYLPELKNLPTLYVHEPWKAPLDVQKECGCIVGRDYPAPMIDLAAASRANANTMNSIRQKLMERGGSTPPHCRPSDVEEIRNFFWLPEDVVADC 545 Q7PYI7 Cryptochrome-1 Cry1 7165 None SL-0198 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}. UNIPROT Q7PYI7 UNIPROT Q0QW08 Pfam PF00875 Pfam PF03441 PROSITE PS00394 PROSITE PS51645 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}. GO:0005737 GO:0005634 GO:0048471 GO:0009882 GO:0003677 GO:0071949 GO:0050660 GO:0032922 GO:0043153 GO:0045892 GO:0006139 GO:0042752 GO:0006950 Unknown UniProt Sequence Analysis MTINNILWFRHGLRLHDNPSLLEALKSDCVNQSSEAVKLFPIFIFDGESAGTRIVGYNRMKFLLESLADLDRQFRDLGGQLLVFRGDSVTVLRRLFEELNIKKLCYEQDCEPIWKERDDAVAKLCRTMDVRCVENVSHTLWNPIEVIQTNGDIPPLTYQMFLHTVNIIGDPPRPVGAPNFEYVEFGRVPALLASELKLCQQMPAPDDFGIHYDGNARIAFQKWIGGETRALEALGARLKQEEEAFREGYYLPTQAKPEILGPATSMSAALRFGCLSVRMFYWCVHDLFAKVQSNSQFKYPGGHHITGQLIWREYFYTMSVQNPHYGEMERNPICLNIPWYKPEDDSLTRWKEGRTGFPMIDAAMRQLLAEGWLHHILRNITATFLTRGGLWLSWEEGLQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSKCTCPIALARRLDPKGDYVKRYLPELANYPAQFVHEPWKASREQQIEYGCVIGEKYPAPMVDLAIVSKRNAHTMASLREKLVDGGSTPPHCRPSDIEEIRQFFWLADDAATEA 545 B0WRR9 Cryptochrome-1 cry 7176 None SL-0198 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}. UNIPROT B0WRR9 Pfam PF03441 PROSITE PS00394 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}. GO:0005737 GO:0005634 GO:0048471 GO:0009882 GO:0050660 GO:0045892 GO:0006139 GO:0042752 GO:0006950 GO:0048511 Unknown UniProt Sequence Analysis MTDKVRNRVQCWPALAQESSCVDFIPARQGATCGSTVVFIPCCGLTRGRRVLCQWFPCLSGGCCSQESSCVDFIPARQGATCGSTVVFIPCCGLTRGRRVLCQWFPCLSGGCCSQHTVNIIGEPPRPVGAPSFEFVEFGRLPSILSTELKLFQRAPVPEDFGIYYEGNADIARQRWTGGEAKALELLGRRLKQEEEAFREGYYLPTQARPDFLAPPSSMSAALRFGCLSVRMFYWCVHDLFARVQANNQLKHPGGHHITGQLIWREYFYTMSVHNPHYAVMELNPICLNIPWYEAKDDSLDRWKEGRTGFPLIDAAMRQLMAEGWLHHILRNITATFLTRGGLWISWEAGVQHFLKYLLDADWSVCAGNWMWVSSSAFEKLLDSSSCTSPVALARRLDPKGEYVKRYLPELEKFPALYVHEPWKAPPELQEQYGCVIGKDYPAPMVNLAEVNKCNANKMNAIRQKLLDQGGSTPAHCRPSDMDEVRQFFWLPEDVAAES 499 O77059 Cryptochrome-1 cry 7227 None SL-0198 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}. UNIPROT O77059 UNIPROT Q9TYA0 PDB 4GU5 PDB 4JZY PDB 4K03 PDB 6WTB Pfam PF00875 Pfam PF03441 PROSITE PS51645 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}. P49021 EBI-872146 0.27 P07663 EBI-872150 0.27 P18431 EBI-1248163 0.40 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0009882 GO:0003677 GO:0071949 GO:0050660 GO:0008020 GO:0009881 GO:0009785 GO:0071482 GO:0048512 GO:0032922 GO:0007623 GO:0050980 GO:0009649 GO:0043153 GO:0042332 GO:0045475 GO:0050958 GO:0045892 GO:0007602 GO:0042752 GO:0045187 GO:0009637 GO:0009416 GO:0071000 GO:0009588 Unknown UniProt Sequence Analysis MATRGANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAATDGRGRLLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVEKVSHTLWDPQLVIETNGGIPPLTYQMFLHTVQIIGLPPRPTADARLEDATFVELDPEFCRSLKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKVEQHAFERGFYLPNQALPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGVQMTGGAHITGQLIWREYFYTMSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEHGLQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQEQYECLIGVHYPERIIDLSMAVKRNMLAMKSLRNSLITPPPHCRPSNEEEVRQFFWLADVVV 542 Q293P8 Cryptochrome-1 cry 46245 None SL-0198 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}. UNIPROT Q293P8 Pfam PF00875 Pfam PF03441 PROSITE PS51645 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}. GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0009882 GO:0071949 GO:0050660 GO:0032922 GO:0050980 GO:0043153 GO:0042332 GO:0045475 GO:0045892 GO:0007602 GO:0042752 GO:0045187 GO:0071000 Unknown UniProt Sequence Analysis MVPRGANVLWFRHGLRLHDNPALLAALEEKDQGIPLIPVFIFDGESAGTKSVGYNRMRFLLDSLQDLDEQLQSATEGRGRLFVFEGEPTLIFRRLHEQVRLHKICAELDCEPIWNERDESARLLCRELGIEYVEKVSHTLWDPRLVIETNGGIPPLTYQMFLHTVQIIGVPPRPAIDAHINDATFIQLAPELRQHLGCFDQVPNPEHFNIYSDNMGFLAKINWRGGETQALALLEERLKVERNAFERGYYLPNQANPNIQEAPKSMSAHLRFGCLSVRRFYWSVHDLFENVQLAACVRGVQIEGGAHITGQLIWREYFYTMSVNNPNYDRMEGNEICLTIPWAKPDENLLQRWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEPGLKHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPEGVYIRRYVPELKNLPKEYIHEPWRLSAEQQVKFECLIGVHYPERIIDLSKAVKRNMMAMTALRNSLITPPPHCRPSNEEEVRQFFWLANY 540 O13671 Importin-alpha kap109 284812 None SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. UNIPROT O13671 UNIPROT Q9USC9 Pfam PF03378 Pfam PF08506 Pfam PF03810 PROSITE PS50166 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}. GO:0005829 GO:0005635 GO:0031965 GO:0034399 GO:0005525 GO:0005049 GO:0031267 GO:0006611 GO:0006606 Unknown UniProt Sequence Analysis MDDIPTLLARTLNPTTSKSAEEALKVWELQDSSFALKLLNIVAEDTVDINIKLAASLYFKNYIKKHWDSEEGASIRISDEVAELIKREIINLMLKSTTIIQVQLGEVIGYIANFDFPDRWDTLLPDLISKLSAVDMNTNIAVLSTAHAIFKRWRPLFRSDALFLEIKYVLDRFCEPFLALFVQTNNLLRNGPQDAESLNSLFQVILLECKLFYDLNCQDIPEFFEDHMSEFMTAFLNYFTYTNPSLEGDEGETNVLIKVKASICEIVELYTLRYEEVFTMLYDFVNVTWTLLTTLTPDEKYDGLVGKAMAFLTSVIRIRKHAEFFQQDQVLQQFIELVVLPNICLRESDEELFEDDPLEYVRRDLEGSNSDSRARSAIVLVRGLLDHFDQKITSVVSTHINANLQQFSTNPSLEWNKKYVALQLFSAIAIKGQSTRLGVTSINLMVDVVAFFENNIKPDLLQPAGVIHPMVLAEDIKYVFTFRNQLNSQQLIDIFPTILRFLEMPSFVVYTYAAIALDQLLTVRHNHVHIFTSLLIAPHILPALNQLFLIVESASTPQKLAENDYLMKAVMRIIIMSQEAILPAASLLLQHLTKITEEVSKNPSNPKFNHYLFESIGALIRSLSKSGPQTVSQLENALLPVFQNVLIEDVTEFIPYVLQLLSQLVEASGNEPLPDFVVNLIQPCLSPALWDSKGNIPALVRLLRAMIFRGPQIFISNKFVEPVLGIFQKLISSKVNDHFGFDLLDRVFTVFNANILAPYINHIFFLLLSRLKNSRTERFVLRCTIFFFFVASEQTGTCGPDNLIQGVDAVQSGVFGQLMTSIILPQAQKLALPLDRKISALGLLRLLTCDLVLAPDAIYENLIIPLLTCILKLFEMPIEQAQTDADEELFMDEIDADSMSFQASFSRLATTGGKRVDPFPQITDLKQYCATEMNLANRNMGGRLSQIISTHLPGDGQSVLQSYGYVI 967 Q08955 Chromosome CSM4 559292 None SL-0178 SL-0182 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}. UNIPROT Q08955 UNIPROT D6W3G9 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}. P47069 EBI-1795681 0.50 GO:0000781 GO:0005789 GO:0016021 GO:0034993 GO:0005640 GO:0140444 GO:0007129 GO:0045132 GO:0045141 GO:0010520 GO:0030435 Transmembrane UniProt Sequence Analysis {ECO:0000255} MMDGSITRKVTSTLSNQLATWKWKLQLSLLERKLATINNDYFLLQWELLFITNEVMKWKEMIAFLESQLFCTTQNFVAQETHDRETFQSLVDDYNKQLSENNLIISVLKSRPQLSSFPIYLSDEVCSHLKFVIAELNSLIIVFFISLVFLWVSIEV 156 Q6PC30 COP9 cops5 7955 None SL-0198 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}. UNIPROT Q6PC30 Pfam PF18323 Pfam PF01398 PROSITE PS50249 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}. GO:0070161 GO:0008180 GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0008021 GO:0019784 GO:0046872 GO:0004222 GO:0008237 GO:0043066 GO:0051091 GO:0000338 GO:0060118 Unknown UniProt Sequence Analysis MAGSSIAMKTWELSNSMQEVQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKLSALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQAEAQLGRGSFMLGLDTHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQVNTSAN 334 Q92905 COP9 COPS5 9606 None SL-0198 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}. UNIPROT Q92905 UNIPROT O15386 UNIPROT Q6AW95 UNIPROT Q86WQ4 UNIPROT Q9BQ17 PDB 4D10 PDB 4D18 PDB 4F7O PDB 4WSN PDB 5JOG PDB 5JOH PDB 5M5Q PDB 6R6H PDB 6R7F PDB 6R7H PDB 6R7I Pfam PF18323 Pfam PF01398 PROSITE PS50249 OMIM 604850 DisGeNET 10987 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}. O15504 EBI-21325777 0.35 O75694 EBI-21325777 0.35 O95831 EBI-21325777 0.35 O95999 EBI-7006208 0.35 P04406 EBI-21325777 0.35 P11802 EBI-21325777 0.35 P31689 EBI-21325777 0.35 P63244 EBI-21325777 0.55 P63279 EBI-3454145 0.00 Q07065 EBI-21325777 0.35 Q14974 EBI-21325777 0.35 Q3TLR7 EBI-11019947 0.35 Q5JTH9 EBI-21325777 0.35 Q7L5N1 EBI-2510150 0.91 Q8IWQ3 EBI-30872909 0.64 Q8N114 EBI-2115585 0.00 Q8NE71 EBI-21325777 0.35 Q8NI35 EBI-2659663 0.35 Q8TEL6 EBI-21325777 0.35 Q92900 EBI-21325777 0.35 P55789 EBI-7286464 0.60 P14174 EBI-7522890 0.59 P10599 EBI-594678 0.74 P46527 EBI-594810 0.60 Q15796 EBI-7224786 0.37 Q5VTD9 EBI-956654 0.00 P09936 EBI-1181897 0.54 P22087 EBI-1182007 0.49 O95273 EBI-1385474 0.54 P40337 EBI-1551755 0.40 O75882 EBI-2115511 0.00 P36507 EBI-2115525 0.00 Q9HB07 EBI-2115530 0.00 Q9NZF1 EBI-2115546 0.00 P50336 EBI-2115551 0.00 P54578 EBI-2115609 0.00 P04004 EBI-2115614 0.00 Q16539 EBI-2116848 0.00 P62256 EBI-2339626 0.37 Q9UDY8 EBI-7006117 0.35 Q9BXL7 EBI-7006135 0.46 Q13098 EBI-7006270 0.93 Q5VTR2 EBI-8566847 0.50 Q15018 EBI-8566862 0.35 P0CG48 EBI-8566988 0.40 P61201 EBI-2510150 0.88 Q86XK2 EBI-2510150 0.56 Q9BX70 EBI-2510150 0.67 Q13620 EBI-2510150 0.85 Q9H496 EBI-2510150 0.56 Q96EF6 EBI-2510150 0.67 Q96M94 EBI-2510150 0.56 Q9BT78 EBI-2510150 0.85 Q92466 EBI-2510150 0.80 Q9P2J3 EBI-2510150 0.56 Q9UBW8 EBI-2510150 0.85 P15374 EBI-2510150 0.40 Q13616 EBI-2510150 0.74 Q99627 EBI-2510150 0.90 Q8NEZ5 EBI-2510150 0.40 Q6TFL4 EBI-2510150 0.56 Q9H9Q2 EBI-2510150 0.85 Q8TEB1 EBI-2510150 0.56 Q13619 EBI-2510150 0.74 Q13309 EBI-2510150 0.56 Q15843 EBI-2510150 0.56 Q13618 EBI-2510150 0.67 Q15048 EBI-2510150 0.56 Q9Y4B6 EBI-2510150 0.67 Q9P2N7 EBI-2510150 0.56 Q13617 EBI-2510150 0.67 Q96L50 EBI-2510150 0.56 Q53GT1 EBI-2510150 0.56 Q9UNS2 EBI-2510150 0.92 Q13216 EBI-2510150 0.56 O94889 EBI-2510150 0.56 B4DN30 EBI-2510150 0.40 Q3U1J4 EBI-2559059 0.40 P53355 EBI-2659621 0.35 Q96N67 EBI-2659621 0.35 P08107 EBI-2659628 0.35 P25705 EBI-2659628 0.35 Q9NZQ3 EBI-2659628 0.35 P80723 EBI-2659628 0.35 Q9NNW5 EBI-2659628 0.35 P34931 EBI-2659628 0.53 O43491 EBI-2659628 0.35 P35579 EBI-2659628 0.35 P08238 EBI-2659628 0.35 Q4VCS5 EBI-2659628 0.35 P48741 EBI-2659628 0.53 Q8IY63 EBI-2659628 0.35 P11021 EBI-2659628 0.53 P17066 EBI-2659628 0.53 P63167 EBI-2659628 0.35 P28289 EBI-2659628 0.35 O75955 EBI-2659628 0.35 Q9UJZ1 EBI-2659628 0.35 O75970 EBI-2659663 0.35 P62877 EBI-2659663 0.35 Q6PJ61 EBI-2659663 0.53 Q9NUP9 EBI-2659663 0.35 O14974 EBI-2659663 0.35 P35580 EBI-2659663 0.35 Q5VUJ6 EBI-2659663 0.53 Q8N3R9 EBI-2659663 0.35 O15085 EBI-2659663 0.35 Q16531 EBI-2659663 0.53 Q9P2K6 EBI-2659663 0.53 Q9Y2D5 EBI-2659663 0.35 Q13573 EBI-7950968 0.35 Q99459 EBI-7954144 0.35 Q16584 EBI-3442917 0.00 Q99759 EBI-3443070 0.00 O43318 EBI-3443260 0.00 Q8IVH8 EBI-3443337 0.00 Q9Y4K4 EBI-3443648 0.00 P61244 EBI-3444880 0.00 Q06413 EBI-3445247 0.00 Q14814 EBI-3445506 0.00 Q12772 EBI-3451285 0.00 P61981 EBI-3453135 0.00 Q9H4A3 EBI-3453687 0.00 O15105 EBI-3861684 0.64 Q13485 EBI-3862454 0.40 P02743 EBI-3907158 0.37 Q99489 EBI-3915505 0.37 Q9NPY3 EBI-3922558 0.37 Q9P0P8 EBI-3922568 0.37 Q8N6T3 EBI-3922578 0.37 P19838 EBI-3936417 0.55 P32119 EBI-3936427 0.37 Q9BYB0 EBI-3942223 0.37 P55085 EBI-4303187 0.64 P36873 EBI-4311588 0.37 Q9H8M7 EBI-4422753 0.54 Q02556 EBI-6115692 0.35 P12520 EBI-6177205 0.35 Q96GG9 EBI-21325177 0.35 Q9C0D3 EBI-21325777 0.35 Q96FX7 EBI-21325777 0.35 P09012 EBI-21325777 0.35 P35250 EBI-21325777 0.35 Q9UKV8 EBI-21325777 0.35 Q9UL18 EBI-21325777 0.35 Q14011 EBI-21325777 0.35 Q8N726 EBI-21325777 0.35 P54132 EBI-21325777 0.35 O94844 EBI-21325777 0.35 Q86YV6 EBI-21325777 0.35 Q8N4N3 EBI-21325777 0.35 Q9UK96 EBI-21325777 0.35 Q96ME1 EBI-21325777 0.35 Q8N1E6 EBI-21325777 0.35 Q96FN4 EBI-21325777 0.35 Q9NWX5 EBI-21325777 0.35 Q86TJ5 EBI-21325777 0.35 Q9NR11 EBI-21325777 0.35 O15231 EBI-21325777 0.35 Q96KR1 EBI-21325777 0.35 Q5TAX3 EBI-21325777 0.35 Q7Z2W4 EBI-21325777 0.35 P63104 EBI-21325777 0.35 Q9H6S0 EBI-21325777 0.35 P67809 EBI-21325777 0.35 Q9H0D6 EBI-21325777 0.35 P12956 EBI-21325777 0.35 Q9Y4P8 EBI-21325777 0.35 Q9GZS3 EBI-21325777 0.35 P61964 EBI-21325777 0.35 Q5TAQ9 EBI-21325777 0.35 Q5T6F0 EBI-21325777 0.35 Q3SXM0 EBI-21325777 0.35 Q8WV16 EBI-21325777 0.53 P08670 EBI-21325777 0.35 P55072 EBI-21325777 0.35 Q93009 EBI-21325777 0.35 Q9Y4E8 EBI-21325777 0.35 P10746 EBI-21325777 0.35 Q9BZI7 EBI-21325777 0.35 Q14157 EBI-21325777 0.35 P22314 EBI-21325777 0.35 P26368 EBI-21325777 0.35 Q06418 EBI-21325777 0.35 P49411 EBI-21325777 0.35 P68371 EBI-21325777 0.35 Q9H4B7 EBI-21325777 0.35 P07437 EBI-21325777 0.35 P68366 EBI-21325777 0.35 Q9BQE3 EBI-21325777 0.35 Q8WZ42 EBI-21325777 0.35 Q6IQ55 EBI-21325777 0.35 Q13263 EBI-21325777 0.35 P62995 EBI-21325777 0.35 Q13595 EBI-21325777 0.35 P11387 EBI-21325777 0.35 Q9UPQ9 EBI-21325777 0.35 Q8TDI8 EBI-21325777 0.35 Q01085 EBI-21325777 0.35 P31483 EBI-21325777 0.35 Q86V81 EBI-21325777 0.35 Q92734 EBI-21325777 0.35 Q00059 EBI-21325777 0.35 P17987 EBI-21325777 0.35 Q15370 EBI-21325777 0.35 Q15369 EBI-21325777 0.35 Q9Y4P3 EBI-21325777 0.35 Q92804 EBI-21325777 0.35 O60506 EBI-21325777 0.35 Q96SI9 EBI-21325777 0.35 Q9Y3F4 EBI-21325777 0.35 Q9NUL3 EBI-21325777 0.35 Q08945 EBI-21325777 0.35 P51571 EBI-21325777 0.35 Q04837 EBI-21325777 0.35 P05455 EBI-21325777 0.35 Q9UQ35 EBI-21325777 0.35 Q96SB4 EBI-21325777 0.35 P37108 EBI-21325777 0.35 O15042 EBI-21325777 0.35 Q01082 EBI-21325777 0.35 Q13813 EBI-21325777 0.35 Q92673 EBI-21325777 0.35 Q9Y5X1 EBI-21325777 0.35 P62308 EBI-21325777 0.35 P62306 EBI-21325777 0.35 P62304 EBI-21325777 0.35 P62318 EBI-21325777 0.35 P62316 EBI-21325777 0.35 P09234 EBI-21325777 0.35 P14678 EBI-21325777 0.35 P08621 EBI-21325777 0.35 O75643 EBI-21325777 0.35 Q9UQE7 EBI-21325777 0.35 Q12824 EBI-21325777 0.35 P51532 EBI-21325777 0.35 Q6IEE8 EBI-21325777 0.35 P12236 EBI-21325777 0.35 P05141 EBI-21325777 0.35 P12235 EBI-21325777 0.35 Q00325 EBI-21325777 0.35 P63208 EBI-21325777 0.35 Q8TBC3 EBI-21325777 0.35 Q16629 EBI-21325777 0.35 Q13247 EBI-21325777 0.35 Q13243 EBI-21325777 0.35 P84103 EBI-21325777 0.35 Q01130 EBI-21325777 0.35 Q07955 EBI-21325777 0.35 P23246 EBI-21325777 0.35 Q15427 EBI-21325777 0.35 Q15393 EBI-21325777 0.35 O75533 EBI-21325777 0.35 Q12874 EBI-21325777 0.35 P48594 EBI-21325777 0.35 P29508 EBI-21325777 0.35 Q9GZR1 EBI-21325777 0.35 Q96EE3 EBI-21325777 0.35 P21912 EBI-21325777 0.35 P31040 EBI-21325777 0.35 Q14151 EBI-21325777 0.35 P06702 EBI-21325777 0.35 P05109 EBI-21325777 0.35 Q9Y265 EBI-21325777 0.35 O76021 EBI-21325777 0.35 Q9Y3B9 EBI-21325777 0.35 P23921 EBI-21325777 0.35 P46781 EBI-21325777 0.35 P62241 EBI-21325777 0.35 P62081 EBI-21325777 0.35 P62753 EBI-21325777 0.35 P62701 EBI-21325777 0.35 P61247 EBI-21325777 0.35 P23396 EBI-21325777 0.35 P42677 EBI-21325777 0.35 P62851 EBI-21325777 0.35 P62847 EBI-21325777 0.35 P62266 EBI-21325777 0.35 P63220 EBI-21325777 0.35 P60866 EBI-21325777 0.35 P15880 EBI-21325777 0.35 P39019 EBI-21325777 0.35 P08708 EBI-21325777 0.35 P62249 EBI-21325777 0.35 P62244 EBI-21325777 0.35 P62841 EBI-21325777 0.35 P62263 EBI-21325777 0.35 P62277 EBI-21325777 0.35 P62280 EBI-21325777 0.35 P46783 EBI-21325777 0.35 P04843 EBI-21325777 0.35 P05387 EBI-21325777 0.35 P05386 EBI-21325777 0.35 P05388 EBI-21325777 0.35 P32969 EBI-21325777 0.35 P62917 EBI-21325777 0.35 P62424 EBI-21325777 0.35 Q02878 EBI-21325777 0.35 P46777 EBI-21325777 0.35 P36578 EBI-21325777 0.35 P63173 EBI-21325777 0.35 P61513 EBI-21325777 0.35 P42766 EBI-21325777 0.35 P62899 EBI-21325777 0.35 P62888 EBI-21325777 0.35 P39023 EBI-21325777 0.35 P46779 EBI-21325777 0.35 P46776 EBI-21325777 0.35 P61353 EBI-21325777 0.35 Q9UNX3 EBI-21325777 0.35 P83731 EBI-21325777 0.35 P62750 EBI-21325777 0.35 P62829 EBI-21325777 0.35 P35268 EBI-21325777 0.35 P84098 EBI-21325777 0.35 Q02543 EBI-21325777 0.35 Q07020 EBI-21325777 0.35 P61313 EBI-21325777 0.35 P50914 EBI-21325777 0.35 P26373 EBI-21325777 0.35 P30050 EBI-21325777 0.35 P62913 EBI-21325777 0.35 Q96L21 EBI-21325777 0.35 P62906 EBI-21325777 0.35 P27635 EBI-21325777 0.35 Q15287 EBI-21325777 0.35 O43148 EBI-21325777 0.35 P13489 EBI-21325777 0.35 Q8WVD3 EBI-21325777 0.35 P78509 EBI-21325777 0.35 Q8NDN9 EBI-21325777 0.35 O75526 EBI-21325777 0.35 P52756 EBI-21325777 0.35 Q9BTD8 EBI-21325777 0.35 Q9BWF3 EBI-21325777 0.35 Q14498 EBI-21325777 0.35 P98179 EBI-21325777 0.35 Q16769 EBI-21325777 0.35 P09417 EBI-21325777 0.35 Q13610 EBI-21325777 0.35 Q9UHX1 EBI-21325777 0.35 P26599 EBI-21325777 0.35 Q14997 EBI-21325777 0.35 O14818 EBI-21325777 0.35 O60256 EBI-21325777 0.35 Q14558 EBI-21325777 0.35 P21108 EBI-21325777 0.35 O75400 EBI-21325777 0.35 Q86UA1 EBI-21325777 0.35 Q8WWY3 EBI-21325777 0.35 Q9UMS4 EBI-21325777 0.35 P78527 EBI-21325777 0.35 P30048 EBI-21325777 0.35 Q06830 EBI-21325777 0.35 O75807 EBI-21325777 0.35 P62937 EBI-21325777 0.35 Q99575 EBI-21325777 0.35 P19388 EBI-21325777 0.35 P19387 EBI-21325777 0.35 Q8WVV4 EBI-21325777 0.35 Q02809 EBI-21325777 0.35 P53350 EBI-21325777 0.35 P14618 EBI-21325777 0.35 Q9P1Y6 EBI-21325777 0.35 O00264 EBI-21325777 0.35 P00558 EBI-21325777 0.35 Q96HS1 EBI-21325777 0.35 Q01813 EBI-21325777 0.35 O00764 EBI-21325777 0.35 Q15084 EBI-21325777 0.35 P29803 EBI-21325777 0.35 O43924 EBI-21325777 0.35 Q6L8Q7 EBI-21325777 0.35 P22061 EBI-21325777 0.35 Q15366 EBI-21325777 0.35 Q15365 EBI-21325777 0.35 P61457 EBI-21325777 0.35 P09874 EBI-21325777 0.35 Q86U42 EBI-21325777 0.35 Q13310 EBI-21325777 0.35 P11940 EBI-21325777 0.35 Q9UBU9 EBI-21325777 0.35 Q7Z417 EBI-21325777 0.35 Q9BRJ7 EBI-21325777 0.35 P36639 EBI-21325777 0.35 Q08J23 EBI-21325777 0.35 P16083 EBI-21325777 0.35 P06748 EBI-21325777 0.35 O00567 EBI-21325777 0.35 P46087 EBI-21325777 0.35 Q9Y3C1 EBI-21325777 0.35 Q15233 EBI-21325777 0.35 O15226 EBI-21325777 0.35 P49821 EBI-21325777 0.35 P19338 EBI-21325777 0.35 Q09161 EBI-21325777 0.35 P55209 EBI-21325777 0.35 Q9NP98 EBI-21325777 0.35 Q9NPC7 EBI-21325777 0.35 Q8WXC6 EBI-21325777 0.35 Q9BQG0 EBI-21325777 0.35 Q6UB35 EBI-21325777 0.35 Q92552 EBI-21325777 0.35 P82663 EBI-21325777 0.35 Q9Y3D9 EBI-21325777 0.35 P82650 EBI-21325777 0.35 P82914 EBI-21325777 0.35 P82912 EBI-21325777 0.35 Q13405 EBI-21325777 0.35 Q8N983 EBI-21325777 0.35 P49406 EBI-21325777 0.35 Q9Y3B7 EBI-21325777 0.35 Q9HCE1 EBI-21325777 0.35 P50219 EBI-21325777 0.35 P40926 EBI-21325777 0.35 P33993 EBI-21325777 0.35 P25205 EBI-21325777 0.35 P43243 EBI-21325777 0.35 P31153 EBI-21325777 0.35 P49137 EBI-21325777 0.35 Q92918 EBI-21325777 0.35 Q9UNF1 EBI-21325777 0.35 Q9NX58 EBI-21325777 0.35 Q9Y383 EBI-21325777 0.35 Q3MHD2 EBI-21325777 0.35 Q8N1G4 EBI-21325777 0.35 Q6ZN17 EBI-21325777 0.35 Q08380 EBI-21325777 0.35 P07195 EBI-21325777 0.35 Q92615 EBI-21325777 0.35 Q6PKG0 EBI-21325777 0.35 P35527 EBI-21325777 0.35 Q6KB66 EBI-21325777 0.35 Q8N1N4 EBI-21325777 0.35 Q01546 EBI-21325777 0.35 O95678 EBI-21325777 0.35 Q3SY84 EBI-21325777 0.35 P48668 EBI-21325777 0.35 P04259 EBI-21325777 0.35 P02538 EBI-21325777 0.35 P13647 EBI-21325777 0.35 P12035 EBI-21325777 0.35 Q2M2I5 EBI-21325777 0.35 P35908 EBI-21325777 0.35 Q04695 EBI-21325777 0.35 P08779 EBI-21325777 0.35 P02533 EBI-21325777 0.35 P13646 EBI-21325777 0.35 P13645 EBI-21325777 0.35 P04264 EBI-21325777 0.35 P52294 EBI-21325777 0.35 Q9P2G9 EBI-21325777 0.35 Q53HC5 EBI-21325777 0.35 Q8NBE8 EBI-21325777 0.35 Q9UJP4 EBI-21325777 0.35 Q53G59 EBI-21325777 0.35 Q8N163 EBI-21325777 0.35 Q9C0C6 EBI-21325777 0.53 Q92945 EBI-21325777 0.35 P50053 EBI-21325777 0.35 Q8NC69 EBI-21325777 0.35 Q9Y597 EBI-21325777 0.35 Q6PI47 EBI-21325777 0.35 Q9H3F6 EBI-21325777 0.35 Q86V97 EBI-21325777 0.35 Q9NVX7 EBI-21325777 0.35 Q15046 EBI-21325777 0.35 P14923 EBI-21325777 0.35 P17535 EBI-21325777 0.35 Q96A47 EBI-21325777 0.35 P61371 EBI-21325777 0.35 O14654 EBI-21325777 0.35 P12268 EBI-21325777 0.35 Q12906 EBI-21325777 0.35 Q12905 EBI-21325777 0.35 O00425 EBI-21325777 0.35 Q9NZI8 EBI-21325777 0.35 P41252 EBI-21325777 0.35 P10809 EBI-21325777 0.35 P04792 EBI-21325777 0.35 P38646 EBI-21325777 0.35 P11142 EBI-21325777 0.35 P34932 EBI-21325777 0.35 P14625 EBI-21325777 0.35 Q58FF8 EBI-21325777 0.35 Q14568 EBI-21325777 0.35 P07900 EBI-21325777 0.35 Q99714 EBI-21325777 0.35 Q7Z5J1 EBI-21325777 0.35 Q86YZ3 EBI-21325777 0.35 P31260 EBI-21325777 0.35 O14979 EBI-21325777 0.35 Q1KMD3 EBI-21325777 0.35 Q9BUJ2 EBI-21325777 0.35 Q00839 EBI-21325777 0.35 O43390 EBI-21325777 0.35 P52272 EBI-21325777 0.35 P14866 EBI-21325777 0.35 P61978 EBI-21325777 0.35 P31942 EBI-21325777 0.35 P31943 EBI-21325777 0.35 P52597 EBI-21325777 0.35 Q14103 EBI-21325777 0.35 O60812 EBI-21325777 0.35 P07910 EBI-21325777 0.35 Q99729 EBI-21325777 0.35 P51991 EBI-21325777 0.35 P22626 EBI-21325777 0.35 P09651 EBI-21325777 0.35 Q13151 EBI-21325777 0.35 Q16778 EBI-21325777 0.35 P16403 EBI-21325777 0.35 Q00341 EBI-21325777 0.35 O14929 EBI-21325777 0.35 P13807 EBI-21325777 0.35 Q7Z2Y8 EBI-21325777 0.35 Q9BZE4 EBI-21325777 0.35 O00178 EBI-21325777 0.35 P09211 EBI-21325777 0.35 Q9BQ67 EBI-21325777 0.35 Q9BVP2 EBI-21325777 0.35 Q92820 EBI-21325777 0.35 Q8IUC8 EBI-21325777 0.35 Q8TAE8 EBI-21325777 0.35 Q9UN86 EBI-21325777 0.35 Q13283 EBI-21325777 0.35 P51114 EBI-21325777 0.35 P35637 EBI-21325777 0.35 Q96I24 EBI-21325777 0.35 Q96AE4 EBI-21325777 0.35 Q8IY81 EBI-21325777 0.35 Q5D862 EBI-21325777 0.35 Q6UN15 EBI-21325777 0.35 Q5HY92 EBI-21325777 0.35 Q96JP0 EBI-21325777 0.35 Q9UK73 EBI-21325777 0.35 P22830 EBI-21325777 0.35 Q5XUX1 EBI-21325777 0.35 Q9UKB1 EBI-21325777 0.35 Q9UK97 EBI-21325777 0.35 Q9Y3I1 EBI-21325777 0.53 Q9H4M3 EBI-21325777 0.35 Q5XUX0 EBI-21325777 0.35 Q9UK99 EBI-21325777 0.35 O94952 EBI-21325777 0.35 Q9UKA1 EBI-21325777 0.53 A6NHQ2 EBI-21325777 0.35 P62861 EBI-21325777 0.35 Q52LJ0 EBI-21325777 0.35 Q8NCA5 EBI-21325777 0.35 Q6ZRV2 EBI-21325777 0.35 Q9NRY5 EBI-21325777 0.35 Q9BTL3 EBI-21325777 0.35 Q06265 EBI-21325777 0.35 Q01844 EBI-21325777 0.35 P07814 EBI-21325777 0.35 P06733 EBI-21325777 0.35 Q15717 EBI-21325777 0.35 Q9BQ52 EBI-21325777 0.35 P63241 EBI-21325777 0.35 P05198 EBI-21325777 0.35 Q8NDI1 EBI-21325777 0.35 Q15029 EBI-21325777 0.35 Q8IYU8 EBI-21325777 0.35 P13639 EBI-21325777 0.35 P26641 EBI-21325777 0.35 Q05639 EBI-21325777 0.35 P68104 EBI-21325777 0.35 Q19T08 EBI-21325777 0.35 Q99848 EBI-21325777 0.35 Q14204 EBI-21325777 0.35 Q9BVJ7 EBI-21325777 0.35 Q9NZJ0 EBI-21325777 0.35 P15924 EBI-21325777 0.35 Q02413 EBI-21325777 0.35 Q92785 EBI-21325777 0.35 O00429 EBI-21325777 0.35 Q8WXX5 EBI-21325777 0.35 Q8IXB1 EBI-21325777 0.35 O60884 EBI-21325777 0.35 Q9P225 EBI-21325777 0.35 P10515 EBI-21325777 0.35 Q08211 EBI-21325777 0.35 Q6P158 EBI-21325777 0.35 Q9H2U1 EBI-21325777 0.35 Q7L2E3 EBI-21325777 0.35 Q7Z478 EBI-21325777 0.35 O43143 EBI-21325777 0.35 P35659 EBI-21325777 0.35 Q9H1M4 EBI-21325777 0.35 P26196 EBI-21325777 0.35 Q9Y2R4 EBI-21325777 0.35 P17844 EBI-21325777 0.35 O00571 EBI-21325777 0.35 Q9NY93 EBI-21325777 0.35 Q9UHI6 EBI-21325777 0.35 Q9UMR2 EBI-21325777 0.35 Q9NVP1 EBI-21325777 0.35 Q92841 EBI-21325777 0.35 Q92499 EBI-21325777 0.35 Q9BW61 EBI-21325777 0.35 Q6V1P9 EBI-21325777 0.35 P81605 EBI-21325777 0.35 Q96EP5 EBI-21325777 0.35 O95886 EBI-21325777 0.35 P19875 EBI-21325777 0.35 Q93034 EBI-21325777 0.35 P17812 EBI-21325777 0.35 P35221 EBI-21325777 0.35 O75534 EBI-21325777 0.35 P16989 EBI-21325777 0.35 O95232 EBI-21325777 0.35 Q96SW2 EBI-21325777 0.53 Q9UBL6 EBI-21325777 0.35 Q8IWV2 EBI-21325777 0.35 P53675 EBI-21325777 0.35 Q00610 EBI-21325777 0.35 P09496 EBI-21325777 0.35 P61024 EBI-21325777 0.35 O14757 EBI-21325777 0.35 Q00526 EBI-21325777 0.35 P24941 EBI-21325777 0.35 Q12834 EBI-21325777 0.35 P06493 EBI-21325777 0.35 P50990 EBI-21325777 0.35 P78371 EBI-21325777 0.35 Q9ULG6 EBI-21325777 0.35 P20248 EBI-21325777 0.35 P78396 EBI-21325777 0.35 Q96A33 EBI-21325777 0.35 Q6YP21 EBI-21325777 0.35 P16152 EBI-21325777 0.35 Q86X55 EBI-21325777 0.35 Q14444 EBI-21325777 0.35 Q86VP6 EBI-21325777 0.35 Q8NCB2 EBI-21325777 0.35 Q9NZT1 EBI-21325777 0.35 Q05682 EBI-21325777 0.35 Q9BRJ6 EBI-21325777 0.35 Q9NRH1 EBI-21325777 0.35 Q9NXF7 EBI-21325777 0.35 Q8N2C7 EBI-21325777 0.35 Q9Y3I0 EBI-21325777 0.35 Q7Z2T5 EBI-21325777 0.35 Q07021 EBI-21325777 0.35 Q9Y224 EBI-21325777 0.35 Q9BRQ4 EBI-21325777 0.35 Q5SWW7 EBI-21325777 0.35 Q13895 EBI-21325777 0.35 O43684 EBI-21325777 0.35 Q96Q07 EBI-21325777 0.35 Q9H0C5 EBI-21325777 0.53 Q9NSI6 EBI-21325777 0.35 Q13867 EBI-21325777 0.35 O95429 EBI-21325777 0.35 P05023 EBI-21325777 0.35 P18846 EBI-21325777 0.35 P08243 EBI-21325777 0.35 P05089 EBI-21325777 0.35 Q10567 EBI-21325777 0.35 Q6UB98 EBI-21325777 0.35 Q9UJX3 EBI-21325777 0.35 Q9UJX6 EBI-21325777 0.35 P23109 EBI-21325777 0.35 Q9C0C7 EBI-21325777 0.35 P09972 EBI-21325777 0.35 O43823 EBI-21325777 0.35 Q12904 EBI-21325777 0.35 P23526 EBI-21325777 0.35 P35573 EBI-21325777 0.35 P61163 EBI-21325777 0.35 Q562R1 EBI-21325777 0.35 P60709 EBI-21325777 0.35 P62736 EBI-21325777 0.35 Q5FVE4 EBI-21325777 0.35 P24666 EBI-21325777 0.35 P35610 EBI-21325777 0.35 Q8N961 EBI-21325777 0.35 Q8WWZ4 EBI-21325777 0.35 P35372 EBI-6918514 0.58 P89884 EBI-9639873 0.37 O41946 EBI-9640254 0.37 P05412 EBI-11323169 0.35 O43172 EBI-11043099 0.35 P04049 EBI-11084972 0.35 B2BTY8 EBI-11510494 0.40 H9XIJ5 EBI-11514210 0.37 B4URF7 EBI-11514901 0.40 O60885 EBI-11773406 0.49 Q969Y2 EBI-24773699 0.56 P06929 EBI-26501685 0.37 P36799 EBI-26502049 0.37 P24830 EBI-16046619 0.37 P06423 EBI-16046569 0.37 P06790 EBI-16046534 0.37 P36780 EBI-16049148 0.00 Q8IWL3 EBI-15104984 0.37 O95704 EBI-21591300 0.35 O43399 EBI-21732177 0.35 Q6JEL2 EBI-21755575 0.35 O43583 EBI-21785701 0.35 P61081 EBI-21805700 0.35 Q7L5Y6 EBI-21846729 0.35 O14775 EBI-21871177 0.35 Q8TF40 EBI-21875885 0.35 O14879 EBI-15606624 0.59 Q9NRI5 EBI-21371075 0.00 Q92879 EBI-21371061 0.00 P05067 EBI-21371087 0.00 P10636 EBI-21371101 0.00 O84326 EBI-22302779 0.40 Q15831 EBI-34582140 0.35 GO:0070161 GO:0008180 GO:0005737 GO:0005829 GO:0005852 GO:0005654 GO:0005634 GO:0048471 GO:0008021 GO:0019784 GO:0019899 GO:0035718 GO:0046872 GO:0140492 GO:0004222 GO:0008237 GO:0003713 GO:0003743 GO:1990182 GO:0043066 GO:0051091 GO:0045944 GO:0043687 GO:0000338 GO:0016579 GO:0045116 GO:0051726 GO:1903894 GO:0046328 GO:2000434 GO:0006412 Unknown UniProt Sequence Analysis MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS 334 O35864 COP9 Cops5 10090 None SL-0198 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}. UNIPROT O35864 UNIPROT Q3UA70 UNIPROT Q8C1S1 Pfam PF18323 Pfam PF01398 PROSITE PS50249 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}. Q99LD4 EBI-8482462 0.35 GO:0070161 GO:0000785 GO:0008180 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0008021 GO:0005667 GO:0019784 GO:0019899 GO:0035718 GO:0046872 GO:0140492 GO:0004222 GO:0008237 GO:0003713 GO:1990182 GO:0043066 GO:0051091 GO:0045944 GO:0000338 GO:0016579 GO:0051726 GO:0006355 GO:1903894 GO:0046328 Unknown UniProt Sequence Analysis MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINVA 334 Q6GLM9 COP9 cops5 8355 None SL-0198 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}. UNIPROT Q6GLM9 Pfam PF18323 Pfam PF01398 PROSITE PS50249 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}. GO:0070161 GO:0008180 GO:0005829 GO:0005634 GO:0048471 GO:0008021 GO:0046872 GO:0004222 GO:0043066 GO:0051091 GO:0006508 Unknown UniProt Sequence Analysis MAGSSVAQKTWELSNNMQEVQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKVSALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVTYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNAEYTTGQVFDLSEKLEQSEAQLGRGSFMLGLESHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINTF 332 Q6P635 COP9 cops5 8364 None SL-0198 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}. UNIPROT Q6P635 UNIPROT Q28HI7 Pfam PF18323 Pfam PF01398 PROSITE PS50249 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}. GO:0070161 GO:0008180 GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0008021 GO:0019784 GO:0046872 GO:0004222 GO:0008237 GO:0043066 GO:0051091 GO:0000338 Unknown UniProt Sequence Analysis MAMAGSSVAQKTWELSNNMQEVQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKVSALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVTYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINTA 334 Q7L5N1 COP9 COPS6 9606 None SL-0198 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}. UNIPROT Q7L5N1 UNIPROT A4D2A3 UNIPROT O15387 PDB 4D10 PDB 4D18 PDB 4QFT PDB 4R14 PDB 4WSN PDB 6R6H PDB 6R7F PDB 6R7H PDB 6R7I Pfam PF01398 Pfam PF13012 PROSITE PS50249 OMIM 614729 DisGeNET 10980 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}. O75569 EBI-730597 0.00 P04406 EBI-21328549 0.35 P11802 EBI-21328549 0.35 P49454 EBI-21328549 0.35 P50402 EBI-731797 0.00 P78406 EBI-21328549 0.35 Q3TLR7 EBI-2562304 0.40 Q5JTH9 EBI-21328549 0.35 P40425 EBI-348673 0.00 P08670 EBI-475271 0.37 P14174 EBI-7523063 0.40 Q9BX70 EBI-2510262 0.75 Q96RU7 EBI-729666 0.00 Q96HD1 EBI-729816 0.00 O43261 EBI-729873 0.00 Q3KQU3 EBI-729987 0.00 Q9GZN7 EBI-730002 0.00 Q16363 EBI-730249 0.00 Q15102 EBI-730441 0.00 Q6P1K2 EBI-730531 0.00 O00231 EBI-730615 0.00 P40937 EBI-730663 0.00 P15927 EBI-730690 0.00 P21673 EBI-730750 0.00 P50453 EBI-730786 0.00 P62308 EBI-730870 0.00 P04183 EBI-7396449 0.55 P17028 EBI-731131 0.00 Q96SN7 EBI-731467 0.00 Q9Y6N8 EBI-731527 0.00 P42773 EBI-731554 0.00 Q14061 EBI-731602 0.00 P20674 EBI-731608 0.00 Q53FE4 EBI-731683 0.00 O14717 EBI-731731 0.00 P05305 EBI-731764 0.00 Q09472 EBI-731824 0.00 P84090 EBI-731839 0.00 Q9NY59 EBI-731947 0.00 P30519 EBI-732133 0.00 Q9BWC9 EBI-732208 0.00 P06858 EBI-732383 0.00 Q13113 EBI-732452 0.00 Q8IYB7 EBI-732497 0.00 Q8N2I9 EBI-732509 0.00 P51948 EBI-732533 0.00 Q99417 EBI-732572 0.00 P09466 EBI-732710 0.00 P17858 EBI-732806 0.00 Q92561 EBI-732833 0.00 P07602 EBI-732965 0.00 P60484 EBI-733013 0.00 Q9BXR0 EBI-733043 0.00 P51159 EBI-733067 0.00 P11166 EBI-733325 0.00 Q16637 EBI-7388742 0.55 Q13190 EBI-733412 0.00 P49888 EBI-733421 0.00 P13385 EBI-733511 0.00 O60315 EBI-733740 0.00 Q9Y4P8 EBI-734305 0.00 P62861 EBI-734475 0.00 Q8IYL3 EBI-734959 0.00 P61313 EBI-21328549 0.55 P60903 EBI-735711 0.00 P05154 EBI-735763 0.00 P11230 EBI-736505 0.00 P23508 EBI-1064987 0.00 Q99816 EBI-2339285 0.37 Q15018 EBI-8566862 0.35 Q92905 EBI-2510150 0.91 Q9C0D3 EBI-2510262 0.40 Q6TFL4 EBI-2510262 0.56 Q96SW2 EBI-2510262 0.67 Q9UNS2 EBI-2510262 0.88 Q96Q07 EBI-2510262 0.56 Q15048 EBI-2510262 0.56 Q96EF6 EBI-2510262 0.67 Q13618 EBI-2510262 0.56 Q96M94 EBI-2510262 0.56 Q8WXC6 EBI-2510262 0.56 P15374 EBI-2510262 0.40 Q13616 EBI-2510262 0.62 Q9UBW8 EBI-2510262 0.74 Q99627 EBI-2510262 0.85 Q8NEZ5 EBI-2510262 0.40 Q9P2J3 EBI-2510262 0.56 Q13619 EBI-2510262 0.74 Q9H078 EBI-2510262 0.40 Q9H4M3 EBI-2510262 0.56 Q9Y3I1 EBI-2510262 0.67 Q13620 EBI-2510262 0.56 Q13617 EBI-2510262 0.67 Q15369 EBI-2510262 0.56 Q53GT1 EBI-2510262 0.56 Q9UK73 EBI-2510262 0.67 B4DN30 EBI-2510262 0.40 Q8TBC3 EBI-2510262 0.40 Q9H496 EBI-2510262 0.56 Q8TEB1 EBI-2510262 0.67 Q13309 EBI-2510262 0.67 Q9P2K6 EBI-2510262 0.56 Q13216 EBI-2510262 0.56 Q9NZJ0 EBI-2510262 0.56 Q86XK2 EBI-2510262 0.56 Q92466 EBI-2510262 0.67 Q9BW61 EBI-2510262 0.56 Q9BT78 EBI-2510262 0.88 Q647K1 EBI-2510262 0.40 Q9P2G9 EBI-2510262 0.56 Q9Y597 EBI-2510262 0.40 Q9H9Q2 EBI-2510262 0.74 P61201 EBI-2510262 0.81 Q9Y2M5 EBI-2510262 0.40 Q96L50 EBI-2510262 0.67 Q13098 EBI-2510262 0.86 Q9Y4B6 EBI-2510262 0.56 Q9H0C5 EBI-2510262 0.67 P61024 EBI-2510262 0.56 Q5XUX1 EBI-2510262 0.56 Q15843 EBI-2510262 0.56 Q9P2N7 EBI-2510262 0.56 Q93034 EBI-2510262 0.56 P24386 EBI-2515120 0.40 Q3U1J4 EBI-2559059 0.40 A0A6L8PK65 EBI-2835415 0.00 Q13573 EBI-7950968 0.35 Q9H3D4 EBI-3936407 0.37 P04083 EBI-7095166 0.37 P20073 EBI-7097023 0.37 P38936 EBI-7121191 0.37 Q16659 EBI-7206027 0.37 Q16644 EBI-7242276 0.37 P31947 EBI-5279534 0.65 Q8NHY2 EBI-5280877 0.52 Q9UBL3 EBI-5654425 0.00 Q02556 EBI-6115692 0.35 P12520 EBI-6177205 0.35 Q96GG9 EBI-21325177 0.35 Q5VW00 EBI-21328549 0.35 O15061 EBI-21328549 0.35 Q96ME1 EBI-21328549 0.35 Q12951 EBI-21328549 0.35 Q9H469 EBI-21328549 0.35 O94844 EBI-21328549 0.53 Q8N1E6 EBI-21328549 0.53 P10599 EBI-21328549 0.35 Q9H4B7 EBI-21328549 0.35 P68366 EBI-21328549 0.35 Q01085 EBI-21328549 0.35 O60506 EBI-21328549 0.35 P09234 EBI-21328549 0.35 P08621 EBI-21328549 0.35 P05141 EBI-21328549 0.35 P31040 EBI-21328549 0.35 P60866 EBI-21328549 0.35 P15880 EBI-21328549 0.35 P62244 EBI-21328549 0.35 P62263 EBI-21328549 0.35 P05386 EBI-21328549 0.35 P62917 EBI-21328549 0.35 Q02878 EBI-21328549 0.35 P36578 EBI-21328549 0.35 P62899 EBI-21328549 0.35 P83731 EBI-21328549 0.35 P62829 EBI-21328549 0.35 Q07020 EBI-21328549 0.35 Q06830 EBI-21328549 0.35 P13647 EBI-21328549 0.35 Q14568 EBI-21328549 0.35 O14979 EBI-21328549 0.35 Q99729 EBI-21328549 0.35 P13639 EBI-21328549 0.35 P53675 EBI-21328549 0.35 Q07021 EBI-21328549 0.35 P60709 EBI-21328549 0.35 P07437 EBI-21328549 0.35 Q9BQE3 EBI-21328549 0.35 Q92804 EBI-21328549 0.35 P62316 EBI-21328549 0.35 P62701 EBI-21328549 0.35 P05387 EBI-21328549 0.35 P62424 EBI-21328549 0.35 P62913 EBI-21328549 0.35 Q13610 EBI-21328549 0.35 P11940 EBI-21328549 0.35 P06748 EBI-21328549 0.35 P19838 EBI-21328549 0.35 P19338 EBI-21328549 0.35 O95678 EBI-21328549 0.35 P38646 EBI-21328549 0.35 P48741 EBI-21328549 0.35 P11021 EBI-21328549 0.35 P52597 EBI-21328549 0.35 Q14103 EBI-21328549 0.35 Q05639 EBI-21328549 0.35 P17844 EBI-21328549 0.35 O00571 EBI-21328549 0.35 P61962 EBI-21328549 0.35 P68371 EBI-21328549 0.35 Q9Y3Z3 EBI-21328549 0.35 P63173 EBI-21328549 0.35 P36639 EBI-21328549 0.35 P34931 EBI-21328549 0.35 Q9BUJ2 EBI-21328549 0.35 P31942 EBI-21328549 0.35 P31943 EBI-21328549 0.35 P22626 EBI-21328549 0.35 P62280 EBI-21328549 0.35 P61626 EBI-21328549 0.35 Q01546 EBI-21328549 0.35 Q2M2I5 EBI-21328549 0.35 P12268 EBI-21328549 0.35 P07900 EBI-21328549 0.35 P35637 EBI-21328549 0.35 P35527 EBI-21328549 0.35 P14625 EBI-21328549 0.35 Q01844 EBI-21328549 0.35 P06493 EBI-21328549 0.35 Q9UQE7 EBI-21328549 0.35 Q71RC2 EBI-21328549 0.35 Q92734 EBI-21328549 0.35 Q6P5R6 EBI-21328549 0.35 P11142 EBI-21328549 0.35 Q9BRP1 EBI-21328549 0.35 Q9H3F6 EBI-21328549 0.35 P35908 EBI-21328549 0.35 P04264 EBI-21328549 0.35 P61081 EBI-21328549 0.53 P13645 EBI-21328549 0.35 Q8N1G4 EBI-21328549 0.35 Q96MP8 EBI-21328549 0.35 Q6PI47 EBI-21328549 0.35 Q9NXK8 EBI-21328549 0.35 Q53G59 EBI-21328549 0.35 P22830 EBI-21328549 0.35 O95219 EBI-21328549 0.35 Q96T23 EBI-21328549 0.35 P49642 EBI-21328549 0.35 O60237 EBI-21328549 0.35 Q8NDI1 EBI-21328549 0.35 Q9UGM3 EBI-21328549 0.35 Q6P3S6 EBI-21328549 0.35 Q96NC0 EBI-21328549 0.35 P13521 EBI-21328549 0.35 Q92834 EBI-21328549 0.35 Q9H4K1 EBI-21328549 0.35 Q05BQ5 EBI-21328549 0.35 Q8WXI2 EBI-21328549 0.35 P01042 EBI-21328549 0.35 Q9NXE8 EBI-21328549 0.35 Q6IMN6 EBI-21328549 0.35 Q9GZY4 EBI-21328549 0.35 Q9BYV9 EBI-21328549 0.35 O75110 EBI-21328549 0.35 Q9Y2J4 EBI-21328549 0.35 Q10570 EBI-21328549 0.35 Q15370 EBI-21328549 0.35 P63208 EBI-21328549 0.35 Q92673 EBI-21328549 0.35 Q00526 EBI-21328549 0.35 P78396 EBI-21328549 0.35 Q9NXF7 EBI-21328549 0.35 Q3SXM0 EBI-21328549 0.35 Q8WVD3 EBI-21328549 0.35 Q16531 EBI-21328549 0.35 O94889 EBI-21328549 0.35 O94952 EBI-21328549 0.35 Q5T6F0 EBI-21328549 0.35 Q92624 EBI-21328549 0.35 Q8WV16 EBI-21328549 0.53 P24941 EBI-21328549 0.35 P20248 EBI-21328549 0.35 Q7Z7A1 EBI-21328549 0.35 Q8N5D0 EBI-21332205 0.35 Q5TAQ9 EBI-21332205 0.35 Q5QP82 EBI-21332205 0.35 Q96JK2 EBI-21332205 0.35 Q8TEL6 EBI-21332205 0.35 Q58WW2 EBI-21332205 0.35 Q9C0C7 EBI-21332205 0.35 Q53HC5 EBI-21332205 0.35 P57775 EBI-21332205 0.35 Q9Y297 EBI-21332205 0.56 Q9UKB1 EBI-21332205 0.35 Q9UK99 EBI-21332205 0.35 Q8NBE8 EBI-21332942 0.35 P05412 EBI-11323169 0.35 P28482 EBI-11477267 0.54 Q6UXH8 EBI-25277037 0.56 Q8N6Y0 EBI-25280965 0.56 Q13515 EBI-24539227 0.56 Q15911 EBI-24561815 0.56 Q92529 EBI-24585832 0.56 O95704 EBI-21591300 0.35 Q9BQ90 EBI-21622599 0.35 A1L190 EBI-21724977 0.35 Q6JEL2 EBI-21755575 0.35 O43583 EBI-21785701 0.35 Q9UKA1 EBI-21796233 0.35 Q7L5Y6 EBI-21846729 0.35 Q5S007 EBI-21360986 0.35 P04156 EBI-21014477 0.35 Q9NRI5 EBI-21371036 0.00 P06241 EBI-21371020 0.00 Q9BYB0 EBI-26513938 0.37 Q15831 EBI-28941407 0.53 GO:0008180 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0000338 GO:0045116 GO:2000434 Unknown UniProt Sequence Analysis MAAAAAAAAATNGTGGSSGMEVDAAVVPSVMACGVTGSVSVALHPLVILNISDHWIRMRSQEGRPVQVIGALIGKQEGRNIEVMNSFELLSHTVEEKIIIDKEYYYTKEEQFKQVFKELEFLGWYTTGGPPDPSDIHVHKQVCEIIESPLFLKLNPMTKHTDLPVSVFESVIDIINGEATMLFAELTYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVKLILEYVKASEAGEVPFNHEILREAYALCHCLPVLSTDKFKTDFYDQCNDVGLMAYLGTITKTCNTMNQFVNKFNVLYDRQGIGRRMRGLFF 327 Q58CQ0 Protein CUSTOS 9913 None SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}. UNIPROT Q58CQ0 UNIPROT Q58CS2 Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}. GO:0005635 GO:0030178 GO:0060061 GO:0016055 Unknown UniProt Sequence Analysis MSDLESSSSSSSDEEELERCREAALPAWGLEQRPRGPEKPGVDATNAKLPANQPSLMHKVDEHEQDGNELQTTPEFRAHVAKKLGALLDSSITISEIVKEPRKSEVQQGALEDDGFRLFFTSIPGGPEKEAAPQPCRKRLPSSSSSDDGDEELRRCREAAVSASDILQESAIHGHVSVEKKKKRKLKKKAKKEDSADVAATATSKAEVGRQEKESAQLNGDQAPPGTKKKKRKKKTKKASEASLSPPTKSAAAVPSN 257 A9C3N6 Protein custos 7955 None SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:P0DPK0}. UNIPROT A9C3N6 UNIPROT A3KNH5 UNIPROT A8WGJ3 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}. GO:0005635 GO:0097065 GO:0030178 GO:0060061 GO:0016055 Unknown UniProt Sequence Analysis MSESSSEDENTARLKEAVWSFKPEDVKINGKENNGRQSHRADVSKHEHDGNELGTTPEFRSHVAKKLGTYLDGCISEVCSDTVEPAQSENREDEEGFRLFSSSTPGKWMEQSPPPPPKRRPVPSSSDSDSEMEMRFREAAVSLSDILGPVAQNLSEKTEEKSTKEETEDTVTKMKKKKKRKTSSEESQDKVNHQTEKQSNVEGNQEQTTAGERLKKKKKKKKKKRKKLEKDIKKDE 236 Q96C57 Protein CUSTOS 9606 None SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}. UNIPROT Q96C57 UNIPROT Q53HF0 UNIPROT Q9H9Z7 DisGeNET 64897 Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}. P0DTD1 EBI-26495696 0.35 P59595 EBI-27129966 0.35 P54274 EBI-11305569 0.51 Q6P5F9 EBI-11603310 0.35 P48426 EBI-21630443 0.35 Q9HBM1 EBI-21702723 0.35 Q8N128 EBI-21714042 0.35 O95619 EBI-21747731 0.35 Q9UQB9 EBI-21807494 0.35 Q00537 EBI-21871053 0.35 Q6NXT4 EBI-21889655 0.35 P03372 EBI-21301141 0.35 P0DTC9 EBI-27129711 0.35 P15130 EBI-27131516 0.35 Q0ZME3 EBI-27131755 0.35 Q6Q1R8 EBI-27132003 0.35 K9N4V7 EBI-27132270 0.35 P33469 EBI-27132272 0.35 GO:0005635 GO:0030178 GO:0060061 GO:0016055 Unknown UniProt Sequence Analysis MAAPSGTVSDSESSNSSSDAEELERCREAAMPAWGLEQRPHVAGKPRAGAANSQLSTSQPSLRHKVNEHEQDGNELQTTPEFRAHVAKKLGALLDSFITISEAAKEPAKAKVQKVALEDDGFRLFFTSVPGGREKEESPQPRRKRQPSSSSEDSDEEWRRCREAAVSASDILQESAIHSPGTVEKEAKKKRKLKKKAKKVASVDSAVAATTPTSMATVQKQKSGELNGDQVSLGTKKKKKAKKASETSPFPPAKSATAIPAN 262 Q3UY34 Protein Custos 10090 None SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}. UNIPROT Q3UY34 UNIPROT Q3TX98 UNIPROT Q8K0K9 UNIPROT Q9CVB7 Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}. GO:0005635 GO:0030178 GO:0060061 GO:0016055 Unknown UniProt Sequence Analysis MVAPSGAMSDSENSSSSSSDAEELARCREAATPAWGLEQRPGAAERPEAGAADKQAPTPQPSRRHEVNQHEEDGNDLRTTPEFRAHVAKKLGALLDSSIAIAEVWKKSQKAKMQQVAKEEDGFRLFFTSIPGGHKKEASPRPCRKRQPPSSSEDSDEELQRCREAAVSASDILQESAIHCPAKAEEKKKLKKKAKKKVDNADLAAAPGLEQVKEAGVVNGDPVSLGIQKKRKKKAKKSREAPLCPPAECAAAKPEN 256 Q5I034 Protein Custos 10116 None SL-0178 Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}. UNIPROT Q5I034 Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}. GO:0005635 GO:0030178 GO:0060061 GO:0016055 Unknown UniProt Sequence Analysis MVAPSGAMSDSESSSSDSSDAEELARCREAATPAWGLEQRPREAERPAAGTADTQAPAPQPSRRREVNQHDEDGNELQTTPEFRAYVAKKLGALLDSSIAIAEVWKKTQQARLQQEAKEQQEAKEQQAAKEEQAAKKEEDGFRLFFTSVPGGHEKEASPRPCRKRQPPSSSEDSDEELQRCREAAVSASDILQESAIHCPAKVEKEAEKKKLKKKAKKKADADLAAATGLEQVKEAGSVNGDPVLSGTKKKKKKKAKKAREASLCPPAECAAAEPKN 277 P0DPK0 Protein custos 8355 None SL-0178 Nucleus envelope {ECO:0000269|PubMed:25157132}. UNIPROT P0DPK0 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}. GO:0005635 GO:0030178 GO:0060061 GO:0016055 Unknown UniProt Sequence Analysis MAAPRRGTQKSDSDSSDEDLDRFREAAWVPPGAHQKVSDEQNEKIALPSLRVRPDCHEHDGNELQTTPEFRSHVAKKLAAILDSSIREVSQNEAVHISKAGNGDSEDEGFRLFRTSLPGEAGIVTSTIPRRKLASSSSEDSEEEQQRCREAAVSACDILRHSTLQQEPQSTPSNVCDNQPPKKKRKKKKKDRGDTSQINSVEETMHIEPGKNELQAKRKKKKKQKLEMAHCDELGNE 237 O43310 CBP80/20-dependent CTIF 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:19648179}. UNIPROT O43310 UNIPROT B3KTR8 UNIPROT Q8IVD5 Pfam PF02854 OMIM 613178 DisGeNET 9811 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}. A0A2U2H131 EBI-2866199 0.00 Q86VS8 EBI-24326289 0.56 Q9NZD8 EBI-24333116 0.56 Q96MH2 EBI-24352467 0.56 Q6P9E2 EBI-24373771 0.56 Q9NUU7 EBI-24377593 0.67 A9UHW6 EBI-24392534 0.56 Q8N5M1 EBI-24400192 0.56 Q9UMR2 EBI-25260673 0.56 GO:0005829 GO:0048471 GO:0003723 GO:0008494 GO:0000184 GO:0006446 Unknown UniProt Sequence Analysis MENSSAASASSEAGSSRSQEIEELERFIDSYVLEYQVQGLLADKTEGDGESERTQSHISQWTADCSEPLDSSCSFSRGRAPPQQNGSKDNSLDMLGTDIWAANTFDSFSGATWDLQPEKLDFTQFHRKVRHTPKQPLPHIDREGCGKGKLEDGDGINLNDIEKVLPAWQGYHPMPHEVEIAHTKKLFRRRRNDRRRQQRPPGGNKPQQHGDHQPGSAKHNRDHQKSYQGGSAPHPSGRPTHHGYSQNRRWHHGNMKHPPGDKGEAGAHRNAKETMTIENPKLEDTAGDTGHSSLEAPRSPDTLAPVASERLPPQQSGGPEVETKRKDSILPERIGERPKITLLQSSKDRLRRRLKEKDEVAVETTTPQQNKMDKLIEILNSMRNNSSDVDTKLTTFMEEAQNSTNSEEMLGEIVRTIYQKAVSDRSFAFTAAKLCDKMALFMVEGTKFRSLLLNMLQKDFTVREELQQQDVERWLGFITFLCEVFGTMRSSTGEPFRVLVCPIYTCLRELLQSQDVKEDAVLCCSMELQSTGRLLEEQLPEMMTELLASARDKMLCPSESMLTRSLLLEVIELHANSWNPLTPPITQYYNRTIQKLTA 598 Q6PEE2 CBP80/20-dependent Ctif 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q6PEE2 UNIPROT Q6A069 Pfam PF02854 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}. GO:0005829 GO:0048471 GO:0003723 GO:0008494 GO:0000184 GO:0006446 Unknown UniProt Sequence Analysis MENSSAASASSEAGSSRSQEIEELERFIDSYVLEYQVQGLLTDKTEGDGESQRTQSHISQWTADCREQLDGSCSFSRGRAPPQQNGNKDNSLDMLGTDIWAANTFDSFSGATWDLQPEKLDFTQFHRKVRHTPKQPLPHIDREGCGKGKLEDGDGISLNDIEKVLPTWQGYHPMPHEAEIAHTKKLFRRRRNDRRRQQRPPGGNKPQQHGDHQPGSAKHNRDHQKSYQGGSGPHPSGRPTHHGYSQNRRWHHGNMKHPPGDKGEAGSHRNAKETVTVENPKLEDGPGDTGHSGLEPPCSPDTLTPAASERPTPQLPGGPEAEIKHKDTVLPERLRERPKITLLQSSKDRLRRRLKEKDRDEVAVETSSPQPSKMDRLMEILNIMRNNSSDVDAKLTSFMEEAQNSTNSEEMLGEIVRTIYQKAVSDRSFAFTAAKLCDKMALFMVEGTKFRSLLLNMLQKDFTVREELQQQDVERWLGFITFLCEVFGTMRSSTGEPFRVLVCPIYTCLRELLQSQDVKEDAVLCCSMELQSTGRLLEEQLPEMMTELLASARDKMLCPSESMLTRSLLLEVIELHANSWNPLTPPITQYYNRTIQKLTA 600 Q0V9S3 CBP80/20-dependent ctif 8364 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q0V9S3 Pfam PF02854 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}. GO:0005829 GO:0048471 GO:0003723 GO:0008494 GO:0000184 GO:0006446 Unknown UniProt Sequence Analysis MESSSVASASSEAGSSRSLEIEELERFIDSYVLEYQVQGLLTDKTEGDGESDKTQSNVSQWTVECTERLEENRTSPRNREPTYSQNGNKEGPLDMLGTDIWAASTVESISGATWDLQPEKLDFTQLQLRQRNSPKHPPPQIDRDGFGKGKRVEGDDINLNDIEKVLPTWQGYSPLPHEADIAQTKKLFRRKRNDRRKQQKPQGGNKQPPSQQNDHQPATAKHNSREHQRQYHGNPPPPHPSGKQGHHGYSQNRRWHHNQKHLPNDLQRNAKETDTLKIEDASVCTVHIPLDIHSNTDSTERHCPPANDSEAKRKESIQSRDRPKISLLQSSKDRLRRRLKEKEDVAVESTNPQKTKMDKLIEILNSMRNNSSDVDYKLTTFMAEAQNSANSEEMLGEIVKTIYQKAVTDRSFAHTAAKLCDRMALFMVEGTKFRSLLLNMLQKDFSIREEMHRSDVERWLGFITFLCEVFGTMRSNMAEPFRVLVCPIYTCLRELLQSEDVKEDAVLCCSMELQSAGRLLEDQLPEMMSELLATARDKMLCPSESMLTRSLLLEVIELHANSWNPLTPTITQYYNKTIQKLTG 583 Q14999 Cullin-7 CUL7 9606 None SL-0198 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}. UNIPROT Q14999 UNIPROT B4DYZ0 UNIPROT F5H0L1 UNIPROT Q5T654 PDB 2JNG Pfam PF03256 Pfam PF11515 Pfam PF00888 PROSITE PS50069 PROSITE PS51284 OMIM 273750 OMIM 609577 DisGeNET 9820 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}. 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. K9N7C7 EBI-27129420 0.35 O75147 EBI-15927148 0.54 P00519 EBI-1958704 0.40 P0C6X4 EBI-27128759 0.35 P0C6X5 EBI-27128956 0.35 P0C6X6 EBI-27128688 0.35 P29991 EBI-8826732 0.37 Q9ULL4 EBI-311651 0.37 Q96KG7 EBI-308874 0.37 P04637 EBI-1781603 0.83 P07939 EBI-6159787 0.35 Q16539 EBI-6256566 0.35 Q15759 EBI-6381006 0.35 Q13616 EBI-21331736 0.35 Q99IB8 EBI-6928202 0.37 Q7TSJ6 EBI-8797641 0.35 P63208 EBI-8835658 0.35 P48039 EBI-11576948 0.00 B4URF7 EBI-12589250 0.35 Q12798 EBI-21576600 0.35 O14958 EBI-21622768 0.35 Q08380 EBI-21628119 0.35 O60293 EBI-21634559 0.35 Q9UBZ4 EBI-21640250 0.35 Q9H9D4 EBI-21642543 0.35 D6R9G5 EBI-21662389 0.35 P04004 EBI-21709311 0.35 O14978 EBI-21712468 0.35 Q16385 EBI-21766591 0.35 Q96BR6 EBI-21784034 0.35 Q9NXS3 EBI-21857519 0.35 Q92990 EBI-21884908 0.35 Q8N3Y1 EBI-15927108 0.35 Q13557 EBI-16812871 0.35 Q13322 EBI-25382050 0.35 P0DOF2 EBI-25603126 0.35 P48431 EBI-26574619 0.35 Q9H9E1 EBI-26656693 0.35 Q9UNH5 EBI-27113106 0.40 Q15375 EBI-32718158 0.42 GO:1990393 GO:0005680 GO:0005813 GO:0031467 GO:0031461 GO:0005737 GO:0005829 GO:0005794 GO:0048471 GO:0031625 GO:0001837 GO:0007030 GO:0000226 GO:0000281 GO:0001890 GO:0050775 GO:0016567 GO:0006508 GO:0007088 GO:0006511 GO:0001570 Unknown UniProt Sequence Analysis MVGELRYREFRVPLGPGLHAYPDELIRQRVGHDGHPEYQIRWLILRRGDEGDGGSGQVDCKAEHILLWMSKDEIYANCHKMLGEDGQVIGPSQESAGEVGALDKSVLEEMETDVKSLIQRALRQLEECVGTIPPAPLLHTVHVLSAYASIEPLTGVFKDPRVLDLLMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLSEHPMSFEGIQLPQVPGRVLFSLVKRYLHVTSLLDQLNDSAAEPGAQNTSAPEELSGERGQLELEFSMAMGTLISELVQAMRWDQASDRPRSSARSPGSIFQPQLADVSPGLPAAQAQPSFRRSRRFRPRSEFASGNTYALYVRDTLQPGMRVRMLDDYEEISAGDEGEFRQSNNGVPPVQVFWESTGRTYWVHWHMLEILGFEEDIEDMVEADEYQGAVASRVLGRALPAWRWRPMTELYAVPYVLPEDEDTEECEHLTLAEWWELLFFIKKLDGPDHQEVLQILQENLDGEILDDEILAELAVPIELAQDLLLTLPQRLNDSALRDLINCHVYKKYGPEALAGNQAYPSLLEAQEDVLLLDAQAQAKDSEDAAKVEAKEPPSQSPNTPLQRLVEGYGPAGKILLDLEQALSSEGTQENKVKPLLLQLQRQPQPFLALMQSLDTPETNRTLHLTVLRILKQLVDFPEALLLPWHEAVDACMACLRSPNTDREVLQELIFFLHRLTSVSRDYAVVLNQLGARDAISKALEKHLGKLELAQELRDMVFKCEKHAHLYRKLITNILGGCIQMVLGQIEDHRRTHQPINIPFFDVFLRYLCQGSSVEVKEDKCWEKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHTELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEILGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDMAEDRRSLLHLSSRLNGALRQEQNFADRFLPDDEAAQALGKTCWEALVSPVVQNITSPDEDGISPLGWLLDQYLECQEAVFNPQSRGPAFFSRVRRLTHLLVHVEPCEAPPPVVATPRPKGRNRSHDWSSLATRGLPSSIMRNLTRCWRAVVEKQVNNFLTSSWRDDDFVPRYCEHFNILQNSSSELFGPRAAFLLALQNGCAGALLKLPFLKAAHVSEQFARHIDQQIQGSRIGGAQEMERLAQLQQCLQAVLIFSGLEIATTFEHYYQHYMADRLLGVVSSWLEGAVLEQIGPCFPNRLPQQMLQSLSTSKELQRQFHVYQLQQLDQELLKLEDTEKKIQVGLGASGKEHKSEKEEEAGAAAVVDVAEGEEEEEENEDLYYEGAMPEVSVLVLSRHSWPVASICHTLNPRTCLPSYLRGTLNRYSNFYNKSQSHPALERGSQRRLQWTWLGWAELQFGNQTLHVSTVQMWLLLYLNDLKAVSVESLLAFSGLSADMLNQAIGPLTSSRGPLDLHEQKDIPGGVLKIRDGSKEPRSRWDIVRLIPPQTYLQAEGEDGQNLEKRRNLLNCLIVRILKAHGDEGLHIDQLVCLVLEAWQKGPCPPRGLVSSLGKGSACSSTDVLSCILHLLGKGTLRRHDDRPQVLSYAVPVTVMEPHTESLNPGSSGPNPPLTFHTLQIRSRGVPYASCTATQSFSTFR 1698 Q8VE73 Cullin-7 Cul7 10090 None SL-0198 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}. UNIPROT Q8VE73 UNIPROT Q3UHY3 UNIPROT Q497I2 UNIPROT Q6A0D6 UNIPROT Q6PB63 UNIPROT Q8R3W4 UNIPROT Q9CVD5 Pfam PF03256 Pfam PF11515 Pfam PF00888 PROSITE PS01256 PROSITE PS50069 PROSITE PS51284 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}. GO:1990393 GO:0005813 GO:0031467 GO:0031461 GO:0005737 GO:0005794 GO:0048471 GO:0031625 GO:0001837 GO:0007030 GO:0000226 GO:0000281 GO:0001890 GO:0050775 GO:0016567 GO:0045601 GO:0007088 GO:0006511 GO:0001570 Unknown UniProt Sequence Analysis MVGELRYREFRVPLGPGLHAYPDELIRQRVGHNGHPEYQIRWLILRRGDDGDRDSTVDCKAEHILLWMSDDEIYANCHKMLGENGQVIAPSRESTEAGALDKSVLGEMETDVKSLIQRALRQLEECVGTVPPAPLLHTVHVLSAYASIEPLTGIFKDRRVVNLLMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLTEHPMSFEGVQLPQVPGRLLFSLVKRYLHVTFLLDRLNGDAGDQGAQNNFIPEELNVGRGRLELEFSMAMGTLISELVQAMRWDGASSRPESSSSSTFQPRPAQFRPYTQRFRRSRRFRPRASFASFNTYALYVRDTLRPGMRVRMLENYEEIAAGDEGQFRQSNDGVPPAQVLWDSTGHTYWVHWHMLEILGFEEDIEDVIDIEELQELGANGALSIVPPSQRWKPITQLFAEPYVVPEEEDREESENLTQAEWWELLFFIRQLSEAERLHIVDLLQDHLEEERVLDYDMLPELTVPVDLAQDLLLSLPQQLEDSALRDLFSCSVYRKYGPEVLVGHLSYPFVPGAQPNLFGANEESEAKDPPLQSASPALQRLVESLGPEGEVLVELEQALGSEAPQETEVKSCLLQLQEQPQPFLALMRSLDTSASNKTLHLTVLRILMQLVNFPEALLLPWHEAMDACVTCLRSPNTDREVLQELIFFLHRLTTTSRDYAVILNQLGARDAISKVLEKHRGKLELAQELRDMVSKCEKHAHLYRKLTTNILGGCIQMVLGQIEDHRRTHRPIQIPFFDVFLRYLCQGSSEEMKKNRYWEKVEVSSNPQRASRLTDRNPKTYWESSGRAGSHFITLHMRPGVIIRQLTLLVAGEDSSYMPAWVVVCGGNSIKSVNKELNTVNVMPSASRVTLLENLTRFWPIIQIRIKRCQQGGINTRIRGLEVLGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDIAEDRRSLLHLSSRLNGALRHEQNFAERFLPDMEAAQALSKTCWEALVSPLVQNITSPDEDSTSSLGWLLDQYLGCREAAYNPQSRAAAFSSRVRRLTHLLVHVEPREAAPPVVAIPRSKGRNRIHDWSYLITRGLPSSIMKNLTRCWRSVVEEQMNKFLTASWKDDDFVPRYCERYYVLQKSSSELFGPRAAFLLAMRNGCADAVLRLPFLRAAHVSEQFARHIDQRIQGSRMGGARGMEMLAQLQRCLESVLIFSPLEIATTFEHYYQHYMADRLLSVGSSWLEGAVLEQIGPCFPSRLPQQMLQSLNVSEELQRQFHVYQLQQLDQELLKLEDTEKKIQVAHEDSGREDKSKKEEAIGEAAAVAMAEEEDQGKKEEGEEEGEGEDEEEERYYKGTMPEVCVLVVTPRFWPVASVCQMLNPATCLPAYLRGTINHYTNFYSKSQSRSSLEKEPQRRLQWTWQGRAEVQFGGQILHVSTVQMWLLLHLNNQKEVSVESLQAISELPPDVLHRAIGPLTSSRGPLDLQEQKNVPGGVLKIRDDSEEPRPRRGNVWLIPPQTYLQAEAEEGRNMEKRRNLLNCLVVRILKAHGDEGLHVDRLVYLVLEAWEKGPCPARGLVSSLGRGATCRSSDVLSCILHLLVKGTLRRHDDRPQVLYYAVPVTVMEPHMESLNPGSAGPNPPLTFHTLQIRSRGVPYASCTDNHTFSTFR 1689 Q5RCJ3 Cullin-7 CUL7 9601 None SL-0198 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}. UNIPROT Q5RCJ3 Pfam PF03256 Pfam PF11515 Pfam PF00888 PROSITE PS50069 PROSITE PS51284 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}. GO:1990393 GO:0005813 GO:0031467 GO:0005737 GO:0005794 GO:0048471 GO:0031625 GO:0001837 GO:0007030 GO:0000226 GO:0000281 GO:0001890 GO:0050775 GO:0016567 GO:0007088 GO:0006511 Unknown UniProt Sequence Analysis MVGELRYREFRVPLGPGLHAYPDELIRQRVGHDGHPEYQIRWLILRRGDEGDGGSGQVDCKAEHILLWMSKDEIYANCHKMLGEDGQVIGPSQESTGEVGALDKSVLEEMETDVKSLIQRALRQLEECVGTIPPAPLLHTVHVLSAYASIEPLTGVFKDPRVLDLLMHMLSSPDYQIRWSAGRMIQALSSHDAGEGQCGEEGKAGEELGRLRDSQDTVAGASDLIRTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLSEHPMSFEGIQLPQVPGRVLFSLVKRYLHVTSLLDQLNDSAAEPGAQNTSAPEEWSGERGQLELEFSMAMGTLISELVQAIRWDQASDRPRSSARSPGSIFQPQLADVSPGLPATQAQPSFRRSRHFRPRSEFASGNTYALYVRDTLQPGMRVRMLDEYEEISAGDEGEFRQSNNGVPPVQVLWESTGRTYWVHWHMLEILGFEEDIEDMVEADEYQGAVASRVLGRALPAWRWRPMTELYAVPYVLPEDEDSEECEHLTLAEWWELLFFIKKLDGPDHQEVLQILQENLDGEILDDEILAELAVPIELAQDLLLTLPQRLNDSALRDLINCHVYKKYGPEALAGNPAYPSLLEAQEDVLLEAQAQAKDSEDAAKVEAKEPPSQSPNTPLQRLVEGYGPAGKILLDLEQALSSEGTQENKVKPLLLQLQRQPQPFLALMQSLDTPETNRTLHLTVLRILKQLVDFPEALLLPWHEAVDACMACLRSPNTDREVLQELIFFLHRLTSVSRDYAVVLNQLGARDAISKALEKHLGKLELAQELRDMVFKCEKHAHLYRELITNILGGCIQMVLGQIEDHRRTHRPINIPFFDVFLRYLCQGSSVEVKEDKCWEKVEVSSNPHRASKLTDRNPKTYWESNGSAGSRYITLHMRQGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHTELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLETLGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDMAEDRRSLLHLSSRLNGALRQEQNFADRFLPDNEAAQALGKTCWEALVSPVVQNITSPDEDGISPLGWLLDQYLECQEAVFNPQSRGPAFFSRVRRLTHLLVHVEPCEAPPPVVATPRPKGRNRSHDWSSLATRGLPSSIMRNLTRCRRAVVEKQVNNFLTSSWRDDDFVPRYCEHFNILQNSSSELFGPRAAFLLALQNGCAGALLKLPFLKAAHVSEQFARHIDQQIQGSRIGGAQEMERLAQLQQCLQAVLIFSGLEIATTFEHYYQHYMADRLLGVVSSWLEGAVLEQIGPCFPNRLPQQMLQSLSTSKELQRQFHVYQLQQLDQELLKLEDTEKKIQVGHGASGKEHKSEKEEEAGAAAAVDVAEGEEEEEENEDLYYEGAMPEVSVLVLSRHCWPVASICHTLNPRTCLPSYLRGTLNRYSNFYNKSQSHPALERGSQRRLQWTWLGWAELQFGNQTLHVSTVQMWLLLYLNDLKAVSVESLLALSGLSADMLNQAIGPLTSSRGPLDLHEQKDIPGGVLKIRDGSKEPRSRWDIVRLIPPQTYLQAEGEEGRNLEKRRNLLNCLIVRILKAHGDEGLHIDQLVCLVLEAWQKGPCPPRGLVSSLGKGSACSSTDVLSCILHLLGKGTLRRHDDRPQVLSYAVPVTVMEPHTESLNPGSSGPNPPLTFHTVQIRSRGVPYASCTATQSFSTFR 1729 D3ZEF4 Cullin-7 Cul7 10116 None SL-0198 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}. UNIPROT D3ZEF4 Pfam PF03256 Pfam PF11515 Pfam PF00888 PROSITE PS50069 PROSITE PS51284 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}. P0DL28 EBI-15927289 0.40 Q9BYV6 EBI-21998606 0.35 GO:1990393 GO:0005813 GO:0031467 GO:0031461 GO:0005737 GO:0005794 GO:0048471 GO:0031625 GO:0001837 GO:0007030 GO:0000226 GO:0000281 GO:0001890 GO:0050775 GO:0016567 GO:0007088 GO:0006511 GO:0001570 Unknown UniProt Sequence Analysis MVGELRYREFRVPLGPGLHAYPDELIRQRVGHNGHPEYQIRWLILRRGDDGDSSQVDCKAEHILLWMTDDEIYANCHKMLGEDGQVIRPSQESAEAGALDKSVLGEMETDVKSLIQRALRQLEECVGAVPPAPLLHTVHVLSAYASIEPLTGVFKDRRVLDLVMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLTEHPMSFEGVQLPQVPGRLLFSLVKRYLCVTFLLDRLNGNAEDQDAQNNFIPEELNAGRGRVELEFSMAMGTLISELVQAMRWDWASSRSESSSPIFQPPPTEFFRPRAQRFRRSRRFRPRTAFASVNTYALYVRDTLRPGMRVRMLEDFEEISAGDEGQFRQSNDGMPPVQVLWDSTGHTYWVHWHMLEILGFEEDIEDVVDIDDQGAMVHGGLGVAPPFQHWKPIAQLFAEPYVVPEEEDREEREHLTQAEWWELFFFIKKLNAEERQHVVELLQEFLEGEHVLDFEILPELTVPVELAQDLMLSLPQQLDDSALRDLFNCYVYRKYGPEVLVGKRNRPFVLDDQLNLFRIETDSEAQDPPSQSASPALRQLVEGLGPSGKLLVDLERALSSEAPQENEVKPCLLQLQEEPQPFLTLMRSLDTPASNKALHLTALRILMQLVNFPEALLLPWHEAMDACMTCLRSPNTDREVLQELIFFLHRLTSTSRDYAVILNQLGARDAISKVLEKHRGKLELAQELRDMVFKCEKHAHLYRKLTTNILGGCIQMVLGQIEDHRRTHRPIQIPFFDVFLRYLCQGSSAEVKKNKYWEKVEVSSNPHRASRLTDRNAKTYWESNGTAGSHFITVHMRPGVLIRQLTLLVAGEDSSYMPAWVVVCGGDSISSVNTELNAVNVMPHASRVILLENLTRFWPIVQIRIKRCQQGGINTRIRGLEVLGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDIAEDRRSLLHLSSRLNGALRQEQNFADRFLPDEEAALALSKTCWEALVSPLVQNITSPDEDSTSSLGWLLNQYLECREAAYNPQSRAAAFSSRVRHLTHLLVHVEPCEAAPPVVAISQSKGRNRSHDWSSLTTRGLPSSIMRNLTRCWRSVVEEQVNKFLTSSWKDDDFVPRYCERYYILQKSSSELFGPRAAFLLAMRNGCADALLRLPFLRAAHVSEQFARHIDQRIQGSRMGGARGMEMLAQLQRCLESVLILSPLEIATTFEHYYQHYMADRLLSVGSSWLEGAVLEQIGPCFPGRLPQQMLQTLNISEELQRRFHVYQLQQLDQELLKLEDTEKKIQVAHEDSGKEHKSKKEDAAGETAAVAMADEEEEEGKKEEGEEEEGEGEEELEEEEERYYEGTMPEVCVLVLSPRFWPVASVCHMLNPTTCLPSYLRGTINHYSNFYSKSQSHSGLEKESPRQLQWTWQGRAEVQFGDQILHVSTVQMWLLLHLNHLKAVSVESLQALSELPPEVLNKAIGPLTSSRGPLDLQEQKNIPGGVLKIRDDSEEPRPRRGNVWLIPPQTYLKAEDEEGRNLEKRRNLLNCLVVRILKAHGDEGLHIDQLVHLVLEAWEKGPCPPRGLVSSLGRGAACRSSDVLSCILHLLGKGTLRRHDDRPQMLFYAVPITVMEPHTESLNPGSSGPNPPLTFHTLQIRSRGVPYASCTGTQTFSTFR 1692 P38937 Tethering cut8 284812 None SL-0178 Nucleus envelope {ECO:0000269|PubMed:11084332, ECO:0000269|PubMed:28974540}. UNIPROT P38937 PDB 3Q5W PDB 3Q5X Pfam PF08559 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}. P50524 EBI-1152618 0.52 P41878 EBI-1152637 0.40 P87048 EBI-1152745 0.54 P40303 EBI-1152891 0.40 P23566 EBI-1153015 0.43 P38937 EBI-15946480 0.62 GO:0000785 GO:0005635 GO:0034399 GO:0005634 GO:0042802 GO:0032934 GO:0034080 GO:0071630 GO:0031144 Unknown UniProt Sequence Analysis METLSYSQIKKRKADFDEDISKRARQLPVGEQLPLSRLLQYSDKQQLFTILLQCVEKHPDLARDIRGILPAPSMDTCVETLRKLLINLNDSFPYGGDKRGDYAFNRIREKYMAVLHALNDMVPCYLPPYSTCFEKNITFLDAATNVVHELPEFHNPNHNVYKSQAYYELTGAWLVVLRQLEDRPVVPLLPLEELEEHNKTSQNRMEEALNYLKQLQKNEPLVHERSHTFQQTNPQNNFHRHTNSMNIGNDNGMGWHSMHQYI 262 P85091 Cytoplasmic CYFIP1 9913 None SL-0198 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}. UNIPROT P85091 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}. GO:0070161 GO:0030027 GO:0005845 GO:0043005 GO:0048471 GO:0001726 GO:0045202 GO:0051015 GO:0031267 GO:0048675 GO:0030032 GO:0008360 GO:0031529 Unknown UniProt Sequence Analysis MYLTPSEKRINLSKVHPTDKLADQIFAYYKEGERDGKDEIIKNVPLKRIRK 51 Q90YM8 Cytoplasmic cyfip1 7955 None SL-0198 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}. UNIPROT Q90YM8 UNIPROT Q58ES3 Pfam PF07159 Pfam PF05994 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}. GO:0070161 GO:0005737 GO:0030027 GO:0043005 GO:0048471 GO:0001726 GO:0031209 GO:0045202 GO:0051015 GO:0000340 GO:0031267 GO:0048675 GO:0007411 GO:0000902 GO:0030031 GO:0030032 GO:0099563 GO:0030833 GO:0008360 GO:0006417 GO:0031529 Unknown UniProt Sequence Analysis MASTVTLEDALSNVDLLEELPLPDQQPCIEPLPSSLIYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNDMLEEGQQYAVMLYTWRCCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVNKLMNFMYFQRTAIDRFCGEVRRLCHAERRKDFVSEAYLLTLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMSEPSSIQESQNLSMFLANHNKITQSLQQQLEVINGYDELLADIVNLCVDYYENKMYLTPSERHMLLKVMGFGLYLMDGSNSNIYKLEAKKRINLTKIDKFFKQLQVVPLFGDMQIELARYIKTSAHYEENKSRWSCTSTGSSPQYNVCEQMIQIREGHMRFISELARYSNSEVVTGSGRQDAQKTDSEYRKLFDLALQGLQLLSQWSAQIMEVYSWKLVHPTDKYSNKECPDNAEEYERATRYNYTSEEKFALVEVLAMIKGLQVLMGRMESVFNHAIRHTIYSALQDFAQVTLREPLRQAIKKKKNVVQSVLQAIRKTVCDWETGREPHNDPALRGEKDPKGGFDIKVPRRAVGPSSTQLYMVRTMLESLVADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLLNFSETLQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVIAGSLLLDKRLRAECKNQGANISWPSSNRYETLLKQRHVQLLGRSIDLNRLITQRVSSALYKSLELAISRFESEDLTSIMELEGLLDINRMTHKLLSKYLTLDSIDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTILPFSQEFQRDKPPNAQPQYLYGSKALNLAYSSIYSLYRNFVGPPHIKAICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKICRLPRHEYGSPGILEFFHHQLKDIVEYAELKSVCFQNLREVGNALLFCLLTEQSLSQEEVCDLLHAAPFQNILPRVHVKEGERLDAKMKRLEAKYTALHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSIFEVILTRVRAYLDDPIWRGPLPSNGVMHVDECVEFHRLWSAMQFVYCIPVGAHEFTVEQCFGDGLNWAGCMIITLLGQHRRFDILDFSYHLLKVQKHDGKDEIIKSVPLKKMVDRIRKFQILNDEIFAILNKYLKSGDGENMPVEHVRCFQPPIHQSLASN 1253 Q7L576 Cytoplasmic CYFIP1 9606 None SL-0198 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}. UNIPROT Q7L576 UNIPROT A8K6D9 UNIPROT Q14467 UNIPROT Q5IED0 UNIPROT Q6ZSX1 UNIPROT Q9BSD9 UNIPROT Q9BVC7 PDB 3P8C PDB 4N78 Pfam PF07159 Pfam PF05994 OMIM 606322 DisGeNET 23191 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}. P00533 EBI-32720286 0.27 Q06787 EBI-3649503 0.49 Q5SQX6 EBI-16086797 0.35 Q8IZP0 EBI-7160735 0.74 Q04917 EBI-307271 0.35 Q96L34 EBI-354787 0.35 P63104 EBI-2433948 0.35 O60861 EBI-7721151 0.40 P61981 EBI-1067488 0.00 Q5S2C4 EBI-1548622 0.37 Q9Y2A7 EBI-1548644 0.81 Q38919 EBI-1548679 0.37 P06730 EBI-2000653 0.44 P63073 EBI-2000573 0.52 Q5NFJ2 EBI-2807484 0.00 Q96F07 EBI-3649667 0.27 P62873 EBI-3917485 0.37 P47872 EBI-3917502 0.37 Q15029 EBI-3917512 0.37 Q8HWS3 EBI-3925636 0.37 P36873 EBI-4311602 0.37 Q8BM65 EBI-7447792 0.40 Q6PFX7 EBI-7447775 0.40 Q9Y6X6 EBI-7447809 0.40 Q92558 EBI-7448569 0.35 Q9NYB9 EBI-9206143 0.83 Q8WUW1 EBI-9208427 0.35 Q9P2E7 EBI-9206479 0.40 Q13200 EBI-9378392 0.40 Q8K2C9 EBI-9378349 0.40 Q15773 EBI-9378370 0.40 Q9UIM3 EBI-9378414 0.40 Q5S007 EBI-9515510 0.53 P50221 EBI-21248543 0.37 Q5JST6 EBI-21248535 0.37 Q9Z1B5 EBI-10996176 0.35 Q921T2 EBI-10996616 0.35 Q8VC57 EBI-11027413 0.35 Q9UHB6 EBI-11058729 0.35 Q99PT9 EBI-11092405 0.35 Q9D902 EBI-11096128 0.35 Q8CAF4 EBI-11096313 0.35 Q96QS3 EBI-11107478 0.35 P12004 EBI-11109663 0.35 Q9UQB8 EBI-11135710 0.35 Q86X19 EBI-11372615 0.27 Q9H251 EBI-12449357 0.35 Q9BSM1 EBI-12553841 0.35 O43639 EBI-21521290 0.35 Q3ZCQ8 EBI-21581953 0.35 Q96EV8 EBI-21651992 0.35 Q9ULV8 EBI-21715242 0.35 Q5HYW2 EBI-21762959 0.35 Q400G9 EBI-21768785 0.35 Q6NT52 EBI-21804311 0.35 Q70UQ0 EBI-21813594 0.35 Q9UPY6 EBI-21852540 0.35 Q8NB15 EBI-21893201 0.35 P63000 EBI-15768401 0.53 Q9Y6W5 EBI-15894678 0.35 P15311 EBI-16791848 0.27 P11142 EBI-16794528 0.35 O43493 EBI-16800982 0.35 Q13557 EBI-16812871 0.35 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 P03372 EBI-21301141 0.35 Q8IWW6 EBI-25410934 0.35 Q9C0B5 EBI-25636144 0.35 P01023 EBI-25830152 0.56 P51608 EBI-25875938 0.56 P07196 EBI-25877581 0.56 O76024 EBI-25898349 0.56 O14901 EBI-25905196 0.56 O60333 EBI-25915439 0.56 Q7Z699 EBI-25931793 0.56 A0A0H3NJM6 EBI-27055677 0.35 A0A0H3NF08 EBI-27055973 0.27 P13569 EBI-27084109 0.35 Q15375 EBI-32721052 0.27 P29323 EBI-32721290 0.27 GO:0044295 GO:0090724 GO:0005829 GO:0044294 GO:0043197 GO:0060076 GO:0070062 GO:0005576 GO:0032433 GO:0005925 GO:0030027 GO:0005845 GO:0043005 GO:0043025 GO:0048471 GO:0090725 GO:0001726 GO:0031209 GO:0034774 GO:0035580 GO:0045202 GO:0043195 GO:1904724 GO:0051015 GO:0000340 GO:0031267 GO:0045182 GO:0048675 GO:0007411 GO:0000902 GO:0030031 GO:0032869 GO:0050890 GO:0097484 GO:0030032 GO:0099563 GO:1903422 GO:2000601 GO:0045773 GO:1900006 GO:0010592 GO:0051388 GO:1900029 GO:0016601 GO:0030833 GO:0008360 GO:1905274 GO:0031641 GO:0006417 GO:0099578 GO:0051602 GO:0031529 Unknown UniProt Sequence Analysis MAAQVTLEDALSNVDLLEELPLPDQQPCIEPPPSSLLYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGQEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMNFMYFQRNAIERFCGEVRRLCHAERRKDFVSEAYLITLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNKITQSLQQQLEVISGYEELLADIVNLCVDYYENRMYLTPSEKHMLLKVMGFGLYLMDGSVSNIYKLDAKKRINLSKIDKYFKQLQVVPLFGDMQIELARYIKTSAHYEENKSRWTCTSSGSSPQYNICEQMIQIREDHMRFISELARYSNSEVVTGSGRQEAQKTDAEYRKLFDLALQGLQLLSQWSAHVMEVYSWKLVHPTDKYSNKDCPDSAEEYERATRYNYTSEEKFALVEVIAMIKGLQVLMGRMESVFNHAIRHTVYAALQDFSQVTLREPLRQAIKKKKNVIQSVLQAIRKTVCDWETGHEPFNDPALRGEKDPKSGFDIKVPRRAVGPSSTQLYMVRTMLESLIADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLINFSETLQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTRFNKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVMAGSLLLDKRLRSECKNQGATIHLPPSNRYETLLKQRHVQLLGRSIDLNRLITQRVSAAMYKSLELAIGRFESEDLTSIVELDGLLEINRMTHKLLSRYLTLDGFDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTVLPFSQEFQRDKQPNAQPQYLHGSKALNLAYSSIYGSYRNFVGPPHFQVICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKICRLPRHEYGSPGILEFFHHQLKDIVEYAELKTVCFQNLREVGNAILFCLLIEQSLSLEEVCDLLHAAPFQNILPRVHVKEGERLDAKMKRLESKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSFLDDPIWRGPLPSNGVMHVDECVEFHRLWSAMQFVYCIPVGTHEFTVEQCFGDGLHWAGCMIIVLLGQQRRFAVLDFCYHLLKVQKHDGKDEIIKNVPLKKMVERIRKFQILNDEIITILDKYLKSGDGEGTPVEHVRCFQPPIHQSLASS 1253 Q7TMB8 Cytoplasmic Cyfip1 10090 None SL-0198 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}. UNIPROT Q7TMB8 UNIPROT O88558 UNIPROT Q3U7Q7 UNIPROT Q5DU50 UNIPROT Q7TSZ5 UNIPROT Q80VN6 UNIPROT Q8CE85 UNIPROT Q99LY1 Pfam PF07159 Pfam PF05994 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}. O08788 EBI-16727444 0.35 P15209 EBI-16727444 0.35 P16054 EBI-16727444 0.35 P35922 EBI-2000004 0.58 P61205 EBI-16727444 0.35 P63318 EBI-16727444 0.35 Q06787 EBI-3649150 0.37 Q5SQX6 EBI-16727444 0.35 Q6ZPE2 EBI-16727444 0.35 P62158 EBI-911456 0.35 P63073 EBI-2000004 0.63 O55135 EBI-2000004 0.40 P62754 EBI-2000004 0.40 Q8BM65 EBI-7448021 0.35 P26450 EBI-7448114 0.46 Q8R5H6 EBI-7448095 0.53 Q5DU14 EBI-7448718 0.35 Q80TE2 EBI-9214306 0.35 Q6ZPJ3 EBI-16727444 0.35 Q8C7R4 EBI-16727444 0.35 Q9QUQ5 EBI-16727444 0.35 Q9CQE1 EBI-16727444 0.35 P61358 EBI-16727444 0.35 Q62159 EBI-16727444 0.35 Q921J2 EBI-16727444 0.35 Q8CHG7 EBI-16727444 0.35 O35239 EBI-16727444 0.35 P48437 EBI-16727444 0.35 Q8C167 EBI-16727444 0.35 Q80U63 EBI-16727444 0.35 Q03717 EBI-16727444 0.35 Q8VI75 EBI-16727444 0.35 P24547 EBI-16727444 0.35 Q9R0I7 EBI-16727444 0.35 Q9R1R2 EBI-16727444 0.35 O55013 EBI-16727444 0.35 Q9CYZ2 EBI-16727444 0.35 B2RWJ3 EBI-16727444 0.35 Q8CC35 EBI-16727444 0.35 F6SEU4 EBI-16727444 0.53 Q68FG2 EBI-16727444 0.35 Q62261 EBI-16727444 0.35 P16546 EBI-16727444 0.35 Q61548 EBI-16727444 0.35 Q8JZR6 EBI-16727444 0.35 Q4ACU6 EBI-16727444 0.35 D3YZU1 EBI-16727444 0.35 Q8VD37 EBI-16727444 0.35 Q8K0T0 EBI-16727444 0.35 Q8BSK8 EBI-16727444 0.35 P63001 EBI-16727444 0.35 P68404 EBI-16727444 0.35 P63087 EBI-16727444 0.35 Q7M6Y3 EBI-16727444 0.35 E9Q3L2 EBI-16727444 0.35 Q2M3X8 EBI-16727444 0.35 O89084 EBI-16727444 0.35 Q9WU78 EBI-16727444 0.35 O88643 EBI-16727444 0.35 Q9Z1M0 EBI-16727444 0.35 P58281 EBI-16727444 0.35 O08919 EBI-16727444 0.35 P46460 EBI-16727444 0.35 Q11011 EBI-16727444 0.35 P08553 EBI-16727444 0.35 P08551 EBI-16727444 0.35 P19246 EBI-16727444 0.35 P28660 EBI-16727444 0.35 Q9Z0E0 EBI-16727444 0.35 P55066 EBI-16727444 0.35 Q99104 EBI-16727444 0.35 Q8K310 EBI-16727444 0.35 Q9QXZ0 EBI-16727444 0.35 Q8BHA1 EBI-16727444 0.35 P28740 EBI-16727444 0.35 Q8R0S2 EBI-16727444 0.35 P35436 EBI-16727444 0.35 Q921M4 EBI-16727444 0.35 P15105 EBI-16727444 0.35 Q8K1B8 EBI-16727444 0.35 F8VPU2 EBI-16727444 0.35 Q8BWY3 EBI-16727444 0.35 Q6PH08 EBI-16727444 0.35 Q9WV92 EBI-16727444 0.35 Q9Z2H5 EBI-16727444 0.35 P62631 EBI-16727444 0.35 Q9JHU4 EBI-16727444 0.35 Q9R0P5 EBI-16727444 0.35 O35098 EBI-16727444 0.35 O08553 EBI-16727444 0.35 Q8BZ98 EBI-16727444 0.35 P39054 EBI-16727444 0.35 Q8K1M6 EBI-16727444 0.35 P39053 EBI-16727444 0.35 Q80TZ3 EBI-16727444 0.35 Q62108 EBI-16727444 0.35 Q91XM9 EBI-16727444 0.35 Q9JLM8 EBI-16727444 0.35 Q9QXS6 EBI-16727444 0.35 Q9JLV5 EBI-16727444 0.35 P97427 EBI-16727444 0.35 O54991 EBI-16727444 0.35 P80318 EBI-16727444 0.35 P47754 EBI-16727444 0.35 Q3UHL1 EBI-16727444 0.35 P28652 EBI-16727444 0.35 P11798 EBI-16727444 0.35 Q8BKX1 EBI-16727444 0.35 P59999 EBI-16727444 0.35 Q60875 EBI-16727444 0.35 Q9DBG3 EBI-16727444 0.35 P17426 EBI-16727444 0.35 P61967 EBI-16727444 0.35 O35643 EBI-16727444 0.35 Q99NH0 EBI-16727444 0.35 Q8C8R3 EBI-16727444 0.35 Q3UHD9 EBI-16727444 0.53 P60710 EBI-16727444 0.35 Q8CBW3 EBI-16727444 0.35 Q3UHJ0 EBI-16727444 0.35 Q9WV60 EBI-16727444 0.35 Q9QYS2 EBI-16727444 0.35 P83510 EBI-16734044 0.35 Q9EP53 EBI-16734894 0.35 Q9D415 EBI-16725590 0.35 GO:0070161 GO:0044295 GO:0090724 GO:0005737 GO:0044294 GO:0043197 GO:0060076 GO:0032433 GO:0030027 GO:0005845 GO:0043005 GO:0043025 GO:0048471 GO:0090725 GO:0098794 GO:0001726 GO:0031209 GO:0045202 GO:0043195 GO:0051015 GO:0005522 GO:0000340 GO:0031267 GO:0045182 GO:0048675 GO:0007411 GO:0000902 GO:0030031 GO:0032869 GO:0050890 GO:0097484 GO:0030032 GO:0099563 GO:1903422 GO:0031175 GO:2000601 GO:0045773 GO:0050772 GO:1900006 GO:0010592 GO:0051388 GO:1900029 GO:0016601 GO:0030833 GO:0008360 GO:1905274 GO:0031641 GO:0006417 GO:0099578 GO:0051602 GO:0031529 Unknown UniProt Sequence Analysis MAAQVTLEDALSNVDLLEELPLPDQQPCIEPPPSSLLYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGQEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMNFMYFQRNAIERFCGEVRRLCHAERRKDFVSEAYLITLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNKITQSLQQQLEVISGYEELLADIVNLCVDYYENRMYLTPSEKHMLLKVMGFGLYLMDGSVSNIYKLDAKKRINLSKIDKYFKQLQVVPLFGDMQIELARYIKTSAHYEENKSRWTCASSSSSPQYNICEQMIQIREDHMRFISELARYSNSEVVTGSGRQEAQKTDAEYRKLFDLALQGLQLLSQWSAHVMEVYSWKLVHPTDKYSNKDCPDNAEEYERATRYNYTTEEKFALVEVIAMIKGLQVLMGRMESVFNHAIRHTVYAALQDFSQVTLREPLRQAIKKKKNVIQSVLQAIRKTVCDWETGHEPFNDPALRGEKDPKSGFDIKVPRRAVGPSSTQLYMVRTMLESLIADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLINFSETLQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTKFNKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVMAGSLLLDKRLRSECKNQGATIHLPPSNRYETLLKQRHVQLLGRSIDLNRLITQRVSAAMYKSLELAIGRFESEDLTSVVELDGLLEINRMTHKLLSRYLTLDSFDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTVLPFSQEFQRDKQPNAQPQYLHGSKALNLAYSSIYGSYRNFVGPPHFQVICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKICRLPRHEYGSPGILEFFHHQLKDIVEYAELKTVCFQNLREVGNAVLFCLLIEQSLSLEEVCDLLHAAPFQNILPRIHVKEGERVDAKMKRLESKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRTFLDDPIWRGPLPSNGVMHVDECVEFHRLWSAMQFVYCIPVGTHEFTVEQCFGDGLHWAGCMIIVLLGQQRRFAVLDFCYHLLKVQKHDGKDEIIKNVPLKKMVERIRKFQILNDEIITILDKYLKSGDGESTPVEHVRCFQPPIHQSLASS 1253 Q96F07 Cytoplasmic CYFIP2 9606 None SL-0198 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}. UNIPROT Q96F07 UNIPROT A6NLT2 UNIPROT D3DQJ3 UNIPROT Q53EN5 UNIPROT Q9NTK4 UNIPROT Q9ULQ2 UNIPROT Q9UN29 Pfam PF07159 Pfam PF05994 OMIM 606323 OMIM 618008 DisGeNET 26999 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}. 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. P00533 EBI-32720286 0.27 Q06787 EBI-3649591 0.53 Q7L576 EBI-3649667 0.27 Q9Y2A7 EBI-7160508 0.32 Q8IZP0 EBI-7160598 0.56 Q9Y6W5 EBI-7160648 0.40 Q04917 EBI-307271 0.53 P63104 EBI-2433948 0.35 O60861 EBI-7721256 0.40 Q9P2A4 EBI-7087991 0.40 A0A6L7HB35 EBI-2817304 0.00 P51116 EBI-3650359 0.37 P51114 EBI-3650316 0.37 Q13485 EBI-3918179 0.49 Q13489 EBI-3929935 0.37 P00747 EBI-3938582 0.37 Q5D1E8 EBI-3943196 0.37 P31946 EBI-8796749 0.35 Q5S007 EBI-9515510 0.35 P15884 EBI-11322276 0.35 O43639 EBI-21521290 0.35 Q3ZCQ8 EBI-21581953 0.35 Q9NSC5 EBI-21639932 0.35 Q96EV8 EBI-21651992 0.35 Q9ULV8 EBI-21715242 0.35 Q969G2 EBI-21754639 0.35 Q5HYW2 EBI-21762959 0.35 Q400G9 EBI-21768785 0.35 Q9NYB9 EBI-21786440 0.35 Q9BQS6 EBI-21789770 0.35 Q6NT52 EBI-21804311 0.35 O60826 EBI-21812182 0.35 Q70UQ0 EBI-21813594 0.35 Q9UPY6 EBI-21852540 0.35 Q8NB15 EBI-21893201 0.35 Q8N3R9 EBI-21912043 0.35 P03950 EBI-16363232 0.35 O15155 EBI-16788067 0.27 P15311 EBI-16791848 0.27 P11142 EBI-16794405 0.27 P11279 EBI-16794808 0.27 O43493 EBI-16800265 0.27 Q13557 EBI-16812871 0.35 P30559 EBI-20811004 0.37 P03372 EBI-21302175 0.35 Q9NRI5 EBI-21377438 0.00 Q8TB24 EBI-26518569 0.35 O14733 EBI-28930089 0.35 O43283 EBI-28930960 0.35 O60566 EBI-28931243 0.35 P23469 EBI-27116439 0.27 P21709 EBI-32720516 0.27 P54764 EBI-32720816 0.27 Q15375 EBI-32721052 0.27 P29323 EBI-32721290 0.27 P11362 EBI-32721578 0.27 P22455 EBI-32722168 0.27 Q16288 EBI-32724526 0.27 Q01974 EBI-32725367 0.27 GO:0070161 GO:0005737 GO:0005829 GO:0070062 GO:0016020 GO:0043005 GO:0005634 GO:0048471 GO:0031209 GO:0045202 GO:0031267 GO:0097202 GO:0006915 GO:0000902 GO:0098609 GO:0097484 GO:0051388 GO:0045862 GO:0030833 Unknown UniProt Sequence Analysis MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLTLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLADIVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKQLQVVPLFGDMQIELARYIKTSAHYEENKSKWTCTQSSISPQYNICEQMVQIRDDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLLSKWSAHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFAFVEVIAMIKGLQVLMGRMESVFNQAIRNTIYAALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGGREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQACQWSPRALFHPTGGTQGRRGCRSLLYMVRTMLESLIADKSGSKKTLRSSLDGPIVLAIEDFHKQSFFFTHLLNISEALQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEPSMMEYVLYPLDLYNDSAYYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKAMAGSVLLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRISAAMYKSLDQAISRFESEDLTSIVELEWLLEINRLTHRLLCKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYCYNGSTNRFVRTAIPFTQEPQRDKPANVQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKIVKSLLQGTILQYVKTLIEVMPKICRLPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAILFCLLIEQALSQEEVCDLLHAAPFQNILPRVYIKEGERLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSYLQDPIWRGPPPTNGVMHVDECVEFHRLWSAMQFVYCIPVGTNEFTAEQCFGDGLNWAGCSIIVLLGQQRRFDLFDFCYHLLKVQRQDGKDEIIKNVPLKKMADRIRKYQILNNEVFAILNKYMKSVETDSSTVEHVRCFQPPIHQSLATTC 1278 Q5SQX6 Cytoplasmic Cyfip2 10090 None SL-0198 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}. UNIPROT Q5SQX6 UNIPROT Q3UH21 UNIPROT Q3UHS8 UNIPROT Q8BSW0 UNIPROT Q8CHA9 UNIPROT Q924D3 UNIPROT Q9R181 Pfam PF07159 Pfam PF05994 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}. P05783 EBI-16086797 0.35 P35922 EBI-16727864 0.35 Q03001 EBI-16086797 0.35 Q62108 EBI-2307988 0.53 Q8CBW3 EBI-2642480 0.53 P50516 EBI-6272793 0.35 Q8BPN8 EBI-6272767 0.35 Q9Y2A7 EBI-16086775 0.35 Q8WUW1 EBI-16086775 0.35 Q9NYB9 EBI-16086775 0.35 Q92558 EBI-16086775 0.35 Q5SYE7 EBI-16086797 0.35 Q92614 EBI-16086797 0.35 Q3ZCQ8 EBI-16086797 0.35 O14735 EBI-16086797 0.35 P13796 EBI-16086797 0.35 Q9UHB6 EBI-16086797 0.35 O00443 EBI-16086797 0.35 P16615 EBI-16086797 0.35 P05787 EBI-16086797 0.35 Q9Y6W5 EBI-16086797 0.35 Q9UPY6 EBI-16086797 0.35 P08727 EBI-16086797 0.35 Q7L576 EBI-16086797 0.35 Q7TMB8 EBI-16727444 0.35 Q7TPH6 EBI-16727864 0.35 Q64514 EBI-16727864 0.35 P83510 EBI-16727864 0.35 Q4ACU6 EBI-16727864 0.50 D3YZU1 EBI-16727864 0.35 Q8BYM5 EBI-16727864 0.35 P17426 EBI-16727864 0.35 Q8R5H6 EBI-16727864 0.35 Q812A2 EBI-16727864 0.35 Q68FG2 EBI-16727864 0.35 Q62261 EBI-16727864 0.35 P16546 EBI-16727864 0.35 A2AQ25 EBI-16727864 0.35 Q8C437 EBI-16727864 0.35 B1AXH1 EBI-16727864 0.35 Q8K1R7 EBI-16727864 0.35 P28660 EBI-16727864 0.35 Q99104 EBI-16727864 0.35 O35099 EBI-16727864 0.35 Q08460 EBI-16727864 0.35 P46660 EBI-16727864 0.35 Q8VDC1 EBI-16727864 0.35 P39053 EBI-16727864 0.35 B9EJA2 EBI-16727864 0.35 Q02248 EBI-16727864 0.35 O54991 EBI-16727864 0.35 P15116 EBI-16727864 0.35 P70408 EBI-16727864 0.35 Q6P9K8 EBI-16727864 0.35 P28652 EBI-16727864 0.35 P11798 EBI-16727864 0.35 Q8K3H0 EBI-16727864 0.35 P62484 EBI-16727864 0.35 Q9EP53 EBI-16734894 0.35 Q9D415 EBI-16725590 0.35 Q3UHD9 EBI-16736255 0.35 F6SEU4 EBI-16737600 0.35 GO:0070161 GO:0005737 GO:0043005 GO:0005634 GO:0048471 GO:0031209 GO:0045202 GO:0031267 GO:0097202 GO:0006915 GO:0000902 GO:0098609 GO:0097484 GO:0031175 GO:0051388 GO:0045862 GO:0030833 Unknown UniProt Sequence Analysis MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHDYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLTLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLADIVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKQLQVVPLFGDMQIELARYIKTSAHYEENKSKWTCTQSSISPQYNICEQMVQIRDDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLLSKWSAHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFAFVEVIAMIKGLQVLMGRMESVFNQAIRNTIYAALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGGREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQLYMVRTMLESLIADKSGSKKTLRSSLDGPIVLAIEDFHKQSFFFTHLLNISEALQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEPSMMEYVLYPLDLYNDSAYYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKAMAGSVLLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRISAAMYKSLDQAISRFESEDLTSIVELEWLLEINRLTHRLLCKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYCYNGSTNRFVRTAIPFTQEPQRDKPANVQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKIVKSLLQGTILQYVKTLIEVMPKICRLPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAILFCLLIEQALSQEEVCDLLHAAPFQNILPRVYIKEGERLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSYLQDPIWRGPPPTNGVMHVDECVEFHRLWSAMQFVYCIPVGTNEFTAEQCFGDGLNWAGCSIIVLLGQQRRFDLFDFCYHLLKVQRQDGKDEIIKNVPLKKMADRIRKYQILNNEVFAILNKYMKSVETDSSTVEHVRCFQPPIHQSLATTC 1253 Q5R414 Cytoplasmic CYFIP2 9601 None SL-0198 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}. UNIPROT Q5R414 UNIPROT Q5R6T9 Pfam PF07159 Pfam PF05994 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}. GO:0070161 GO:0005737 GO:0043005 GO:0005634 GO:0048471 GO:0045202 GO:0031267 GO:0006915 GO:0098609 GO:0030833 Unknown UniProt Sequence Analysis MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLTLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLADIVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKQLQVVPLFGDMQIELARYIETSAHYEENKSKWTCTQSSISPQYNICEQMVQIRDDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLLSKWSAHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFAFVEVIAMIKGLQVLMGRMESVFNQAIRNTIYAALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGGREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQLYMVRTMLESLIADKSGSKKTLRSSLDGPIVLAIEDFHKQSFFFTHLLNISEALQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEPSMMEYVLYPLDLYNDSAYYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKAMAGSVLLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRISAAMYKSLDQAISRFESEDLTSIVELEWLLEINRLTHRLLCKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYCYNGSTNRFVRTAIPFTQEPQRDKPANIQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKIVESLLQGTILQYVKTLIEVMPKICRLPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAILFCLLIEQALSQEEVCDLLHAAPFQNILPRVYIKEGERLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSYLQDPIWRGPPPTNGVMHVDECVEFHRLWSAMQFVYCIPVGTNEFTAEQCFGDGLNWAGCSIIVLLGQQRRFDLFDFCYHLLKVQRQDGKDEIIKNVPLKKMADRIRKYQILNNEVFAILNKYMKSVETDSSTVEHVRCFQPPIHQSLATTC 1253 Q1RMU2 Ubiquitin CYLD 9913 None SL-0198 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}. UNIPROT Q1RMU2 Pfam PF01302 Pfam PF00443 PROSITE PS00845 PROSITE PS50245 PROSITE PS00972 PROSITE PS50235 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}. GO:0005813 GO:0036064 GO:0097542 GO:0005881 GO:0005829 GO:0031234 GO:0030496 GO:0048471 GO:0005819 GO:0004843 GO:0061578 GO:0070064 GO:0019901 GO:0008270 GO:0045087 GO:0070266 GO:0090090 GO:0050728 GO:2000493 GO:0046329 GO:0032088 GO:1901223 GO:1903753 GO:2001238 GO:0016579 GO:0070536 GO:1990108 GO:1902017 GO:0050727 GO:2001242 GO:0070507 GO:0007346 GO:0060544 GO:0010803 GO:0006511 GO:0016055 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q9NQC7} MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQNIQDRSVGLSRIPSAKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDTGLESDYAGPVDTMQVELPPLEINSRVSLKLGETIESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTILLHINDIIPESVTQERRPPKLAFMSRGVGDKGSFSHNKPKATGSTSDPGTRNRSELFYTLNGSSVDSQPQSKSKNSWYIDEVAEDPAKSLTEIPPDFGHASPPLQPPSMNSLSSENRFHSLPFSLTKMPNTNGSISHSPLSLSVQSVMGELNNAPVQESPPLAVSSGNSHGLEVGSLAEVKENPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGFEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFMEKNEKVGVPTIQQLLECSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCNAQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLDDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK 953 Q9NQC7 Ubiquitin CYLD 9606 None SL-0198 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}. UNIPROT Q9NQC7 UNIPROT O94934 UNIPROT Q7L3N6 UNIPROT Q96EH0 UNIPROT Q9NZX9 PDB 1IXD PDB 1WHL PDB 1WHM PDB 2VHF PDB 7OWD Pfam PF01302 Pfam PF00443 PROSITE PS00845 PROSITE PS50245 PROSITE PS00972 PROSITE PS50235 OMIM 132700 OMIM 601606 OMIM 605018 OMIM 605041 OMIM 619132 DisGeNET 1540 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}. 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. P02545 EBI-16796283 0.27 P0DTD1 EBI-27030072 0.35 Q6ZMQ8 EBI-32723474 0.27 P06463 EBI-2117974 0.35 P03126 EBI-2118003 0.35 O95786 EBI-8021116 0.52 Q7Z434 EBI-8021151 0.40 Q14164 EBI-8021199 0.40 Q9UHD2 EBI-8021169 0.40 P0CG48 EBI-6965887 0.44 Q8TEP8 EBI-2510419 0.40 Q9UM54 EBI-2510419 0.40 Q8IUW3 EBI-2510419 0.40 Q13557 EBI-2510419 0.40 Q9UM82 EBI-2510419 0.59 O60502 EBI-2510419 0.40 Q92995 EBI-2511562 0.40 Q71U36 EBI-7572503 0.58 Q9UBN7 EBI-7572848 0.58 A0A3N4B3K9 EBI-2848127 0.00 Q9Y6K9 EBI-3928546 0.55 Q96J02 EBI-5326486 0.40 P31946 EBI-8796749 0.35 Q7TSJ6 EBI-8798662 0.27 P04083 EBI-9028892 0.35 Q5BJF6 EBI-11367291 0.27 Q6ZU80 EBI-11370150 0.27 Q66GS9 EBI-11386281 0.27 Q8N137 EBI-11392655 0.27 Q9Y2I6 EBI-11399685 0.27 Q6P5F9 EBI-11603310 0.35 Q8IWL3 EBI-13943458 0.35 P62993 EBI-21557652 0.35 Q14314 EBI-21816328 0.35 Q9NYA1 EBI-21871146 0.35 P61981 EBI-21905461 0.35 P15311 EBI-16791848 0.27 Q15388 EBI-16801791 0.27 Q9NPJ6 EBI-25472202 0.27 Q68FS2 EBI-22254510 0.35 Q80W92 EBI-22254510 0.35 Q9WUD9 EBI-22254510 0.35 Q5XIA5 EBI-22254510 0.35 P09875 EBI-22254510 0.35 A0A0G2K064 EBI-22254510 0.35 B0BNB9 EBI-22254510 0.35 P0C0A2 EBI-22254510 0.35 B0BN56 EBI-22254510 0.35 P15651 EBI-22254510 0.35 D3ZYG0 EBI-22254510 0.35 P36972 EBI-22254510 0.35 B5DFA5 EBI-22254510 0.35 D3Z9C0 EBI-22254510 0.35 P14604 EBI-22254510 0.35 G3V8S2 EBI-22254510 0.35 M0R7K1 EBI-22254510 0.35 D3ZT90 EBI-22254510 0.35 D3ZIL6 EBI-22254510 0.35 P15650 EBI-22254510 0.35 P63252 EBI-27067929 0.27 P41212 EBI-29015445 0.27 Q9UM73 EBI-32719830 0.27 P22455 EBI-32722168 0.27 Q96ED9 EBI-34575530 0.27 GO:0005813 GO:0036064 GO:0097542 GO:0005829 GO:0031234 GO:0005874 GO:0048471 GO:0005819 GO:0004843 GO:0061578 GO:0070064 GO:0019901 GO:0008270 GO:0007049 GO:0045087 GO:0070266 GO:0090090 GO:0050728 GO:2000493 GO:0046329 GO:0032088 GO:1901223 GO:1903753 GO:0032480 GO:0070423 GO:2001238 GO:0016579 GO:0070536 GO:1990108 GO:1902017 GO:0050727 GO:2001242 GO:0070507 GO:0007346 GO:0060544 GO:0010803 GO:0006511 GO:0016055 Peripheral UniProt Sequence Analysis MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRIPSAKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDTALESDYAGPGDTMQVELPPLEINSRVSLKVGETIESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFACVESTILLHINDIIPALSESVTQERRPPKLAFMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAKSLTEISTDFDRSSPPLQPPPVNSLTTENRFHSLPFSLTKMPNTNGSIGHSPLSLSAQSVMEELNTAPVQESPPLAMPPGNSHGLEVGSLAEVKENPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCNTQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQNMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK 956 Q80TQ2 Ubiquitin Cyld 10090 None SL-0198 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}. UNIPROT Q80TQ2 UNIPROT Q80VB3 UNIPROT Q8BXZ3 UNIPROT Q8BYL9 UNIPROT Q8CGB0 Pfam PF01302 Pfam PF00443 PROSITE PS00845 PROSITE PS50245 PROSITE PS00972 PROSITE PS50235 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}. Q9Z2F6 EBI-943890 0.67 P68369 EBI-7572707 0.56 Q9Z2V5 EBI-7572735 0.50 Q8C863 EBI-5326509 0.40 P01375 EBI-16186378 0.35 Q9D415 EBI-16725590 0.35 Q4ACU6 EBI-16726570 0.35 Q9QWI6 EBI-27100778 0.35 GO:0005813 GO:0036064 GO:0097542 GO:0005881 GO:0005829 GO:0031234 GO:0030496 GO:0048471 GO:0005819 GO:0004843 GO:1990380 GO:0061578 GO:0070064 GO:0019901 GO:0008270 GO:0043369 GO:0048872 GO:0045087 GO:0070266 GO:0090090 GO:0050728 GO:2000493 GO:0046329 GO:0032088 GO:1901223 GO:1903753 GO:2001238 GO:1903829 GO:0045582 GO:0050862 GO:0016579 GO:0070536 GO:1990108 GO:0045577 GO:1902017 GO:0050727 GO:2001242 GO:0070507 GO:0007346 GO:0060544 GO:0043393 GO:0050856 GO:0010803 GO:1901026 GO:0006511 GO:0016055 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q9NQC7} MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRVPSTKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERLSLFRNRLRLSKGLQVDVGSPVKVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDNGLESDFAGPGDTMQVEPPPLEINSRVSLKVGESTESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTILLHINDIIPDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQQSKSKNPWYIDEVAEDPAKSLTEMSSDFGHSSPPPQPPSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPLPISSGNAHGLEVGSLAEVKENPPFYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSALDTVLLRPKEKNDIEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCSTQVHLHPRRLNHSYHPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK 952 Q5RED8 Ubiquitin CYLD 9601 None SL-0198 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}. UNIPROT Q5RED8 Pfam PF01302 Pfam PF00443 PROSITE PS00845 PROSITE PS50245 PROSITE PS00972 PROSITE PS50235 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}. GO:0005813 GO:0036064 GO:0097542 GO:0005829 GO:0005874 GO:0048471 GO:0005886 GO:0005819 GO:0004843 GO:0061578 GO:0008270 GO:0045087 GO:0090090 GO:0050728 GO:2000493 GO:0046329 GO:0032088 GO:1901223 GO:1903753 GO:0016579 GO:0070536 GO:1990108 GO:1902017 GO:0050727 GO:0010803 GO:0006511 GO:0016055 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q9NQC7} MSSGLWSQDKVTSPYWEERVFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRIPSAKGKKNRIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDTALESDYAGPGDTMQVELPPLEINSRVSLKVGETIESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFACVESTILLHINDIIPALSESVTQERRPPKLAFMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAKSLTEISTDFDRSSPPLQPPPVNSLSTENRFHSLPFSLTKMPNTNGSIGHSPLSLSAQSVMEELNTAPVQESPPLAMPPGNSHGLEVGSLAEVKENPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCNTQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQNMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK 956 Q66H62 Ubiquitin Cyld 10116 None SL-0198 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}. UNIPROT Q66H62 Pfam PF01302 Pfam PF00443 PROSITE PS00845 PROSITE PS50245 PROSITE PS00972 PROSITE PS50235 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}. GO:0005813 GO:0036064 GO:0097542 GO:0005829 GO:0031234 GO:0005874 GO:0048471 GO:0005819 GO:0004843 GO:1990380 GO:0061578 GO:0070064 GO:0019901 GO:0008270 GO:0043369 GO:0048872 GO:0045087 GO:0070266 GO:0090090 GO:0050728 GO:2000493 GO:0046329 GO:0032088 GO:1901223 GO:1903753 GO:2001238 GO:1903829 GO:0045582 GO:0050862 GO:0016579 GO:0070536 GO:1990108 GO:0045577 GO:1902017 GO:0050727 GO:2001242 GO:0070507 GO:0007346 GO:0060544 GO:0043393 GO:0010803 GO:1901026 GO:0006511 GO:0016055 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q9NQC7} MSSGLWNQEKVTSPYWEERLFYLLLQECSVTDKQTQKLLRVPKGSIGQYIQDRSVGHSRVPSAKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERLSLFRNRIRLSKGLQVDVGSPVRVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDNGLESDFAGPGDTVQVEPPPLEINSRVSLKVGESTESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTVLLHINDIIPDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQQQSKSKNPWYIDEVAEDPAKSLTEMSSDFGHSSPPPQPPSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPMPSSSGNAHGLEVGSLAEVKENPPFYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSALDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCSTQVHLHPRRLNHTYHPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK 953 Q6NUT2 Probable DPY19L2 9606 None SL-0178 SL-0179 SL-0182 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}. UNIPROT Q6NUT2 UNIPROT A4FVC1 UNIPROT B4E191 UNIPROT Q3ZCX2 UNIPROT Q6UWG8 UNIPROT Q96LZ9 Pfam PF10034 OMIM 613893 OMIM 613958 DisGeNET 283417 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}. 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. P0DTC7 EBI-26495729 0.35 Q16774 EBI-21888393 0.40 P19739 EBI-25685423 0.35 P0DTD8 EBI-25687199 0.35 Q7TFA1 EBI-25688644 0.35 GO:0016021 GO:0005637 GO:0005634 GO:0000030 GO:0018406 GO:0007286 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRKQGVSSKRLQSSGRSQSKGRRGASLAREPEVEEEMEKSALGGGKLPRGSWRSSPGRIQSLKERKGLELEVVAKTFLLGPFQFVRNSLAQLREKVQELQARRFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRVLKVN 758 P0CW70 Probable Dpy19l2 10090 None SL-0178 SL-0179 SL-0182 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}. UNIPROT P0CW70 Pfam PF10034 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}. GO:0016021 GO:0005637 GO:0000030 GO:0018406 GO:0007286 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVGPTRSKLREGSSDRPQSSCTGQARRRWSAATMEPQQERSAPQERTKWSLLQHFLLGGRKLPSGARNYAARRIQSLNAQNYFQLEEVAKLLLLNRFQFLFTLLDHFREKVQALQMHRFSHRTLFGLAIFVGILHWLHLITLFENDHHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLVINTVKRFHLYPEVVIAYWYRTIIGIMNLFGIETKTCWNVTRMEPLNEVQSCEGLGDPACFYIGVIFILNGLMMGLFFIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKIQKLGGTELQFWLIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYIKTLLLPLILVITYLIFKKIVRDIMCVLYTNTYVRKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMASLICSQRLFGWLFCRIHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSILLKDSRPYFTTVFQNSMYRVLKIN 773 A6RC50 ATP-dependent DBP5 2059318 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A6RC50 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MATETPAGGPLEARISRAEPKTDASATSEPATGDTTETPAATKPSAADGQTDGASEGFGGSQLQEPEYSVNVKLSDLQADPNNPLYSIKSFEELGLHPSILQGLHSMSFRRPSKIQEKALPLLLNNPPANMIGQSQSGTGKTAAFVLNILSRLDLSPQMELAPQALVLAPSRELARQIVGVIQVMGSYVDKLKVATAVPMESNRNQKVEAPVVVGTPGTVMDLIRKRLFNPQHLKVIVLDEADNMLDQQGLGDQCIRVKGLLPKNIQVVLFSATFPDHVVRYANKFAPNANQITLKHEELTVEGIKQLYLDCDSDEHKFDILVKFYGLLTIGSSIIFVKTRASAVEIERRMVAEGHTVVSLTGGVEGQKRDEIIDKFRQGDAKVLITTNVLARGIDVQTVSMVINYDIPELHAPKATKRIADAQTYLHRIGRTGRFGRVGVAVSFVASKEEWQMLQDIKTYFNTEIQRVNTQDWDEVEEVVKTIIRSSRAGSNFQRS 497 Q75C39 ATP-dependent DBP5 284811 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q75C39 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005634 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MSGNAQKPDASEMLADLDLNKKTKETTLEAGSAESAPSAPAENQAKSDSNLINSEYEVKVRLADIQADPNSPLYSVKSFEELGLAPELLKGLYAMKFQKPSKIQERALPLLLHNPPRNMIAQSQSGTGKTAAFSLTMLSRVDVAVPATQAICLAPSRELARQTLEVIQEMGKFTKIASQLIVPDSYEKNKAINAHIIVGTPGTVLDLMRRKMIQLGKVKTFVLDEADNMLDKQGLGDQCIRVKKFLPKDTQLVLFSATFDDSVREYARRVVPNANSLELQRNEVNVSAIKQLFMDCNDERHKFTVLCDLYGLLTIGSSIIFVQTKQTANMLYTELKREGHQVSILHGDLQSADRDRLIGDFREGRSKVLITTNVLARGIDIPTVSMVVNYDLPMTANGQPDPSTYVHRIGRTGRFGRTGVAISFIHDKKSYETLAAIQSYFGDIQITKVPTDDMDEMEKIVKKVLK 466 A1CFV3 ATP-dependent dbp5 344612 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A1CFV3 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MASEQPVEAAPLGGSLSDRISKPDEPTASETPEQTSDQADGASAPLGGSDLREPEYNVEVKLSDLQADPNNPLYSVKNFEDLGLDPRILKGLSAMNFRKPSKIQERALPLLLGNPPKNLVGQSQSGTGKTAAFVLNALSRVDLSTEQMQKTPQALILAPTRELARQIVGVVSVMGQFLDGLIIGTAVPADINNRPKRLECSIAVGTPGTVMDMIKRRIMVPNKLKVLVLDEADNMLDQQGLGDQCIRVKALLPRDIQVVLFSATFPDHVHAYAAKFAPNANELTLQHEELTVEGIKQLYLDCSDEEDKYKTLVQLYGLLTVGSSIIFVQTRTSASEIEKRMVAEGHTVASLTGGIDVTKRDEIIDKFRSGEAKVLITTNVLARGIDVSTVSMVINYDIPELHRPGVPERQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWDMLNQIQRYFNTEIQRVDTKDWDEVEDIIKKTIKNTRANAQFGKQ 487 Q4WIN6 ATP-dependent dbp5 330879 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q4WIN6 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005634 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MASEQPVEAAPTGGSLADRITKPDESNTSETPAPIGDQTDGAPAQLGGSDLHEPEYNVEVKLSDLQADPNNPLYSVKNFEDLGLDPRILKGLSSMNFRKPSKIQERALPLLLNNPPKNLVGQSQSGTGKTAAFVLNALSRVDLSTEQMQKTPQALILAPTRELARQILGVVQVMGQFVDGLIIGAAVPTDRDSRPKRLECSIVVGTPGTVGDMIKRRTFIPNKLKVLVLDEADNMLDQQGLGDQCIRVKALLPRDIQVVLFSATFPEHVHQYASKFAPNANEITLQHEELTVEGIKQLYLDCADGEDKYRTLVQLYGLLTVGSSIIFVQTRAAAQEIERRMTAEGHTVVSLTGERDPSVRDAIIDQFRRGEAKVLIATNVLARGIDVSTVSMVINYDIPELHQPNVPGRQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWEMLNQIQTYFNCEIQRVDTKDWDEVEDIIKKTIKNSRANPKFAGGKD 489 A2QUY7 ATP-dependent dbp5 425011 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A2QUY7 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MASEQPEAGSLADRITKPEEPAPAEAPEQTEDIPQTDGAAAQQGGSDLHEPDYTVEVKLSDLQADPNNPLFSVKNFEDLGLDPRILQGLSAMNFRKPSKIQERALPLLLGNPAKNLVGQSQSGTGKTAAFVLNILSRLDLSSEQLQKTPQALILAPTRELARQIVGVIQVMGQFLDGLVIGTAVPADTGARPAKMECSVVVGTPGTVMDMIKRRIMIANKLRVLVLDEADNMLDQQGLGDQCIRVKALLPRDIQVVLFSATFPAHVHEYASKFAPQANEITLQHEELTVEGIKQLYLDCSNDEDKYQTLVNLYGLLTVGSSIIFVKTRASAQEIEKRMVAEGHTVASLTGGIEGSQRDAVIDQFRAGHAKVLITTNVLARGIDVSTVSMVINYDIPEIHQPGARQRQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWEMLNQIQRYFNTNIQRIDTKDWDEVEEIIKKTIKSSRAQLGFR 482 Q2U8K6 ATP-dependent dbp5 510516 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q2U8K6 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MSAEQPAETASAGNPLADRITTADGSKPEGTTETTDNEQADGAAAQLGGSELNEPDYTVEVKLSDLQADPNNPLYSVKSFEDLGLDPRILQGLSAMNFRKPSKIQERALPLLLNNPPKNLVGQSQSGTGKTAAFVLNALSRLDLSTEQAQKTPQALILAPTRELARQIVGVIQCMGQFLDGLNVSTAVPADTNSRHSKIESSVVVGTPGTVMDMIRKRVMVANKLKVLVLDEADNMLDQQGLGDQCIRVKALLPKDIQVVLFSATFPTHVHQYASKFAPQANELTLQHEELTVEGIKQLYLDCSDEEDKYKTLVQLYGLLTVASSIIFVKTRASAAEIEKRMVAEGHTVASLTGGIEGSQRDAVIDQFRAGQAKVLITTNVLARGIDVSTVSMVINYDIPELHQPGAPERQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWNMLNQIQQYFNCTIQRVDTKDWDEVEDIIKKTIKNTRAQAQFGR 487 Q0CDT1 ATP-dependent dbp5 341663 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q0CDT1 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MSSEQPTEAPAGGSLADRISKPEESKPADSTQQPTDNGQTDGAPAQLGGSELHEPEYNVEVKLSDLQADPNNPLFSVKNFEDLGLDPRILQGLSAMNFRKPSKIQERALPLLLSNPPKNLVGQSQSGTGKTAAFVLNILSRLDLSTEQMQKTPQALILAPTRELARQIVGVIQVMGQFLDNLIIGTAVPADTNNRPARMEASVVVGTPGTVMDMIKKRIMVPAKLQVLVLDEADNMLDQQGLGDQCIRVKALLPRTIQVVLFSATFPTHVHQYASKFAPQANELTLQHEELTVEGIKQLYLDCSDEEDKYRTLVSLYGLLTVGSSIIFVKTRQSAMEIEKRMVAEGHTVASLTGGIEGSQRDAVIDQFRAGAAKVLITTNVLARGIDVSTVSMVINYDIPELHLPPNQPRQADFQTYLHRIGRTGRFGRVGVSISFVSNRDEWNMLNQIQKYFNTSIQRIDTKDWDEVEDIIKKTIKNPRSQATFGK 487 A6SBT4 ATP-dependent dbp5 332648 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A6SBT4 Pfam PF00270 Pfam PF00271 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0051028 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MAESKSTSWADEVASPTIEKNEGNPLEEAQLDGATEPLGGGTLQDGQYEVEVKLSDIQGDETSPLYSVETFEQLGIDASILKGLYAMNFKKPSKIQEKALPLLLRNPPTNMIAQSQSGTGKTAAFVITILSRLDFSKPTTPQALCLAPSRELARQIEGVIRSIGQFVDGLTVQAAIPGAVERNAKVNAMVVVGTPGTVMDLIKRRSIDASQMKILCLDEADNMLDQQGLGDQCMRVKSMIRVEQILLFSATFPDEVYGFAQDFSPRANEIKLKRDELTVSGIKQMFMDCPNEVGKYEILVKLYGLMTIGSSIIFVKRRDTASNIAERLTKEGHKVAAVHGAFEGSERDQVLEDFRQGKAKVLITTNVLARGIDVQSVSMVINYDVPMKGRSDSDPPPETYLHRIGRTGRFGRVGVSISFVFDRKSYDALNQIANHYNIDLIKLNQDDWDETEEIVKKVIKSSRAGTNLQS 470 Q5AJD0 ATP-dependent DBP5 237561 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q5AJD0 UNIPROT A0A1D8PJB3 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005634 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MSSEKVKRVEADATDLLASLSIDKSGEKLEEIKKGSTPDPSDLLGGLSLKEGDSKKPEEKKEVVEEPENKEINDDKKDEDKKDESKDEVKDGDGAKEETKEEVKEESKEEPKEPKEPKEPATNLIKSSYEVKVKLADIQADPNSPLYSVKSFEELGLSPELLKGLYAMKFNKPSKIQEKALPLLLSNPPRNMIGQSQSGTGKTAAFSLTMLSRVDPTIKMPQCLCLSPTRELARQTLEVITTMGKFTNITTQLVVPNAIPRGSSVNAQVLVGTPGIAIDLIRRRQLNLSKMKVFVLDEADNMLEAQGLGDQAIRVKKALPRGVQLVLFSATFPTEVREYAERLVPDANSLELKQEELNVDGIKQLYMDCRSEQHKFEVLCELYGLLTIGSSIIFVEKKETADVLYGKMKKEGHTVSVLHGGLDNTDRDRLIDDFREGRSKVLITTNVLARGIDIASVSMVVNYDMPTDKYGKPDPSTYLHRIGRTGRFGRVGVSISFIHDRRSYDILMAIKAYFGNVEMTRVPTDDWDEVEKIVKKVIKS 540 Q6FKN8 ATP-dependent DBP5 284593 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q6FKN8 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MSATEDKKDPASMLAELKLDKDEGNKTPETKTPESNSAETKTTEEVKELKNPFTQKKEDVENDAAEEKTNEVNKDDAKDERENKDTNLIKSEYEVKVNLADLQADPNSPLYSVKSFDELGLSPELLKGIYAMKFQKPSKIQERALPLLLSNPPRNMIAQSQSGTGKTAAFSLTMLSRVDETQNVPQAICLAPSRELARQTLEVIQEMGKYTKITTQLIVPDSFEKNTKINANVVVGTPGTLLDLIRRKLIQLQNVKIFVLDEADNMLDKQGLGDQCIRVKKFLPKDTQLVLFSATFADAVKAYAQKVIPNANTLELQRNEVNVKAIKQLYMDCNDEAHKYEVLCELYGLLTIGSSIIFVAKKDTANLLYGKLKHEGHQVSILHSDLRTDERDRLIDDFREGRSKVLITTNVLARGIDIPSVSMVVNYDLPTLPNGMPDYATYVHRIGRTGRFGRTGVAISFVHDKKSFKILSAIQDYFKDIELTRVPTDDWDEVEDIVKKVLKQ 504 Q2HGF7 ATP-dependent DBP5 306901 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q2HGF7 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0051028 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MADLASRITKPSDEPVDAVAPAPTATTGEGNGTEEPVDDGVNKGLVETTYDVEVKLSGLQADDESLLYSGVASFEELGLAKSINDGLLAMNFKKPSKIQEKALPLMLSNPPRNMIAQSQSGTGKTAAFVLTVLSRVDLTKPTQPQALLLAPSRELARQIQSVIQTIGQFCENLNVEAAIPGSISRETGVRANVVVGTPGTVMDLIRRRQFDVSQLKIMVIDEADNMLDQQGMGDQCVRVKGMLPKDIQTLLFSATFPEKVMIFARKYATNAHEIKLRHTDLTVKGISQMYMDCPDESKKYDILCKLYGLMTIGSSVIFVRTRESASEIQRRMEADGHKVSALHGAHEGQNRDALLDDFRSGRSKVLITTNVLARGIDVSSVSMVINYDIPMKGPGDKEPDMETYLHRIGRTGRFGRVGVSISFVYDRKSYDALSKIADHYGLDLVQLAPDDWDATETKVQEVIKSSRARPDYVPNAGDK 479 Q1EB85 ATP-dependent DBP5 246410 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q1EB85 UNIPROT J3KGE1 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0051028 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MASENTTETPSVPAGGPLAARISRPEGDANPPSTEAEKPAAEDDSGKGPSIPQVDGASEDQRGSELQDSEFDVNVKLSDLQADPNNPLYSIKSFEELGLAEPIQMGLSKMNFRRPSKIQERALPLLMANPPTNMIAQSQSGTGKTAAFVLNILSRLELTPEKQKSPQALVLAPSRELARQIVGVIQAMGTFVEGLFVATAVPMEMNRNQRVEASIVVGTPGTVQDLIKKRLFNTQHLRVLVLDEADNMLDQQGLGDQCIRVKSLLPRTIQVVLFSATFPDFVVRYAHKFAPNSNQLTLKHEELTVEGIKQLYLDCESDEHKYEILVKFYGLLTIGSSIIFVKTRASAAEIERRMVAEGHTVVSLTGGIEGQKRDEIIDRFRNGTAKVLITTNVLARGIDVSTVSMVINYDIPELHLPGAARRMADAQTYLHRIGRTGRFGRVGVAVSFVSNQEEWQMLQDIQKYFSTNIERVDTRDWDDVEKKVKKIIKPSAVAR 495 P0CQ87 ATP-dependent DBP5 283643 None SL-0178 SL-0182 SL-0185 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}. UNIPROT P0CQ87 UNIPROT Q55NB1 UNIPROT Q5KBP4 UNIPROT Q5KBP5 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0051028 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MSDAQAPPASTSWADMVDEDEKQKQEQNMSNQNDGWGETATETSAPAPPPASAPVSSSNNDGWGEPAPSAPADNGWADAGASNGGSGANNNDGWFDAPVPPSSQPPKKEASDIQLQDDTEGLITNTFQVEVKLADLQGDPNSPLYSVQSFKELNLHEDLMKGIIAAGFQKPSKIQEKALPLLLSNPPRNLIGQSQSGTGKTAAFTLNMLSRVDPTIPTPQAICIAPSRELARQIQEVVDQIGQFTQVGTFLAIPGSWSRNSRIDKQILIGTPGTLVDMLMRGSRILDPRMIRVLVLDEADELIAQQGLGEQTFRIKQLLPPNVQNVLFSATFNDDVQEFADRFAPEANKIFLRKEDITVDAIRQLYLECDSEDQKYEALSALYDCLVIGQSIVFCKRKVTADHIAERLISEGHAVASLHGDKLSQERDAILDGFRNGETKVLITTNVIARGIDIPAVNMVVNYDVPDLGPGGNGPDIETYIHRIGRTGRFGRKGCSVIFTHDYRSKSDVERIMNTLGKPMKKIDARSTTDIEQLEKALKLAMKGPA 546 P0CQ86 ATP-dependent DBP5 214684 None SL-0178 SL-0182 SL-0185 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}. UNIPROT P0CQ86 UNIPROT Q55NB1 UNIPROT Q5KBP4 UNIPROT Q5KBP5 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0010494 GO:0031965 GO:0005643 GO:0005634 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0016973 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MSDAQAPPASTSWADMVDEDEKQKQEQNMSNQNDGWGETATETSAPAPPPASAPVSSSNNDGWGEPAPSAPADNGWADAGASNGGSGANNNDGWFDAPVPPSSQPPKKEASDIQLQDDTEGLITNTFQVEVKLADLQGDPNSPLYSVQSFKELNLHEDLMKGIIAAGFQKPSKIQEKALPLLLSNPPRNLIGQSQSGTGKTAAFTLNMLSRVDPTIPTPQAICIAPSRELARQIQEVIDQIGQFTQVGTFLAIPGSWSRNSRIDKQILIGTPGTLVDMLMRGSRILDPRMIRVLVLDEADELIAQQGLGEQTFRIKQLLPPNVQNVLFSATFNDDVQEFADRFAPEANKIFLRKEDITVDAIRQLYLECDSEDQKYEALSALYDCLVIGQSIVFCKRKVTADHIAERLISEGHAVASLHGDKLSQERDAILDGFRNGETKVLITTNVIARGIDIPAVNMVVNYDVPDLGPGGNGPDIETYIHRIGRTGRFGRKGCSVIFTHDYRSKSDVERIMNTLGKPMKKIDARSTTDIEQLEKALKLAMKGPA 546 Q6BRE4 ATP-dependent DBP5 284592 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q6BRE4 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0051028 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MSKEDTRVESDAAELLSSLSLDKKEQTEATVPKVDAKEDKSNDESKQTIKPASTEESKPADVKDATKSEEQEAESNLIKSSYEVKVKLADLQADPNSPLYSVKSFEELGLSSELLKGLYAMKFNKPSKIQEKALPLLISNPPKNMIGQSQSGTGKTAAFSLTMLSRVDESDPNTQCICLAPARELARQTLEVITTMSKFTKITSQLIVPDAMQRGQSTCAHVLVGTPGTLLDLIRRKLINTSKVKVFVLDEADNMLESQGLGDQCVRVKRTLPKATQLVLFSATFPDEVRKYAEKFVPNANSLELKQEELNVEGIKQLYMDCDSANHKFEVLSELYGLLTIGSSIIFVKTKDTANILYAKMKKEGHKCSILHAGLETSERDRLIDDFREGRSKVLITTNVLARGIDIASVSMVVNYDLPVDQKGAPDPSTYLHRIGRTGRFGRVGVSISFVHDQKSYQDLMAIRSYFGNIEMTRVPTDDWDEVEKIVKKVIKN 493 Q5AVM1 ATP-dependent dbp5 227321 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q5AVM1 UNIPROT C8VC14 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005634 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MASDAPTGGSLADRISNPAETTEPVADKAQLDGAASNQGGSDLAEPEYNVEVKLSDLQADPNNPLYSVKNFEDLGLDPRILQGLSAMNFRKPSKIQERALPLLMGNPPKNLVGQSQSGTGKTAAFVLNILSRLDLSSEQAQKTPQALILAPTRELARQIVGVIQVMGKFLDGLHIGTAVPADTNARPTRMEASVVVGTPGTVMDMIKKRIMVAAKLKVIVLDEADNMLDQQGLGDQCIRVKALLPRDIQVVLFSATFPAHVHQYASKFAPAANELTLQHEELTVEGIKQLYLDCASEEDKYRTLVQLYGLLTVGSSIIFVKTRASAVEIERRMVAEGHTVASLTGGIEGSQRDQIIDQFRAGHAKVLITTNVLARGIDVSTVSMVINYDIPELHQPPNRPRQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWEMLNQIQKYFNTDIQRIDTKDWDEVEDIIKKTIKNTRAQAGFR 477 Q4HY71 ATP-dependent DBP5 229533 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q4HY71 UNIPROT A0A0E0RW04 UNIPROT V6RQB4 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0051028 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MADLASRITKPDEVAAETPAETPAETAPAASGELGQADGNIEDLGGSGLQEPEWDVEVSLSELQNNEATPFHSATTWQDLGLREDLLKGLLSLNFLKPSKVQGKSLPLMLSDPPRNMLAQSQSGTGKTAAFVTAILSRVDFSKPDQPQALALAPSRELARQIEGVINAIGRFVENKKVAAAIPGVLPRGEPVRASVIVGTPGTVMDIIRRRQLDISQLRVLVLDEADNMLDQQGLGDQCLKVKNMLPKEIQVLLFSATFPENVMKYAGKFAPNAHSLKLQRSELTVKGISQMFIDCPDDNMKYDILCKLYGLMTIGQSVIFVKTRDSASEIERRMVADGHKVSALHAAFDGAERDNLLTKFRQGENKVLITTNVLARGIDVSSVSMVINYDIPMKGRGDTEPDAETYLHRIGRTGRFGRVGVSISFVYDKKSFDALSKIAEMYGIDLVKLDTEDWDEAEERVKEVIKKNRAQASYAPSATEPKAAAGA 488 Q6CJU1 ATP-dependent DBP5 284590 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q6CJU1 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MAQLSKEASDLMARLNIKEPAKKASEDNDTTSETKVEKEDAKETKAEEPANKVINSEYEVKVNLADLQADANSPLYSVKSFEELGLSEELLKGLYAMKFQKPSKIQEKALPLLIRDPPHNMIAQSQSGTGKTAAFSLTMLTRVDPNVNSTQAICLSPARELARQTLEVIQEMGKFTKTSSQLVVPDSFERNKPITANIVVGTPGTVLDLIRRKMLNLGSIKVFVLDEADNMLDKQGLGDQCIRVKKFLPKTCQLVLFSATFDDGVRQYAKKIIPTAVSLELQKNEVNVSAIKQLFMDCDNEEHKYTILSELYGLLTIGSSIIFVKTKQTANLLYAKLKKEGHQVSILHGDLQSQDRDRLIDDFREGRSKVLITTNVLARGIDIPSVSMVVNYDLPTLPNGQADPSTYVHRIGRTGRFGRTGVAISFIHDKKSFEVLSAIQKYFGDIEITKVPTDDLDEMETIVKKALKA 469 A5DZX2 ATP-dependent DBP5 379508 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A5DZX2 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0051028 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MSNTKDVDADASNLLASLSVSKEKKEDTSNILAGLSLNGDESNKKEGSGVKDTESDKQKGNGKVEKVEKDENKDKSQSEAKDDSKRETNLIENRYEVEVKLDDIQADPNSPLYSVKSFEELGLKPELLKGLYAMKFNKPSKIQERALPLLISNPPKNMIGQSQSGTGKTAAFSLTMLSRVDESIKAPQCICLAPTRELARQTLEVVETMGKYSNITYQLVVPDSVPRGQAISAQVLVGTPGIVHDLINRKAINVAKVKVFVLDEADNMLDAQGLADTCLRVKKRLPRDCQLVLFSATFPTEVRKYAEKFVPNANSLALKQEELNVKGIKQLYMDCKNQEHKFEVLCELYGLLTIGSSIIFVEQKATADSLYLRMKEEGHTVSILHGGLEVADRDRLIDDFREGRSKVLITTNVLARGIDIATVSMVVNYDLPRTKEGRPDPSTYLHRIGRTGRFGRVGVSVSFVANEKDYQTLKYIAEYFGIEDQMTVVPTDDWDEVEKIVTRVIKEKKMT 511 A4RIF1 ATP-dependent DBP5 242507 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A4RIF1 UNIPROT G4MVD6 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MSDLASRITAPAAATPATETDAPAAASSTLAVPDGAADGANSSGLQESNYDVEVQLGDPDTDSPLSSISSFSELGLPQGIIDGLLAMNFKKPSKIQARALPLMLSNPPRNMIAQSQSGTGKTGAFVVTILSRVDFNQPNQPQALALAPSRELARQIQSVIQSIGQFCTGLVVDAAIPGAISRETGVKANVVVGTPGTVMDLIRRRQFDVSQLKLLVVDEADNMLDQQGLGEQCVRVKNMLPKTIQTLLFSATFPDHVKSYAEKFAPQANQMKLRQQELTVKGISQMYMDCPSLKEKYEVLCKLYGLMTIGSSVIFVKTRESADEIQRRMEADGHKVSALHGAFQGQERDQLLDDFRSGKSKVLITTNVLARGIDVSSVSMVINYDIPMKGPGDQSPDAETYLHRIGRTGRFGRVGVSISFVHDRKSFTALSSIAEHYGIDLIQLSPDDWDDTEVKVQDVIKSSRAKPDYAPTQEKAA 477 A1CYG5 ATP-dependent dbp5 331117 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A1CYG5 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MASEQPVEAAPTGGSLADRITKPDESNTSETPAPAADQTDGAPAQLGGSDLHEPEYNVEVKLSDLQADPNNPLYSVKNFEDLGLDPRILKGLSNMNFRKPSKIQERALPLLLNNPPKNLVGQSQSGTGKTAAFVLNALSRVDLSTEQMQKTPQALILAPTRELARQILGVVQVMGQFVDGLIIGAAVPTDRDSRPKRLECSIVVGTPGTVGDMIKRRTFIPNKLKVLVLDEADNMLDQQGLGDQCIRVKALLPRDIQVVLFSATFPEHVHQYASKFAPNANEITLQHEELTVEGIKQLYLDCADGEDKYKTLVQLYGLLTVGSSIIFVQTRAAAQEIEKRMTAEGHTVVSLTGERDPSVRDAIIDQFRRGEAKVLIATNVLARGIDVSTVSMVINYDIPELHQPSVPGRQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWEMLNQIQTYFNCEIQRVDTKDWDEVEDIIKKTIKNSRANPKFAGGKE 489 Q8X0X2 ATP-dependent dbp 367110 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q8X0X2 UNIPROT Q1K870 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005634 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MADLASRITKPDEAPAAAPEAAPVSAPASEEPKAPENETSIEESQSNLVKNEYEVEIKLSDLQNDTESPLYSVSSFDELGLPEAVNRGLLAINFKKPSKVQEKCLPLMLSDPPRNMIAQSQSGTGKTAAFVLTVLSRIDLSKPHQPQALLLAPSRELARQIQTVVQTIGQFCENLIVEAAIPGAISRETGVRGSVVVGTPGTVMDLVKRRQFDISQLKVLVIDEADNMLDQQGLGDQCVRVKNMLPKTIQILLFSATFPDKVLRFAERFAPNANQMKLKHKELTVKGISQMFMDCPTEKDKYDILCKLYGLMTIGSSVIFVRTRETANEIQKRMEADGHKVSALHGAYEGQSRDVLLDEFRSGRSKVLITTNVLARGIDVSSVSMVINYDIPMKGPGEREPDAETYLHRIGRTGRFGRVGVSISFVHDRRSFEALSQIAQFYGIDLIQLNPNDLDDTERKVQEVIKSSRAQAEYVPSATDSAV 483 Q0UCB9 ATP-dependent DBP5 321614 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q0UCB9 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005634 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MSATEPTKEPAKEEVAEQSTVAQAQVDGSGEPANGSPLTETEYKVEVKLADMQADPNNPLYSAQSFEELQLSEELLKGVRNMNFRKPSKIQEKALPLLLMNPPTNMIAQSQSGTGKTAAFSLNILSRIDLSRNEPQAIALAPSRELARQILGVITHMGQFMEGLKTMAAIPDPTKRNQRLDAHVLVGTPGTVQEQLKRRLIKSDSIKILVLDEADNMLDQQGMGDQCTRVKSLLPKNIQTVLFSATFPPAVINYANKFAPNSNVLTLAHEELTIEGIKQLYIDIDKDQDKYSTLLKFYGLMTQASSIIFVRTRRTAEELERRMVAEGHKVAQLSGALEGQDRDRVIDQFRSGEAKVLITTNVLARGIDVESVTMVINYDVPTMADGREADPETYLHRIGRTGRFGRVGVALTFVHDKASWQQLHDIASYFKTDLHPIDTSDWDNVEEMIQKIIKSSRAGKSTKEMTEMITS 471 A5DBI5 ATP-dependent DBP5 294746 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A5DBI5 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0051028 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MPEEPVDSDASKLLESLSINKQGDSAPIKDEKPVVESENKVSDEQNSEPTKEPETKTETENNDSNLISSSYEVQVKLADLQADPNSPLYSVKSFEELGLSPELLKGLYAMKFNKPSKIQEKALPLLISNPPKNMIGQSQSGTGKTAAFSLTMLSRVDVNDPNTQCICLSPTRELARQTLEVITTMGKFTKVTTQLVVPQAMEKNQGTQAHIVVGTPGTLLDMIKRKLLRTGKVKVFVLDEADNMLDGQGLAAQCIRVKKVLPTSCQLVLFSATFPTEVRKYAEKFVPNANSLELKQEELNVDAIKQLYMDCDSEKHKAEVLSELYGLLTIGSSIIFVKTKATANYLYAKMKSEGHACSILHSDLDNSERDKLIDDFREGRSKVLITTNVLARGIDIASVSMVVNYDIPVDKDDKPDPSTYLHRIGRTGRFGRVGVAVSFVHDKKSYEDLEQIRSYFNDIEMTRVPTDDWDEVEKIVKKVLKK 482 A3GH91 ATP-dependent DBP5 322104 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A3GH91 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0051028 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MSAEKRVEADAAELLSSLSLGESPAEKKDEKTEEVKKEEAKSEELNKVVEKTEEKVKEANAEDAKPEELKEVGKEENEEPKTNLIQSTYEVKVKLADIQADPNSPLFSVKSFEELGLTPELLKGLYAMKFNKPSKIQEKALPLLISNPPRNMIGQSQSGTGKTAAFSLTMLSRVDPKVPSTQCLCLAPTRELARQTLEVISTMGKFTNITTQLIVPDALPRGSSTNAHIIVGTPGIVMDLIRRKQINVNGVKVFVLDEADNMLDAQGLGDQCVRVKRTLPKTTQLVLFSATFPTKVRQYAEKFVPNANSLELKQEELNVDGIKQLYMDCDSEKHKFEVLCELYGLLTIGSSIIFVERKDTANLLYAKMKAEGHACSILHGGLETSERDRLIDDFREGRSKVLITTNVLARGIDIASVSMVVNYDLPTDKDGNADPSTYLHRIGRTGRFGRVGVSISFIYDKRSYEILMKIKDYFGNVEMTRVPTDDWDEVEKIVKKVIKS 500 Q09747 ATP-dependent dbp5 284812 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q09747 PDB 3FHO Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0010494 GO:0005829 GO:0005635 GO:0031965 GO:0005643 GO:0005634 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0002184 GO:0016973 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MSTTLGQESKTDWASLDSDEEVQRISDKVNQLNTSENKNEDQKATNLSDRLGPKITENVDAKSEQDKATNTIAEDANTKQSENDESNLIPNKNEVRVKLADLQADPNSPLFSVKSFEELELKPELLKGIYSMKFQKPSKIQEKALPLLLSNPPRNMIGQSQSGTGKTAAFALTMLSRVDASVPKPQAICLAPSRELARQIMDVVTEMGKYTEVKTAFGIKDSVPKGAKIDAQIVIGTPGTVMDLMKRRQLDARDIKVFVLDEADNMLDQQGLGDQSMRIKHLLPRNTQIVLFSATFSERVEKYAERFAPNANEIRLKTEELSVEGIKQLYMDCQSEEHKYNVLVELYGLLTIGQSIIFCKKKDTAEEIARRMTADGHTVACLTGNLEGAQRDAIMDSFRVGTSKVLVTTNVIARGIDVSQVNLVVNYDMPLDQAGRPDPQTYLHRIGRTGRFGRVGVSINFVHDKKSWEEMNAIQEYFQRPITRVPTDDYEELEKVVKNALKM 503 A7EY76 ATP-dependent dbp5 665079 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A7EY76 Pfam PF00270 Pfam PF00271 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005634 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MSESKSTSWADEVASPSTEKNEESSLEDAQVDGATEPLGGGTLQDGQYEVEVKLSDIQGDQTSPLYSVDTFEQLGIDASILKGLYAMNFKKPSKIQEKALPLLLGNPPTNMIAQSQSGTGKTAAFVITILSRLDFSKPTTPQALCLAPSRELARQIEGVVRSIGQFVEGLSVQAAIPGAVERNARVNAMVIVGTPGTVMDLIKRKSIDASQMKVLCLDEADNMLDQQGLGDQCLRVKSMIKVEQILLFSATFPDEVYGFAQQFSPRANEIKLKRDELTVSGIKQMFMDCPNEVGKYEILVKLYGLMTIGSSIIFVKRRDTASHIAERLTAEGHKVAAIHGAFEGAERDTVLEDFRQGKAKVLITTNVLARGIDVQSVSMVINYDIPMKGRSDFEPDPETYLHRIGRTGRFGRVGVSISFVFDRKSYDALNKIAHHYNIDLIKLNQDDWDETEEIVKKVIKSSRAGTNLRA 470 Q4P7Z8 ATP-dependent DBP5 237631 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q4P7Z8 UNIPROT A0A0D1E0C9 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0010494 GO:0031965 GO:0005643 GO:0005634 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0016973 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MSESKDKTTAPAADSNVNEIASGISGLLSSKDVAESNLRESSHEVQVTLADQQADPNSPLYSAKSFEALGLHENLLKGIYAMKYQKPSKIQEKALPLLLQNPPKNMIGQSQSGTGKTAAFILTMLSRIDYDLQKPQAIALAPSRELARQIMDVARTMSKFTNVTTCLCLPDEVKRGEKITAQLIIGTPGKTFDMIKSKGIDTAAIKVFVLDEADNMLDQQSLGEQSIRVKNTMPKSCQLVLFSATFPTNVYDFAVRIAPGANEIRLKQEELSVEGIKQFYMDCKDEDHKYEVLVELYNLLTIGQSIIFCAKRETADRIAQKMTQEGHKVDSLHGRLETADRDRTIDAFRDGKSKVLISTNVIARGIDIQQVTLVINYDMPLTQTGEADAETYLHRIGRTGRFGRKGVSINFVHDQQSWSYMDQIEKALKCQITRVATNDLEEMEYTIKEALKQIGK 456 Q6C3X7 ATP-dependent DBP5 284591 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q6C3X7 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005934 GO:0010494 GO:0031965 GO:0044614 GO:0005634 GO:0005844 GO:0005524 GO:0016887 GO:0000822 GO:0003723 GO:0003724 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt By Similarity {ECO:0000250} MSDQVSDMLEKLELQKEKNQAAATEAKVEEVKEDDKKDVKEELNEDDKKVAKEDDKKEDAKEESKEDAEENNLIQTEYEVRVKLADLQADPNSPLYSAKRFEDLGLDENLLKGLYAMKFNKPSKIQEKALPLLLSDPPHNMIGQSQSGTGKTGAFSLTMLSRVDPNLKAVQCICLAPSRELARQTLDVVDEMKKFTDITTHLIVPESTERGQKVTSQILVGTPGSVAGLLQKKQIDAKHVKVFVLDEADNMVDSSMGSTCARIKKYLPSSTQVVLFSATFPESVLDLAGKMCPNPNEIRLKANELNVDAITQLYMDCEDGEEKFKMLEELYSMLTIASSVIFVAQRSTANALYQRMSKNGHKVSLLHSDLSVDERDRLMDDFRFGRSKVLISTNVIARGIDIATVSMVVNYDLPTDKNGKPDPETYLHRIGRTGRFGRSGVSISFVHDEASFEVLDSIQQSLGMTLTQVPTDDIDEVEEIIKKAIKGK 488 A6ZNQ1 ATP-dependent DBP5 307796 None SL-0178 SL-0182 SL-0185 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}. UNIPROT A6ZNQ1 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0031965 GO:0005643 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0034641 GO:0043170 GO:0051028 GO:0044238 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MSDTKRDPADLLASLKIDNEKEDTSEVSTKETVKSQPEKTADSIKPAEKLVPKVEEKKTKQEDSNLISSEYEVKVKLADIQADPNSPLYSAKSFDELGLAPELLKGIYAMKFQKPSKIQERALPLLLHNPPRNMIAQSQSGTGKTAAFSLTMLTRVNPEDASPQAICLAPSRELARQTLEVVQEMGKFTKITSQLIVPDSFEKNKQINAQVIVGTPGTVLDLMRRKLMQLQKIKIFVLDEADNMLDQQGLGDQCIRVKRFLPKDTQLVLFSATFADAVRQYAKKIVPNANTLELQTNEVNVDAIKQLYMDCKNEADKFDVLTELYGLMTIGSSIIFVATKKTANVLYGKLKSEGHEVSILHGDLQTQERDRLIDDFREGRSKVLITTNVLARGIDIPTVSMVVNYDLPTLANGQADPATYIHRIGRTGRFGRKGVAISFVHDKNSFNILSAIQKYFGDIEMTRVPTDDWDEVEKIVKKVLKD 482 P20449 ATP-dependent DBP5 559292 None SL-0178 SL-0182 SL-0185 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. UNIPROT P20449 UNIPROT D6W2B2 PDB 2KBE PDB 2KBF PDB 3GFP PDB 3PEU PDB 3PEV PDB 3PEW PDB 3PEY PDB 3RRM PDB 3RRN PDB 5ELX Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. Q02159 EBI-860380 0.00 P40477 EBI-7266119 0.66 Q04839 EBI-7998113 0.66 P50111 EBI-2132816 0.51 P32491 EBI-2617619 0.35 P40484 EBI-2617649 0.35 Q12529 EBI-2887496 0.00 P40564 EBI-3656740 0.35 P33416 EBI-3744163 0.35 P11484 EBI-3778915 0.35 P39987 EBI-3787386 0.35 P04147 EBI-7082780 0.40 Q12315 EBI-15806702 0.76 GO:0005934 GO:0005737 GO:0010494 GO:0031965 GO:0044614 GO:0005634 GO:0005844 GO:0005524 GO:0016887 GO:0008186 GO:0003723 GO:0003724 GO:0006406 GO:0016973 GO:0015031 GO:0006415 GO:0006409 Peripheral UniProt Sequence Analysis MSDTKRDPADLLASLKIDNEKEDTSEVSTKETVKSQPEKTADSIKPAEKLVPKVEEKKTKQEDSNLISSEYEVKVKLADIQADPNSPLYSAKSFDELGLAPELLKGIYAMKFQKPSKIQERALPLLLHNPPRNMIAQSQSGTGKTAAFSLTMLTRVNPEDASPQAICLAPSRELARQTLEVVQEMGKFTKITSQLIVPDSFEKNKQINAQVIVGTPGTVLDLMRRKLMQLQKIKIFVLDEADNMLDQQGLGDQCIRVKRFLPKDTQLVLFSATFADAVRQYAKKIVPNANTLELQTNEVNVDAIKQLYMDCKNEADKFDVLTELYGLMTIGSSIIFVATKKTANVLYGKLKSEGHEVSILHGDLQTQERDRLIDDFREGRSKVLITTNVLARGIDIPTVSMVVNYDLPTLANGQADPATYIHRIGRTGRFGRKGVAISFVHDKNSFNILSAIQKYFGDIEMTRVPTDDWDEVEKIVKKVLKD 482 Q5E9V1 DCN1-like DCUN1D3 9913 None SL-0198 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}. UNIPROT Q5E9V1 Pfam PF03556 PROSITE PS51229 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}. GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0000151 GO:0097602 GO:0031624 GO:0032182 GO:0030308 GO:2000134 GO:2000435 GO:0043065 GO:2000436 GO:0051443 GO:0045116 GO:0010564 GO:2000434 GO:0010332 GO:0010225 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:Q8IWE4,} MGQCVTKCKNPSSTLGSKNGDRDPSSKSHGRRSASHREEQLPTCGKPGGDILVNGTKKAEAAPEACQLPTSSGDAGREPKSNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT 304 Q8IWE4 DCN1-like DCUN1D3 9606 None SL-0198 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}. UNIPROT Q8IWE4 UNIPROT B3KVY4 PDB 4GBA Pfam PF03556 PROSITE PS51229 OMIM 616167 DisGeNET 123879 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}. P01112 EBI-27045317 0.27 Q6IQ23 EBI-16398399 0.35 Q96Q27 EBI-21879621 0.35 Q13618 EBI-15794277 0.58 Q13617 EBI-15794136 0.35 Q13616 EBI-15794136 0.35 P61081 EBI-15794345 0.44 Q16695 EBI-20937612 0.40 P01116 EBI-27041844 0.27 P01111 EBI-27042293 0.27 GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0000151 GO:0097602 GO:0031624 GO:0032182 GO:0030308 GO:2000134 GO:2000435 GO:0043065 GO:2000436 GO:0051443 GO:0045116 GO:0010564 GO:2000434 GO:0010332 GO:0010225 Lipid-Anchored UniProt Sequence Analysis MGQCVTKCKNPSSTLGSKNGDREPSNKSHSRRGAGHREEQVPPCGKPGGDILVNGTKKAEAATEACQLPTSSGDAGRESKSNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT 304 Q8K0V2 DCN1-like Dcun1d3 10090 None SL-0198 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}. UNIPROT Q8K0V2 Pfam PF03556 PROSITE PS51229 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}. GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0000151 GO:0097602 GO:0031624 GO:0032182 GO:0030308 GO:2000134 GO:2000435 GO:0043065 GO:2000436 GO:0051443 GO:0045116 GO:0010564 GO:2000434 GO:0010332 GO:0010225 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:Q8IWE4,} MGQCVTKCKNPSSTLGSKNGDRDPSNKSHSRRGASHREEQVPPCGKPAGDILVNGTKKAEAATEACQLPTSSGDAGRESKTNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREVEGRGTLSSGQEGLCPEEQT 304 Q5R9G1 DCN1-like DCUN1D3 9601 None SL-0198 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}. UNIPROT Q5R9G1 Pfam PF03556 PROSITE PS51229 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}. GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0097602 GO:0030308 GO:2000134 GO:2000435 GO:0043065 GO:2000436 GO:0010564 GO:2000434 GO:0010332 GO:0010225 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:Q8IWE4,} MGQCVTKCKNPSSTLGSKNGDRDPSNKSHSRRGAGHREEQVPPCGKPGGDILVNGTKKAEAATEACQLPTSSGDAGRESKSNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT 304 Q4V8B2 DCN1-like Dcun1d3 10116 None SL-0198 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}. UNIPROT Q4V8B2 Pfam PF03556 PROSITE PS51229 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}. GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0000151 GO:0097602 GO:0031624 GO:0032182 GO:0030308 GO:2000134 GO:2000435 GO:0043065 GO:2000436 GO:0051443 GO:0045116 GO:0010564 GO:2000434 GO:0010332 GO:0010225 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:Q8IWE4,} MGQCVTKCKNPSSTLGSKNGDRDPSSKSHSRRGASHREEQVPPCGKPAGDILVNGTKKAEAATEACQLPTSSGDAGRESKTNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREVEGRGALSSGPEGLCPEEQT 304 Q6DFA1 DCN1-like dcun1d3 8355 None SL-0198 Cell membrane {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm {ECO:0000250|UniProtKB:Q8IWE4}. Nucleus {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWE4}. UNIPROT Q6DFA1 Pfam PF03556 PROSITE PS51229 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}. GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0097602 GO:2000435 GO:2000436 GO:0010564 GO:2000434 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:Q8IWE4,} MGQCVTKCKNPSSTLGSKNGERESSKPHKRSSSHKEEHMSICGKASGEILVNGTKKGDASLEASQPLAVGVDTKKKEQGVGAELSSLQRIEELFRRYKDEREDAILEEGMERFCDDLCVDPTEFRVLVLAWKFQAATMCKFTRREFFEGCKSINADGIESICSQFPGLLNEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNKPLILDQWLEFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKSEEKTDCIPCLGTDHQSRDEQT 303 A4IHK8 DCN1-like dcun1d3 8364 None SL-0198 Cell membrane {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm {ECO:0000250|UniProtKB:Q8IWE4}. Nucleus {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWE4}. UNIPROT A4IHK8 Pfam PF03556 PROSITE PS51229 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}. GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0000151 GO:0097602 GO:0031624 GO:0032182 GO:2000435 GO:2000436 GO:0051443 GO:0045116 GO:0010564 GO:2000434 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:Q8IWE4,} MGQCVTKCKNPSSTLGSKNGERESSKPHKRSSSHKDEHLSICGKASREILVNGTKKGDVSLEASQPLAAGGDTKKKEQGTGAELSSVQRIEELFWRYKDEREDAILEEGMERFCNDLYVDPTEFRVLVLAWKFQAATMCKFTRREFFEGCKAINADGIEGICARFPSLLNEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNKPLILDQWLDFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKNEEETKCIPCSGTDDQSTEGQT 303 O62255 m7GpppN-mRNA dcap 6239 None SL-0198 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}. UNIPROT O62255 UNIPROT A0A061ACN4 UNIPROT A0A061ADX7 UNIPROT B3VKU3 UNIPROT O62257 UNIPROT Q2YS49 UNIPROT Q2YS50 UNIPROT Q45F95 Pfam PF05026 Pfam PF00293 PROSITE PS51462 PROSITE PS00893 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}. GO:0005737 GO:0043186 GO:0000932 GO:0048471 GO:0050072 GO:0030145 GO:0003723 GO:0000290 GO:0008340 GO:0006397 GO:0002119 GO:0000184 GO:0040012 GO:0000003 GO:0009408 GO:0006979 GO:0009411 Unknown UniProt Sequence Analysis MEISTENWCKKPKNRSIFSKNISFQKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQPSTSKPKKNEKRKKAVAQAPASAPAPGPEEKKKQPKRASVGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGPRIPTDILDELEFRFISNMVECEINDNIRVCFHLELAHWYYIDHMVEDDKISGCPNVGSRDFNFQMCQHCRVLRKYAHRADEVLAKFREYKSTVPTYGAILVDPEMDHVVLVQSYFAKGKNWGFPKGKINQAEPPRDAAIRETFEETGFDFGIYSEKEKKFQRFINDGMVRLYLVKNVPKDFNFQPQTRKEIRKIEWFKIDDLPTDKTDELPAYLQGNKFYMVMPFVKDIQIYVQKEKEKLRRRKAEAVQSTPSSSIFSQLFPAQPPPPVPEDATPTRPMYKRLTSEELFSAFKNPPAGEVARPTLPDMSPAVNGLDTLAVLGICTPLKPGASLNEFSGAPQNCPMISEEAGSPADPSAEIGFAMPMDLKQPVVTSDHPWQHHKISDSSAPPQTLESHQGWLDTQLVNTIMHSPNHPLPPTSNSPATPTAVLGHLIGKPIQPQAILPQAATPTALGSAEKPKSSRISLSDNSAFKAISSTQKQSIPKATAAPPSTEKTRSASLSGSSQVVGKPARNLFNSVVSPVSSGIQSIQGDGGAWEDVWFREQLAATTTAGTSISSLAASNQELAMINREETPIEDPYFKQQAYQKAQKAQSLIPACSQWTNSIKLDIDYVVGPLSFWMQQFSTKSPVSGTGPQLP 786 Q06151 m7GpppX DCS1 559292 None SL-0198 Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body. Note=Predominantly cytoplasmic. UNIPROT Q06151 UNIPROT D6VYR7 UNIPROT Q6Q5L1 PDB 5BV3 PDB 6TRQ Pfam PF05652 PROSITE PS00892 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}. P25491 EBI-3764256 0.35 P32356 EBI-390849 0.67 Q12123 EBI-786407 0.87 Q12179 EBI-7885875 0.44 P28240 EBI-7998723 0.40 P38009 EBI-6344412 0.00 P25303 EBI-3659022 0.35 P53940 EBI-3768133 0.35 P40150 EBI-3797766 0.35 P48363 EBI-3817134 0.35 Q06151 EBI-15484526 0.75 P14680 EBI-16286565 0.35 GO:0005737 GO:0106095 GO:0005739 GO:0005634 GO:0000932 GO:0048471 GO:0044692 GO:0016818 GO:0042802 GO:0050072 GO:0046982 GO:0042803 GO:0000340 GO:0009267 GO:0000290 GO:0000956 GO:0000288 GO:0031086 GO:1901919 GO:1903398 GO:0009408 GO:0007584 GO:0006970 GO:0006979 Unknown UniProt Sequence Analysis MSQLPTDFASLIKRFQFVSVLDSNPQTKVMSLLGTIDNKDAIITAEKTHFLFDETVRRPSQDGRSTPVLYNCENEYSCINGIQELKEITSNDIYYWGLSVIKQDMESNPTAKLNLIWPATPIHIKKYEQQNFHLVRETPEMYKRIVQPYIEEMCNNGRLKWVNNILYEGAESERVVYKDFSEENKDDGFLILPDMKWDGMNLDSLYLVAIVYRTDIKTIRDLRYSDRQWLINLNNKIRSIVPGCYNYAVHPDELRILVHYQPSYYHFHIHIVNIKHPGLGNSIAAGKAILLEDIIEMLNYLGPEGYMNKTITYAIGENHDLWKRGLEEELTKQLERDGIPKIPKIVNGFK 350 Q12123 Inactive DCS2 559292 None SL-0198 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. UNIPROT Q12123 UNIPROT D6W2M9 Pfam PF05652 PROSITE PS00892 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}. Q06151 EBI-786407 0.87 P37366 EBI-791370 0.53 Q06218 EBI-816740 0.27 P40024 EBI-817974 0.27 Q08004 EBI-819653 0.27 P07245 EBI-821183 0.27 P38829 EBI-855499 0.00 Q12179 EBI-7886118 0.40 P47035 EBI-7998776 0.40 P11484 EBI-3687179 0.35 P14680 EBI-16286565 0.35 Q12123 EBI-21322203 0.37 GO:0005737 GO:0005634 GO:0000932 GO:0048471 GO:0004857 GO:0050072 GO:0046982 GO:0042803 GO:0000340 GO:0031670 GO:0009267 GO:0000290 GO:0000956 GO:0000184 GO:1903398 GO:0009408 GO:0007584 GO:0006970 GO:0006979 Unknown UniProt Sequence Analysis MGSQDLASLIGRFKYVRVLDSNPHTKVISLLGSIDGKDAVLTAEKTHFIFDETVRRPSQSGRSTPIFFHREIDEYSFLNGITDLKELTSNDIYYWGLSVLKQHILHNPTAKVNLIWPASQFHIKGYDQQDLHVVRETPDMYRNIVVPFIQEMCTSERMKWVNNILYEGAEDDRVVYKEYSSRNKEDGFVILPDMKWDGINIDSLYLVAIVYRDDIKSLRDLNPNHRDWLIRLNKKIKTIIPQHYDYNVNPDELRVFIHYQPSYYHFHVHIVNIRHPGVGEERGSGMTILLEDVIEALGFLGPEGYMKKTLTYVIGENHDLWKKGFKEEVEKQLKHDGIATSPEKGSGFNTNLG 353 Q14203 Dynactin DCTN1 9606 None SL-0178 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}. UNIPROT Q14203 UNIPROT A8MY36 UNIPROT B4DM45 UNIPROT E9PFS5 UNIPROT E9PGE1 UNIPROT G5E9H4 UNIPROT O95296 UNIPROT Q6IQ37 UNIPROT Q9BRM9 UNIPROT Q9UIU1 UNIPROT Q9UIU2 PDB 1TXQ PDB 2COY PDB 2HKN PDB 2HKQ PDB 2HL3 PDB 2HL5 PDB 2HQH PDB 3E2U PDB 3TQ7 Pfam PF01302 Pfam PF12455 PROSITE PS00845 PROSITE PS50245 OMIM 105400 OMIM 168605 OMIM 601143 OMIM 607641 DisGeNET 1639 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}. 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. O00423 EBI-11366138 0.27 O08788 EBI-2561198 0.56 O15027 EBI-11083608 0.35 P29991 EBI-8829140 0.37 P43034 EBI-11382201 0.48 P58546 EBI-11382201 0.27 Q9UBN7 EBI-25840647 0.56 P42025 EBI-367597 0.54 Q96KM6 EBI-7216721 0.37 P18669 EBI-736541 0.00 P30622 EBI-15657003 0.76 P20340 EBI-8604645 0.40 P49662 EBI-1063339 0.00 P43360 EBI-25840462 0.56 Q9H8T0 EBI-1070932 0.00 P01106 EBI-1072184 0.00 P62330 EBI-1073142 0.00 P40337 EBI-1073742 0.00 O14593 EBI-1079448 0.00 Q9Y2Q3 EBI-1080223 0.00 Q7L1Q6 EBI-1082566 0.00 O76071 EBI-1083392 0.00 Q9NRI5 EBI-1105616 0.00 Q96G01 EBI-7141949 0.43 P10636 EBI-7637855 0.70 Q8NFJ9 EBI-25840415 0.56 Q96RK4 EBI-1805881 0.63 P54256 EBI-8013384 0.65 P61164 EBI-2559425 0.40 Q99KJ8 EBI-2559460 0.56 Q9Z0Y1 EBI-2560063 0.56 P47753 EBI-2563793 0.40 Q0VEJ0 EBI-2563897 0.40 Q99551 EBI-2690077 0.00 A0JNT9 EBI-7894392 0.43 Q921C5 EBI-7894652 0.35 Q13573 EBI-7950968 0.35 Q9JK25 EBI-8098108 0.46 O14777 EBI-8098382 0.45 P42224 EBI-3451713 0.00 Q8TCX1 EBI-8568044 0.46 O95817 EBI-8568339 0.35 P31749 EBI-7094924 0.37 Q16543 EBI-7112856 0.37 Q6ZU52 EBI-7140179 0.37 O14576 EBI-25840452 0.56 P51955 EBI-7257818 0.37 O60925 EBI-7284860 0.37 P13929 EBI-5658334 0.00 Q96S44 EBI-5665262 0.00 P62136 EBI-5564400 0.37 O75381 EBI-5911953 0.35 P10209 EBI-6509331 0.37 Q13618 EBI-21329068 0.35 Q9Y496 EBI-8847255 0.27 P28741 EBI-8847318 0.40 P88996 EBI-9641406 0.37 O41964 EBI-9641478 0.37 Q14980 EBI-10039064 0.27 Q14653 EBI-11321946 0.35 P05412 EBI-11324725 0.35 E9QKK1 EBI-10995761 0.35 Q8R1Q8 EBI-11000601 0.35 Q8VC57 EBI-11027413 0.35 Q96H55 EBI-11031416 0.35 P62627 EBI-11032607 0.35 Q9WUM4 EBI-11065690 0.35 Q8R5C5 EBI-11073047 0.35 Q8CBY8 EBI-11074062 0.35 Q9QZB9 EBI-11074142 0.35 Q15691 EBI-11091481 0.86 Q9WTI7 EBI-11093786 0.35 P47755 EBI-11117728 0.48 Q14134 EBI-11137164 0.35 Q14204 EBI-11148090 0.48 P14635 EBI-11366138 0.27 Q96T17 EBI-11366138 0.27 Q9BT25 EBI-11366138 0.27 P31930 EBI-11366138 0.27 Q3KQU3 EBI-11366138 0.27 O00139 EBI-11366138 0.27 Q9P0I2 EBI-11366138 0.27 Q9NQ86 EBI-11366138 0.27 P36776 EBI-11366138 0.27 Q99643 EBI-11366138 0.27 Q96GD4 EBI-11366138 0.27 Q9HAU0 EBI-11366138 0.27 P61019 EBI-11366138 0.27 Q08AD1 EBI-11366138 0.27 Q96R06 EBI-11366138 0.27 Q01130 EBI-11366138 0.27 Q96P70 EBI-11366138 0.27 Q9Y5Y2 EBI-11366138 0.27 Q15555 EBI-11366138 0.27 Q8WWK9 EBI-11366138 0.27 O75330 EBI-11366138 0.27 Q9BRR8 EBI-11366138 0.27 Q8WVK7 EBI-11366138 0.27 Q9NZ32 EBI-11366138 0.62 P11137 EBI-11366138 0.27 Q8IWC1 EBI-11366138 0.27 Q9NYZ3 EBI-11366138 0.27 Q7Z460 EBI-11366138 0.27 Q9UJW0 EBI-11366138 0.62 Q9UPY8 EBI-11366138 0.27 Q5SW79 EBI-11366138 0.27 O00487 EBI-11366138 0.27 Q8WU90 EBI-11366138 0.27 Q969S3 EBI-11366138 0.27 Q14847 EBI-11366138 0.27 P43897 EBI-11366138 0.27 Q9Y4F5 EBI-11366138 0.27 P50570 EBI-11366138 0.27 Q9ULD2 EBI-11366138 0.27 O95373 EBI-11366138 0.27 Q8N2U0 EBI-11366138 0.27 Q8IX90 EBI-11366138 0.27 O15075 EBI-11366138 0.27 Q15286 EBI-11366138 0.27 P51665 EBI-11366138 0.27 Q53H12 EBI-11366138 0.27 Q9H3G5 EBI-11366138 0.27 Q99733 EBI-11366138 0.27 Q86V48 EBI-11366138 0.27 P61163 EBI-11366138 0.62 Q96K17 EBI-11366138 0.27 Q9HC35 EBI-11366138 0.27 O00399 EBI-11366138 0.62 Q9Y4L1 EBI-11366138 0.27 Q49MG5 EBI-11366138 0.27 Q00610 EBI-11366138 0.27 Q8IYA6 EBI-11366138 0.27 Q9GZQ8 EBI-11366138 0.27 Q99848 EBI-11366138 0.27 Q66K74 EBI-11366138 0.27 P20290 EBI-11366138 0.27 Q13561 EBI-11366138 0.62 O75935 EBI-11366138 0.62 P61006 EBI-11366138 0.27 Q13423 EBI-11366138 0.27 Q9Y6M1 EBI-11366138 0.27 Q14244 EBI-11366138 0.27 O94905 EBI-11366138 0.27 P30419 EBI-11366138 0.27 P22570 EBI-11366138 0.27 P55209 EBI-11366138 0.27 Q9Y448 EBI-11366138 0.27 Q5JU00 EBI-11367780 0.27 Q8N4C6 EBI-11374469 0.27 Q8NBT2 EBI-11382201 0.27 Q6P1N0 EBI-11382201 0.27 P07203 EBI-11382201 0.27 Q99661 EBI-11382201 0.27 Q9BXJ9 EBI-11382201 0.27 Q9P1F3 EBI-11382201 0.27 Q5EBL8 EBI-11382201 0.27 Q9P289 EBI-11382201 0.27 Q92900 EBI-11382201 0.27 Q9Y5B9 EBI-11382201 0.27 Q96CT7 EBI-11382201 0.27 Q7Z4H7 EBI-11382201 0.27 Q9BX40 EBI-11382201 0.27 Q13409 EBI-11382201 0.27 Q9Y5A9 EBI-11382201 0.27 O76041 EBI-11382201 0.27 Q96GY0 EBI-11382201 0.27 P41227 EBI-11382201 0.27 Q7KZI7 EBI-11382201 0.27 Q9H6D7 EBI-11382201 0.27 O75122 EBI-11382201 0.27 O14640 EBI-11382201 0.27 Q8TAT6 EBI-11382201 0.27 P33981 EBI-11382201 0.27 Q5QJ74 EBI-11382201 0.27 P04083 EBI-11382201 0.27 Q9H4H8 EBI-11382201 0.27 O43663 EBI-11382201 0.27 Q2NL82 EBI-11382201 0.27 Q9H6S0 EBI-11382201 0.27 Q8N568 EBI-11382201 0.27 Q96BD8 EBI-11382201 0.27 Q9BYV8 EBI-11382201 0.27 Q9C0F1 EBI-11382201 0.27 Q5T5Y3 EBI-11382201 0.27 Q16718 EBI-11382201 0.27 E9PAV3 EBI-11382201 0.27 Q9NX55 EBI-11382201 0.27 Q9UHG0 EBI-11382201 0.27 Q9UNY4 EBI-11382201 0.27 Q9H7E2 EBI-11382201 0.27 P49458 EBI-11382201 0.27 Q9BWT3 EBI-11382201 0.27 Q9BYJ9 EBI-11382201 0.27 Q15058 EBI-11382201 0.27 Q96GA3 EBI-11382201 0.27 Q92974 EBI-11382201 0.27 Q15398 EBI-11382201 0.27 Q8NHV4 EBI-11382201 0.27 Q9Y3Y2 EBI-11382201 0.27 Q9P2B7 EBI-11382201 0.27 Q99871 EBI-11382201 0.27 Q9P270 EBI-11382201 0.27 Q86XJ1 EBI-11382201 0.27 Q9BTE1 EBI-21619572 0.35 H9XIJ5 EBI-11514215 0.37 P47756 EBI-12449631 0.51 P52907 EBI-12449631 0.51 Q9Y2I6 EBI-12451292 0.35 G3G960 EBI-11688985 0.40 Q9UQM7 EBI-11913229 0.00 Q8N157 EBI-11922091 0.00 Q16082 EBI-15187599 0.37 P02511 EBI-15187643 0.37 Q3KP66 EBI-21617875 0.35 Q99797 EBI-21619572 0.35 Q6XUX3 EBI-21619572 0.35 P62736 EBI-21619572 0.35 D6R9G5 EBI-21619572 0.35 Q96MC5 EBI-21663233 0.35 Q86WX3 EBI-21663135 0.35 Q9NPQ8 EBI-21663468 0.35 Q9GZP0 EBI-21663347 0.35 Q13748 EBI-15642149 0.44 Q9UNH7 EBI-16042701 0.50 O95219 EBI-16042750 0.35 Q08345 EBI-22227061 0.35 A2A935 EBI-21024514 0.35 P14404 EBI-21026252 0.35 Q5S007 EBI-21360986 0.35 Q9NQ75 EBI-21373041 0.00 Q9Y5K6 EBI-21373015 0.00 Q9UKE5 EBI-21373000 0.00 O84166 EBI-22302598 0.35 P0DOF2 EBI-25603126 0.35 P0DTC6 EBI-26495724 0.35 P18847 EBI-25840405 0.56 O15392 EBI-25840395 0.56 P63010 EBI-25840385 0.56 O60479 EBI-25840435 0.56 P42574 EBI-25840425 0.56 Q9ULX5 EBI-25840575 0.56 Q8WUW1 EBI-25840565 0.56 P62987 EBI-25840555 0.56 Q15554 EBI-25840542 0.56 P19474 EBI-25840525 0.56 Q92834 EBI-25840515 0.56 P17980 EBI-25840505 0.56 Q9BR81 EBI-25840495 0.56 O15381 EBI-25840483 0.56 Q6NXG1 EBI-25840813 0.56 Q9H0E2 EBI-25840803 0.56 P57075 EBI-25840793 0.56 Q96RL1 EBI-25840783 0.56 O95777 EBI-25840771 0.56 Q04323 EBI-25840761 0.56 Q9UJ41 EBI-25840749 0.56 Q9Y2M5 EBI-25840739 0.56 Q99932 EBI-25840729 0.56 Q96EK5 EBI-25840719 0.56 Q8N488 EBI-25840708 0.56 O00308 EBI-25840688 0.56 Q15436 EBI-25840677 0.56 Q9BSL1 EBI-25840667 0.56 O75886 EBI-25840657 0.56 Q6DN90 EBI-25840625 0.56 Q9UHY8 EBI-25840615 0.56 O95671 EBI-25840605 0.56 Q9UNS2 EBI-25840595 0.56 P46379 EBI-25840585 0.56 Q6ZTN6 EBI-25840998 0.56 Q8NBM4 EBI-25840983 0.56 Q8TC29 EBI-25840966 0.56 Q8IYW5 EBI-25840956 0.56 Q96D59 EBI-25840946 0.56 Q8WVJ9 EBI-25840936 0.56 Q9BYZ2 EBI-25840926 0.56 Q8IY31 EBI-25840916 0.56 Q8N594 EBI-25840906 0.56 Q96JM7 EBI-25840896 0.56 Q9GZS3 EBI-25840886 0.56 Q71RG4 EBI-25840876 0.56 A4FUJ8 EBI-25840866 0.56 Q9HCE7 EBI-25840856 0.56 Q6GQQ9 EBI-25840844 0.56 Q96FW1 EBI-25840833 0.56 Q9NV79 EBI-25840823 0.56 P05067 EBI-25938504 0.56 P51114 EBI-26510253 0.37 P49639 EBI-26512419 0.37 P13569 EBI-27087549 0.35 Q12792 EBI-28939213 0.35 Q8NCK7 EBI-27103180 0.35 Q6ZMQ8 EBI-32723474 0.27 GO:0030424 GO:0005938 GO:0099738 GO:0031252 GO:0120103 GO:0005814 GO:0005813 GO:0036064 GO:0005737 GO:0005829 GO:0030286 GO:0045171 GO:0000776 GO:0016020 GO:0005874 GO:0005875 GO:0015630 GO:0035371 GO:0072686 GO:0043005 GO:0043025 GO:0005635 GO:0005634 GO:0005819 GO:0000922 GO:0008017 GO:0051010 GO:0019901 GO:0048156 GO:0015631 GO:0051301 GO:0010457 GO:0031122 GO:0000132 GO:0099558 GO:0032402 GO:0034454 GO:0000278 GO:0061744 GO:0007399 GO:0007528 GO:0050905 GO:0070050 GO:1990535 GO:1905515 GO:0051081 GO:0007097 GO:0090063 GO:0031116 GO:1904398 GO:0060236 GO:0042147 GO:0021517 Unknown UniProt Sequence Analysis MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFELSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDCTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGPQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLLVAALEELAFKASEQIYGTPSSSPYECLRQSCNILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEQQRGAIPGQAPGSVPGPGLVKDSPLLLQQISAMRLHISQLQHENSILKGAQMKASLASLPPLHVAKLSHEGPGSELPAGALYRKTSQLLETLNQLSTHTHVVDITRTSPAAKSPSAQLMEQVAQLKSLSDTVEKLKDEVLKETVSQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGFGQRHRLVLTQEQLHQLHSRLIS 1278 O08788 Dynactin Dctn1 10090 None SL-0178 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}. UNIPROT O08788 UNIPROT E9QLJ1 UNIPROT Q3TZG7 Pfam PF01302 Pfam PF12455 PROSITE PS00845 PROSITE PS50245 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}. Q64368 EBI-6946418 0.40 P33175 EBI-8013466 0.40 P06493 EBI-2561198 0.40 Q9UJW0 EBI-2561198 0.56 P61163 EBI-2561198 0.56 Q9NZ32 EBI-2561198 0.56 Q9BTE1 EBI-2561198 0.56 Q14203 EBI-2561198 0.56 O00399 EBI-2561198 0.56 P47755 EBI-2561198 0.56 A8K8J9 EBI-2561198 0.40 O75935 EBI-2561198 0.40 P42025 EBI-2561198 0.56 O35685 EBI-7691158 0.35 Q61768 EBI-7691193 0.35 A0JNT9 EBI-7894187 0.27 Q8CG73 EBI-4284701 0.35 Q13561 EBI-6857116 0.53 P28741 EBI-8847308 0.46 Q8BKC8 EBI-9085471 0.35 P48651 EBI-11066549 0.35 Q9Y592 EBI-11066549 0.35 Q9NP97 EBI-11066549 0.35 P47756 EBI-11066549 0.35 P52907 EBI-11066549 0.35 O14949 EBI-11066549 0.35 Q86XL3 EBI-11066549 0.35 O15235 EBI-11066549 0.35 Q9BV73 EBI-11066549 0.35 Q15643 EBI-11066549 0.35 B4E1G1 EBI-11066549 0.35 Q9Y6G9 EBI-11066549 0.35 Q96L93 EBI-11066549 0.35 Q80VJ8 EBI-11666413 0.35 Q6A078 EBI-11784184 0.50 O88485 EBI-15640911 0.35 Q7TMB8 EBI-16727444 0.35 Q7TPH6 EBI-16731507 0.35 Q4ACU6 EBI-16726570 0.35 Q9NRI5 EBI-26612017 0.35 Q96LT7 EBI-26613562 0.35 GO:0030424 GO:0005938 GO:0099738 GO:0031252 GO:0120103 GO:0005814 GO:0005813 GO:0036064 GO:0005737 GO:0005868 GO:0005829 GO:0045171 GO:0000776 GO:0005874 GO:0005875 GO:0015630 GO:0035371 GO:0072686 GO:0043005 GO:0043025 GO:0005635 GO:0005634 GO:0032991 GO:0030904 GO:0005819 GO:0000922 GO:0042802 GO:0008017 GO:0051010 GO:0019901 GO:0015631 GO:0051301 GO:0010457 GO:0031122 GO:0000132 GO:0032402 GO:0034454 GO:0061744 GO:0007528 GO:0050905 GO:0070050 GO:1990535 GO:1905515 GO:0051081 GO:0007097 GO:0090316 GO:0090063 GO:0031116 GO:1904398 GO:0060236 GO:0042147 GO:0021517 Unknown UniProt Sequence Analysis MAQSRRHMSSRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMGVEVGRLRAFLQGGQEATDIALLLRDLETSCSDTRQFCKKIRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSPSSSPYECLRQSCTILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEPQRGGAPGQAPGALPGPGLVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKASLAALPPLHVAKLSLPPHEGPGGNLVAGALYRKTSQLLEKLNQLSTHTHVVDITRSSPAAKSPSAQLMEQVAQLKSLSDTIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHSRLIS 1281 P28023 Dynactin Dctn1 10116 None SL-0178 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}. UNIPROT P28023 PDB 2M02 PDB 2MPX Pfam PF01302 Pfam PF12455 PROSITE PS00845 PROSITE PS50245 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}. A0JNT9 EBI-7894963 0.27 P54256 EBI-9639028 0.49 P54645 EBI-16399805 0.35 P80386 EBI-16400563 0.35 P28023 EBI-16128725 0.56 Q969Q1 EBI-21997483 0.35 P19332 EBI-26374040 0.35 GO:0030424 GO:0005938 GO:0099738 GO:0031252 GO:0120103 GO:0005814 GO:0005813 GO:0036064 GO:0005737 GO:0005868 GO:0005829 GO:0000776 GO:0005874 GO:0005875 GO:0035371 GO:0043005 GO:0043025 GO:0005635 GO:0005634 GO:0032991 GO:0005819 GO:0000922 GO:0042802 GO:0008017 GO:0051010 GO:0060090 GO:0019901 GO:0015631 GO:0051301 GO:0010457 GO:0031122 GO:0000132 GO:0032402 GO:0034454 GO:0061744 GO:0007528 GO:0050905 GO:0070050 GO:1990535 GO:1905515 GO:0051081 GO:0007097 GO:0090316 GO:0090063 GO:0031116 GO:1904398 GO:0060236 GO:0042147 GO:0021517 Unknown UniProt Sequence Analysis MAQSKRHMYNRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKILKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRDQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEAKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEESTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSPSSSPYECLRQSCSILISTMNKLATAMQEGEYDAERPPSKPPPVEPWPAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQTLLRKKEKEFEETMDALQADIDQLEAEKTELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEQQRGGTPGQAPGALPGPGPVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKASLAALPPLHVAKFSLPPHEGPGGNLLSGALYRKTSQLLEKLNQLSTYTHVVDITRSSPACKSPSAQLMEQVAQLKSLSDTIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHGRLIS 1280 Q5W5U4 Probable DDX4 9913 None SL-0198 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}. UNIPROT Q5W5U4 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0033391 GO:0005737 GO:0048471 GO:0071546 GO:0071547 GO:0005524 GO:0016887 GO:0003676 GO:0003724 GO:0030154 GO:0043046 GO:0031047 GO:0007141 GO:0007140 GO:0010529 GO:1990511 GO:0034587 GO:0007283 Unknown UniProt Sequence Analysis MGDEDWEAEIIKPHISSYVPVFEKDRYSSGANGDTFNRTPASSSEMGDGSSRRDHFMRSGFASGRSLGNRDPGESNKRENTSTVGGFGVGKSFGNRGFSNNKFEEGDSSGFWRESSIDCEDNQTRNRGFSKRGGYQDGNDSEALGSSRRGGRGSFRGCRGGFGRGSPNSDYEQDEGTQRSGGIFGSRRSALSGAGNGDTFQSRSGGGSGRGGYKGLNEEVITGSGKNSWKSEAEGGESGDTQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDPPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIIQGGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDVIGKEKIGLRQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAGEFLKSNYLFVAVGQVGGACRDVQQTILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDSQLAQPLVKVLSDAQQDVPAWLEEIAFSTYGPGFSGNARGNVFASVDTRKNYPGKSSLNTAGFSSTQAPNPVDDESWD 729 Q9NQI0 Probable DDX4 9606 None SL-0198 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}. UNIPROT Q9NQI0 UNIPROT A8K8Q2 UNIPROT B3KSF4 UNIPROT D6RDK4 UNIPROT E9PCD8 UNIPROT Q5M7Z3 UNIPROT Q86VX0 UNIPROT Q9NT92 UNIPROT Q9NYB1 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 OMIM 605281 DisGeNET 54514 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}. P12931 EBI-7609853 0.40 Q8JPQ9 EBI-6159460 0.35 Q86VP6 EBI-21322532 0.35 Q96GG9 EBI-21325177 0.35 Q13618 EBI-21329068 0.35 Q9NZ43 EBI-10887976 0.35 Q9Y2H1 EBI-20624829 0.27 GO:0005737 GO:0005634 GO:0043186 GO:0048471 GO:0071546 GO:0071547 GO:0005524 GO:0016887 GO:0140693 GO:0003723 GO:0003724 GO:0030154 GO:0043046 GO:0030317 GO:0007276 GO:0031047 GO:0007141 GO:0007140 GO:0010529 GO:1990511 GO:0034587 GO:0007283 Unknown UniProt Sequence Analysis MGDEDWEAEINPHMSSYVPIFEKDRYSGENGDNFNRTPASSSEMDDGPSRRDHFMKSGFASGRNFGNRDAGECNKRDNTSTMGGFGVGKSFGNRGFSNSRFEDGDSSGFWRESSNDCEDNPTRNRGFSKRGGYRDGNNSEASGPYRRGGRGSFRGCRGGFGLGSPNNDLDPDECMQRTGGLFGSRRPVLSGTGNGDTSQSRSGSGSERGGYKGLNEEVITGSGKNSWKSEAEGGESSDTQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQTVLQVGQFSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSTLNTAGFSSSQAPNPVDDESWD 724 Q4R5S7 Probable DDX4 9541 None SL-0198 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}. UNIPROT Q4R5S7 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0005737 GO:0048471 GO:0071546 GO:0071547 GO:0005524 GO:0016887 GO:0003676 GO:0003724 GO:0030154 GO:0043046 GO:0031047 GO:0007141 GO:0007140 GO:0010529 GO:1990511 GO:0034587 GO:0007283 Unknown UniProt Sequence Analysis MGDEDWEAEINPHMSSYVPIFEKDRYSSGENGDNFNRTPTSSSEMDDGPSRRDHFMKSGFASGRNFGNRDAGESNKRDNTSTMGGFGVGKSFGNRGFSNSKFEDGDSSGFWRESSNDCEDNPTRNRGFSKRGGYRDGNNSEASGPSRRGGRSSFRGCRGGFGLGSPNNDLDPDECMQRTGGLFGSRRPALSGTGNGDTSQSRSGSGSERGGYKGLNEEVITGSGKNSWKSEAEGGESSDTQGPKVTYIPPPPPEDEDSIFAHYQTGISFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASCFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQTVLQVGQFSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSSLNTAGFSSSQAPNPVDDESWD 725 Q61496 ATP-dependent Ddx4 10090 None SL-0198 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}. UNIPROT Q61496 UNIPROT Q9D5X7 PDB 5JIU Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. Q9UPY3 EBI-15569634 0.54 GO:0033391 GO:0005737 GO:0005829 GO:0005634 GO:0043186 GO:0048471 GO:0071546 GO:0071547 GO:1990904 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0030154 GO:0043046 GO:0030317 GO:0007276 GO:0031047 GO:0007141 GO:0007140 GO:0010529 GO:1990511 GO:0034587 GO:0032880 GO:0007283 Unknown UniProt Sequence Analysis MGDEDWEAEILKPHVSSYVPVFEKDKYSSGANGDTFNRTSASSDIGESSKKENTSTTGGFGRGKGFGNRGFLNNKFEEGDSSGFWKESNNDCEDNQTRSRGFSKRGGCQDGNDSEASGPFRRGGRGSFRGCRGGFGLGRPNSESDQDQGTQRGGGLFGSRKPAASDSGNGDTYQSRSGSGRGGYKGLNEEVVTGSGKNSWKSETEGGESSDSQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFVAVGQVGGACRDVQQTILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSDNHLAQPLVKVLSDAQQDVPAWLEEIAFSTYVPPSFSSSTRGGAVFASVDTRKNYQGKHTLNTAGISSSQAPNPVDDESWD 702 Q6GWX0 Probable DDX4 9823 None SL-0198 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}. UNIPROT Q6GWX0 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0033391 GO:0005737 GO:0005634 GO:0043186 GO:0048471 GO:0071546 GO:0071547 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0030154 GO:0043046 GO:0007276 GO:0031047 GO:0007141 GO:0007140 GO:0010529 GO:1990511 GO:0034587 GO:0007283 Unknown UniProt Sequence Analysis MGDEDWEAEINPHVSSYVPIFEKDGYSGENGDKFNRTTASSSEMDDGPSGRDHFMKSGFTSGRSYGKRDAGESNKRENTSTTGGFGVGKSFGNRGFSNNRFEDGDSSGFWRESTNDCEDNTTRNRGFSKRGGSRDGNKSEASGPFRRGGRGSFRGCRGGFGLGSQNSELDPDQGMQRGGGLFGSGRPAASDTGNGDTYQSRSGRGRGGYKGLNEEVVTGSGKNSWKSEAEGGESSDTQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQADLQVGQYSKREKLLEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSTLNTAGFSSSQAPNPVDDESWD 722 Q64060 Probable Ddx4 10116 None SL-0198 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}. UNIPROT Q64060 Pfam PF00270 Pfam PF00271 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 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}. GO:0033391 GO:0005737 GO:0005634 GO:0043186 GO:0048471 GO:0071546 GO:0071547 GO:1990904 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0030154 GO:0043046 GO:0030317 GO:0007276 GO:0031047 GO:0007141 GO:0007140 GO:0010529 GO:1990511 GO:0034587 GO:0032880 GO:0080021 GO:0032526 GO:0007283 Unknown UniProt Sequence Analysis MGDEDWEAEILKPHVSSYVPVFEKDKYSSGANGDTFNRTSASSSEMEDGPSGRDHFMRSGFSSGRNLGNRDIGESSKRETTSTTGGFGRGKGFGNRGFLNNKFEEGDSSGFWKESTNDCEDTQTRSRGFSKRGGYPDGNDSEASGPFRRGGRDSEYDQDQGSQRGGGLFGSRKPAASDSGSGDTFQSRSGNARGAYKGLNEEVVTGSGKNSWKSEAEGGESSDIQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFLKSNYLFVAVGQVGGACRDVQQSILQVGPVFKKRKLVEILRNIGDERPMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFNLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNHLAQPLVKVLSDAQQDVPAWLEEIAFSSYAPPSFSNSTRGAVFASFDTRKNFQGKNTLNTAGISSAQAPNPVDDESWD 713 Q9H4E7 Differentially DEF6 9606 None SL-0198 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}. UNIPROT Q9H4E7 UNIPROT Q86VF4 Pfam PF00169 PROSITE PS50003 OMIM 610094 OMIM 619573 DisGeNET 50619 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}. 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. O15162 EBI-10306705 0.56 Q9H0H0 EBI-24620161 0.56 Q9BUH8 EBI-754471 0.37 Q61738 EBI-1786346 0.37 Q8ZAR2 EBI-2871608 0.00 Q8D0E1 EBI-2871601 0.00 I6L996 EBI-10306695 0.72 Q8IX15 EBI-10306735 0.56 P15884 EBI-10306715 0.67 Q00587 EBI-10306725 0.56 Q96AQ6 EBI-10306747 0.56 Q9NRA8 EBI-10306757 0.56 A6NEM1 EBI-24304101 0.56 Q96JM7 EBI-24305175 0.56 Q86T90 EBI-24326579 0.56 A6NC98 EBI-24344394 0.56 P25786 EBI-24699153 0.56 Q96N21 EBI-24729596 0.56 O95391 EBI-24748905 0.56 O00422 EBI-24753175 0.56 Q8WZA2 EBI-23888902 0.56 Q86YV0 EBI-24370130 0.56 Q9NYA3 EBI-24382536 0.56 Q04864 EBI-24401680 0.56 Q15323 EBI-24408384 0.56 Q7Z5H3 EBI-25263076 0.56 Q0VD86 EBI-24580521 0.56 P0C7X2 EBI-24745278 0.56 Q9ULK0 EBI-21558763 0.35 Q9P258 EBI-21558763 0.35 Q9NXR7 EBI-21558763 0.35 Q9NXF7 EBI-21558763 0.35 Q9NWV8 EBI-21558763 0.35 Q9HCJ0 EBI-21558763 0.35 Q96JM3 EBI-21558763 0.35 Q92625 EBI-21558763 0.35 Q8N6N3 EBI-21558763 0.35 Q8IUH3 EBI-21558763 0.35 Q7Z4W1 EBI-21558763 0.35 Q15018 EBI-21558763 0.35 Q04759 EBI-21558763 0.35 Q00653 EBI-21558763 0.35 P46736 EBI-21558763 0.35 P35612 EBI-21558763 0.35 P28370 EBI-21558763 0.35 A6NI28 EBI-21558763 0.35 GO:0005737 GO:0005856 GO:0005829 GO:0030175 GO:0016020 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0005085 GO:0051056 GO:0098876 Unknown UniProt Sequence Analysis MALRKELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLHIPHDPVALEEHFRDDDDGPVSSQGYMPYLNKYILDKVEEGAFVKEHFDELCWTLTAKKNYRADSNGNSMLSNQDAFRLWCLFNFLSEDKYPLIMVPDEVEYLLKKVLSSMSLEVSLGELEELLAQEAQVAQTTGGLSVWQFLELFNSGRCLRGVGRDTLSMAIHEVYQELIQDVLKQGYLWKRGHLRRNWAERWFQLQPSCLCYFGSEECKEKRGIIPLDAHCCVEVLPDRDGKRCMFCVKTANRTYEMSASDTRQRQEWTAAIQMAIRLQAEGKTSLHKDLKQKRREQREQRERRRAAKEEELLRLQQLQEEKERKLQELELLQEAQRQAERLLQEEEERRRSQHRELQQALEGQLREAEQARASMQAEMELKEEEAARQRQRIKELEEMQQRLQEALQLEVKARRDEESVRIAQTRLLEEEEEKLKQLMQLKEEQERYIERAQQEKEELQQEMAQQSRSLQQAQQQLEEVRQNRQRADEDVEAAQRKLRQASTNVKHWNVQMNRLMHPIEPGDKRPVTSSSFSGFQPPLLAHRDSSLKRLTRWGSQGNRTPSPNSNEQQKSLNGGDEAPAPASTPQEDKLDPAPEN 631 Q8C2K1 Differentially Def6 10090 None SL-0198 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}. UNIPROT Q8C2K1 UNIPROT A1KXF9 UNIPROT B2KF17 UNIPROT Q0VBU6 UNIPROT Q3V3M7 UNIPROT Q80XA9 UNIPROT Q9CRJ2 Pfam PF00169 PROSITE PS50003 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}. 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}. Q61738 EBI-1786373 0.54 Q3U1F9 EBI-12603117 0.40 GO:0005911 GO:0005737 GO:0005856 GO:0005829 GO:0030175 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0098876 Unknown UniProt Sequence Analysis MALRKELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLNIPHDPVALEEHFRDDDDGPVSSQGYMPYLNKYILDKVEEGAFVKEHFDELCWTLTAKKNYRADGIGSSPLSNQDAFRLWCLFNFLSEDKYPLIMVPDEVEYLLKKLLGSLSLEMGLGELEELLAQDAQSAQTAVGLSVWQFLELFNSGRCLRGVGRDSLSMAIQEVYQELIQDVLKQGYLWKRGHLRRNWAERWFQLQPSSLCYFGSEECKEKRGTIPLDAHCCVEVLPDREGKRCMFCVKTASRTYEMSASDTRQRQEWTAAIQTAIRLQAEGKTSLHKDLKQKRREQREQRERRRAAKEEELLRLQQLQEEKERKLQELELLQEAQRQAERLLQEEEERRRSQHKELQQALEGQLREAEQARASMQAEMELKKEEAARQRQRIAELEEMQERLQEALQLEVKARRDEEAVRLAQTRLLEEEEEKLKQLMHLKEEQERYIERAQQEKQELQQEMALQSRSLQHAQQQLEEVRQNRQRADEDVEAAQRKLRQASTNVKHWNVQMNRLMHPIEPGDKRPTTSSSFTGFQPPPLARRDSSLKRLTRWGSQGNRTLSVNSSEQKSLNGGDETPILALASQEEKLDPAPGN 630 Q08DM1 Dematin DMTN 9913 None SL-0198 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}. UNIPROT Q08DM1 Pfam PF16182 Pfam PF02209 PROSITE PS51089 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}. GO:0015629 GO:0005884 GO:0031253 GO:0031410 GO:0005829 GO:0012505 GO:0048471 GO:0005886 GO:0031095 GO:0014731 GO:0003779 GO:0051015 GO:0043621 GO:0005102 GO:0030507 GO:0030036 GO:0051017 GO:0051693 GO:0090527 GO:0035585 GO:0035584 GO:0071277 GO:0071320 GO:0048821 GO:0030032 GO:0010812 GO:0051895 GO:0033137 GO:0010801 GO:0050732 GO:0090315 GO:1900025 GO:0030194 GO:0010763 GO:2001046 GO:1901731 GO:1900026 GO:0090303 GO:0070560 GO:0065003 GO:0032956 GO:0008360 GO:0051489 GO:0010591 Unknown UniProt Sequence Analysis MERLQKQPLTSPGSVSSSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRERSLSPKSTSPPPSPEVWAESRSPGTISQASAPRTAGTPRTSLPHFHHPETTRPDSNIYKKPPIYKQRAESTGGSPQSKHPIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHAGTSKSSSLPAYGRTTLSRLQSTDFSPSGSEAESPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNRGRTKLPPGVDRMRLERHLSAEDFSRVFSMSPEEFGKLALWKRNELKKKASLF 406 Q08495 Dematin DMTN 9606 None SL-0198 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. UNIPROT Q08495 UNIPROT A8K0T5 UNIPROT B3KP70 UNIPROT B3KRH3 UNIPROT B4DI75 UNIPROT E9PEJ0 UNIPROT Q13215 UNIPROT Q9BRE3 PDB 1QZP PDB 1ZV6 Pfam PF16182 Pfam PF02209 PROSITE PS51089 OMIM 125305 DisGeNET 2039 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}. O43237 EBI-731827 0.00 Q9UNN8 EBI-734445 0.00 Q86YD1 EBI-735504 0.00 P62316 EBI-736673 0.00 P31946 EBI-8796749 0.35 P14618 EBI-9355736 0.44 Q08379 EBI-10225555 0.56 Q8TAP6 EBI-24382670 0.56 Q8IYF3 EBI-24387259 0.56 Q12933 EBI-24472525 0.56 Q8IWV7 EBI-21864310 0.35 Q86TI2 EBI-21864310 0.35 P63104 EBI-21864310 0.35 P62258 EBI-21864310 0.35 P61981 EBI-21864310 0.35 Q04917 EBI-21907689 0.35 P50552 EBI-30845230 0.44 GO:0015629 GO:0005884 GO:0031253 GO:0030863 GO:0031410 GO:0005829 GO:0012505 GO:0048471 GO:0005886 GO:0031095 GO:0014069 GO:0014731 GO:0003779 GO:0051015 GO:0043621 GO:0005102 GO:0030507 GO:0030036 GO:0051017 GO:0051693 GO:0090527 GO:0035585 GO:0035584 GO:0071277 GO:0071320 GO:0007010 GO:0048821 GO:0030032 GO:0010812 GO:0051895 GO:0033137 GO:0010801 GO:0050732 GO:0090315 GO:1900025 GO:0030194 GO:0010763 GO:2001046 GO:1901731 GO:1900026 GO:0090303 GO:0070560 GO:0065003 GO:0032956 GO:0008360 GO:0051489 GO:0010591 Unknown UniProt Sequence Analysis MERLQKQPLTSPGSVSPSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRERSLSPKSTSPPPSPEVWADSRSPGIISQASAPRTTGTPRTSLPHFHHPETSRPDSNIYKKPPIYKQRESVGGSPQTKHLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHQGTSKSSSLPAYGRTTLSRLQSTEFSPSGSETGSPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKKKASLF 405 Q9WV69 Dematin Dmtn 10090 None SL-0198 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}. UNIPROT Q9WV69 UNIPROT F8WIF9 UNIPROT Q3TYC5 UNIPROT Q8JZV5 UNIPROT Q9WVM2 Pfam PF16182 Pfam PF02209 PROSITE PS51089 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}. P63104 EBI-6271507 0.35 GO:0015629 GO:0005884 GO:0031253 GO:0030863 GO:0031410 GO:0005829 GO:0012505 GO:0016020 GO:0048471 GO:0005886 GO:0031095 GO:0014069 GO:0014731 GO:0003779 GO:0051015 GO:0043621 GO:0005102 GO:0030507 GO:0030036 GO:0051017 GO:0051693 GO:0090527 GO:0035585 GO:0035584 GO:0071277 GO:0071320 GO:0048821 GO:0030032 GO:0010812 GO:0051895 GO:0033137 GO:0010801 GO:0050732 GO:0090315 GO:1900025 GO:0030194 GO:0010763 GO:2001046 GO:1901731 GO:1900026 GO:0090303 GO:0070560 GO:0065003 GO:0032956 GO:0008360 GO:0051489 GO:0010591 Unknown UniProt Sequence Analysis MERLQKQPLTSPGSVSSSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRECSLSPKSTSPPPSPEVWAESRTLGIISQASTPRTTGTPRTSLPHFHHPETTRPDSNIYKKPPIYKQRESVGGSPQSKHLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRKGAEEEEEEEDDDSEEEIKAIRERQKEELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHSGTSKSSSLPSYGRTTLSRLQSTEFSPSGSEAGSPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKKKASLF 405 Q5R4B6 Dematin DMTN 9601 None SL-0198 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}. UNIPROT Q5R4B6 Pfam PF16182 Pfam PF02209 PROSITE PS51089 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}. GO:0005884 GO:0031253 GO:0030863 GO:0031410 GO:0005829 GO:0012505 GO:0048471 GO:0005886 GO:0031095 GO:0014069 GO:0014731 GO:0003779 GO:0043621 GO:0005102 GO:0030507 GO:0030036 GO:0051017 GO:0051693 GO:0090527 GO:0035585 GO:0035584 GO:0071277 GO:0071320 GO:0048821 GO:0010812 GO:0051895 GO:0033137 GO:0010801 GO:0050732 GO:0090315 GO:1900025 GO:0030194 GO:0010763 GO:2001046 GO:1901731 GO:1900026 GO:0090303 GO:0070560 GO:0065003 GO:0032956 GO:0008360 GO:0051489 GO:0010591 Unknown UniProt Sequence Analysis MERLQKQPLTSPGSVSPSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRERSLSPKSTSPPPSPEVWADSRSPGIISQASAPRTTGTPRTSLPHFHHPETSRPDSNIYKKPPIYKQRESVGGSPQTKHLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHQGTSKSSSLPAYGRTTLSRLQSTEFSPSGSETGSPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKKKASLF 405 O75140 GATOR DEPDC5 9606 None SL-0198 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}. UNIPROT O75140 UNIPROT A6H8V6 UNIPROT A8MPX9 UNIPROT B4DH93 UNIPROT B9EGN9 UNIPROT Q5K3V5 UNIPROT Q5THY9 UNIPROT Q5THZ0 UNIPROT Q5THZ1 UNIPROT Q5THZ3 UNIPROT Q68DR1 UNIPROT Q6MZX3 UNIPROT Q6PEZ1 UNIPROT Q9UGV8 UNIPROT Q9UH13 PDB 6CES PDB 6CET PDB 7T3A PDB 7T3B PDB 7T3C Pfam PF00610 Pfam PF19418 Pfam PF12257 PROSITE PS50186 OMIM 604364 OMIM 614191 DisGeNET 9681 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}. 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}. P05412 EBI-11323169 0.35 P58043 EBI-11102804 0.35 Q6W0C5 EBI-24665620 0.56 O75604 EBI-24681385 0.56 Q13257 EBI-24703582 0.56 P49368 EBI-24741275 0.56 Q6FHY5 EBI-24434236 0.56 Q9BSW7 EBI-24642109 0.56 Q96QG7 EBI-24656502 0.56 Q9UI95 EBI-24775208 0.56 Q1RMZ1 EBI-21587773 0.35 Q8WTW4 EBI-21720164 0.53 Q9Y664 EBI-21890520 0.35 Q96MD2 EBI-21890520 0.35 Q969R8 EBI-21890520 0.35 Q5T011 EBI-21890520 0.35 Q12980 EBI-16126226 0.35 Q9HB90 EBI-16126252 0.35 Q7L523 EBI-16126252 0.35 Q5VZM2 EBI-16752640 0.35 Q96S15 EBI-16752640 0.35 Q9NXC5 EBI-16752640 0.35 Q93079 EBI-20935716 0.40 Q99459 EBI-21392827 0.00 P63010 EBI-30815544 0.44 GO:0005829 GO:1990130 GO:0005765 GO:0005764 GO:0048471 GO:0005096 GO:0044877 GO:0034198 GO:0035556 GO:0032007 GO:1904262 GO:0010508 Unknown UniProt Sequence Analysis MRTTKVYKLVIHKKGFGGSDDELVVNPKVFPHIKLGDIVEIAHPNDEYSPLLLQVKSLKEDLQKETISVDQTVTQVFRLRPYQDVYVNVVDPKDVTLDLVELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAGIRAQAGELWVKNEKVMCGYISEDTRVVFRSTSAMVYIFIQMSCEMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEINRASIRQDHKGRFYEDFYKVVVQNERREEWTSLLVTIKKLFIQYPVLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVITPGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFKLHNRSAPRDSRLGDDYNIPHWINHSFYTSKSQLFCNSFTPRIKLAGKKPASEKAKNGRDTSLGSPKESENALPIQVDYDAYDAQVFRLPGPSRAQCLTTCRSVRERESHSRKSASSCDVSSSPSLPSRTLPTEEVRSQASDDSSLGKSANILMIPHPHLHQYEVSSSLGYTSTRDVLENMMEPPQRDSSAPGRFHVGSAESMLHVRPGGYTPQRALINPFAPSRMPMKLTSNRRRWMHTFPVGPSGEAIQIHHQTRQNMAELQGSGQRDPTHSSAELLELAYHEAAGRHSNSRQPGDGMSFLNFSGTEELSVGLLSNSGAGMNPRTQNKDSLEDSVSTSPDPILTLSAPPVVPGFCCTVGVDWKSLTTPACLPLTTDYFPDRQGLQNDYTEGCYDLLPEADIDRRDEDGVQMTAQQVFEEFICQRLMQGYQIIVQPKTQKPNPAVPPPLSSSPLYSRGLVSRNRPEEEDQYWLSMGRTFHKVTLKDKMITVTRYLPKYPYESAQIHYTYSLCPSHSDSEFVSCWVEFSHERLEEYKWNYLDQYICSAGSEDFSLIESLKFWRTRFLLLPACVTATKRITEGEAHCDIYGDRPRADEDEWQLLDGFVRFVEGLNRIRRRHRSDRMMRKGTAMKGLQMTGPISTHSLESTAPPVGKKGTSALSALLEMEASQKCLGEQQAAVHGGKSSAQSAESSSVAMTPTYMDSPRKDGAFFMEFVRSPRTASSAFYPQVSVDQTATPMLDGTSLGICTGQSMDRGNSQTFGNSQNIGEQGYSSTNSSDSSSQQLVASSLTSSSTLTEILEAMKHPSTGVQLLSEQKGLSPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVTDKEPDRVAMQQPATTWHTAGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASYASRHSSFSRSFGGRSQAAALLAATVPEQRTVTLDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRAQLFIPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSKRKFSGQQRRRRNSTSSTNQNMFCEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDNRLVTFWTSCLEKMHASAP 1603 P61460 GATOR Depdc5 10090 None SL-0198 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}. UNIPROT P61460 UNIPROT E9Q5J2 UNIPROT E9Q5Y0 Pfam PF00610 Pfam PF19418 Pfam PF12257 PROSITE PS50186 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}. Q9R1S0 EBI-11784907 0.35 GO:0031463 GO:0005829 GO:1990130 GO:0005765 GO:0005764 GO:0048471 GO:0005096 GO:0044877 GO:0034198 GO:0035556 GO:0032007 GO:1904262 GO:0010508 Unknown UniProt Sequence Analysis MRTTKVYKLVIHKKGFGGSDDELVVNPKVFPHIKLGDIVEIAHPNDEYSPLLLQVKSLKEDLQKETISVDQTVTQVFRLRPYQDVYVNVVDPKDVTLDLVELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAGIRAQAGELWVKNEKVMCGYISEETRVVFRSTSAMVYIFIQMSCEMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSIDEFPEINRASIQEDHKGRFYEDFYKVVVQNERREEWTSLLVTIKKLFIQYPVLVRLEQAGGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVITPGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFKLHNRSVPRDSRLGDDYNIPHWINHSFYTSKSQLFCNSFTPRIKLAGKKSASEKTKNGRDTSLGTPKESENTLPIQVDYDAYDAQVFRLPGPSRAQRLATCRSVREQENHSRKSASSCDVSSSPSLPSRALPTEEVRSQASDDSSLGKSTNILMIPNPHLHQYEVSSSLGYTSTRDVLENMIEPPQRDSSAPGRFHVGSAESMLHVRPGGYTPQRALINPFAPSRMPMKLTSNRRRWMHTFPVGPSGEAIQIHHQTRQNMAELQGSRQRDPTHSSAELLELAYHEAAGRHSTSRQPGDSMSLNFSGTEELSVSLLSNSSTGVNPRTQNKDSLEDSVSTSPDPMPGFCCTVGVDWKSLTTPACLPLTTDYFPDRQGLQNDYTEGCYDLLPEADMDRRDEEGVQMTAQQVFEEFICQRLMQGYQIIVQPKTQKPNTTVPPPLSSSPLYSRGLVSRNRPEEEGQYWLSMGRTFHKVTLKDKMITVTRYLPKYPYESAQIHYTYSLCPSHSDSEFVSCWVDFCHERLEEYKWNYLDQYICSAGSEDFSLIESLKFWRTRFLLLPACVTATKRITEGEVHCDIYGDKPRADEDEWQLLDGFIRFVEGLNRIRRRHRSDRMIRKGTAMKGLQMTGPISAHSLEAAGPPVGKKGTSALSALLEMEASQKSLGEQQTTVHGKSSTQPAENSSVAMTPTYVDSPRKDGAFFMEFVRSPRTASSAFYPQASVDQTAPLVLDSTSLGVSTGQPMDRGNNQTFGNSQNIEQAFPSANSGDYSSQQHVASSLTSSSTLVEILEAMKHPSTGVQLLSEQKGLSPCCFISAEVVHWLMNNVEGVQTQAMGIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVMDKEPERVAMQQPSAPWYTAGADDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASYASRHSSFSRSFGGRSQAAALLAATVPEQRTVTLDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTATVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRAQLFIPLNLSCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSVSAFNFPAENKPQYIHVTGTVFLQLPYSKRKFSGQQRRRRNSTSSTNQNMFCEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDNRLVTFWTNCLEKMHASAP 1591 Q9N303 P-granule-associated deps 6239 None SL-0198 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}. UNIPROT Q9N303 UNIPROT V6CLC9 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}. GO:0043186 GO:0048471 GO:0031047 Unknown UniProt Sequence Analysis MSERQSKYFDYQGIVISSTGQDNQDSETDLVYLIQAHGKAAPKNIMYGVSKCAFVPTNLERNFDNIEEAKNLERRSKIPLKFGEVILWNESDCDHDKRIILHIKREKPIYEASSSRNGLILKVGGVIQPTSTTSFWTPLCTVTMPETEATRAEPDVWLYAWIRFETTMKSGLDPFNMTATFESFDSCDPSDQARVCEAPWNAGSPDSKFGVWRPDPKPADSDDEIDIEPREGWHLPEDKWAEVIKMQLGLYVGERLLICKELSQFDFIIPLQKPFSRGTDKTLIYPAVGEYFHFSAIWSMQHNGFLIYELQPVPLLRQHVTSVNGNLLTRVVPASIRGLFVDKEGTLGLIDDPHHLLSFFEFHPAGYEFLKAMAEVRAVRTSENKSVRYRIVRTSGMSIFENWLRDTQFVVGPVKGIRINEDTVICAKHPNVYFKIPNNLKEGIPIGGGVQFVGKRQAGVDSEIMITECSPCPAFTCKNYSVSGDTRLFQVYLKPNCDHEQLAESDSMGFVDFRELETPCRGKFLAWVRESITVNDCRRAATIMEVCSTAICPPLIAMSANSSRATSARTTPAGSSIGSRSSIQSRASAATSVSSNRFVGPSSRRTPSGTPQSSTSSRV 619 Q70VZ8 Diacylglycerol DGAT2 9913 None SL-0198 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}. UNIPROT Q70VZ8 UNIPROT A5D9B3 UNIPROT Q6B852 UNIPROT Q6PP93 UNIPROT Q6PP94 UNIPROT Q6PP95 UNIPROT Q6PP96 Pfam PF03982 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}. GO:0005783 GO:0005789 GO:0030176 GO:0016021 GO:0005811 GO:0016020 GO:1990578 GO:0048471 GO:0003846 GO:0004144 GO:0050252 GO:0071400 GO:0035356 GO:0042632 GO:0006651 GO:0046339 GO:0060613 GO:0055089 GO:0006071 GO:0006629 GO:0019915 GO:0035336 GO:0034383 GO:0006640 GO:0097006 GO:0019432 Transmembrane UniProt Sequence Analysis {ECO:0000255} MKTLIAAYSGVLRGTGSSILSALQDLFSVTWLNRAKVEKQLQVISVLQWVLSFLVLGVACSVILMYTFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTSRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPRLERPTQQDIDLYHAMYVQALVKLFDQHKTKFGLPETEVLEVN 361 Q4V9F0 Diacylglycerol dgat2 7955 None SL-0198 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}. UNIPROT Q4V9F0 Pfam PF03982 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}. GO:0005789 GO:0016021 GO:0005811 GO:1990578 GO:0004144 GO:0050252 GO:0006651 GO:0006071 GO:0055088 GO:0006629 GO:1905897 GO:0061959 GO:0019432 Transmembrane UniProt Sequence Analysis {ECO:0000255} MKTILAAYSGVKKGSGSSILSALHDLPTVPWLTRSKMVKHLQVISVLQFIMTFLTMGIACSLLLMYMFCTDFWVISVLYVAWLIYDWNTPGQGGRRSTWVRDWTVWKYMRDYFPIRLIKTHNLLPSRNYIFGYHPHGILCFGAFCNFGTEATGFTKVFPGIKPSLATLAGNFRLPMFREYLMCGGICPVNRNSIDYLLSSNGTGNAVVIVIGGAAESLDCAPGRNSVMLKKRKGFVKLALKQGADLVPVYSFGENEVYKQLIFEEGSWWRTIQRKLQKFLGFAPCLFHGCGLFFPESWGLVPYCKPITTVVGEPITVPKIEEPTQDVIDMYHAMYIRSLKSLFDNYKTRFGLNESDTLIIH 361 Q96PD7 Diacylglycerol DGAT2 9606 None SL-0198 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}. UNIPROT Q96PD7 UNIPROT A6ND76 UNIPROT Q5U810 UNIPROT Q68CL3 UNIPROT Q68DJ0 UNIPROT Q8NDB7 UNIPROT Q96BS0 UNIPROT Q9BYE5 Pfam PF03982 OMIM 606983 DisGeNET 84649 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}. P55072 EBI-9519939 0.40 Q9UKV5 EBI-9520083 0.40 GO:0005829 GO:0005783 GO:0005789 GO:0030176 GO:0016021 GO:0043231 GO:0005811 GO:0005739 GO:1990578 GO:0048471 GO:0003846 GO:0004144 GO:0042803 GO:0050252 GO:0038183 GO:0071400 GO:0035356 GO:0042632 GO:0006651 GO:0046339 GO:0060613 GO:0055089 GO:0006071 GO:0006629 GO:0019915 GO:0035336 GO:0034383 GO:0006640 GO:0046322 GO:0045722 GO:0010867 GO:0090181 GO:0050746 GO:0097006 GO:0019432 Transmembrane UniProt Sequence Analysis {ECO:0000255} MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHTMYMEALVKLFDKHKTKFGLPETEVLEVN 388 Q9DCV3 Diacylglycerol Dgat2 10090 None SL-0198 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}. UNIPROT Q9DCV3 Pfam PF03982 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}. GO:0005829 GO:0005783 GO:0005789 GO:0030176 GO:0016021 GO:0043231 GO:0005811 GO:0016020 GO:1990578 GO:0048471 GO:0003846 GO:0004144 GO:0042803 GO:0050252 GO:0038183 GO:0071400 GO:0035356 GO:0042632 GO:0006651 GO:0046339 GO:0060613 GO:0055089 GO:0006071 GO:0006629 GO:0019915 GO:0035336 GO:0034383 GO:0006640 GO:0046322 GO:0045722 GO:0010867 GO:0090181 GO:0050746 GO:0097006 GO:0019432 Transmembrane UniProt Sequence Analysis {ECO:0000255} MKTLIAAYSGVLRGERRAEAARSENKNKGSALSREGSGRWGTGSSILSALQDIFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSVILMYTFCTDCWLIAVLYFTWLAFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLKNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITVPKLEHPTQKDIDLYHAMYMEALVKLFDNHKTKFGLPETEVLEVN 388 Q5FVP8 Diacylglycerol Dgat2 10116 None SL-0198 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}. UNIPROT Q5FVP8 UNIPROT Q8K4Y4 Pfam PF03982 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}. GO:0005829 GO:0005783 GO:0005789 GO:0030176 GO:0016021 GO:0043231 GO:0005811 GO:0016020 GO:0005739 GO:1990578 GO:0048471 GO:0003846 GO:0004144 GO:0042803 GO:0050252 GO:0038183 GO:0071400 GO:0035356 GO:0042632 GO:0006651 GO:0046339 GO:0060613 GO:0055089 GO:0006071 GO:0006629 GO:0019915 GO:0035336 GO:0034383 GO:0006640 GO:0046322 GO:0045722 GO:0010867 GO:0090181 GO:0050746 GO:0097006 GO:0019432 Transmembrane UniProt Sequence Analysis {ECO:0000255} MKTLIAAYSGVLRGERRAEAARSENKNKGSALSREGSGRWGTGSSILSALQDIFSVTWLNRSKVEKHLQVISVLQWVLSFLVLGVACSVILMYTFCTDCWLIAALYFTWLAFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIVIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITVPKLEHPTQKDIDLYHTMYMEALVKLFDNHKTKFGLPETEVLEVN 388 Q6PAZ3 Diacylglycerol dgat2 8355 None SL-0198 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}. UNIPROT Q6PAZ3 Pfam PF03982 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}. GO:0005789 GO:0016021 GO:0005811 GO:1990578 GO:0004144 GO:0050252 GO:0006651 GO:0006071 GO:0006640 GO:0019432 Transmembrane UniProt Sequence Analysis {ECO:0000255} MKTIIAAYSGVLRGTGSSLLSAVHDLPSIPWLSKSSVVRHLQIISVLQWVLSFLILGVACTAVLVYIFCTDLWLIAALYFTWMVLDWNTPYKGGRRSSWVRNWAVWRYFRDYFPVKLVKTHNLLPSRNYIFGYHPHGIMCLGAFCNFGTEATGVSKKFPGIKCHLATLAGNFRMPVLREYLMSGGICPVNRDTINYILSKNGTGNAVVIAVGGAAESLNCRPGKNTVTLLHRKGFVKVALQHGADLVPIYSFGENETYKQVVFEEGSWGRWIQQKFQKYVGFAPCLFHGCSFFSSNSWGLVPYANPITTVVGEPITVPKIEQPTQKDVELYHSMYLSSLHRLFDKYKTKLGLPDSETLEFI 361 Q6P342 Diacylglycerol dgat2 8364 None SL-0198 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}. UNIPROT Q6P342 Pfam PF03982 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}. GO:0005789 GO:0016021 GO:0005811 GO:1990578 GO:0004144 GO:0050252 GO:0006651 GO:0046339 GO:0006071 GO:0006629 GO:0006640 GO:0019432 Transmembrane UniProt Sequence Analysis {ECO:0000255} MKTIIAAYSGVLRGTGSSLLSAVHDLPNIPWLSKSSVVRHLQIISVLQWVLSFLILGVACTAVLVYIFCTDLWLIAALYLTWMVLDWNTPYKGGRRSSWVRNWAVWRYFRDYFPIKLVKTHNLLPSRNYIFGYHPHGIMCLGAFCNFGTEATGVSKKFPGIKCHLATLAGNFRMPVLREYLMSGGICPVARDTIDYILSKNGTGNAVVIAVGGAAESLNCRPGKNTVTLKQRKGFVKVALQHGADLVPVYSFGENEAYKQVVFEEGSWGRWIQKKFQKYVGFAPCLFHGCSFFSSNSWGLVPYANPITTVVGEPITVPKIEQPTQKDVELYHAMYVTSLQRLFDKYKTKLGLHDSEMLEIV 361 Q753I3 CTP-dependent DGK1 284811 None SL-0178 SL-0182 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}. UNIPROT Q753I3 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}. GO:0030176 GO:0031965 GO:0004143 GO:0006654 GO:0016310 GO:0016192 Transmembrane UniProt Sequence Analysis {ECO:0000255} MANEEELQTAESAFVTGARRYSNDYSESESSSKHSGCSTPVEGTPAEAATTIGARASGGSTTWQRLRQLLMERGSDVHLPVTEIHLKSQEWFGDFITKHEVPRKVFHSSIGFFTLALYVRDVDYRNVRLPLIVGFVHVLLLDVIRLHWPAFNTLYCQVTGLLMRKKEVHTYNGVLWYLLGLIFAFSFFSKDVALVSLFLLSWCDTAASTVGRLYGHLTPRISRNKSLAGSLAAFVVGVISCAVFYGYFVPAYSHVNHPGEIMWNPETSRLSLVQLSLLGGFVASLSEGIDLFNWDDNFTIPVLSAIFMHTIIAFSQR 317 P87170 CTP-dependent ptp4 284812 None SL-0178 SL-0182 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}. UNIPROT P87170 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}. GO:0005783 GO:0030176 GO:0031965 GO:0097038 GO:0004143 GO:0006654 GO:0016310 GO:0016192 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSTKLTWSQWSKKHEIPRKALHTSIGFFALLLQGCGYHAAQIIPVIEIGFIPAFTGDVIRFNWPAFSRLYNRVIGPLMRESEKNAWNGVIFYMIGVWIVLKVFPEEIAVMSVLLLSWCDTTASTVGRKWGKYTPKIAKNKSLAGSLGAFVCGVFCCYVYWGLFRTGPDSLAAQSRIPFPWLCLINGFIGAFAEAMDVWGLDDNLVIPVVSACLLYLIM 218 Q12382 CTP-dependent DGK1 559292 None SL-0178 SL-0182 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}. UNIPROT Q12382 UNIPROT D6W310 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}. P11484 EBI-3689295 0.35 Q96BA8 EBI-11537340 0.56 Q8N6L0 EBI-11537331 0.56 P50112 EBI-16254616 0.00 GO:0005783 GO:0030176 GO:0031965 GO:0004143 GO:0006654 GO:0016310 GO:2001210 GO:0016192 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGTEDAIALPNSTLEPRTEAKQRLSSKSHQVSAKVTIPAKEEISSSDDDAHVPVTEIHLKSHEWFGDFITKHEIPRKVFHSSIGFITLYLYTQGINYKNVLWPLIYAFIILFILDLIRLNWPFFNMLYCRTVGALMRKKEIHTYNGVLWYILGLIFSFNFFSKDVTLISLFLLSWSDTAAATIGRKYGHLTPKVARNKSLAGSIAAFTVGVITCWVFYGYFVPAYSYVNKPGEIQWSPETSRLSLNMLSLLGGVVAALSEGIDLFNWDDNFTIPVLSSLFMNAVIKTFKK 290 Q86CZ2 Hybrid dhkK 44689 None SL-0178 SL-0182 Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. UNIPROT Q86CZ2 UNIPROT Q54Y10 UNIPROT Q95PH2 Pfam PF02518 Pfam PF00512 Pfam PF00072 PROSITE PS50109 PROSITE PS50110 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. GO:0016021 GO:0005635 GO:0031965 GO:0005524 GO:0000155 GO:0140582 GO:0031154 Transmembrane UniProt Sequence Analysis {ECO:0000255} MIELNNHSKINKNENNTNTRNNSSNNNNNNNNINKTNTNKYFEYNQNSIIYSSIPNSFLSHHPNSVGSQCLSLNSFLPPKPPILLSIFNSDTIGNNNNNNYSSSSSRNNSSGCSSSNNNNNNNNNNNNNNNNNNNNNNNNCNIEQYKNNQKQPKQQQQQKDQTIATQHRISLSSSSSSSSLSSSSSSSSVKQSFQIVKRLFGSLSEYMFPQKDEILYETDPYYLYQDDTQSNDSNEFYDDTDIGSDIDEANLNNTYNIQNCNKTLYNKQQQQAHFVNMNKNVNSNNGTGNSNQSNNVNKNQQNNNNNNNNNSHNNNNGNQNSSSSSSNSGASGSGGNGNNNNNNNNNNNNNNNNNNNSNSNSNNNSKSNNNNKKEGKDGATMNGSHPLIPFRKKPAQVPSPCFRMNSPNSDNDQYLDQLALENSSKKSLVVYNTDNLDQWKHSHLNENFDILQNDLIDIQQQQQQQQQQDNTLQYSSPINKRQEQEQQHIPFQFTTEQQQQLQQQQQQQQQNKTKQHPILLQRQQQQKQKQQQQQQIQQEQIGNNNSNNNNNINNNNNINNNYNNVNDLMNKFEIDQKQHDSQQNLVEEKRTPSFHEHNIIFNSFNFICSIVLDGSNIKSTEKYKAKLIIGFCFTILSFIPSWIIFFWLSGINKPAVMAIIAMPMSISSLVILKRTGSIHYPCHILCFTLCFALTINSYYTGGHQSTIRLLMSTVPIISALVLGRKASIQWSLMVLSIYLLFFVANLYGHEYVQGIPSIIIRSHMNFIIDVTIIIMTLIFTLCYQYFIDEAHRETKLKNAQLTIAKDAAIEAYQARQEFLATMSHEIRTPLNGLIGMATLLRDSHNLPPEEKTMAKAVKSCGDILLRLVNDILDLSKLEANQMGLEHIPFRMRELTQQICHVLSGQANEKNIHLSCEVSDKIPSILLGDSGRILQILMNLTGNALKFTQSGYVKIIIDLIEEESELVSLKKGEYNISFRVKDTGIGVPVESHQKIFEAFVQADPSDSRKYGGSGLGLYLCAKLVRLMKGEIGVYNNPDCDGSTFWFILPLEEGTDQSMQQMNNGARHKAFPQDCVKVLIAEDNIINQRVAVKFLEKIGIKAEVAGNGNEVLEILERQHYDLIFMDFQMPILDGLRCSKTIREFEQNHKWNRICPSIFICGLTANTMSTDKKRCFDHGMNHFISKPFQLEQLRSAIEMAIEHKQRNLMNLNIRN 1213 Q8IY37 Probable DHX37 9606 None SL-0178 SL-0182 Nucleus, nucleolus {ECO:0000269|PubMed:30582406, ECO:0000269|PubMed:31337883}. Cytoplasm {ECO:0000269|PubMed:31337883}. Nucleus membrane {ECO:0000269|PubMed:31337883}. UNIPROT Q8IY37 UNIPROT Q9BUI7 UNIPROT Q9P211 PDB 7MQA Pfam PF00270 Pfam PF04408 Pfam PF00271 Pfam PF07717 PROSITE PS51192 PROSITE PS51194 OMIM 273250 OMIM 617362 OMIM 618731 DisGeNET 57647 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}. 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. P0C6X7 EBI-26377216 0.35 O75051 EBI-308790 0.37 P01106 EBI-1069119 0.00 Q9NY93 EBI-1075155 0.00 P54253 EBI-6450099 0.37 P05412 EBI-11324725 0.35 Q6PGB6 EBI-11027782 0.35 O00567 EBI-11069711 0.35 Q5VWQ0 EBI-21719701 0.35 Q14684 EBI-16686997 0.35 Q9NWT8 EBI-16786806 0.27 Q96GD4 EBI-16787973 0.27 P22087 EBI-16792282 0.27 P68431 EBI-16793336 0.27 P62753 EBI-16798663 0.27 P14404 EBI-21028244 0.35 Q9UGL1 EBI-25480242 0.35 K9N4V0 EBI-26375098 0.35 P0DTC9 EBI-27102259 0.53 Q9BXK1 EBI-29018137 0.27 O43763 EBI-29786140 0.27 P54760 EBI-32721396 0.27 GO:0005737 GO:0031965 GO:0005730 GO:0005654 GO:0005524 GO:0016887 GO:0003723 GO:0003724 GO:0034511 GO:0007420 GO:0000462 GO:2000020 GO:0042255 GO:0042254 Unknown UniProt Sequence Analysis MGKLRRRYNIKGRQQAGPGPSKGPPEPPPVQLELEDKDTLKGVDASNALVLPGKKKKKTKAPPLSKKEKKPLTKKEKKVLQKILEQKEKKSQRAEMLQKLSEVQASEAEMRLFYTTSKLGTGNRMYHTKEKADEVVAPGQEKISSLSGAHRKRRRWPSAEEEEEEEEESESELEEESELDEDPAAEPAEAGVGTTVAPLPPAPAPSSQPVPAGMTVPPPPAAAPPLPRALAKPAVFIPVNRSPEMQEERLKLPILSEEQVIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGFSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLSQRVVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLRYKVVIIDEAHERSVYTDILIGLLSRIVTLRAKRNLPLKLLIMSATLRVEDFTQNPRLFAKPPPVIKVESRQFPVTVHFNKRTPLEDYSGECFRKVCKIHRMLPAGGILVFLTGQAEVHALCRRLRKAFPPSRARPQEKDDDQKDSVEEMRKFKKSRARAKKARAEVLPQINLDHYSVLPAGEGDEDREAEVDEEEGALDSDLDLDLGDGGQDGGEQPDASLPLHVLPLYSLLAPEKQAQVFKPPPEGTRLCVVATNVAETSLTIPGIKYVVDCGKVKKRYYDRVTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALNVEKVINFPFPTPPSVEALLAAEELLIALGALQPPQKAERVKQLQENRLSCPITALGRTMATFPVAPRYAKMLALSRQHGCLPYAITIVASMTVRELFEELDRPAASDEELTRLKSKRARVAQMKRTWAGQGASLKLGDLMVLLGAVGACEYASCTPQFCEANGLRYKAMMEIRRLRGQLTTAVNAVCPEAELFVDPKMQPPTESQVTYLRQIVTAGLGDHLARRVQSEEMLEDKWRNAYKTPLLDDPVFIHPSSVLFKELPEFVVYQEIVETTKMYMKGVSSVEVQWIPALLPSYCQFDKPLEEPAPTYCPERGRVLCHRASVFYRVGWPLPAIEVDFPEGIDRYKHFARFLLEGQVFRKLASYRSCLLSSPGTMLKTWARLQPRTESLLRALVAEKADCHEALLAAWKKNPKYLLAEYCEWLPQAMHPDIEKAWPPTTVH 1157 Q8VXU6 Protein DI19 3702 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:16786289}. Note=May be part of the endoplasmic reticulum. UNIPROT Q8VXU6 UNIPROT Q9M7Y2 Pfam PF14571 Pfam PF05605 GO:0048471 Unknown UniProt Sequence Analysis MDSNWINCPSVFSSSSSSSRRCQSRSDLYLGGGYEDLEGEDDLKAEFICPFCAEDFDIVGLCCHIDEEHPVEAKNGVCPVCTKRVGLDIVGHITTQHANFFKVQRRRRLRRGGYSSTYLALKKELREANLQSLLGGSSSFTSSTNIDSDPLLSSFMFNSPSVNQSANKSATPVTVGNAATKVSIKESLKRDIQEAPLSGEDQEKAKKSEFVRGLLLSTMLEDDF 224 Q9UPY3 Endoribonuclease DICER1 9606 None SL-0198 Cytoplasm {ECO:0000269|PubMed:16424907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19022417}. UNIPROT Q9UPY3 UNIPROT A7E2D3 UNIPROT B3KRG4 UNIPROT E0AD28 UNIPROT O95943 UNIPROT Q9UQ02 PDB 2EB1 PDB 4NGB PDB 4NGC PDB 4NGD PDB 4NGF PDB 4NGG PDB 4NH3 PDB 4NH5 PDB 4NH6 PDB 4NHA PDB 4WYQ PDB 5ZAK PDB 5ZAL PDB 5ZAM Pfam PF00271 Pfam PF02170 Pfam PF04851 Pfam PF00636 PROSITE PS51327 PROSITE PS50137 PROSITE PS51192 PROSITE PS51194 PROSITE PS50821 PROSITE PS00517 PROSITE PS50142 OMIM 138800 OMIM 180295 OMIM 601200 OMIM 606241 OMIM 618272 DisGeNET 23405 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}. 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}. A0A142I5B9 EBI-20625330 0.35 K9N7C7 EBI-27129420 0.35 O15027 EBI-20621391 0.35 O15234 EBI-20621391 0.35 O75569 EBI-8031519 0.74 P0C6X1 EBI-27129362 0.35 P0C6X4 EBI-27128759 0.35 P0C6X5 EBI-27128956 0.35 P0C6X6 EBI-27128688 0.35 P19525 EBI-6116026 0.50 P27958 EBI-9392140 0.40 P35658 EBI-20621391 0.35 P49790 EBI-20621330 0.50 P52948 EBI-20621391 0.35 P55735 EBI-20621391 0.35 Q06787 EBI-20621391 0.35 Q14974 EBI-20621330 0.35 Q15633 EBI-8031567 0.96 Q61496 EBI-15569634 0.54 Q8TB72 EBI-20621391 0.35 Q92900 EBI-20621391 0.35 Q99523 EBI-11154667 0.35 Q99567 EBI-20621391 0.35 Q9H6S0 EBI-20621391 0.35 Q9NZI8 EBI-20621391 0.35 Q9NWA0 EBI-394834 0.35 Q9NX70 EBI-394875 0.35 Q96J94 EBI-527373 0.50 Q9UKV8 EBI-527585 0.94 Q7Z3Z4 EBI-528620 0.37 Q9UL18 EBI-528294 0.72 Q8CJG0 EBI-528561 0.52 P02768 EBI-1222961 0.35 Q70CQ1 EBI-2512828 0.40 P0C205 EBI-8332957 0.61 O43741 EBI-3937984 0.37 Q96C10 EBI-6115711 0.50 Q13618 EBI-21329068 0.35 Q96DB2 EBI-6598272 0.46 Q9UHI6 EBI-6598911 0.35 P57678 EBI-6598937 0.35 P55265 EBI-6913036 0.65 Q14686 EBI-8756175 0.44 P16150 EBI-10049049 0.35 Q9UI95 EBI-11059438 0.35 Q9H9G7 EBI-11090247 0.35 Q9Y5L4 EBI-11125620 0.35 Q96EQ0 EBI-11152414 0.35 Q14103 EBI-11152836 0.35 O60506 EBI-11153302 0.53 P22415 EBI-11158458 0.35 Q9H9F9 EBI-11160007 0.35 P61224 EBI-11160765 0.35 Q96LK0 EBI-11376319 0.27 Q9Y6A4 EBI-12449464 0.51 C5E524 EBI-12584280 0.35 Q8IWL3 EBI-13943458 0.35 A2AM67 EBI-15101712 0.35 Q6IQ23 EBI-16398399 0.35 Q9H0B3 EBI-21526575 0.35 P13727 EBI-21570605 0.35 Q8N490 EBI-21596986 0.35 Q8IZ69 EBI-21636338 0.35 Q8WV44 EBI-21636495 0.35 O14965 EBI-21639587 0.53 O75173 EBI-21640424 0.35 P61313 EBI-21697528 0.35 Q3SYB3 EBI-21720692 0.35 Q8N4T0 EBI-21731449 0.35 Q96SI9 EBI-21752787 0.35 Q8N1E6 EBI-21820146 0.35 Q92945 EBI-15781931 0.40 O14980 EBI-15819105 0.35 P04156 EBI-15979960 0.35 P24928 EBI-16106916 0.50 P35637 EBI-20621391 0.35 P23396 EBI-20621391 0.35 P62917 EBI-20621391 0.35 P62701 EBI-20621391 0.35 P61247 EBI-20621391 0.35 P15880 EBI-20621391 0.35 P12236 EBI-20621391 0.35 P05141 EBI-20621391 0.35 P07910 EBI-20621391 0.35 P22626 EBI-20621391 0.35 Q15365 EBI-20621391 0.35 Q8IU99 EBI-20621391 0.35 P09651 EBI-20621391 0.35 P38159 EBI-20621391 0.35 Q9UN86 EBI-20621391 0.35 P10809 EBI-20621391 0.35 Q96I24 EBI-20621391 0.35 Q9Y5A9 EBI-20621391 0.35 O00425 EBI-20621391 0.35 Q7Z739 EBI-20621391 0.35 Q9Y6M1 EBI-20621391 0.35 Q4G0J3 EBI-20621391 0.35 Q96AE4 EBI-20621391 0.35 Q01844 EBI-20621391 0.35 P17844 EBI-20621391 0.35 Q96PK6 EBI-20621391 0.35 P51114 EBI-20621391 0.35 P11940 EBI-20621391 0.35 Q13310 EBI-20621391 0.35 P11142 EBI-20621391 0.35 O43390 EBI-20621391 0.35 Q92841 EBI-20621391 0.35 P38646 EBI-20621391 0.35 P51116 EBI-20621391 0.35 O75746 EBI-20621391 0.35 P23246 EBI-20621391 0.35 P52272 EBI-20621391 0.35 Q14444 EBI-20621391 0.35 Q92499 EBI-20621391 0.35 Q00839 EBI-20621391 0.35 O43143 EBI-20621391 0.35 P43243 EBI-20621391 0.35 Q9Y2W1 EBI-20621391 0.35 Q8WWM7 EBI-20621391 0.35 Q14157 EBI-20621391 0.35 Q5T6F2 EBI-20621391 0.35 Q99700 EBI-20621391 0.35 Q9NZB2 EBI-20621391 0.35 Q14671 EBI-20621391 0.35 Q7L2E3 EBI-20621391 0.35 Q08211 EBI-20621391 0.35 Q6Y7W6 EBI-20621391 0.35 Q6P158 EBI-20621391 0.35 Q9BY12 EBI-20621391 0.35 Q04637 EBI-20621391 0.35 Q9UPQ9 EBI-20621391 0.35 P48634 EBI-20621391 0.35 Q15077 EBI-21262943 0.35 Q9NQB0 EBI-21265942 0.35 O43508 EBI-21195246 0.54 P03372 EBI-21301141 0.35 A0A0H3LBU6 EBI-25402078 0.35 P59633 EBI-25688366 0.35 Q9IK90 EBI-25747350 0.50 K9N4V0 EBI-26375098 0.35 P98179 EBI-26967387 0.35 Q96T52 EBI-27050444 0.35 P35226 EBI-27108918 0.35 P53350 EBI-28938281 0.35 GO:0005737 GO:0005829 GO:0070062 GO:0005634 GO:0048471 GO:0016442 GO:0070578 GO:0005524 GO:0004530 GO:0003677 GO:0003725 GO:0004521 GO:0004386 GO:0046872 GO:0070883 GO:0019904 GO:0004525 GO:0003723 GO:0035197 GO:0006309 GO:0098795 GO:0010586 GO:0035196 GO:0010629 GO:0010626 GO:0000122 GO:0032720 GO:0021675 GO:0048812 GO:0038061 GO:0032290 GO:0031643 GO:0014040 GO:0031054 GO:0070922 GO:0090501 GO:0090502 GO:0030422 GO:0016078 Unknown UniProt Sequence Analysis MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWNQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYTSQPCEIVVDCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFVTPKVIKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDIDPVMDDDDVFPPYVLRPDDGGPRVTINTAIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETVKYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRDSYPRPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFMLSLQMLELITRLHQYIFSHILRLEKPALEFKPTDADSAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPNLDFGWKKSIDSKSFISISNSSSAENDNYCKHSTIVPENAAHQGANRTSSLENHDQMSVNCRTLLSESPGKLHVEVSADLTAINGLSYNQNLANGSYDLANRDFCQGNQLNYYKQEIPVQPTTSYSIQNLYSYENQPQPSDECTLLSNKYLDGNANKSTSDGSPVMAVMPGTTDTIQVLKGRMDSEQSPSIGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNTDKWEKDEMTKDCMLANGKLDEDYEEEDEEEESLMWRAPKEEADYEDDFLEYDQEHIRFIDNMLMGSGAFVKKISLSPFSTTDSAYEWKMPKKSSLGSMPFSSDFEDFDYSSWDAMCYLDPSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTDREKALCPTRENFNSQQKNLSVSCAAASVASSRSSVLKDSEYGCLKIPPRCMFDHPDADKTLNHLISGFENFEKKINYRFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLETVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS 1922 B9U3F2 Protein DISP3 9031 None SL-0178 SL-0182 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}. UNIPROT B9U3F2 UNIPROT F1NH44 Pfam PF02460 PROSITE PS50156 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}. GO:0005737 GO:0030659 GO:0005783 GO:0005789 GO:0016021 GO:0031965 GO:0030154 GO:0042632 GO:0008203 GO:0045665 GO:0045834 GO:2000179 GO:0009725 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDTEDDPLLQDAWLDEEDEEVAFSSRKRREGALLCGKSSCRVRPLRVTLPVSGFWNIVGWIFTNPYCAGFILFLGCAIPAVLAVVMFLHYPALDIDISYNAFEIRNHESSQRFDALALALKSQFGSWGRNRRDLADFTSETLQRLIFEQLQQLHLNASHLQVSTRAKRSAPQGRTSSPEPRAHPHPGNETSRVTRGAPRWDYSNTYISANTQTHAHWRIELIFLARGDSENNIFTTERLVTIHEVERKIMDHPRFREFCWKPHEVLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIQGSLELAMTHPEFYWYVDEGLSAENKKSSLLRSEILFGAPLPNYYSVEDRWEEQRHKFQNFVVTYVAMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAVLVYILTSCSVFLSFFGIASIGLSCLVALFLYHVVFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATHLKDLRLRMIHTIQTAGKATFFTSLTTAAAYAANIFSQIPAVHDFGLFMSLIVSCCWVAVLFTMPAALGIWTLYVSPLESSCQNSCSQKCTKKSTLHLAEDLFVASEGTSRAGRETLPYLDDDIPLLSVEEEPVSLEMGDVPLVSVMPENLQLPVEKSNRGHLIAHLQELLEHWVLWSAVKSRWVIVGLFLLVLLLSIFFASRLRPASRAPVLFRPDTNIQVLLDLKYNLSAEGISCITCSGLFQEKPHSLQNNFRTSLEKKKRGSASPWGSKGSISDTGQQDLQGTVYISKSRSKGRPAIYRFSLNASIPAPWQMVSPGDGEVPSFQVYRVPFGNFTRKLTACVSTVGLLKQTSPRKWMMTTLSCDSKRGWKFDFSFYVAAKEQQRTRKLYFAQSHKPPYHGRVCVAPPGCLLSSSPDGPTKGILYVPSEKAAPKARLSATSGFNPCMNMGCGKPAVRPLVDTGAMVFVVFGIRGVNRTKNSDNHVIGDMGSVIYDDSFDLFKEIGNLCRLCKAIASNTELVKPGGAQCLPSGYSISSFLQMLHPECKNIPEPNLLPGQLSHGAVGVKDGKVQWISMAFESTTYKGKSSFQTYADYLKWETFLQQQLQLFPEGSALRHGFQTCEHWKQIFMEIIGVQSALYGLILSLVICVAAVAVFTTHILLLLPVLLSILGVVCLVVTIMYWSGWEMGAVEAISLSILVGSSVDYCVHLVEGYLLAGENLPLHHAEDPTACRQWRTIEAIRHVGVAIVSSAVTTVIATVPLFFCIIAPFAKFGKIVALNTGVSILYTLTVSTALLSIMGPGTFTRSRTSCLKAVAGVLLAGLLGLCICLALLKGGFKIPLPNGTAL 1338 Q9P2K9 Protein DISP3 9606 None SL-0178 SL-0182 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}. UNIPROT Q9P2K9 UNIPROT Q5VTU9 UNIPROT Q9UJD6 Pfam PF02460 PROSITE PS50156 OMIM 611251 DisGeNET 57540 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}. Q99417 EBI-735190 0.00 Q7LDG7 EBI-735584 0.00 P00918 EBI-736439 0.00 P49286 EBI-11576414 0.37 P62263 EBI-20908096 0.40 Q9NR30 EBI-20930416 0.40 GO:0005737 GO:0030659 GO:0005783 GO:0005789 GO:0016021 GO:0031965 GO:0030154 GO:0042632 GO:0008203 GO:0045665 GO:0045834 GO:2000179 GO:0032368 GO:0007224 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDTEDDPLLQDVWLEEEQEEEEATGETFLGAQKPGPQPGAGGQCCWRHWPLASRPPASGFWSTLGWAFTNPCCAGLVLFLGCSIPMALSAFMFLYYPPLDIDISYNAFEIRNHEASQRFDALTLALKSQFGSWGRNRRDLADFTSETLQRLISEQLQQLHLGNRSRQASRAPRVIPAASLGGPGPYRDTSAAQKPTANRSGRLRRETPPLEDLAANQSEDPRNQRLSKNGRYQPSIPPHAAVAANQSRARRGASRWDYSRAYVSANTQTHAHWRIELIFLARGDAERNIFTSERLVTIHEIERKIMDHPGFREFCWKPHEVLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIRGSLELAMTHPEFYWYVDEGLSADNLKSSLLRSEILFGAPLPNYYSVDDRWEEQRAKFQSFVVTYVAMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSCLVALFLYHVVFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATHLEDPQLRMIHTVQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVSCCWLAVLVTMPAALGLWSLYLAPLESSCQTSCHQNCSRKTSLHFPGDVFAAPEQVGGSPAQGPIPYLDDDIPLLEVEEEPVSLELGDVSLVSVSPEGLQPASNTGSRGHLIVQLQELLHHWVLWSAVKSRWVIVGLFVSILILSLVFASRLRPASRAPLLFRPDTNIQVLLDLKYNLSAEGISCITCSGLFQEKPHSLQNNIRTSLEKKRRGSGVPWASRPEATLQDFPGTVYISKVKSQGHPAVYRLSLNASLPAPWQAVSPGDGEVPSFQVYRAPFGNFTKKLTACMSTVGLLQAASPSRKWMLTTLACDAKRGWKFDFSFYVATKEQQHTRKLYFAQSHKPPFHGRVCMAPPGCLLSSSPDGPTKGFFFVPSEKVPKARLSATFGFNPCVNTGCGKPAVRPLVDTGAMVFVVFGIIGVNRTRQVDNHVIGDPGSVVYDSSFDLFKEIGHLCHLCKAIAANSELVKPGGAQCLPSGYSISSFLQMLHPECKELPEPNLLPGQLSHGAVGVREGRVQWISMAFESTTYKGKSSFQTYSDYLRWESFLQQQLQALPEGSVLRRGFQTCEHWKQIFMEIVGVQSALCGLVLSLLICVAAVAVFTTHILLLLPVLLSILGIVCLVVTIMYWSGWEMGAVEAISLSILVGSSVDYCVHLVEGYLLAGENLPPHQAEDARTQRQWRTLEAVRHVGVAIVSSALTTVIATVPLFFCIIAPFAKFGKIVALNTGVSILYTLTVSTALLGIMAPSSFTRTRTSFLKALGAVLLAGALGLGACLVLLQSGYKIPLPAGASL 1392 A3KFU9 Protein Disp3 10090 None SL-0178 SL-0182 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}. UNIPROT A3KFU9 UNIPROT Q0EEE3 UNIPROT Q69ZL6 UNIPROT Q6GQX3 UNIPROT Q6NS63 Pfam PF02460 PROSITE PS50156 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}. GO:0005737 GO:0030659 GO:0005789 GO:0016021 GO:0031965 GO:0030154 GO:0008203 GO:0045665 GO:0045834 GO:2000179 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDSEDDPLLQDVWLEEEQPEDEACRGIPGPGLQSGAQGCWRRWTLPSRPPTLGFWSTLGWAFTNPCCAGLVLFLGCSIPMVLSAFMFLYYPPLDIDISYNAFEIRNHEASQRFDALALALKSQFGSWGRNRRDLADFTSETLQRLISEQLQQLHLGNHSRPASRAPRSAPRDTVATQTSAANSSERRRREAPSPEGQVTNQSRARRGASRWDYSRTYVSANTQTHAHWRIELIFLARGDAERNIFTSERLVTIHEIERKIMDHPGFREFCWKPHEVLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIRGSLELAMTHPEFYWYVDEGLSVDNLKSSLLRSEILFGAPLPNYYSVDDRWEEQRAKFQSFVVTYVAMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSCLVALFLYHVVFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATHLEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVTCCWLAVLFTMPAALGLWSLYMAPLESSCQNSCHQKCGRKSSLHFPGDLFTAPERAGGGPAQGPLPYLDDDIPLLNVEDEPASLELGDVSLVSVHCEGLQPTPDANSRGQLLAQLQELLHHWVLWAAVKSRWVIVGLFASILILSLVFASRLRPASRAPLLFRPDTNIQVLLDLKYNLSAEGISCITCSGLFQEKPHSLQNNVRTSLEKKKRGSGVSWASRTETTAQESMSTVYISKVKSKGHPAVYRLSLNASLPAPWQAVSPGDGEVPSFQVYRAPFGDFTKKLTACMSTVGLLQAASPSRKWMVTALACDARRGWKFDFSFYVATKEQQHTRKLYFAQSHKPPFHGRLCVAPPGCLLSSSPDGPTKGFFYVPSDKVPKARISATFGFNPCVNTGCGKPAVRPLVDTGAMVFVVFGIIGLNRTQQMDNHVIGDPGSVIYDSSFDLFKEIGHLCRLCKAIAGNSELVKPGGAQCLPSGYSISSFLQMLHPECKELPEPNLLPGQLSHGAVGVKEGRVQWISMAFESTTYKGKSSFQTYSDYLRWESFLRQQLQTFPEGSALHRGFQTCEHWKQIFMEIIGVQSALYGLVLSLLICVAAVAVFTTHVLLLLPVLLSILGIVCLVVTIMYWSGWEMGAVEAISLSILVGSSVDYCVHLVEGYLLAGENLPPQLSQDPSSQRQWRTLEAVRHVGVAIVSSALTTVIATVPLFFCIIAPFAKFGKIVALNTGVSILYTLTVSTALLGIMAPGSFTRTRTSFLKALGAVLLAGALGLGACLVLLRSGYKIPLPSGATL 1347 Q58DR2 DnaJ DNAJB12 9913 None SL-0178 SL-0182 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}. UNIPROT Q58DR2 Pfam PF00226 Pfam PF09320 PROSITE PS00636 PROSITE PS50076 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}. GO:0005783 GO:0005789 GO:0030176 GO:0031965 GO:0030544 GO:0071218 GO:0051085 GO:0036503 GO:0065003 GO:0030433 Transmembrane UniProt Sequence Analysis {ECO:0000255} MESNKDEAERCISIALKAIQSNQPDRALRFLEKAQRLYPTPRVHALIESLNQKPQPAGDQPQPTEATHTTHRKAAGANTASANGEAGGESTKGYTAEQVAAVKRVKQCKDYYEILGVSRGASDEDLKKAYRKLALKFHPDKNHAPGATEAFKAIGTAYAVLSNPEKRKQYDQFGDDKGQAARHGHGHGDFHRGFEADISPEDLFNMFFGGGFPSSNVHVYSNGRMRYTYHQRQDRRENQGDGGLGVFVQLMPILILILVSALSQLMVSSPPYSLSLRPSVGHVHKRVTDHLNVVYYVADTFSQEYTGSSLKMVERNVEDDYIANLRNNCWKEKQQKEGLLYRARYFGDADMYNKAQKDGAPQAVTDCQRL 370 Q9NXW2 DnaJ DNAJB12 9606 None SL-0178 SL-0182 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}. UNIPROT Q9NXW2 UNIPROT B7Z7I3 UNIPROT Q9H6H0 PDB 2CTP Pfam PF00226 Pfam PF09320 PROSITE PS00636 PROSITE PS50076 OMIM 608376 DisGeNET 54788 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}. P04626 EBI-32718334 0.35 P19438 EBI-364378 0.00 P08473 EBI-1389788 0.35 P01106 EBI-3893169 0.35 P0DOE9 EBI-6138583 0.35 O95429 EBI-9393134 0.35 Q96BE0 EBI-9394503 0.35 O43765 EBI-9395484 0.35 Q16659 EBI-12502733 0.35 P57078 EBI-12503575 0.35 P03182 EBI-11721938 0.35 P06792 EBI-11724527 0.35 P03431 EBI-12579142 0.35 Q1K9H5 EBI-12588098 0.35 B4URF7 EBI-12588729 0.35 Q6IQ23 EBI-16398399 0.35 Q13011 EBI-16813992 0.35 P14404 EBI-21026252 0.35 P04233 EBI-21258980 0.35 Q15077 EBI-21262943 0.35 F5H1C8 EBI-21264930 0.35 Q9H1C4 EBI-21266770 0.35 P05067 EBI-21132574 0.35 P49768 EBI-21132675 0.35 P03372 EBI-21301141 0.35 P17813 EBI-22197897 0.35 P51617 EBI-28935882 0.35 Q9UM73 EBI-32717464 0.35 Q5JZY3 EBI-32717780 0.35 P08069 EBI-32718669 0.35 P04629 EBI-32719115 0.35 Q16288 EBI-32719212 0.35 GO:0005783 GO:0005789 GO:0030176 GO:0016020 GO:0031965 GO:0030544 GO:0071218 GO:0051085 GO:0036503 GO:0065003 GO:0030433 Transmembrane UniProt Sequence Analysis {ECO:0000255} MESNKDEAERCISIALKAIQSNQPDRALRFLEKAQRLYPTPRVRALIESLNQKPQTAGDQPPPTDTTHATHRKAGGTDAPSANGEAGGESTKGYTAEQVAAVKRVKQCKDYYEILGVSRGASDEDLKKAYRRLALKFHPDKNHAPGATEAFKAIGTAYAVLSNPEKRKQYDQFGDDKSQAARHGHGHGDFHRGFEADISPEDLFNMFFGGGFPSSNVHVYSNGRMRYTYQQRQDRRDNQGDGGLGVFVQLMPILILILVSALSQLMVSSPPYSLSPRPSVGHIHRRVTDHLGVVYYVGDTFSEEYTGSSLKTVERNVEDDYIANLRNNCWKEKQQKEGLLYRARYFGDTDMYHRAQKMGTPSCSRLSEVQASLHG 375 Q9QYI4 DnaJ Dnajb12 10090 None SL-0178 SL-0182 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}. UNIPROT Q9QYI4 UNIPROT Q8K037 Pfam PF00226 Pfam PF09320 PROSITE PS00636 PROSITE PS50076 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}. P52927 EBI-9986179 0.35 GO:0005783 GO:0005789 GO:0030176 GO:0031965 GO:0030544 GO:0071218 GO:0051085 GO:0036503 GO:0065003 GO:0030433 Transmembrane UniProt Sequence Analysis {ECO:0000255} MESNKDEAERCISIALKAIQSNQPERALRFLEKAQRLYPTPRVSALIESLNQKPQSTGDHPQPTDTTHTTTKKAGGTETPSANGEAGGGESAKGYTSEQVAAVKRVKQCKDYYEILGVSRSASDEDLKKAYRKLALKFHPDKNHAPGATEAFKAIGTAYAVLSNPEKRKQYDQFGDDKSQAARHGHSHGDFHRGFEADISPEDLFNMFFGGGFPSSNVHVYSNGRMRYTYQQRQDRRDNQGDGGLGVFVQLMPILILILVSALSQLMVSSPPYSLSPRPSVGHIHKRVTDHLNVAYYVADTFSEEYTGSSLKTVERNVEDDYIANLRNNCWKEKQQKEGLLYRARYFGDTDMYHRAQKMGTPSCNRLSEVQASLHG 376 Q0IIE8 DnaJ DNAJB14 9913 None SL-0178 SL-0182 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}. UNIPROT Q0IIE8 Pfam PF00226 Pfam PF09320 PROSITE PS00636 PROSITE PS50076 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}. GO:0005783 GO:0005789 GO:0016021 GO:0031965 GO:0030544 GO:0071218 GO:0051085 GO:0065003 GO:0030433 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGGGDQSKPNCTKDSSSGSGESGKGYTKDQVDGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNQQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSNQHQHRHSGHEREEERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGSGQTIKMQTENLGVIYYVNKDFKNEYKGMLLQKVEKSVEEDYVTNIRNNCWKERQQKTDMQYAAKVYHDERLRRKAEALSMDNCKELERLTSIYKGG 379 Q8TBM8 DnaJ DNAJB14 9606 None SL-0178 SL-0182 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}. UNIPROT Q8TBM8 UNIPROT Q6UXN1 UNIPROT Q7Z3P0 UNIPROT Q86TA7 UNIPROT Q86TM0 UNIPROT Q9GZU9 Pfam PF00226 Pfam PF09320 PROSITE PS00636 PROSITE PS50076 OMIM 617487 DisGeNET 79982 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}. P28702 EBI-2689805 0.00 P57078 EBI-12503575 0.35 P06461 EBI-11723785 0.35 P50053 EBI-21871951 0.40 P0DOF2 EBI-25603126 0.35 GO:0005783 GO:0005789 GO:0016021 GO:0016020 GO:0031965 GO:0030544 GO:0071218 GO:0051085 GO:0065003 GO:0030433 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGSGDQSKPNCTKDSTSGSGEGGKGYTKDQVDGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSQQHQHRHSGHEREEERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGTGQTIKMQTENLGVVYYVNKDFKNEYKGMLLQKVEKSVEEDYVTNIRNNCWKERQQKTDMQYAAKVYRDDRLRRKADALSMDNCKELERLTSLYKGG 379 Q149L6 DnaJ Dnajb14 10090 None SL-0178 SL-0182 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}. UNIPROT Q149L6 UNIPROT Q3TU54 UNIPROT Q3UTE5 Pfam PF00226 Pfam PF09320 PROSITE PS00636 PROSITE PS50076 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}. GO:0005783 GO:0005789 GO:0016021 GO:0031965 GO:0030544 GO:0071218 GO:0051085 GO:0065003 GO:0030433 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEGNRDEAEKCVQIAREALSAGNRDKAQRFLQKAEKLYPLPAARALLEIIMKNGSTAGSSTHCRKPPGSSDQSKPSCGKDGTSGAGEGGKVYTKDQVEGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGSEEQACNHQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAAYSHQHQHRHSGHEREEERADGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGSGQTIKMQTENLGVVYYVSKDFKSEYKGTLLQKVEKSVEEDYVTNIRNNCWKERQQKTDMQYAAKVYRDEQLRRKADALSMENCKELERLTSLYKGG 379 Q5R6H3 DnaJ DNAJB14 9601 None SL-0178 SL-0182 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}. UNIPROT Q5R6H3 Pfam PF00226 Pfam PF09320 PROSITE PS00636 PROSITE PS50076 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}. GO:0005783 GO:0005789 GO:0016021 GO:0031965 GO:0051085 GO:0065003 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGSGDQSKPNCTKDSTSGSGEGGKGYTKDQVDGVLSINKCKNCYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSQQHQHRHSGHEREEERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGTGQTIKMQTENLGVVYYVNKDFKNEYKGMLLQKVEKSVEEDYVTNIRNNCWKERQQKTDMQYAAKVYRDDRLRRKADALSMDNCKELERLTSLYKGG 379 Q6RHR6 Ion DMI1 3880 None SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:17173544, ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000269|PubMed:17173544}. UNIPROT Q6RHR6 UNIPROT Q1SKV5 Pfam PF06241 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}. GO:0016021 GO:0031965 GO:0006811 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAKSNEESSNLNVMNKPPLKKTKTLPSLNLRVSVTPPNPNDNNGIGGTSTTKTDFSEQQWNYPSFLGIGSTSRKRRQPPPPPSKPPVNLIPPHPRPLSVNDHNKTTSSLLPQPSSSSITKQQQQHSTSSPIFYLLVICCIILVPYSAYLQYKLAKLKDMKLQLCGQIDFCSRNGKTSIQEEVDDDDNADSRTIALYIVLFTLILPFVLYKYLDYLPQIINFLRRTESNKEDVPLKKRVAYMVDVFFSIYPYAKLLALLCATLFLIAFGGLALYAVTGGSMAEALWHSWTYVADAGNHAETEGTGQRIVSVSISAGGMLIFAMMLGLVSDAISEKVDSLRKGKSEVIERNHVLILGWSDKLGSLLKQLAIANKSVGGGVIVVLAEKEKEEMEMDIAKLEFDFMGTSVICRSGSPLILADLKKVSVSKARAIIVLAADENADQSDARALRVVLSLAGVKEGLRGHVVVEMSDLDNEPLVKLVGGELIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIKRWPELDDLLFKDILISFPDAIPCGVKVAADGGKIVINPDDNYVLRDGDEVLVIAEDDDTYAPGPLPEVRKGYFPRIRDPPKYPEKILFCGWRRDIDDMIMVLEAFLAPGSELWMFNEVPEKERERKLAAGELDVFGLENIKLVHREGNAVIRRHLESLPLETFDSILILADESVEDSVAHSDSRSLATLLLIRDIQSRRLPYRDTKSTSLRLSGFSHNSWIREMQQASDKSIIISEILDSRTRNLVSVSRISDYVLSNELVSMALAMVAEDKQINRVLEELFAEEGNEMCIKPAEFYLFDQEELCFYDIMIRGRTRKEIVIGYRLANQERAIINPSEKSVPRKWSLDDVFVVLASGE 882 Q09013 Myotonin-protein DMPK 9606 None SL-0178 SL-0182 SL-0183 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. UNIPROT Q09013 UNIPROT E5KR08 UNIPROT Q16205 UNIPROT Q6P5Z6 PDB 1WT6 PDB 2VD5 Pfam PF08826 Pfam PF00069 PROSITE PS51285 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 160900 OMIM 605377 DisGeNET 1760 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}. 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}. P54259 EBI-951106 0.00 O14974 EBI-7816696 0.57 P26678 EBI-692834 0.56 O95166 EBI-736628 0.00 Q9NRR5 EBI-950164 0.00 P54253 EBI-25979988 0.67 A0A380PIN1 EBI-2871448 0.00 A0A5P8YAW1 EBI-2871441 0.00 P57678 EBI-3937335 0.37 P20073 EBI-7097427 0.37 Q13526 EBI-7301228 0.37 P46783 EBI-7366739 0.37 Q16637 EBI-7388858 0.37 P04183 EBI-7397010 0.37 P08238 EBI-6422924 0.40 O43364 EBI-21249174 0.37 Q8N488 EBI-27110926 0.35 GO:0005829 GO:0005789 GO:0031307 GO:0031965 GO:0005640 GO:0005886 GO:0033017 GO:0005524 GO:0046872 GO:0017020 GO:0106310 GO:0004674 GO:0006874 GO:0035556 GO:0010657 GO:0006998 GO:0018105 GO:0006468 GO:0014853 GO:0008016 GO:0010830 GO:0014722 GO:0002028 GO:0051823 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP 629 P54265 Myotonin-protein Dmpk 10090 None SL-0178 SL-0182 SL-0183 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. UNIPROT P54265 Pfam PF08826 Pfam PF00069 PROSITE PS51285 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0005829 GO:0005789 GO:0031307 GO:0016020 GO:0031965 GO:0005640 GO:0005886 GO:0033017 GO:0005524 GO:0046872 GO:0017020 GO:0106310 GO:0004674 GO:0006874 GO:0035556 GO:0010657 GO:0006998 GO:0018105 GO:0006468 GO:0014853 GO:0008016 GO:0010830 GO:0014722 GO:0002028 GO:0051823 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSAEVRLRQLQQLVLDPGFLGLEPLLDLLLGVHQELGASHLAQDKYVADFLQWVEPIAARLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVKGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLQPDGMVRSLVAVGTPDYLSPEILQAVGGGPGAGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYAKIVHYREHLSLPLADTVVPEEAQDLIRGLLCPAEIRLGRGGAGDFQKHPFFFGLDWEGLRDSVPPFTPDFEGATDTCNFDVVEDRLTAMVSGGGETLSDMQEDMPLGVRLPFVGYSYCCMAFRDNQVPDPTPMELEALQLPVSDLQGLDLQPPVSPPDQVAEEADLVAVPAPVAEAETTVTLQQLQEALEEEVLTRQSLSRELEAIRTANQNFSSQLQEAEVRNRDLEAHVRQLQERMEMLQAPGAAAITGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARIPRPGLSEARCLLLFAAALAAAATLGCTGLVAYTGGLTPVWCFPGATFAP 631 Q95JF4 DnaJ DNAJA1 9534 None SL-0198 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}. UNIPROT Q95JF4 Pfam PF00226 Pfam PF01556 Pfam PF00684 PROSITE PS00636 PROSITE PS50076 PROSITE PS51188 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}. GO:0005783 GO:0016020 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0001671 GO:0051087 GO:0030544 GO:0046872 GO:0051082 GO:0043066 GO:0043508 GO:0043065 GO:0006457 GO:0070585 GO:0051223 GO:0009408 Lipid-Anchored UniProt By Similarity {ECO:0000250} MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKINFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS 397 P00639 Deoxyribonuclease-1 DNASE1 9913 None SL-0178 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}. UNIPROT P00639 UNIPROT A5PK44 UNIPROT Q8MJ27 PDB 1ATN PDB 1DNK PDB 2A3Z PDB 2A40 PDB 2A41 PDB 2A42 PDB 2D1K PDB 2DNJ PDB 3CJC PDB 3DNI PDB 3W3D PDB 7NXV PDB 7NZM Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. P68133 EBI-8545980 0.44 P68135 EBI-15622376 0.72 P60010 EBI-15635389 0.44 GO:0005576 GO:0005635 GO:0005634 GO:0042588 GO:0003779 GO:0004530 GO:0003677 GO:0006915 GO:0006308 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis MRGTRLMGLLLALAGLLQLGLSLKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTLT 282 Q767J3 Deoxyribonuclease-1 DNASE1 9615 None SL-0178 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}. UNIPROT Q767J3 Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. GO:0005576 GO:0005635 GO:0005634 GO:0042588 GO:0003779 GO:0004530 GO:0003677 GO:0006915 GO:0006308 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis MRGARLMGALLALAGLLQGALALRMAAFNIRTFGETKMSNATLSKYIVQILSRYDVAVVQEVRDSHLTAVGKLLDTLNQDDPNAYHYVVSEPLGRSSYKERYLFLFRPDRVSVLDSYQYDDGCEPCGNDTFSREPAIVRFHSPLTEVKEFAVVPLHAAPLDAVAEIDALYDVYLDVQHKWDLEDIVLMGDFNAGCSYVAASQWSSIRLRTNPAFQWLIPDTADTTSTSTHCAYDRIVVAGSQLQHAVVPESAAPFNFQVAYGLSSQLAQAISDHYPVEVTLKRA 284 Q9YGI5 Deoxyribonuclease-1 DNASE1 9031 None SL-0178 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}. UNIPROT Q9YGI5 Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. GO:0005576 GO:0005635 GO:0042588 GO:0003779 GO:0004530 GO:0006915 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis MARLVLELLAAALLLRVAATLRISAFNIRTFGDSKMSNQTVAGFIVSILVQYDITLVQEVRDADLSSVKKLVSQLNSASSYPYSFLSSIPLGRNSYKEQYVFIYRSDIVSVLESYYYDDGCESCGTDIFSREPFIVKFSSPTTQLDEFVIVPLHAEPSSAPAEINALTDVYTDVINKWETNNIFFMGDFNADCSYVTAEQWPSIRLRSLSSCEWLIPDSADTTVTSTDCAYDRIVACGSALRQAVEYGSATVNNFQETLRIQNKDALAISDHFPVEVTLKAR 282 Q4AEE3 Deoxyribonuclease-1 DNASE1 9796 None SL-0178 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}. UNIPROT Q4AEE3 Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. GO:0005576 GO:0005635 GO:0005634 GO:0042588 GO:0003779 GO:0004530 GO:0003677 GO:0006915 GO:0006308 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis MRGARLTGALLALAGLLQVALSLRIAAFNIRTFGETKMSNDTLSNYIVQILNRYDIALIQEVRDSHLTAVGKLLDRLNQDDPNTYHFVVSEPLGRNNYKERYLFVFRPDQVSLLDSYQYNDGCEPCGNDTFSREPAIVKFSSPFTQVKEFAIVPLHAAPSDALAEIDSLYDVYLDVQQKWDMEDIMLMGDFNAGCSYVTSSQWPSIRLRRNPAFWWLIPDTADTTVKSTHCAYDRIVVAGTLLQEAVVPDSAVPFDFQAAYGLNDQTAEAISDHYPVEVTLM 282 P24855 Deoxyribonuclease-1 DNASE1 9606 None SL-0178 Secreted {ECO:0000269|PubMed:2277032}. Zymogen granule {ECO:0000305}. Nucleus envelope. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. UNIPROT P24855 UNIPROT B4DV35 UNIPROT Q14UU9 UNIPROT Q14UV0 PDB 4AWN Pfam PF03372 PROSITE PS00919 PROSITE PS00918 OMIM 125505 OMIM 152700 DisGeNET 1773 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}. 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}. GO:0070062 GO:0005576 GO:0005635 GO:0005634 GO:0042588 GO:0003779 GO:0004530 GO:0003677 GO:0006915 GO:0006308 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis MRGMKLLGALLALAALLQGAVSLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK 282 P49183 Deoxyribonuclease-1 Dnase1 10090 None SL-0178 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}. UNIPROT P49183 UNIPROT O70532 Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. Q9WVE0 EBI-3870545 0.35 GO:0005576 GO:0005635 GO:0005634 GO:0042588 GO:0003779 GO:0004536 GO:0004530 GO:0003677 GO:0006915 GO:0006308 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis MRYTGLMGTLLTLVNLLQLAGTLRIAAFNIRTFGETKMSNATLSVYFVKILSRYDIAVIQEVRDSHLVAVGKLLDELNRDKPDTYRYVVSEPLGRKSYKEQYLFVYRPDQVSILDSYQYDDGCEPCGNDTFSREPAIVKFFSPYTEVQEFAIVPLHAAPTEAVSEIDALYDVYLDVWQKWGLEDIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTVTSTHCAYDRIVVAGALLQAAVVPNSAVPFDFQAEYGLSNQLAEAISDHYPVEVTLRKI 284 O42446 Deoxyribonuclease-1 dnase1 8127 None SL-0178 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}. UNIPROT O42446 Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. GO:0005576 GO:0005635 GO:0042588 GO:0004530 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis MQTYRSRMHLVCSLGLFLTLLHLSNSLLLGAFNIKSFGDTKASNATLMNIITKIVKRYDVILIQEVRDSDLSATQTLMNYVNKDSPQYKYIVSEPLGASTYKERYLFLYREALVSVVKSYTYDDGPEETGQDTFSREPFVVMFSSKNTAVRDFTLIPQHTSPDLAVRELNALYDVVLDVRARWNTNDIVLLGDFNAGCSYVSGSAWQQIRIFTDKTFHWLITDAADTTVSQTVCPYDRIVVTTDMMRGVVQNSAKVYNYMTDLNLKQDLALAVSDHFPVEVKLS 284 P11936 Deoxyribonuclease-1 DNASE1 9823 None SL-0178 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}. UNIPROT P11936 UNIPROT Q95KK2 Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. GO:0005576 GO:0005635 GO:0005634 GO:0042588 GO:0003779 GO:0004530 GO:0003677 GO:0006915 GO:0006308 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis MRAARLMGALLALAGLLQLALSLRIAAFNIRTFGETKMSNATLSNYIVRILSRYDIALIQEVRDSHLTAVGKLLNELNQDDPNNYHHVVSEPLGRSTYKERYLFVFRPDQVSVLDSYLYDDGCEPCGNDTFNREPSVVKFSSPSTQVKEFAIVPLHAAPSDAAAEIDSLYDVYLNVRQKWDLEDIMLMGDFNAGCSYVTTSHWSSIRLRESPPFQWLIPDTADTTVSSTHCAYDRIVVAGPLLQRAVVPDSAAPFDFQAAFGLSEQTALAISDHYPVEVTLKRA 284 O18998 Deoxyribonuclease-1 DNASE1 9986 None SL-0178 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}. UNIPROT O18998 Pfam PF03372 PROSITE PS00919 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}. GO:0005576 GO:0005635 GO:0042588 GO:0003779 GO:0004530 GO:0006915 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis MRSEMLTALLTLAVLLQVAGSLKIAAFNIRSFGETKMSNATLTSYIVRILQRYDIALIQEVRDSHLTAVGKLLDKLNEKAADTYRFVASEPLGRRTYKERYLFVYRPDQVSVLDSYYYDDGCEPCGTDTFSREPAVVRFSSPSTKVREFAIVPLHSAPEDAVAEIDALYDVYLDVQKKWGLQDVMLMGDFNADYSYVTSSQWSSIRLRTNPAFKWLIPDTADTTATSTNCAYDRIVVAGPLLQDAVVPNSAAPFNFQAAYGLSNQLAQAISDHYPVEVTLA 281 P21704 Deoxyribonuclease-1 Dnase1 10116 None SL-0178 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}. UNIPROT P21704 UNIPROT Q5FVU6 Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. GO:0005576 GO:0005635 GO:0005634 GO:0042588 GO:0003779 GO:0004536 GO:0004530 GO:0003677 GO:0006915 GO:0006308 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis MRYTGLMGILLTLVNLLQLAATLRIAAFNIRTFGDTKMSNATLSSYIVKILSRYDIAVVQEVRDTHLVAVGKLLDELNRDIPDNYRYIISEPLGRKSYKEQYLFVYRPSQVSVLDSYHYDDGCEPCGNDTFSREPAIVKFFSPYTEVREFAIVPLHSAPTEAVSEIDALYDVYLDVRQKWGLEDIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTATSTHCAYDRIVVAGALLQAAVVPSSAVPFDFQAEYRLTNQMAEAISDHYPVEVTLRKT 284 P11937 Deoxyribonuclease-1 DNASE1 9940 None SL-0178 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}. UNIPROT P11937 Pfam PF03372 PROSITE PS00919 PROSITE PS00918 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}. GO:0005576 GO:0005635 GO:0042588 GO:0003779 GO:0004530 GO:0006915 GO:0000737 GO:0002283 GO:0002673 GO:0070948 Unknown UniProt Sequence Analysis LKIAAFNIRTFGETKMSNATLSSYIVRILRRYDIALIEQVRDSHLVAVGKLLDDLNQDDPNSYHYVVSEPLGRNSYKERYLFVFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSSPSTKVKAFAIVPLHSAPSDAVAEINSLYDVYLDVQQKWDLNDIMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVGPSAVPFDFQAAYGLSNEMALAISDHYPVEVTLT 260 Q5FWN8 DnaJ dnajb6 8355 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. UNIPROT Q5FWN8 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. Q6P5F9 EBI-11606853 0.35 GO:0005634 GO:0048471 Unknown UniProt Sequence Analysis MVEYYEVLGVQRNASADDIKKAYRRLALKWHPDKNPDNKDEAERRFKEVAEAYEVLSDSKKRDIYDKYGKEGLTNRGGGSHFDEAPFQFGFTFRSPDDVFRDFFGGRDPFSFDLFADDPFDDFFGRSRHRANRSRPAGGGGGPFLSTFGGFPAFGPSFSPFDSGFSSSFGSFGGHGGHGGFTSFSSSSFGGSEMGNFRSVSTSTKVVNGRRVTTKRIVENGQERVEVEEDGQLKSLTVNGKEQLLRLDNK 250 Q5XGU5 DnaJ dnajb6 8355 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. UNIPROT Q5XGU5 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. GO:0005634 GO:0048471 Unknown UniProt Sequence Analysis MVEYYDVLGVQRNSSPDDIKKAYRRLALKWHPDKNPDNKEEAERRFKEVAEAYEVLSDSKKRDIYDKYGKEGLAGGGGGGGSHYDVPFQFGFTFRSPDDVFREFFGGRDPFSFDLFAEDPFDDFFGRRGHRGNRSRPGGGSFLSTFGGFPAFGPSFSPFDSGFSSSFGSFGGHGGFTSFSSSSFGGSGMGNVRSVSTSTKIVNGRRVTTKRIVENGQERVEVEEDGQLKSLTINGKEQLLRLDNK 245 Q5E954 DnaJ DNAJA1 9913 None SL-0198 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}. UNIPROT Q5E954 UNIPROT Q3SZU2 Pfam PF00226 Pfam PF01556 Pfam PF00684 PROSITE PS00636 PROSITE PS50076 PROSITE PS51188 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}. GO:0005737 GO:0005829 GO:0005783 GO:0016020 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0001671 GO:0051087 GO:0030544 GO:0050750 GO:0046872 GO:0051082 GO:0030521 GO:0030317 GO:0043066 GO:0043508 GO:0043065 GO:0070585 GO:0042026 GO:0051223 GO:0009408 GO:0007283 Lipid-Anchored UniProt By Similarity {ECO:0000250} MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLTVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS 397 Q54ED3 DnaJ dnaja1 44689 None SL-0198 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}. UNIPROT Q54ED3 Pfam PF00226 Pfam PF01556 Pfam PF00684 PROSITE PS00636 PROSITE PS50076 PROSITE PS51188 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}. GO:0005737 GO:0005829 GO:0005783 GO:0016020 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0051087 GO:0030544 GO:0046872 GO:0051082 GO:0042026 GO:0009408 Lipid-Anchored UniProt Sequence Analysis {ECO:0000255} MVKEKEYYERLGVKPDCTEDELKKAYRKMAVKYHPDKNQGPGKDAAEAKFKDISEAYEVLSDPEKRKMYDSYGSEGMKESGFHASSAEDLFSHFFGAGGGGGGFSFGGGGGDDFGGFSFGNMGGMGGMGGMGGGHKKRRKGEDIEHEMNRSLEELYNGKLVKISISRDEVCKTCKGSGSNKPGVTTTCPTCNGSRYVFQKKQVGPGMIQQVQTACHTCHGTGEKIKEEDKCKECKGKRVIQGKKIVQFQVEKGTRDGERIMLQGQGSEYPGVPPGDVIITIREKPNVNFKRNGDNLIYTKRLKLLDSIAGSQFIINTLDQRKLWVNHEKGDIIKQGDMRYIENEGMPIKGTSRKGKLIIAFDIEYPSNLTNDDIEKLSKILPKAATPSVSKSDCKSVGLSKVNFNTNEQSSHGGAGGAYQQHGGAYGHQKQQQQGFNPADFGAQFGGGGPQQAQQCQQQ 459 P31689 DnaJ DNAJA1 9606 None SL-0198 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}. UNIPROT P31689 UNIPROT Q5T7Q0 UNIPROT Q86TL9 PDB 2LO1 PDB 2M6Y PDB 6E8M Pfam PF00226 Pfam PF01556 Pfam PF00684 PROSITE PS00636 PROSITE PS50076 PROSITE PS51188 OMIM 602837 DisGeNET 3301 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}. A0A142I5B9 EBI-20625330 0.35 O43542 EBI-11129266 0.35 O95831 EBI-16786283 0.27 P00533 EBI-702075 0.35 P04626 EBI-8770853 0.53 P05129 EBI-25379555 0.35 P0DTD1 EBI-25509375 0.35 Q9Y333 EBI-348751 0.00 Q13233 EBI-361839 0.00 Q99759 EBI-362154 0.00 Q00653 EBI-362743 0.00 Q99558 EBI-362977 0.00 Q04206 EBI-363259 0.00 Q13546 EBI-363616 0.00 Q9Y572 EBI-363772 0.00 Q15750 EBI-363982 0.00 Q9NYJ8 EBI-364051 0.00 O43318 EBI-364144 0.00 P19438 EBI-364369 0.00 P20333 EBI-364603 0.00 Q15628 EBI-364837 0.00 Q13077 EBI-364942 0.00 Q12933 EBI-365035 0.00 Q9Y4K3 EBI-365134 0.00 A0JLT2 EBI-394580 0.35 Q9NX70 EBI-394875 0.35 Q8IXH7 EBI-733541 0.00 P49703 EBI-733840 0.00 P19256 EBI-734132 0.00 P30408 EBI-736034 0.00 Q9UM11 EBI-736796 0.00 Q9NPF4 EBI-1062592 0.00 O75365 EBI-1068254 0.00 O00422 EBI-1076324 0.00 P31930 EBI-1078266 0.00 Q9Y2Q3 EBI-1081237 0.00 Q92956 EBI-1082988 0.00 P01889 EBI-1083927 0.00 P13569 EBI-1171566 0.64 Q9H9G7 EBI-2267899 0.35 Q9HCK5 EBI-2269711 0.35 P99024 EBI-2555184 0.40 P05213 EBI-2558640 0.40 Q9Z1B5 EBI-2560653 0.40 P83887 EBI-2561869 0.40 P68372 EBI-2562208 0.40 Q13573 EBI-7950968 0.35 Q99459 EBI-7954144 0.35 Q9H492 EBI-3044058 0.35 P60520 EBI-3046676 0.35 O95166 EBI-3050465 0.35 P15822 EBI-3930535 0.37 Q13042 EBI-3930976 0.37 Q15051 EBI-4286917 0.35 P07900 EBI-4310841 0.35 Q9Y276 EBI-7104167 0.37 P51636 EBI-7110722 0.37 P35914 EBI-7174982 0.37 O95989 EBI-7273627 0.37 Q9GZX7 EBI-7553697 0.50 P0DOE9 EBI-6138583 0.35 Q8JPQ9 EBI-6159460 0.35 Q77M19 EBI-6270503 0.35 Q13616 EBI-21323857 0.35 Q92905 EBI-21325777 0.35 Q13617 EBI-21327106 0.35 Q13620 EBI-21327757 0.35 Q13618 EBI-21329068 0.35 Q93034 EBI-21331078 0.35 Q92769 EBI-6597828 0.35 Q9UBN7 EBI-6597993 0.53 Q969S8 EBI-6598258 0.35 Q96DB2 EBI-6598272 0.35 Q7Z6J6 EBI-6911571 0.35 Q15334 EBI-6911667 0.35 P35240 EBI-6911783 0.35 P21860 EBI-8770321 0.35 P34969 EBI-9027817 0.35 Q8WW22 EBI-9393722 0.35 Q96BE0 EBI-9394503 0.35 Q9Y266 EBI-9395024 0.35 Q5S007 EBI-9515510 0.53 Q16659 EBI-12502733 0.35 P57078 EBI-12503575 0.35 Q13043 EBI-10049645 0.35 P03372 EBI-9996267 0.35 Q6ZMQ8 EBI-10101253 0.35 P10398 EBI-10101587 0.35 Q13418 EBI-10103376 0.35 P51617 EBI-10103481 0.53 P53671 EBI-10103591 0.35 P04049 EBI-10104226 0.35 Q96FW1 EBI-10770028 0.35 P03179 EBI-11721697 0.35 P03220 EBI-11722152 0.35 P03225 EBI-11722220 0.35 P06463 EBI-11724048 0.35 P0CK49 EBI-11725356 0.35 P0CK56 EBI-11725466 0.35 P0CK58 EBI-11732874 0.35 P30119 EBI-11733103 0.35 P69901 EBI-11733364 0.35 Q2MG95 EBI-11733653 0.35 Q69117 EBI-11733954 0.35 P05214 EBI-10992821 0.35 P35550 EBI-11044604 0.35 Q9BQE3 EBI-11139064 0.35 O75665 EBI-11365691 0.27 Q15468 EBI-11383475 0.27 Q92834 EBI-11394826 0.27 Q9C0F1 EBI-11397104 0.27 Q9NXB0 EBI-11397893 0.27 Q14CZ7 EBI-11426979 0.35 Q9WMX2 EBI-11513409 0.35 Q13509 EBI-11897134 0.35 Q71U36 EBI-11897791 0.57 P56945 EBI-15099384 0.35 O14829 EBI-14024386 0.35 Q9Y2T4 EBI-14027932 0.42 Q8IVT5 EBI-14035664 0.35 Q6IQ23 EBI-16398399 0.35 Q05322 EBI-15481401 0.35 Q9BXB4 EBI-21817602 0.35 Q96SU4 EBI-21817602 0.35 Q14249 EBI-21817602 0.35 O95714 EBI-21817602 0.35 P54645 EBI-16361875 0.35 P80386 EBI-16362252 0.35 Q14684 EBI-16686997 0.35 Q6ZNJ1 EBI-16749633 0.35 Q9H9B4 EBI-16799442 0.27 P09622 EBI-20304669 0.35 O00429 EBI-20305770 0.35 P08559 EBI-20306509 0.35 Q86U44 EBI-20594935 0.35 Q9HCE5 EBI-20595531 0.35 P10636 EBI-20799058 0.35 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 Q9Y251 EBI-21260107 0.35 Q9HC29 EBI-21262102 0.35 Q15077 EBI-21262943 0.35 P03427 EBI-21268420 0.35 P05067 EBI-21132308 0.35 P49768 EBI-21132675 0.35 P42858 EBI-21132926 0.67 Q16526 EBI-21981854 0.35 O15524 EBI-25373793 0.35 Q13163 EBI-25374437 0.35 Q13164 EBI-25374538 0.35 P41240 EBI-25376544 0.35 P46734 EBI-25377403 0.35 Q02156 EBI-25378052 0.35 P19419 EBI-25378580 0.35 Q13153 EBI-25379067 0.35 Q05513 EBI-25380056 0.35 P41743 EBI-25380638 0.35 P30530 EBI-25383128 0.35 Q13882 EBI-25385709 0.35 P15498 EBI-25385501 0.35 P36507 EBI-25391779 0.35 Q9H1R3 EBI-25392649 0.35 P61586 EBI-25394264 0.35 P06239 EBI-25394571 0.35 P0DOF2 EBI-25603126 0.35 P83110 EBI-25471693 0.35 P69479 EBI-25568051 0.35 P0DTC3 EBI-25510118 0.35 P0DTD8 EBI-25510237 0.35 P0DTC8 EBI-25510273 0.35 Q96CS3 EBI-25770166 0.35 O60260 EBI-25879547 0.56 Q6PB30 EBI-26354359 0.35 Q9Y5P2 EBI-26354638 0.35 P52298 EBI-26399642 0.35 Q8TB24 EBI-26518569 0.35 P48431 EBI-26574478 0.35 O60303 EBI-26582514 0.35 Q9NRI5 EBI-26610886 0.35 A0A0H3NJM6 EBI-27055978 0.27 A0A0H3NB75 EBI-27055983 0.27 P35226 EBI-27109494 0.35 P22612 EBI-28934688 0.35 Q8NCK7 EBI-27103180 0.35 A4FU01 EBI-27113520 0.35 A6NLX3 EBI-28997370 0.35 Q9BXK1 EBI-29019783 0.35 P04637 EBI-29628346 0.35 P11362 EBI-32718427 0.42 P08069 EBI-32718669 0.35 P06213 EBI-32718777 0.35 P04629 EBI-32719115 0.42 Q16288 EBI-32719212 0.35 Q01974 EBI-32719482 0.35 Q06418 EBI-32719716 0.35 P35916 EBI-32722728 0.27 GO:0005737 GO:0098554 GO:0005829 GO:0070062 GO:0016020 GO:0015630 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0001671 GO:0055131 GO:0051087 GO:0001664 GO:0030544 GO:0050750 GO:0046872 GO:0030957 GO:0031625 GO:0051082 GO:0030521 GO:0030317 GO:0043066 GO:1903748 GO:0043508 GO:1905259 GO:0031397 GO:0043065 GO:0006457 GO:0070585 GO:0042026 GO:0051223 GO:0009408 GO:0006986 GO:0007283 GO:1901998 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:14752510,} MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS 397 P63037 DnaJ Dnaja1 10090 None SL-0198 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}. UNIPROT P63037 UNIPROT P54102 Pfam PF00226 Pfam PF01556 Pfam PF00684 PROSITE PS00636 PROSITE PS50076 PROSITE PS51188 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}. P03332 EBI-8484283 0.37 P20263 EBI-3043810 0.35 Q8BP00 EBI-4283417 0.35 Q8CG73 EBI-4284701 0.35 O55222 EBI-6914965 0.35 Q80Z64 EBI-8820601 0.35 P52927 EBI-9986179 0.35 Q15637 EBI-11298350 0.00 O54957 EBI-12602113 0.35 A0A0F6AZL3 EBI-13950507 0.35 P00441 EBI-15753536 0.35 Q61584 EBI-16729686 0.35 Q9EP53 EBI-16734894 0.35 Q9EPK7 EBI-17171503 0.35 Q83B01 EBI-21287663 0.49 GO:0005737 GO:0005829 GO:0005783 GO:0016020 GO:0015630 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0001671 GO:0055131 GO:0051087 GO:0001664 GO:0030544 GO:0050750 GO:0046872 GO:0030957 GO:0031625 GO:0051082 GO:0030521 GO:0030317 GO:0043066 GO:1903748 GO:0043508 GO:1905259 GO:0031397 GO:0043065 GO:0070585 GO:0042026 GO:0051223 GO:0009408 GO:0007283 GO:1901998 Lipid-Anchored UniProt By Similarity {ECO:0000250} MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLADSKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS 397 Q5NVI9 DnaJ DNAJA1 9601 None SL-0198 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}. UNIPROT Q5NVI9 Pfam PF00226 Pfam PF01556 Pfam PF00684 PROSITE PS00636 PROSITE PS50076 PROSITE PS51188 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}. GO:0005783 GO:0016020 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0001671 GO:0051087 GO:0030544 GO:0046872 GO:0051082 GO:0043066 GO:0043508 GO:0043065 GO:0006457 GO:0070585 GO:0051223 GO:0009408 Lipid-Anchored UniProt By Similarity {ECO:0000250} MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS 396 P63036 DnaJ Dnaja1 10116 None SL-0198 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. UNIPROT P63036 UNIPROT P54102 Pfam PF00226 Pfam PF01556 Pfam PF00684 PROSITE PS00636 PROSITE PS50076 PROSITE PS51188 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}. P06536 EBI-1187343 0.35 P54645 EBI-16399805 0.35 GO:0005737 GO:0005829 GO:0005783 GO:0016020 GO:0015630 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0001671 GO:0055131 GO:0051087 GO:0001664 GO:0030544 GO:0050750 GO:0046872 GO:0030957 GO:0031625 GO:0051082 GO:0030521 GO:0030317 GO:0043066 GO:1903748 GO:0043508 GO:1905259 GO:0031397 GO:0043065 GO:0070585 GO:0042026 GO:0051223 GO:0009408 GO:0007283 GO:1901998 Lipid-Anchored UniProt By Similarity {ECO:0000250} MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLADSKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS 397 Q0III6 DnaJ DNAJB6 9913 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}. UNIPROT Q0III6 UNIPROT Q8WN90 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. GO:0005737 GO:0005634 GO:0048471 GO:0030018 GO:0051087 GO:0044183 GO:0051082 GO:0061077 Unknown UniProt Sequence Analysis MVDYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDRYGKEGLNGGGGGGSHFDSPFEFGFTFRNPEDVFREFFGGRDPFSFDFFEDPFEDFFGHRRGPRGSRSRGTGSFFSTFSGFPSFGGAFPSFDAGFSSFGSLGHGGLTAFSSSSAFGGSGMGNYKSISTSTKVVNGRKITTKRIVENGQERVEVEEDGQLKSLTINGKEQLLRLDNK 242 Q5F3Z5 DnaJ DNAJB6 9031 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}. UNIPROT Q5F3Z5 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. GO:0005737 GO:0005634 GO:0048471 GO:0030018 GO:0051087 GO:0044183 GO:0051082 GO:0061077 Unknown UniProt Sequence Analysis MVDYYEVLGVQKHASAEDIKKAYRKLALKWHPDKNPENKEEAEQQFKQVAEAYEVLSDAKKRDIYDRFGKEGLINGGGGGSHHDNPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGGRRGPRGSRSRAGGSFLSAFGGFPAFGNAFPSFDTGFTSFGSLGHGGLTSFSSTSFGGSGMGNFKSVSTSTKIVNGRKITTKRIVENGQERVEVEEDGQLRSLTINGEANEEAFAEECRRRGQHALPFQPTNTRLLKPHKPASSPRYAYHYNSDEVEEQEKSRVASSLETPFYLSGYKEGSKRRKQKQREEQKKKKSTKGSY 326 O75190 DnaJ DNAJB6 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:10954706}. Nucleus {ECO:0000269|PubMed:10954706}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22366786}. UNIPROT O75190 UNIPROT A4D232 UNIPROT A8K7D8 UNIPROT A8KAG0 UNIPROT B4DN73 UNIPROT E9PCZ2 UNIPROT O95806 UNIPROT Q53EN8 UNIPROT Q59EF2 UNIPROT Q6FIC8 UNIPROT Q75MA2 UNIPROT Q9UIK6 PDB 6U3R PDB 6U3S PDB 7JSQ PDB 7QBY Pfam PF00226 PROSITE PS00636 PROSITE PS50076 OMIM 603511 OMIM 611332 DisGeNET 10049 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}. 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}. Q9Y5J5 EBI-1073616 0.00 Q15714 EBI-1082393 0.00 P01241 EBI-1084628 0.00 Q9HCU9 EBI-1199948 0.51 P01106 EBI-1237540 0.35 P05783 EBI-1255173 0.62 P05787 EBI-1255584 0.40 P11142 EBI-1255642 0.48 Q8AZK7 EBI-9632715 0.53 P42336 EBI-2116670 0.00 Q8IY92 EBI-2371263 0.35 P0DPB6 EBI-3941479 0.37 O75923 EBI-5357236 0.45 Q13326 EBI-5357396 0.45 Q9ULH1 EBI-5656165 0.00 Q15327 EBI-5656148 0.00 P58340 EBI-9360287 0.57 O75155 EBI-5656188 0.00 Q15773 EBI-9360330 0.63 Q9UKD2 EBI-5656239 0.00 Q00872 EBI-5656274 0.00 P52179 EBI-5656292 0.00 P36871 EBI-5656311 0.00 O75563 EBI-5656329 0.00 Q7KZ85 EBI-5656346 0.00 Q8WZ42 EBI-5656363 0.00 Q96CW5 EBI-5656400 0.00 Q13617 EBI-21327106 0.35 Q13618 EBI-21329068 0.35 Q96DB2 EBI-6598272 0.35 P04626 EBI-8770853 0.35 Q9Y468 EBI-8833199 0.53 Q13398 EBI-8837070 0.35 Q8K2C9 EBI-9360309 0.40 Q13200 EBI-9360352 0.40 Q9BTE6 EBI-9360374 0.40 Q99933 EBI-9392988 0.35 O95816 EBI-9393030 0.35 O95817 EBI-9393075 0.35 O95429 EBI-9393134 0.35 Q13451 EBI-9393873 0.35 Q96BE0 EBI-9394503 0.35 P31948 EBI-9395526 0.35 Q9UNE7 EBI-9395575 0.35 Q62925 EBI-9971410 0.00 Q13404 EBI-9971410 0.00 P22314 EBI-9971410 0.00 P61088 EBI-9971410 0.00 Q9NWT6 EBI-12502476 0.35 Q16659 EBI-12502733 0.35 P57078 EBI-12503575 0.35 Q6ZWV7 EBI-10997876 0.35 E9Q2H1 EBI-11033563 0.35 Q91YN9 EBI-11052510 0.35 P43243 EBI-11071398 0.35 O55187 EBI-11125708 0.35 P26447 EBI-11158347 0.35 Q5JU00 EBI-11367780 0.27 Q9UPV0 EBI-11379107 0.27 Q6P5F9 EBI-11603310 0.35 Q9BW83 EBI-12453281 0.35 Q71U36 EBI-11897791 0.53 P03452 EBI-12577240 0.35 P03431 EBI-12579142 0.35 P03428 EBI-12579909 0.35 I6T1Z2 EBI-12581764 0.35 Q5EP37 EBI-12582596 0.35 C5E527 EBI-12585514 0.35 Q1K9H5 EBI-12588098 0.35 B4URF7 EBI-12588729 0.35 O75190 EBI-12593128 0.40 Q9BY84 EBI-14027455 0.35 Q8N5I9 EBI-21859350 0.35 P25686 EBI-21859350 0.35 Q6ZNJ1 EBI-16749633 0.35 Q86U44 EBI-20594935 0.35 P10636 EBI-20799058 0.35 Q8TED1 EBI-20902320 0.40 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 P54253 EBI-21132804 0.35 P42858 EBI-25945964 0.56 Q5S007 EBI-22228108 0.40 Q5JSP0 EBI-25409226 0.35 P0DOF2 EBI-25603126 0.35 O95072 EBI-25483697 0.35 Q9IK92 EBI-25747216 0.35 O43572 EBI-26451580 0.35 P15313 EBI-25909736 0.56 O94778 EBI-25909728 0.56 P09525 EBI-25909720 0.56 Q9NP70 EBI-25909712 0.56 P54687 EBI-25909745 0.56 Q8TD91 EBI-25910153 0.56 P06276 EBI-25909753 0.56 Q96QF0 EBI-25910137 0.56 Q96CS2 EBI-25910129 0.56 Q9UII2 EBI-25910121 0.56 Q9Y605 EBI-25910113 0.56 Q86TI2 EBI-25910103 0.56 Q8WTV1 EBI-25910095 0.56 Q8NHS9 EBI-25910087 0.56 Q9BRX9 EBI-25910079 0.56 Q96JB6 EBI-25910069 0.56 Q9BQS8 EBI-25910059 0.56 Q9BRX5 EBI-25910051 0.56 Q9H270 EBI-25910033 0.56 Q96LR2 EBI-25910025 0.56 Q96FW1 EBI-25910017 0.56 Q96EN9 EBI-25910001 0.56 Q9BUL9 EBI-25909993 0.56 Q9BY12 EBI-25909975 0.56 Q9NNX6 EBI-25909967 0.56 Q9H0W9 EBI-25909959 0.56 Q9UBP4 EBI-25909951 0.56 Q9UH77 EBI-25909941 0.56 Q6PID6 EBI-25909933 0.56 Q96H20 EBI-25909925 0.56 Q99871 EBI-25909915 0.56 Q8IXS7 EBI-25909907 0.56 Q9UJX2 EBI-25909897 0.56 Q14457 EBI-25909889 0.56 O75558 EBI-25909881 0.56 O15273 EBI-25909873 0.56 Q99598 EBI-25909865 0.56 Q12888 EBI-25909857 0.56 Q15293 EBI-25909849 0.56 P30154 EBI-25909841 0.56 I6L9F6 EBI-25909833 0.56 Q13123 EBI-25909817 0.56 P80217 EBI-25909809 0.56 H3BUJ7 EBI-25909801 0.56 A0A024RCP2 EBI-25909793 0.56 P53672 EBI-25909785 0.56 P24310 EBI-25909777 0.56 Q13191 EBI-25909769 0.56 Q13887 EBI-25909761 0.56 Q6XD76 EBI-25910145 0.56 Q6ZTN6 EBI-25910219 0.56 Q494V2 EBI-25910227 0.56 Q8NBB4 EBI-25910203 0.56 Q6PJW8 EBI-25910195 0.56 Q8N6F8 EBI-25910187 0.56 Q8NA54 EBI-25910179 0.56 Q6P1L5 EBI-25910169 0.56 Q6P597 EBI-25910161 0.56 Q6NXT2 EBI-25910261 0.56 Q3KNS6 EBI-25910243 0.56 Q7Z6I5 EBI-25910235 0.56 Q8IV33 EBI-25910211 0.56 P48431 EBI-26574478 0.35 O60303 EBI-26582514 0.35 Q9Y224 EBI-26615064 0.35 Q8N488 EBI-27110926 0.35 P35226 EBI-27109494 0.35 P04049 EBI-28931531 0.35 P22612 EBI-28934688 0.35 P80192 EBI-28938802 0.35 Q8IY84 EBI-28942464 0.35 Q8IWB6 EBI-28942423 0.35 Q8NFD2 EBI-28943481 0.35 Q96D53 EBI-28944341 0.35 Q99558 EBI-28944828 0.35 Q9NR20 EBI-28946409 0.35 Q9NSY0 EBI-28946547 0.35 Q9UGI9 EBI-28946731 0.35 Q8NCK7 EBI-27103180 0.35 Q05DH4 EBI-34574576 0.27 GO:0005737 GO:0005829 GO:0016020 GO:0005654 GO:0005634 GO:0048471 GO:0030018 GO:0001671 GO:0051087 GO:0003677 GO:0031072 GO:0042802 GO:0044183 GO:0051082 GO:0030036 GO:0061077 GO:0060710 GO:0060717 GO:0030198 GO:0045109 GO:0043154 GO:0045892 GO:0090084 GO:0006457 GO:0034504 GO:1900034 GO:0032880 GO:0060715 Unknown UniProt Sequence Analysis MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFGSGFSSFDTGFTSFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKMVNGRKITTKRIVENGQERVEVEEDGQLKSLTINGVADDDALAEERMRRGQNALPAQPAGLRPPKPPRPASLLRHAPHCLSEEEGEQDRPRAPGPWDPLASAAGLKEGGKRKKQKQREESKKKKSTKGNH 326 Q4R7Y5 DnaJ DNAJB6 9541 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}. UNIPROT Q4R7Y5 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. GO:0005634 GO:0048471 GO:0030018 Unknown UniProt Sequence Analysis MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFEFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFGSGFSSFDTGFTSFGSLGHGGLTSFSSTSFGGGGMGNFKSISTSTKMVNGRKITTKRIVENGQERVEVEEDGQLKSLTINGKEQLLRLDNK 241 O54946 DnaJ Dnajb6 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}. UNIPROT O54946 UNIPROT Q3TE94 UNIPROT Q3U6L0 UNIPROT Q3UNJ5 UNIPROT Q3UYT7 UNIPROT Q99LA5 UNIPROT Q9QYI9 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. Q8BWG8 EBI-649852 0.37 Q8CG73 EBI-4284701 0.35 Q13686 EBI-13941029 0.37 P0CB42 EBI-13941082 0.40 P56524 EBI-13941106 0.40 Q6P1J9 EBI-20729673 0.35 Q9NRI5 EBI-26612017 0.35 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0030018 GO:0001671 GO:0051087 GO:0003677 GO:0031072 GO:0042802 GO:0044183 GO:0051082 GO:0030036 GO:0061077 GO:0060710 GO:0060717 GO:0030198 GO:0045109 GO:0043154 GO:0045892 GO:0090084 GO:0006457 GO:0034504 GO:0032880 GO:0060715 Unknown UniProt Sequence Analysis MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGIHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGNRSRGAGSFFSTFSGFPSFGSGFPAFDTGFTPFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALAEECQRRGQPTPALAPGPAPAPVRVPSQARPLAPTPAPTPAPTPAPAPAQTPAPSVSTRPQKPPRPAPTAKLGSKSNWEDDEQDRQRVPGNWDAPMTSAGLKEGGKRKKQKQKEDLKKKKSTKGNH 365 Q5R8H0 DnaJ DNAJB6 9601 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}. UNIPROT Q5R8H0 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. GO:0005634 GO:0048471 GO:0030018 Unknown UniProt Sequence Analysis MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFGSGFSSFDTGFTSFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKMVNGRKITTKRIVENGQERVEVGEDGQLKSLTINGVADDDALAEERMRRGQNALPAQPAGLRPPKPPRPASLLRHAPHCLSEEEGEQDRPRAPGPWDPLASAAGLKEGGKRKKQKQREESKKKKSTKGNH 326 Q6AYU3 DnaJ Dnajb6 10116 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}. UNIPROT Q6AYU3 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. Q9EPX0 EBI-12593062 0.27 Q5U2U8 EBI-12593066 0.27 D4A4T0 EBI-12593095 0.27 P63018 EBI-12593099 0.27 GO:0005737 GO:0005634 GO:0048471 GO:0030018 GO:0001671 GO:0051087 GO:0003677 GO:0031072 GO:0044183 GO:0051082 GO:0030036 GO:0061077 GO:0060710 GO:0060717 GO:0030198 GO:0045109 GO:0043154 GO:0045892 GO:0090084 GO:0006457 GO:0034504 GO:0032880 GO:0060715 Unknown UniProt Sequence Analysis MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGSRSRGAGSFFSAFSGFPSFGSGFPAFDTGFTPFGSLGHGGLTSFSSASFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALAEECRRRGQPTPALAPGPAPAPARVPSQARPPTPAPTPAPAQTPAPSVSTRPQKPPRPAPTAKLVSKSNWEDEEQDRQRVPGNCDAPMTSAGLKEGGKRKKQKQKEDSKKKKSTKGNH 357 Q6P642 DnaJ dnajb6 8364 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. UNIPROT Q6P642 Pfam PF00226 PROSITE PS00636 PROSITE PS50076 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}. GO:0005737 GO:0005634 GO:0048471 GO:0051087 GO:0044183 GO:0051082 GO:0061077 Unknown UniProt Sequence Analysis MVEYYDVLGVQRNASPEDIKKAYRKLALKWHPDKNPDNKDEAERRFKEVAEAYEVLSDSKKRDIYDKYGKEGLTGGGGGSHFDNPYEFGFTFRSPDDVFRDFFGGRDPFSFDLFADDPFDDFFGRRGHRANRSRPGGSFLSTFGGFPAFGPTFSPFDSGFSSSFGSFGGHGGFSSFSSSSFGGSGMGNFRSVSTSTKVVNGRRVTTKRIVENGQERIEVEEDGQLKSLTINGKEQLLRLDNK 242 P82539 DnaJ DNAJC1 9615 None SL-0178 SL-0182 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}. UNIPROT P82539 GO:0005789 GO:0016021 GO:0031965 GO:0003677 Unknown UniProt Sequence Analysis WESGDLELFDLVEEVXLNFY 20 Q96KC8 DnaJ DNAJC1 9606 None SL-0178 SL-0182 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}. UNIPROT Q96KC8 UNIPROT B0YIZ8 UNIPROT Q5VX89 UNIPROT Q9H6B8 PDB 2CQQ PDB 2CQR Pfam PF00226 Pfam PF00249 PROSITE PS00636 PROSITE PS50076 PROSITE PS51293 OMIM 611207 DisGeNET 64215 May modulate protein synthesis. {ECO:0000250}. P01112 EBI-27045317 0.27 P03246 EBI-11722343 0.35 P0C6X7 EBI-26377188 0.35 Q5SNT2 EBI-24662993 0.56 P80294 EBI-296562 0.37 P01011 EBI-296913 0.58 O95870 EBI-348775 0.00 Q6NUS6 EBI-11368748 0.27 Q96GX1 EBI-11375285 0.27 Q9P0N5 EBI-11378021 0.27 Q04941 EBI-24673775 0.56 P78329 EBI-24723472 0.56 P27449 EBI-24645899 0.56 Q96FZ5 EBI-25186763 0.56 Q6RW13 EBI-24762587 0.56 O14798 EBI-24762712 0.56 Q13296 EBI-21513670 0.35 Q9UHP7 EBI-21517465 0.35 P58658 EBI-21588759 0.35 Q15884 EBI-21620222 0.35 P15498 EBI-21631629 0.35 Q5QGZ9 EBI-21633112 0.35 P33151 EBI-21650356 0.35 Q8NBR6 EBI-21714170 0.35 Q9NWS8 EBI-21842948 0.35 P31146 EBI-21842948 0.35 P10321 EBI-21842948 0.35 P27824 EBI-16788621 0.27 Q14409 EBI-20900375 0.40 Q15077 EBI-21262943 0.35 Q9H1C4 EBI-21266770 0.35 P03372 EBI-21301141 0.35 P13473 EBI-25873928 0.56 Q9Y371 EBI-25922422 0.56 P01116 EBI-27041844 0.27 P01111 EBI-27042293 0.27 GO:0012505 GO:0005783 GO:0005789 GO:0016021 GO:0016020 GO:0031965 GO:0005886 GO:0001671 GO:0051087 GO:0003677 GO:0045861 GO:0006457 GO:0050708 GO:0006417 Transmembrane UniProt Sequence Analysis {ECO:0000255} MTAPCSQPAQLPGRRQLGLVPFPPPPPRTPLLWLLLLLLAAVAPARGWESGDLELFDLVEEVQLNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDILINGLPDWRQPVFYYRRVRKMSNAELALLLFIILTVGHYAVVWSIYLEKQLDELLSRKKREKKKKTGSKSVDVSKLGASEKNERLLMKPQWHDLLPCKLGIWFCLTLKALPHLIQDAGQFYAKYKETRLKEKEDALTRTELETLQKQKKVKKPKPEFPVYTPLETTYIQSYDHGTSIEEIEEQMDDWLENRNRTQKKQAPEWTEEDLSQLTRSMVKFPGGTPGRWEKIAHELGRSVTDVTTKAKQLKDSVTCSPGMVRLSELKSTVQNSRPIKTATTLPDDMITQREDAEGVAAEEEQEGDSGEQETGATDARPRRRKPARLLEATAKPEPEEKSRAKRQKDFDIAEQNESSDEESLRKERARSAEEPWTQNQQKLLELALQQYPRGSSDRWDKIARCVPSKSKEDCIARYKLLVELVQKKKQAKS 554 Q61712 DnaJ Dnajc1 10090 None SL-0178 SL-0182 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. UNIPROT Q61712 Pfam PF00226 Pfam PF00249 PROSITE PS00636 PROSITE PS50076 PROSITE PS51293 May modulate protein synthesis. {ECO:0000250}. P70168 EBI-15558601 0.44 GO:0012505 GO:0005783 GO:0005788 GO:0005789 GO:0016021 GO:0031965 GO:0005634 GO:0005886 GO:0051087 GO:0003677 GO:0043022 GO:0006457 GO:0050708 GO:0006417 Transmembrane UniProt Sequence Analysis {ECO:0000255} MWVPGFGSARLPQRRRSGLESSSVRPLWLLLLFLLAAVRPVRAWESGDLELFDLVEEVQLNFYEFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDVLINGLPDWRQPVFYYRRVRKMSNAELALLLFIILTVGHYAVVWSIYLEKQLDELLGRKKRERKKKTGSKSVDAAKLGASEKNERLLIKPQWHDLLPCKLGIWFCLTLKALPHLIQDAGQFYAKYKETKLKEKEDALARIEIETLQKQKKVKVKKPKPEFPVYMPLENTYIQSYDHGTSIEEIEEQMDDWLENRKRTQKRQAPEWTEEDLSQLTRSMVKFPGGTPGRWDKIAHELGRSVTDVTTKAKELKDSVTSSPGMTRLSELKSNGQNSRPIKIATALPDDIITQREDSAGAMEDEEHEAAEGEQESATTEARPRRRKSARAAEAVTRVEPEEKLRGKRQKDFDISEQNDSSDEEKQRKERTRAAEEAWTQSQQKLLELALQQYPKGASDRWDKIAKCVPSKSKEDCIARYKLLVELVQKKKQAKS 552 P40318 ERAD-associated SSM4 559292 None SL-0178 SL-0179 SL-0182 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}. UNIPROT P40318 UNIPROT D6VVQ1 PDB 2M6M Pfam PF12906 PROSITE PS51292 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}. P39015 EBI-939185 0.44 Q04121 EBI-7756909 0.37 P47137 EBI-939093 0.44 P40513 EBI-939098 0.44 P06738 EBI-939105 0.44 Q12007 EBI-939110 0.44 P38758 EBI-939115 0.44 P39683 EBI-939120 0.44 P16467 EBI-939125 0.44 P11154 EBI-939130 0.44 P33399 EBI-939135 0.44 P25617 EBI-939140 0.44 P32288 EBI-939145 0.44 P53982 EBI-939150 0.44 P10963 EBI-939155 0.44 P00925 EBI-939160 0.44 P40825 EBI-939165 0.44 P30952 EBI-939170 0.44 Q04697 EBI-939175 0.44 P32835 EBI-939180 0.44 P23542 EBI-939190 0.44 P38998 EBI-939195 0.44 P38720 EBI-939200 0.44 P35202 EBI-939205 0.44 P80210 EBI-939210 0.44 P40217 EBI-939215 0.44 P38009 EBI-939220 0.44 Q04458 EBI-939225 0.44 P40959 EBI-939230 0.44 Q05979 EBI-939235 0.44 P40892 EBI-939240 0.44 P08524 EBI-939245 0.44 P25561 EBI-939250 0.44 P38787 EBI-939255 0.44 P46655 EBI-939260 0.44 P38158 EBI-939265 0.44 P38081 EBI-939270 0.44 Q01454 EBI-939275 0.44 Q08968 EBI-939280 0.44 P41816 EBI-939285 0.44 P46151 EBI-939290 0.44 P54885 EBI-939295 0.44 Q08686 EBI-939300 0.44 Q08444 EBI-939305 0.44 P50278 EBI-939310 0.44 P37254 EBI-939315 0.44 Q10740 EBI-939320 0.44 P50101 EBI-939325 0.44 P00331 EBI-939330 0.44 P16862 EBI-939335 0.44 P46680 EBI-939340 0.44 Q04212 EBI-939345 0.44 P15274 EBI-939350 0.44 P54007 EBI-939355 0.44 Q99260 EBI-939360 0.44 Q04491 EBI-939365 0.44 P31539 EBI-939370 0.44 P10592 EBI-939375 0.44 P41903 EBI-939380 0.44 P38716 EBI-939385 0.44 P17076 EBI-939390 0.44 P53051 EBI-939395 0.44 P53265 EBI-939400 0.44 P53101 EBI-939405 0.44 P53183 EBI-939410 0.44 P10356 EBI-939415 0.44 P21524 EBI-939420 0.44 P25044 EBI-939425 0.44 Q07505 EBI-939430 0.44 P16120 EBI-939435 0.44 P25576 EBI-939440 0.44 P17967 EBI-939445 0.44 P00817 EBI-939450 0.44 Q04228 EBI-982121 0.71 P38428 EBI-982234 0.56 P38911 EBI-982234 0.35 P25694 EBI-982234 0.71 P33296 EBI-1102319 0.40 Q02159 EBI-1102333 0.40 P53044 EBI-1008654 0.46 P12866 EBI-1637277 0.64 P32589 EBI-3807868 0.35 P38360 EBI-15787591 0.40 P53756 EBI-20814404 0.37 GO:0000837 GO:0005783 GO:0030176 GO:0016021 GO:0005635 GO:0005637 GO:0061630 GO:0004842 GO:0008270 GO:0071712 GO:0030970 GO:0030433 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDVDSDVNVSRLRDELHKVANEETDTATFNDDAPSGATCRICRGEATEDNPLFHPCKCRGSIKYMHESCLLEWVASKNIDISKPGADVKCDICHYPIQFKTIYAENMPEKIPFSLLLSKSILTFFEKARLALTIGLAAVLYIIGVPLVWNMFGKLYTMMLDGSSPYPGDFLKSLIYGYDQSATPELTTRAIFYQLLQNHSFTSLQFIMIVILHIALYFQYDMIVREDVFSKMVFHKIGPRLSPKDLKSRLKERFPMMDDRMVEYLAREMRAHDENRQEQGHDRLNMPAAAADNNNNVINPRNDNVPPQDPNDHRNFENLRHVDELDHDEATEEHENNDSDNSLPSGDDSSRILPGSSSDNEEDEEAEGQQQQQQPEEEADYRDHIEPNPIDMWANRRAQNEFDDLIAAQQNAINRPNAPVFIPPPAQNRAGNVDQDEQDFGAAVGVPPAQANPDDQGQGPLVINLKLKLLNVIAYFIIAVVFTAIYLAISYLFPTFIGFGLLKIYFGIFKVILRGLCHLYYLSGAHIAYNGLTKLVPKVDVAMSWISDHLIHDIIYLYNGYTENTMKHSIFIRALPALTTYLTSVSIVCASSNLVSRGYGRENGMSNPTRRLIFQILFALKCTFKVFTLFFIELAGFPILAGVMLDFSLFCPILASNSRMLWVPSICAIWPPFSLFVYWTIGTLYMYWFAKYIGMIRKNIIRPGVLFFIRSPEDPNIKILHDSLIHPMSIQLSRLCLSMFIYAIFIVLGFGFHTRIFFPFMLKSNLLSVPEAYKPTSIISWKFNTILLTLYFTKRILESSSYVKPLLERYWKTIFKLCSRKLRLSSFILGKDTPTERGHIVYRNLFYKYIAAKNAEWSNQELFTKPKTLEQAEELFGQVRDVHAYFVPDGVLMRVPSSDIVSRNYVQTMFVPVTKDDKLLKPLDLERIKERNKRAAGEFGYLDEQNTEYDQYYIVYVPPDFRLRYMTLLGLVWLFASILMLGVTFISQALINFVCSFGFLPVVKLLLGERNKVYVAWKELSDISYSYLNIYYVCVGSVCLSKIAKDILHFTEGQNTLDEHAVDENEVEEVEHDIPERDINNAPVNNINNVEEGQGIFMAIFNSIFDSMLVKYNLMVFIAIMIAVIRTMVSWVVLTDGILACYNYLTIRVFGNSSYTIGNSKWFKYDESLLFVVWIISSMVNFGTGYKSLKLFFRNRNTSKLNFLKTMALELFKQGFLHMVIYVLPIIILSLVFLRDVSTKQIIDISHGSRSFTLSLNESFPTWTRMQDIYFGLLIALESFTFFFQATVLFIQWFKSTVQNVKDEVYTKGRALENLPDES 1319 Q96HP0 Dedicator DOCK6 9606 None SL-0198 Cytoplasm {ECO:0000269|PubMed:17196961}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17196961}. Note=Mainly located near the cell surface. UNIPROT Q96HP0 UNIPROT A6H8X5 UNIPROT Q7Z7P4 UNIPROT Q9P2F2 Pfam PF06920 Pfam PF14429 Pfam PF11878 PROSITE PS51650 PROSITE PS51651 OMIM 614194 OMIM 614219 DisGeNET 57572 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}. 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. O95271 EBI-30838480 0.44 P0DTD1 EBI-26375521 0.35 P10909 EBI-11117520 0.35 Q8IUI8 EBI-8795913 0.35 Q8NF50 EBI-8795967 0.53 Q96II8 EBI-8796001 0.53 Q9H8S9 EBI-8796143 0.42 Q7L9L4 EBI-8796201 0.42 Q96N67 EBI-8797541 0.35 Q6P5D4 EBI-10991106 0.35 E9PUA5 EBI-10999661 0.35 P13533 EBI-11004546 0.35 P26041 EBI-11010611 0.35 Q8BUN5 EBI-11016066 0.35 Q2M1P5 EBI-11100577 0.35 O75792 EBI-11115131 0.35 Q13637 EBI-11116348 0.35 Q14114 EBI-11117560 0.35 Q00765 EBI-11120162 0.35 P70335 EBI-11124658 0.35 P61019 EBI-11127113 0.35 O00400 EBI-11135399 0.35 Q6P5F9 EBI-11603310 0.35 A8K8V0 EBI-21612043 0.35 Q9NQX6 EBI-21675860 0.35 Q14315 EBI-20912382 0.40 Q32P51 EBI-20922858 0.40 O15371 EBI-25408957 0.35 O00232 EBI-25408957 0.35 O75427 EBI-25408957 0.50 Q9Y2L9 EBI-25408957 0.35 Q9Y6G9 EBI-25408957 0.35 P10515 EBI-25408957 0.35 P35226 EBI-27108918 0.35 GO:0005829 GO:0048471 GO:0005085 GO:0043547 GO:0007264 Unknown UniProt Sequence Analysis MAASERRAFAHKINRTVAAEVRKQVSRERSGSPHSSRRCSSSLGVPLTEVVEPLDFEDVLLSRPPDAEPGPLRDLVEFPADDLELLLQPRECRTTEPGIPKDEKLDAQVRAAVEMYIEDWVIVHRRYQYLSAAYSPVTTDTQRERQKGLPRQVFEQDASGDERSGPEDSNDSRRGSGSPEDTPRSSGASSIFDLRNLAADSLLPSLLERAAPEDVDRRNETLRRQHRPPALLTLYPAPDEDEAVERCSRPEPPREHFGQRILVKCLSLKFEIEIEPIFGILALYDVREKKKISENFYFDLNSDSMKGLLRAHGTHPAISTLARSAIFSVTYPSPDIFLVIKLEKVLQQGDISECCEPYMVLKEVDTAKNKEKLEKLRLAAEQFCTRLGRYRMPFAWTAVHLANIVSSAGQLDRDSDSEGERRPAWTDRRRRGPQDRASSGDDACSFSGFRPATLTVTNFFKQEAERLSDEDLFKFLADMRRPSSLLRRLRPVTAQLKIDISPAPENPHFCLSPELLHIKPYPDPRGRPTKEILEFPAREVYAPHTSYRNLLYVYPHSLNFSSRQGSVRNLAVRVQYMTGEDPSQALPVIFGKSSCSEFTREAFTPVVYHNKSPEFYEEFKLHLPACVTENHHLLFTFYHVSCQPRPGTALETPVGFTWIPLLQHGRLRTGPFCLPVSVDQPPPSYSVLTPDVALPGMRWVDGHKGVFSVELTAVSSVHPQDPYLDKFFTLVHVLEEGAFPFRLKDTVLSEGNVEQELRASLAALRLASPEPLVAFSHHVLDKLVRLVIRPPIISGQIVNLGRGAFEAMAHVVSLVHRSLEAAQDARGHCPQLAAYVHYAFRLPGTEPSLPDGAPPVTVQAATLARGSGRPASLYLARSKSISSSNPDLAVAPGSVDDEVSRILASKLLHEELALQWVVSSSAVREAILQHAWFFFQLMVKSMALHLLLGQRLDTPRKLRFPGRFLDDITALVGSVGLEVITRVHKDVELAEHLNASLAFFLSDLLSLVDRGFVFSLVRAHYKQVATRLQSSPNPAALLTLRMEFTRILCSHEHYVTLNLPCCPLSPPASPSPSVSSTTSQSSTFSSQAPDPKVTSMFELSGPFRQQHFLAGLLLTELALALEPEAEGAFLLHKKAISAVHSLLCGHDTDPRYAEATVKARVAELYLPLLSIARDTLPRLHDFAEGPGQRSRLASMLDSDTEGEGDIAGTINPSVAMAIAGGPLAPGSRASISQGPPTASRAGCALSAESSRTLLACVLWVLKNTEPALLQRWATDLTLPQLGRLLDLLYLCLAAFEYKGKKAFERINSLTFKKSLDMKARLEEAILGTIGARQEMVRRSRERSPFGNPENVRWRKSVTHWKQTSDRVDKTKDEMEHEALVEGNLATEASLVVLDTLEIIVQTVMLSEARESVLGAVLKVVLYSLGSAQSALFLQHGLATQRALVSKFPELLFEEDTELCADLCLRLLRHCGSRISTIRTHASASLYLLMRQNFEIGHNFARVKMQVTMSLSSLVGTTQNFSEEHLRRSLKTILTYAEEDMGLRDSTFAEQVQDLMFNLHMILTDTVKMKEHQEDPEMLIDLMYRIARGYQGSPDLRLTWLQNMAGKHAELGNHAEAAQCMVHAAALVAEYLALLEDHRHLPVGCVSFQNISSNVLEESAISDDILSPDEEGFCSGKHFTELGLVGLLEQAAGYFTMGGLYEAVNEVYKNLIPILEAHRDYKKLAAVHGKLQEAFTKIMHQSSGWERVFGTYFRVGFYGAHFGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDDVVEIIKDSNPVDKSKLDSQKAYIQITYVEPYFDTYELKDRVTYFDRNYGLRTFLFCTPFTPDGRAHGELPEQHKRKTLLSTDHAFPYIKTRIRVCHREETVLTPVEVAIEDMQKKTRELAFATEQDPPDAKMLQMVLQGSVGPTVNQGPLEVAQVFLAEIPEDPKLFRHHNKLRLCFKDFCKKCEDALRKNKALIGPDQKEYHRELERNYCRLREALQPLLTQRLPQLMAPTPPGLRNSLNRASFRKADL 2047 Q8VDR9 Dedicator Dock6 10090 None SL-0198 Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Mainly located near the cell surface. {ECO:0000250}. UNIPROT Q8VDR9 UNIPROT E9QKQ0 UNIPROT Q3UM59 UNIPROT Q6PFY0 UNIPROT Q8BJS1 UNIPROT Q9D461 Pfam PF06920 Pfam PF14429 Pfam PF11878 PROSITE PS51650 PROSITE PS51651 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}. GO:0005829 GO:0048471 GO:0005085 GO:0043547 GO:0007264 Unknown UniProt Sequence Analysis MAASERRAFAHKINRTVAAEVRKQVSRERSGSPHSSRRSSSSLGVPLTEVIEPLDFEDVLLSRPPEVEPGPLRDLIEFPVDDLELLKQPRECRTTESGVPEDGQLDAQVRAAVEMYSEDWVIVRRRYQHLSTAYSPITTETQREWQKGLTCQVFEQDTPGDERTGPEDVDDPQHCSGSPEDTPRSSGASGIFSLRNLAADSLLPTLLEQAAPEDVDRRNEALRRQHRAPTLLTLYPAPDEDEAVERCSRPEPPREHFGQRILVKCLSLKFEIEIEPIFGTLALYDVREKKKISENFYFDLNSDSVKGLLRAHGTHPAISTLARSAIFSVTYPSPDIFLVVKLEKVLQQGDISECCEPYMVMKEADTAKNKEKLEKLRLAAEQFCTRLGRYRMPFAWTAVHLANIVSRPQDRDSDSEGERRPTWAERRRRGPQDRGYSGDDACSFSSFRPATLTVTNFFKQEAERLSDEDLFKFLADMRRPSSLLRRLRPVTAQLKLDISPAPENLHFCLSPDLLHVKPYPDPRGRPTKEILEFPAREVYAPHSCYRNLLFVYPHSLNFSSRQGSVRNLAVRIQYMAGEDQSQALPVIFGKSSCSEFTREAFTPVVYHNKSPEFYEEFKLRLPACVTENHHLFFTFYHVSCQPRPGTALETPVGFTWIPLLQHGRLRTGPFCLPVSVDQPPPSYSVLTPDVALPGMRWVDGHKGVFSVELTAVSSVHPQDPHLDKFFTLVHVLEEGIFPFRLKETVLSEGTMEQELRASLAALRLASPEPLVAFSHLVLDKLVRLVVRPPIICGQMVNLGRGAFEAMAHVASLVHRNLEAVQDSRGHCPLLASYVHYAFRLPGGDLSLPGEAPPATVQAATLARGSGRPASLYLARSKSISSSNPDLAVVPGSVDDEVSRILASKGVDRSHSWVNSAYAPGGSKAVLRRVPPYCGADPRQLLHEELALQWVVSGSAVRELVLQHAWFFFQLMVKSMELHLLLGQRLDTPRKLRFPGRFLDDIAALVASVGLEVITRVHKDMKLAERLNASLAFFLSDLLSIADRGYIFSLVRAHYKQVATRLQSAPNPTALLTLRMDFTRILCSHEHYVTLNLPCCPLSPPASPSPSVSSTTSQSSTFSSQAPDPKVTSMFELSGPFRQQHFLSGLLLTELALALDPEAEGASLLHKKAISAVHSLLCSHDVDSRYAEATVKAKVAELYLPLLSLARDTLPQLHGFAEGSGQRSRLASMLDSDTEGEGDIGSTINPSVAMAIAGGPLAPGSRTSISQGPSTAARSGCPLSAESSRTLLVCVLWVLKNAEPTLLQRWAADLALPQLGRLLDLLYLCLAAFEYKGKKAFERINSLTFKKSLDMKARLEEAILGTIGARQEMVRRSRERSPFGNQENVRWRKSATHWRQTSDRVDKTKDEMEHEALVDGNLATEASLVVLDTLETIVQTVMLSEARESILSAVLKVVLYSLGSAQSALFLQHGLATQRALVSKFPELLFEEDTELCADLCLRLLRHCGSRISTIRMHASASLYLLMRQNFEIGHNFARVKMLVTMSLSSLVGTTQNFSEEHLRKSLKTILTYAEEDIGLRDSTFAEQVQDLMFNLHMILTDTVKMKEHQEDPEMLMDLMYRIARGYQGSPDLRLTWLQNMAGKHAELGNHAEAAQCMVHAAALVAEYLALLEDSRHLPVGCVSFQNVSSNVLEESAISDDILSPDEEGFCSGKNFTELGLVGLLEQAAGYFTMGGLYEAVNEVYKNLIPILEAHRDYKKLAAVHGKLQEAFTKIMHQSSGWERVFGTYFRVGFYGTRFGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDDVVEIIKDSNPVDKSKLDPQKAYIQITYVEPHFDTYELKDRVTYFDRNYGLRAFLFCTPFTPDGRAHGELAEQHKRKTLLSTEHAFPYIKTRIRVCHREETVLTPVEVAIEDMQKKTRELAFATEQDPPDAKMLQMVLQGSVGPTVNQGPLEVAQVFLSEIPEDPKLFRHHNKLRLCFKDFCKKCEDALRKNKALIGPDQKEYHRELERHYSRLREALQPLLTQRLPQLLAPSSTSLRSSMNRSSFRKADL 2080 Q99704 Docking DOK1 9606 None SL-0198 [Isoform 1]: Cytoplasm. Nucleus. [Isoform 3]: Cytoplasm, perinuclear region. UNIPROT Q99704 UNIPROT O43204 UNIPROT Q53TY2 UNIPROT Q9UHG6 PDB 2V76 Pfam PF02174 Pfam PF00169 PROSITE PS51064 OMIM 602919 DisGeNET 1796 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}. P00533 EBI-9688841 0.55 P04626 EBI-7878971 0.44 O60880 EBI-7298602 0.46 Q06124 EBI-7380741 0.35 Q9GZQ8 EBI-3045543 0.35 P60520 EBI-3046676 0.35 Q9H0R8 EBI-3048562 0.35 P31016 EBI-7969766 0.44 Q9Q2G4 EBI-6176962 0.50 Q9JIY2 EBI-7645406 0.52 Q9H3Y6 EBI-8541291 0.64 Q7L591 EBI-10694731 0.49 P46109 EBI-10695513 0.49 O43639 EBI-21521290 0.35 Q8IYK4 EBI-21827478 0.35 P51957 EBI-20721387 0.35 Q06884 EBI-22253692 0.35 Q9JJ31 EBI-22253692 0.35 G3V8S2 EBI-22253692 0.35 Q2LC84 EBI-22253796 0.35 F1LRI5 EBI-22253796 0.35 O08776 EBI-22253796 0.35 A0A0G2JV77 EBI-22253796 0.35 F1LMZ8 EBI-22253796 0.35 A0A0G2K064 EBI-22253796 0.35 B5DFA5 EBI-22253796 0.35 P62845 EBI-22253796 0.35 P09875 EBI-22253796 0.35 D3ZZM3 EBI-22253796 0.35 G3V619 EBI-22253796 0.35 GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0007166 GO:0038145 GO:0007265 GO:0007165 GO:0007169 Unknown UniProt Sequence Analysis MDGAVMEGPLFLQSQRFGTKRWRKTWAVLYPASPHGVARLEFFDHKGSSSGGGRGSSRRLDCKVIRLAECVSVAPVTVETPPEPGATAFRLDTAQRSHLLAADAPSSAAWVQTLCRNAFPKGSWTLAPTDNPPKLSALEMLENSLYSPTWEGSQFWVTVQRTEAAERCGLHGSYVLRVEAERLTLLTVGAQSQILEPLLSWPYTLLRRYGRDKVMFSFEAGRRCPSGPGTFTFQTAQGNDIFQAVETAIHRQKAQGKAGQGHDVLRADSHEGEVAEGKLPSPPGPQELLDSPPALYAEPLDSLRIAPCPSQDSLYSDPLDSTSAQAGEGVQRKKPLYWDLYEHAQQQLLKAKLTDPKEDPIYDEPEGLAPVPPQGLYDLPREPKDAWWCQARVKEEGYELPYNPATDDYAVPPPRSTKPLLAPKPQGPAFPEPGTATGSGIKSHNSALYSQVQKSGASGSWDCGLSRVGTDKTGVKSEGST 481 Q9NZJ0 Denticleless DTL 9606 None SL-0178 SL-0182 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. UNIPROT Q9NZJ0 UNIPROT A8K8H8 UNIPROT D3DT98 UNIPROT Q5VT77 UNIPROT Q96SN0 UNIPROT Q9NW03 UNIPROT Q9NW34 UNIPROT Q9NWM5 PDB 6QC0 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 OMIM 610617 DisGeNET 51514 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}. Q3TLR7 EBI-2562304 0.40 Q7L5N1 EBI-2510262 0.56 Q92905 EBI-21325777 0.35 Q13620 EBI-1176116 0.53 Q13619 EBI-1176157 0.53 P61964 EBI-1176605 0.40 Q16531 EBI-1176630 0.56 Q9BQ67 EBI-1176630 0.35 Q3U1J4 EBI-2559059 0.40 O60232 EBI-21543889 0.35 Q99832 EBI-21594461 0.35 P49368 EBI-21594293 0.35 Q8NB37 EBI-21611026 0.35 Q9UHV9 EBI-21645427 0.35 Q6ZN54 EBI-21689078 0.35 Q15170 EBI-21699650 0.35 Q13557 EBI-21719478 0.35 Q8N4J0 EBI-21736494 0.35 Q99627 EBI-21875970 0.35 Q92990 EBI-21884908 0.35 P97784 EBI-21991345 0.40 P40337 EBI-25895784 0.56 GO:0005813 GO:0005694 GO:0080008 GO:0031464 GO:0031465 GO:0005829 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0030674 GO:0006974 GO:0006260 GO:0007095 GO:0010971 GO:0045732 GO:0043161 GO:0006513 GO:0000209 GO:0051726 GO:0009411 GO:0048511 GO:0019985 GO:0006511 Peripheral UniProt Sequence Analysis MLFNSVLRQPQLGVLRNGWSSQYPLQSLLTGYQCSGNDEHTSYGETGVPVPPFGCTFSSAPNMEHVLAVANEEGFVRLYNTESQSFRKKCFKEWMAHWNAVFDLAWVPGELKLVTAAGDQTAKFWDVKAGELIGTCKGHQCSLKSVAFSKFEKAVFCTGGRDGNIMVWDTRCNKKDGFYRQVNQISGAHNTSDKQTPSKPKKKQNSKGLAPSVDFQQSVTVVLFQDENTLVSAGAVDGIIKVWDLRKNYTAYRQEPIASKSFLYPGSSTRKLGYSSLILDSTGSTLFANCTDDNIYMFNMTGLKTSPVAIFNGHQNSTFYVKSSLSPDDQFLVSGSSDEAAYIWKVSTPWQPPTVLLGHSQEVTSVCWCPSDFTKIATCSDDNTLKIWRLNRGLEEKPGGDKLSTVGWASQKKKESRPGLVTVTSSQSTPAKAPRAKCNPSNSSPSSAACAPSCAGDLPLPSNTPTFSIKTSPAKARSPINRRGSVSSVSPKPPSSFKMSIRNWVTRTPSSSPPITPPASETKIMSPRKALIPVSQKSSQAEACSESRNRVKRRLDSSCLESVKQKCVKSCNCVTELDGQVENLHLDLCCLAGNQEDLSKDSLGPTKSSKIEGAGTSISEPPSPISPYASESCGTLPLPLRPCGEGSEMVGKENSSPENKNWLLAMAAKRKAENPSPRSPSSQTPNSRRQSGKKLPSPVTITPSSMRKICTYFHRKSQEDFCGPEHSTEL 730 Q3TLR7 Denticleless Dtl 10090 None SL-0178 SL-0182 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}. UNIPROT Q3TLR7 UNIPROT Q3TTE9 UNIPROT Q6PAN1 UNIPROT Q80WY1 UNIPROT Q80WY2 UNIPROT Q8BW38 UNIPROT Q9CZ76 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. Q13620 EBI-2562304 0.40 P61201 EBI-2562304 0.56 Q9NZJ0 EBI-2562304 0.40 Q9BT78 EBI-2562304 0.56 Q16531 EBI-2562304 0.56 Q13619 EBI-2562304 0.56 Q7L5N1 EBI-2562304 0.40 O15078 EBI-11019947 0.35 Q92905 EBI-11019947 0.35 Q9NP92 EBI-11019947 0.35 Q9BW61 EBI-11019947 0.35 Q9UNS2 EBI-11019947 0.35 P50991 EBI-11019947 0.35 P48643 EBI-11019947 0.35 P12004 EBI-11019947 0.35 Q99832 EBI-11019947 0.35 P17987 EBI-11019947 0.35 Q9UBW8 EBI-11019947 0.35 P50990 EBI-11019947 0.35 O75150 EBI-11019947 0.35 P62877 EBI-11019947 0.35 A1L170 EBI-11019947 0.35 E9PGT6 EBI-11019947 0.35 C9JFE4 EBI-11019947 0.35 Q9C0J8 EBI-11019947 0.35 E7EM64 EBI-11019947 0.35 P49368 EBI-11019947 0.35 P78371 EBI-11019947 0.35 P40227 EBI-11019947 0.35 B4DSW0 EBI-11019947 0.35 Q96EB6 EBI-11019947 0.35 GO:0005813 GO:0005694 GO:0080008 GO:0031464 GO:0031465 GO:0005829 GO:0031965 GO:0005730 GO:0005654 GO:0005634 GO:0030674 GO:0004842 GO:0006974 GO:0006260 GO:0007095 GO:0010971 GO:0045732 GO:0043161 GO:0006513 GO:0000209 GO:0051726 GO:0009411 GO:0048511 GO:0019985 GO:0006511 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q9NZJ0} MLFNSVLRQPQLGVLRNGWSSHYPLQSLLSGYQCNCNDEHTSYGETGVPVPPFGCTFCTAPSMEHILAVANEEGFVRLYNTESQTSKKTCFKEWMAHWNAVFDLAWVPGELKLVTAAGDQTAKFWDVRAGELMGTCKGHQCSLKSVAFPKFQKAVFSTGGRDGNIMIWDTRCNKKDGFYRQVNQISGAHNTADKQTPSKPKKKQNSKGLAPAVDSQQSVTVVLFQDENTLVSAGAVDGIIKVWDLRKNYTAYRQEPIASKSFLYPGTSTRKLGYSSLVLDSTGSTLFANCTDDNIYMFNMTGLKTSPVAVFNGHQNSTFYVKSSLSPDDQFLISGSSDEAAYIWKVSMPWHPPTVLLGHSQEVTSVCWCPSDFTKIATCSDDNTLKIWRLNRGLEEKPGDKHSIVGWTSQKKKEVKACPVTVPSSQSTPAKAPRAKSSPSISSPSSAACTPSCAGDLPLPSSTPTFSVKTTPATTRSSVSRRGSISSVSPKPLSSFKMSLRNWVTRTPSSSPPVTPPASETKISSPRKALIPVSQKSSQADACSESRNRVKRRLDSSCLESVKQKCVKSCNCVTELDGQAESLRLDLCCLSGTQEVLSQDSEGPTKSSKTEGAGTSISEPPSPVSPYASEGCGPLPLPLRPCGEGSEMVGKENSSPENKNWLLAIAAKRKAENSSPRSPSSQTPSSRRQSGKTSPGPVTITPSSMRKICTYFRRKTQDDFCSPEHSTEL 729 Q24246 Cytoplasmic sw 7227 None SL-0178 SL-0182 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. UNIPROT Q24246 UNIPROT O96508 UNIPROT O96510 UNIPROT O96511 UNIPROT O96512 UNIPROT O96513 UNIPROT O96514 UNIPROT O96515 UNIPROT O96516 UNIPROT Q5U0Z1 UNIPROT Q86BQ5 UNIPROT Q9NG49 UNIPROT Q9TZR7 UNIPROT Q9TZR8 UNIPROT Q9TZR9 UNIPROT Q9TZS0 UNIPROT Q9VR78 PDB 2P2T PDB 3FM7 PDB 3L9K Pfam PF11540 PROSITE PS50082 PROSITE PS50294 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}. Q8T0I9 EBI-213466 0.00 Q4V5A7 EBI-253285 0.00 Q9XZ56 EBI-9919028 0.46 O61307 EBI-9921261 0.35 P18431 EBI-9925534 0.35 Q9VLS7 EBI-9929131 0.35 Q24568 EBI-9944837 0.35 GO:0005868 GO:0005765 GO:0005874 GO:0043005 GO:0031965 GO:0032991 GO:0034452 GO:0045504 GO:0045503 GO:0060090 GO:0008088 GO:0007349 GO:0051642 GO:0001754 GO:0000226 GO:0007018 GO:0034501 GO:0007291 GO:0007051 GO:0010970 Peripheral UniProt Sequence Analysis MDRKAELERKKAKLAALREEKDRRRREKEIKDMEEAAGRIGGGAGIDKDQRKDLDEMLSSLGVAPVSEVLSSLSSVNSMTSDNSNTQTPDASLQATVNGQSGGKKQPLNLSVYNVQATNIPPKETLVYTKQTQTTSTGGGNGDVLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFTDDEESSLQNLGNGFTSKLPPGYLTHGLPTVKDVAPAITPLEIKKETEVKKEVNELSEEQKQMIILSENFQRFVVRAGRVIERALSENVDIYTDYIGGGDSEEANDERSHARLSLNRVFYDERWSKNRCITSMDWSTHFPELVVGSYHNNEESPNEPDGVVMVWNTKFKKSTPEDVFHCQSAVMSTCFAKFNPNLILGGTYSGQIVLWDNRVQKRTPIQRTPLSAAAHTHPVYCLQMVGTQNAHNVISISSDGKLCSWSLDMLSQPQDTLELQQRQSKAIAITSMAFPANEINSLVMGSEDGYVYSASRHGLRSGVNEVYERHLGPITGISTHYNQLSPDFGHLFLTSSIDWTIKLWSLKDTKPLYSFEDNSDYVMDVAWSPVHPALFAAVDGSGRLDLWNLNQDTEVPTASIVVAGAPALNRVSWTPSGLHVCIGDEAGKLYVYDVAENLAQPSRDEWSRFNTHLSEIKMNQSDEV 663 Q759T0 Dynein DYN2 284811 None SL-0178 SL-0185 Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}. UNIPROT Q759T0 Pfam PF01221 PROSITE PS01239 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}. GO:0005868 GO:0005881 GO:0005643 GO:1990429 GO:0005777 GO:0045505 GO:0008574 GO:0044877 GO:0040001 GO:0051028 GO:0030473 GO:0051292 GO:0015031 Unknown UniProt Sequence Analysis MSKPAILKASDITDELRDEIFGISVQAVEQFQLEREVAAYIKKELDSKHGQTWHVIVGKNFGSYVTHEKGHFIYFYIGPLAFLVFKTA 88 Q22799 Dynein dlc 6239 None SL-0178 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}. UNIPROT Q22799 Pfam PF01221 PROSITE PS01239 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}. O02101 EBI-25615276 0.35 Q17902 EBI-2413132 0.75 G5EBV6 EBI-342182 0.00 Q18192 EBI-342185 0.00 O16474 EBI-342197 0.00 O17641 EBI-342188 0.00 P34766 EBI-342191 0.00 Q18529 EBI-6456071 0.55 P91249 EBI-342206 0.00 O45335 EBI-342200 0.00 G5EG76 EBI-342203 0.00 Q19816 EBI-6456097 0.55 Q9XVX4 EBI-342209 0.00 Q93572 EBI-342212 0.00 P48150 EBI-342224 0.00 O45436 EBI-342218 0.00 Q19988 EBI-342221 0.00 G5ECT7 EBI-2418552 0.62 Q20805 EBI-342227 0.00 P48154 EBI-342230 0.00 G5EBX2 EBI-342239 0.00 P55853 EBI-342236 0.00 C6KRN1 EBI-2420006 0.71 P34574 EBI-342248 0.00 Q22696 EBI-342251 0.00 G5EDQ5 EBI-342245 0.00 Q9U2M6 EBI-342260 0.00 P55954 EBI-342254 0.00 Q9N432 EBI-342257 0.00 H2L0C9 EBI-342263 0.00 Q9XUM8 EBI-2420748 0.49 Q23064 EBI-2905315 0.53 Q7K714 EBI-6455746 0.37 O45599 EBI-6456841 0.37 P30642 EBI-6456967 0.37 Q18194 EBI-6456947 0.37 P46502 EBI-6456957 0.37 Q22799 EBI-6456977 0.37 G5EFV3 EBI-6456987 0.37 Q19207 EBI-6457073 0.37 O45087 EBI-6458000 0.37 G5EBL8 EBI-6458325 0.37 GO:0005737 GO:0005868 GO:0005874 GO:0005875 GO:0005635 GO:0045505 GO:0006915 GO:0051301 GO:0051321 GO:0030473 Unknown UniProt Sequence Analysis MVDRKAVIKNADMSDDMQQDAIDCATQALEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG 89 Q6FUJ0 Dynein DYN2 284593 None SL-0178 SL-0185 Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}. UNIPROT Q6FUJ0 Pfam PF01221 PROSITE PS01239 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}. GO:0005868 GO:0005881 GO:0005643 GO:1990429 GO:0005777 GO:0008574 GO:0044877 GO:0040001 GO:0051028 GO:0030473 GO:0051292 GO:0015031 Unknown UniProt Sequence Analysis MDQVIVKASDMGDEMQQEVFRIAEEAMREHTLEREIASVIKKEMDSRYGHTWHVIVGRSFGSYVTHEKGKFVYFYVGPLALLVFKT 86 Q6BZF8 Dynein DYN2 284592 None SL-0178 SL-0185 Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}. UNIPROT Q6BZF8 Pfam PF01221 PROSITE PS01239 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}. GO:0005737 GO:0030286 GO:0005874 GO:0005643 GO:0007017 GO:0051028 GO:0015031 Unknown UniProt Sequence Analysis MSEKEQEPILKASDLPEEMQTRIFELSNEAVSNYKIEKDIATYLKKELDQLYGATWHVIVGKSFGSYVTHEQGFFTYFYIGQLAFLIFKSG 91 O94111 Dynein nudG 227321 None SL-0178 SL-0185 Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}. UNIPROT O94111 UNIPROT C8VTG5 UNIPROT Q547D6 UNIPROT Q5BGB0 Pfam PF01221 PROSITE PS01239 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}. GO:0005868 GO:0005881 GO:0005643 GO:1990429 GO:0005777 GO:0045505 GO:0008574 GO:0044877 GO:0048315 GO:0040001 GO:0051028 GO:0030473 GO:0051292 GO:0015031 GO:0043935 Unknown UniProt Sequence Analysis MASEKKDKLEPQIKSVDMSEDMQQEAVEVAIEAMEKYHIEKDIAQYIKREFDSRKGATWHCVVGRNFGSFVTHETKHFIYFYLGHCAILLFKTQ 94 Q6CWX4 Dynein DYN2 284590 None SL-0178 SL-0185 Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}. UNIPROT Q6CWX4 Pfam PF01221 PROSITE PS01239 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}. GO:0005868 GO:0005881 GO:0005643 GO:1990429 GO:0005777 GO:0008574 GO:0044877 GO:0040001 GO:0051028 GO:0030473 GO:0051292 GO:0015031 Unknown UniProt Sequence Analysis MSKPVLKASDITDELRDEIFELSSNATANYKLEREIAAYIKKQLDVSQGETWHVIVGKNFGSYVTHEKGYFVYFYIGPLAFLVFKTA 87 Q9UR05 Dynein dlc2 284812 None SL-0178 SL-0185 Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}. UNIPROT Q9UR05 Pfam PF01221 PROSITE PS01239 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}. GO:0005868 GO:0005829 GO:0035974 GO:0005874 GO:0034399 GO:0005643 GO:0005634 GO:0045505 GO:0030437 GO:0030989 GO:0051028 GO:0000743 GO:0015031 Unknown UniProt Sequence Analysis MAVIKAVDMSEKMQQEAIHAAVQAMEKFTIEKDIAAFIKREFDKKFSPTWHCIVGRNFGSFVTHESRHFIYFYLGTVAFLLFKSG 85 Q02647 Dynein DYN2 559292 None SL-0178 SL-0185 Cytoplasm, cytoskeleton. Nucleus, nuclear pore complex {ECO:0000269|PubMed:17546040, ECO:0000269|PubMed:23223634, ECO:0000269|PubMed:25646085}. UNIPROT Q02647 UNIPROT D6VT54 PDB 4DS1 PDB 4HT6 PDB 7N9F Pfam PF01221 PROSITE PS01239 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}. P36161 EBI-8466751 0.40 P40960 EBI-8480342 0.81 P40494 EBI-2613029 0.35 P24869 EBI-2617071 0.35 P32589 EBI-3724582 0.35 Q8IYA8 EBI-11534278 0.56 O96015 EBI-11534269 0.56 Q02647 EBI-15483402 0.44 P36022 EBI-15483422 0.43 GO:0005737 GO:0005868 GO:0005881 GO:0005635 GO:0034399 GO:0005643 GO:1990429 GO:0045505 GO:0044877 GO:0040001 GO:0000132 GO:0051028 GO:0030473 GO:0051292 GO:0006913 GO:0015031 Unknown UniProt Sequence Analysis MSDENKSTPIVKASDITDKLKEDILTISKDALDKYQLERDIAGTVKKQLDVKYGNTWHVIVGKNFGSYVTHEKGHFVYFYIGPLAFLVFKTA 92 Q03001 Dystonin DST 9606 None SL-0178 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}. UNIPROT Q03001 UNIPROT B7Z3H1 UNIPROT E7ERU0 UNIPROT O94833 UNIPROT Q12825 UNIPROT Q13266 UNIPROT Q13267 UNIPROT Q13775 UNIPROT Q5TBT0 UNIPROT Q5TBT2 UNIPROT Q5TF23 UNIPROT Q5TF24 UNIPROT Q8N1T8 UNIPROT Q8N8J3 UNIPROT Q8WXK8 UNIPROT Q8WXK9 UNIPROT Q96AK9 UNIPROT Q96DQ5 UNIPROT Q96J76 UNIPROT Q96QT5 UNIPROT Q9H555 UNIPROT Q9UGD7 UNIPROT Q9UGD8 UNIPROT Q9UN10 PDB 3GJO Pfam PF00307 Pfam PF13499 Pfam PF02187 Pfam PF00681 Pfam PF17902 Pfam PF00435 Pfam PF18373 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS00018 PROSITE PS50222 PROSITE PS51460 PROSITE PS50002 OMIM 113810 OMIM 614653 OMIM 615425 DisGeNET 667 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. 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. O95295 EBI-5664296 0.00 P04626 EBI-25367963 0.37 P29991 EBI-8828450 0.37 Q9NYQ7 EBI-311579 0.37 Q9HCM3 EBI-311727 0.37 P62993 EBI-350217 0.35 Q9BZL6 EBI-7235479 0.37 O15198 EBI-7263646 0.37 Q15287 EBI-1065372 0.00 P15121 EBI-1067054 0.00 Q9UHX1 EBI-1077592 0.00 Q9NRI5 EBI-1105693 0.00 Q9NV70 EBI-1105725 0.00 Q9UKE5 EBI-1105730 0.00 Q8TDR0 EBI-1105735 0.00 Q15691 EBI-2409886 0.73 P19838 EBI-2680933 0.00 Q13951 EBI-2691963 0.00 P25054 EBI-3436852 0.00 Q16659 EBI-3444390 0.00 Q13952 EBI-3446173 0.00 Q13177 EBI-3446930 0.00 Q96CV9 EBI-5357450 0.45 Q9UKG1 EBI-5357625 0.45 Q8IZP0 EBI-5652673 0.00 Q15327 EBI-5653401 0.00 P0C862 EBI-5654717 0.00 Q8N3C7 EBI-5655638 0.00 Q14324 EBI-5660966 0.00 O75386 EBI-5666780 0.00 Q13188 EBI-6256382 0.35 Q61166 EBI-8062428 0.70 Q99IB8 EBI-6928217 0.37 Q9H8S9 EBI-8798967 0.27 Q7L9L4 EBI-8799069 0.27 O00161 EBI-11294079 0.37 O41952 EBI-9640619 0.37 P88986 EBI-9640971 0.37 O41970 EBI-9641577 0.37 Q9NQW6 EBI-11009421 0.35 Q9D6P8 EBI-11062262 0.35 Q3UH45 EBI-11090763 0.35 P35579 EBI-11144042 0.35 Q5JU00 EBI-11367780 0.27 Q86X19 EBI-11390509 0.27 P49286 EBI-11577533 0.00 Q67020 EBI-11514491 0.37 P43355 EBI-21634905 0.35 Q9H9Q2 EBI-21739689 0.35 Q5SQX6 EBI-16086797 0.35 O15155 EBI-16788067 0.27 P15311 EBI-16791848 0.27 P49841 EBI-16793176 0.27 P11279 EBI-16794808 0.27 P51151 EBI-16798325 0.27 O43493 EBI-16800265 0.27 Q15388 EBI-16801791 0.27 Q9NS69 EBI-16802054 0.27 P46013 EBI-20562326 0.35 P35408 EBI-20811489 0.37 P51957 EBI-20721387 0.35 P05455 EBI-20900824 0.40 Q02878 EBI-20907504 0.40 O76021 EBI-20920060 0.40 P50993 EBI-20925034 0.40 Q12996 EBI-20929904 0.40 Q9NPJ6 EBI-25472202 0.27 Q14108 EBI-21264396 0.35 Q96GC9 EBI-21267986 0.35 P03372 EBI-21302175 0.35 Q96AC1 EBI-21387090 0.00 Q99459 EBI-21387226 0.00 O60239 EBI-21387213 0.00 Q96MT8 EBI-21387200 0.00 P61764 EBI-21387187 0.00 Q96BS2 EBI-21387161 0.00 Q9BY11 EBI-21387148 0.00 P13569 EBI-25416349 0.35 Q9C0B5 EBI-25637382 0.35 Q9Y5P2 EBI-26354638 0.35 P06702 EBI-27037935 0.37 Q13363 EBI-27044482 0.35 F1PAA9 EBI-27079701 0.27 A0A0H3NFP4 EBI-27055788 0.27 A0A0H3NF08 EBI-27055973 0.27 P63252 EBI-28956270 0.27 P35226 EBI-27108918 0.35 Q92630 EBI-28952196 0.27 Q93009 EBI-30842049 0.44 Q9NZR4 EBI-29000642 0.35 P21709 EBI-32720516 0.27 P29317 EBI-32720711 0.27 P29320 EBI-32720767 0.27 P21802 EBI-32721907 0.27 Q06124 EBI-32723738 0.27 P04629 EBI-32724282 0.27 Q16620 EBI-32724423 0.27 P16234 EBI-32724889 0.27 P09619 EBI-32724964 0.27 P34925 EBI-32731802 0.27 Q6J9G0 EBI-32731895 0.27 P38398 EBI-34581773 0.35 GO:0015629 GO:0030424 GO:1904115 GO:0009925 GO:0005604 GO:0005938 GO:0031252 GO:0005737 GO:0031410 GO:0005829 GO:0005789 GO:0005925 GO:0031673 GO:0030056 GO:0016021 GO:0005882 GO:0045111 GO:0016020 GO:0015630 GO:0035371 GO:0005635 GO:0005654 GO:0005634 GO:0030018 GO:0003779 GO:0005509 GO:0005178 GO:0008017 GO:0051010 GO:0008022 GO:0042803 GO:0005198 GO:0007155 GO:0048870 GO:0031122 GO:0007010 GO:0031581 GO:0007229 GO:0045104 GO:0030011 GO:0000226 GO:0009611 GO:0008090 GO:0042060 Lipid-Anchored UniProt By Similarity {ECO:0000250} MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDEKSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIRHHVTTMSERTFPNNPVELKALYNQYLQFKETEIPPKETEKSKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVERLEMLQQIANRVQRDSVICEDKLILAGNALQSDSKRLESGVQFQNEAEIAGYILECENLLRQHVIDVQILIDGKYYQADQLVQRVAKLRDEIMALRNECSSVYSKGRILTTEQTKLMISGITQSLNSGFAQTLHPSLTSGLTQSLTPSLTSSSMTSGLSSGMTSRLTPSVTPAYTPGFPSGLVPNFSSGVEPNSLQTLKLMQIRKPLLKSSLLDQNLTEEEINMKFVQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISEIQMTAPLKLTYAEKLHRLESQYAKLLNTSRNQERHLDTLHNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYRAAMQTQWSWILQLCQCVEQHIKENTAYFEFFNDAKEATDYLRNLKDAIQRKYSCDRSSSIHKLEDLVQESMEEKEELLQYKSTIANLMGKAKTIIQLKPRNSDCPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVPPPNKEAVDLANRIEQQYQNVLTLWHESHINMKSVVSWHYLINEIDRIRASNVASIKTMLPGEHQQVLSNLQSRFEDFLEDSQESQVFSGSDITQLEKEVNVCKQYYQELLKSAEREEQEESVYNLYISEVRNIRLRLENCEDRLIRQIRTPLERDDLHESVFRITEQEKLKKELERLKDDLGTITNKCEEFFSQAAASSSVPTLRSELNVVLQNMNQVYSMSSTYIDKLKTVNLVLKNTQAAEALVKLYETKLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALEDELQKAKAISDEMFKTYKERDLDFDWHKEKADQLVERWQNVHVQIDNRLRDLEGIGKSLKYYRDTYHPLDDWIQQVETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQKYAEQYSATVKDYELQTMTYRAMVDSQQKSPVKRRRMQSSADLIIQEFMDLRTRYTALVTLMTQYIKFAGDSLKRLEEEEKSLEEEKKEHVEKAKELQKWVSNISKTLKDAEKAGKPPFSKQKISSEEISTKKEQLSEALQTIQLFLAKHGDKMTDEERNELEKQVKTLQESYNLLFSESLKQLQESQTSGDVKVEEKLDKVIAGTIDQTTGEVLSVFQAVLRGLIDYDTGIRLLETQLMISGLISPELRKCFDLKDAKSHGLIDEQILCQLKELSKAKEIISAASPTTIPVLDALAQSMITESMAIKVLEILLSTGSLVIPATGEQLTLQKAFQQNLVSSALFSKVLERQNMCKDLIDPCTSEKVSLIDMVQRSTLQENTGMWLLPVRPQEGGRITLKCGRNISILRAAHEGLIDRETMFRLLSAQLLSGGLINSNSGQRMTVEEAVREGVIDRDTASSILTYQVQTGGIIQSNPAKRLTVDEAVQCDLITSSSALLVLEAQRGYVGLIWPHSGEIFPTSSSLQQELITNELAYKILNGRQKIAALYIPESSQVIGLDAAKQLGIIDNNTASILKNITLPDKMPDLGDLEACKNARRWLSFCKFQPSTVHDYRQEEDVFDGEEPVTTQTSEETKKLFLSYLMINSYMDANTGQRLLLYDGDLDEAVGMLLEGCHAEFDGNTAIKECLDVLSSSGVFLNNASGREKDECTATPSSFNKCHCGEPEHEETPENRKCAIDEEFNEMRNTVINSEFSQSGKLASTISIDPKVNSSPSVCVPSLISYLTQTELADISMLRSDSENILTNYENQSRVETNERANECSHSKNIQNFPSDLIENPIMKSKMSKFCGVNETENEDNTNRDSPIFDYSPRLSALLSHDKLMHSQGSFNDTHTPESNGNKCEAPALSFSDKTMLSGQRIGEKFQDQFLGIAAINISLPGEQYGQKSLNMISSNPQVQYHNDKYISNTSGEDEKTHPGFQQMPEDKEDESEIEEYSCAVTPGGDTDNAIVSLTCATPLLDETISASDYETSLLNDQQNNTGTDTDSDDDFYDTPLFEDDDHDSLLLDGDDRDCLHPEDYDTLQEENDETASPADVFYDVSKENENSMVPQGAPVGSLSVKNKAHCLQDFLMDVEKDELDSGEKIHLNPVGSDKVNGQSLETGSERECTNILEGDESDSLTDYDIVGGKESFTASLKFDDSGSWRGRKEEYVTGQEFHSDTDHLDSMQSEESYGDYIYDSNDQDDDDDDGIDEEGGGIRDENGKPRCQNVAEDMDIQLCASILNENSDENENINTMILLDKMHSCSSLEKQQRVNVVQLASPSENNLVTEKSNLPEYTTEIAGKSKENLLNHEMVLKDVLPPIIKDTESEKTFGPASISHDNNNISSTSELGTDLANTKVKLIQGSELPELTDSVKGKDEYFKNMTPKVDSSLDHIICTEPDLIGKPAEESHLSLIASVTDKDPQGNGSDLIKGRDGKSDILIEDETSIQKMYLGEGEVLVEGLVEEENRHLKLLPGKNTRDSFKLINSQFPFPQITNNEELNQKGSLKKATVTLKDEPNNLQIIVSKSPVQFENLEEIFDTSVSKEISDDITSDITSWEGNTHFEESFTDGPEKELDLFTYLKHCAKNIKAKDVAKPNEDVPSHVLITAPPMKEHLQLGVNNTKEKSTSTQKDSPLNDMIQSNDLCSKESISGGGTEISQFTPESIEATLSILSRKHVEDVGKNDFLQSERCANGLGNDNSSNTLNTDYSFLEINNKKERIEQQLPKEQALSPRSQEKEVQIPELSQVFVEDVKDILKSRLKEGHMNPQEVEEPSACADTKILIQNLIKRITTSQLVNEASTVPSDSQMSDSSGVSPMTNSSELKPESRDDPFCIGNLKSELLLNILKQDQHSQKITGVFELMRELTHMEYDLEKRGITSKVLPLQLENIFYKLLADGYSEKIEHVGDFNQKACSTSEMMEEKPHILGDIKSKEGNYYSPNLETVKEIGLESSTVWASTLPRDEKLKDLCNDFPSHLECTSGSKEMASGDSSTEQFSSELQQCLQHTEKMHEYLTLLQDMKPPLDNQESLDNNLEALKNQLRQLETFELGLAPIAVILRKDMKLAEEFLKSLPSDFPRGHVEELSISHQSLKTAFSSLSNVSSERTKQIMLAIDSEMSKLAVSHEEFLHKLKSFSDWVSEKSKSVKDIEIVNVQDSEYVKKRLEFLKNVLKDLGHTKMQLETTAFDVQFFISEYAQDLSPNQSKQLLRLLNTTQKCFLDVQESVTTQVERLETQLHLEQDLDDQKIVAERQQEYKEKLQGICDLLTQTENRLIGHQEAFMIGDGTVELKKYQSKQEELQKDMQGSAQALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKKELDKVVTTAIKEETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDEVNGNLLETDVDGQVGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLSPEEKEKLQKNMKELKVHYETALAESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENLEAGADDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRVLEAAKSCSKRDGGKVDTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCGLLAGLQACEATASKHLSEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVNERNEKLQITLTRSLSVQDGLDEMLDWMGNVESSLKEQGQVPLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMETTDPSTASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQTFLETKTQALTEVDVPGKDVTELSQYMQESTSEFLEHKKHLEVLHSLLKEISSHGLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVPIVQPSFGAEDLGKSLEDTKKLQEKWSLKTPEIQKVNNSGISLCNLISAVTTPAKAIAAVKSGGAVLNGEGTATNTEEFWANKGLTSIKKDMTDISHGYEDLGLLLKDKIAELNTKLSKLQKAQEESSAMMQWLQKMNKTATKWQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPDTPEAPRWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEAQLKQWLVEKELMVSVLGPLSIDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSLRGIVKEQLAAVTQKWDSLTGQLSDRCDWIDQAIVKSTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEYLKAELSRQLEGILKSFKDVEQKAENHVQHLQSACASSHQFQQMSRDFQAWLDTKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESLEKALKYKEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDENKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQALKHQVDLAKRLAQDLVVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLETKLQGIGHFQNTIREMFSQFAEFDDELDSMAPVGRDAETLQKQKETIKAFLKKLEALMASNDNANKTCKMMLATEETSPDLVGIKRDLEALSKQCNKLLDRAQAREEQVEGTIKRLEEFYSKLKEFSILLQKAEEHEESQGPVGMETETINQQLNMFKVFQKEEIEPLQGKQQDVNWLGQGLIQSAAKSTSTQGLEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALESLLSWMVDTEELVANQKPPSAEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIATTAEPADKVKILKQLSLLDSRWEALLNKAETRNRQLEGISVVAQQFHETLEPLNEWLTTIEKRLVNCEPIGTQASKLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLKVLSSREDKDMVQSKLDFSQVWYIEIQEKSHSRSELLQQALCNAKIFGEDEVELMNWLNEVHDKLSKLSVQDYSTEGLWKQQSELRVLQEDILLRKQNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQALQLARRLHSTHEELCTWLDKVEVELLSYETQVLKGEEASQAQMRPKELKKEAKNNKALLDSLNEVSSALLELVPWRAREGLEKMVAEDNERYRLVSDTITQKVEEIDAAILRSQQFDQAADAELSWITETEKKLMSLGDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEEKQSMKKKLDKVLKNYDTICQINSERYLQLERAQSLVNQFWETYEELWPWLTETQSIISQLPAPALEYETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYVAADTLYSQIKEDVKKRAVALDEAISQSTQFHDKIDQILESLERIVERLRQPPSISAEVEKIKEQISENKNVSVDMEKLQPLYETLKQRGEEMIARSGGTDKDISAKAVQDKLDQMVFIWENIHTLVEEREAKLLDVMELAEKFWCDHMSLIVTIKDTQDFIRDLEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAACGEPDKPIVKKSIDELNSAWDSLNKAWKDRIDKLEEAMQAAVQYQDGLQAVFDWVDIAGGKLASMSPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKHTVQDPLMELKLIWDSLEERIINRQHKLEGALLALGQFQHALDELLAWLTHTEGLLSEQKPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSAGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHGEIEDLQQWLTDTERHLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAETNIDQDINNLKEKWESVETKLNERKTKLEEALNLAMEFHNSLQDFINWLTQAEQTLNVASRPSLILDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDDARKRAKQFHEAWSKLMEWLEESEKSLDSELEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEKTSLADDNLKLDDMLSELRDKWDTICGKSVERQNKLEEALLFSGQFTDALQALIDWLYRVEPQLAEDQPVHGDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQELSTRWETVCALSISKQTRLEAALRQAEEFHSVVHALLEWLAEAEQTLRFHGVLPDDEDALRTLIDQHKEFMKKLEEKRAELNKATTMGDTVLAICHPDSITTIKHWITIIRARFEEVLAWAKQHQQRLASALAGLIAKQELLEALLAWLQWAETTLTDKDKEVIPQEIEEVKALIAEHQTFMEEMTRKQPDVDKVTKTYKRRAADPSSLQSHIPVLDKGRAGRKRFPASSLYPSGSQTQIETKNPRVNLLVSKWQQVWLLALERRRKLNDALDRLEELREFANFDFDIWRKKYMRWMNHKKSRVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAYKPITDADKIEDEVTRQVAKCKCAKRFQVEQIGDNKYRFFLGNQFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRVHHHGSKMLRSESNSSITTTQPTIAKGRTNMELREKFILADGASQGMAAFRPRGRRSRPSSRGASPNRSTSVSSQAAQAASPQVPATTTPKGTPIQGSKLRLPGYLSGKGFHSGEDSGLITTAAARVRTQFADSKKTPSRPGSRAGSKAGSRASSRRGSDASDFDISEIQSVCSDVETVPQTHRPTPRAGSRPSTAKPSKIPTPQRKSPASKLDKSSKR 7570 Q91ZU6 Dystonin Dst 10090 None SL-0178 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. UNIPROT Q91ZU6 UNIPROT E9PXE5 UNIPROT E9QL23 UNIPROT Q1KP04 UNIPROT Q3I6J6 UNIPROT Q60824 UNIPROT Q60845 UNIPROT Q8K5D4 UNIPROT Q91ZU7 UNIPROT Q91ZU8 UNIPROT Q9WU50 UNIPROT S4R1U5 PDB 2IAK Pfam PF00307 Pfam PF13499 Pfam PF02187 Pfam PF00681 Pfam PF17902 Pfam PF00435 Pfam PF18373 PROSITE PS00019 PROSITE PS00020 PROSITE PS50021 PROSITE PS00018 PROSITE PS50222 PROSITE PS51460 PROSITE PS50002 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. P21807 EBI-446225 0.54 P19527 EBI-446339 0.37 P16884 EBI-446356 0.37 O70589 EBI-3647717 0.35 P35279 EBI-11566531 0.35 Q4U2R1 EBI-16730475 0.35 Q7TPH6 EBI-16731507 0.35 P83510 EBI-16734044 0.35 Q9QWI6 EBI-27100778 0.35 GO:0015629 GO:0030424 GO:1904115 GO:0005938 GO:0031252 GO:0005737 GO:0009898 GO:0031410 GO:0005829 GO:0005789 GO:0005925 GO:0031673 GO:0030056 GO:0016021 GO:0014704 GO:0005882 GO:0045111 GO:0016020 GO:0015630 GO:0035371 GO:0005635 GO:0005654 GO:0005634 GO:0097038 GO:0048471 GO:0014069 GO:0042383 GO:0001725 GO:0045098 GO:0030018 GO:0003779 GO:0005509 GO:0005178 GO:0008017 GO:0051010 GO:0008022 GO:0042803 GO:0005198 GO:0007409 GO:0007155 GO:0048870 GO:0031122 GO:0007010 GO:0031581 GO:0045104 GO:0046907 GO:0030011 GO:0000226 GO:0009611 GO:0008090 GO:0042060 Lipid-Anchored UniProt Sequence Analysis MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQATEGYAGVRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDEKSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIRHHVVTMSERTFPNNPLELKALYNQYLQFKEKEIPPKEMEKSKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVERLDMLQQIATRVQRDSVSCEDKLILARNALQSDSKRLESGVQFQNEAEIAGYILECENLLRQHVIDVQILIDGKYYQADQLVQRVAKLRDEIMALRNECSSVYSKGRMLTTEQTKLMISGITQSLNSGFAQTLHPSLNSGLTQSLTPSLTSSSVTSGLSSGMTSRLTPSVTPVYAPGFPSVVAPNFSLGVEPNSLQTLKLMQIRKPLLKSSLLDQNLTEEEVNMKFVQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISEIQMTAPLKLSYTDKLHRLESQYAKLLNTSRNQERHLDTLHNFVTRATNELIWLNEKEESEVAYDWSERNSSVARKKSYHAELMRELEQKEESIKAVQEIAEQLLLENHPARLTIEAYRAAMQTQWSWILQLCQCVEQHIQENSAYFEFFNDAKEATDYLRNLKDAIQRKYSCDRSSSIHKLEDLVQESMEKEELLQYRSVVAGLMGRAKTVVQLKPRNPDNPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVPPPNKEAVDFANRIEQQYQSVLTLWHESHINMKSVVSWHYLVNEIDRIRASNVASIKTMLPGEHQQVLSNLQSRLEDFLEDSQESQIFSGSDISQLEKEVSVCRKYYQELLKSAEREEQEESVYNLYISEVRNIRLRLESCEDRLIRQIRTPLERDDLHESMLRITEQEKLKKELDRLKDDLGTITNKCEEFFSQAADSPSVPALRSELSVVIQSLSQIYSMSSTYIEKLKTVNLVLKNTQAAEALVKLYETKLCEEEAVIADKNNIENLMSTLKQWRSEVDEKREVFHALEDELQKAKAISDEMFKTHKERDLDFDWHKEKADQLVERWQSVHVQIDNRLRDLEGIGKSLKHYRDSYHPLDDWIQHIETTQRKIQENQPENSKALALQLNQQKMLVSEIEVKQSKMDECQKYSEQYSAAVKDYELQTMTYRAMVESQQKSPVKRRRIQSSADLVIQEFMDLRTRYTALVTLMTQYIKFAGDSLKRLEEEEKSLDEEKKQHIEKAKELQKWVSNISKTLGDGEKAGKPLFSKQQMSSKEISTKKEQFSEALQTTQIFLAKHGDKLTEEERSDLEKQVKTLQEGYNLLFSESLKQQELQPSGESKVPEKPDKVIAGTINQTTGEVLSVFQAVLRGLIDYETGIRLLEAQLVITGLISPELRKCFDLRDAESHGLIDEQVLRQLKELNRAKQLISTASPTSIPVLDSLAQGMVSESMAIRVLEILLSAGPLLVPATGEHLTLQQAFQQNLISSALFSKVLERQDTCKDLIDPCTSEKVSLTDMVQRSILQENTRMWLLPVRPQEAGRITLKCGRSVSILRAAHEGLIDRETMFRLLGAQLLSGGLIDCNSGQKMTVEEAVAEGVIDRDTASSILTYQVQTGGIVHSNPAKRLTVDEAVQCELITSSSALLVLEAQRGYVGLIWPHSGEIFPTSSSLQQELITNELASKILNGRQKIAALYIPESSQVIGLDAAKQLGIIDNNTASVLKSVTLPDKMPDLGDLEDCKNAKRWLSFCKLQPSTVHDYRQEEGGSDGEEPVTAQSSEQTKKLFLSYLMVNSYMDAHTGQRLLLYDGDLDEAVGMLLESCGTELGADTSTRESLSVLTIPDAFPDCALSEEKHECSAAAAGPDKCHYSHPGHKESLENAKWDMNEAFCKMGNNDSNGELPRPENLADTTVVQKGSESPSRVRVPKPTSSSTQPEGSVLRPESGSILKGCKSQSEPVTKKYPDGANHSHFLTSETSRPCDSNEREDEENIQKGPSVFDYSPRLSALLSHDELRQSQGRFSDTSTPQNTGYLCEASTLSPSDQRVLADQSTREKFQDQFLGIAAISVSLQGAPCGQKPVDTECSSSQVHYHSEESMSDASAESGATRQTDESEKTGSKVEDNSCTMVPGGGSRNDNTSDCGPLSHKGAIDAGDYETSLLAGQQSDTATDSDSDDYFYDTPLFEDEDHDSLILQGDDRDCLQPEDYDTSLQEENDRTPPPDDIFYDVMKEKENPEFPHGGMDESLGVENKVCCPQGFPVGIEKPELYLAGEKEFNSGGSEQLVESVSESENPPGLWDSESDSLTEGEIIGRKERLGASLTPDGHWRGDREECDTSRESQSDTDGVGSIQSSESYRPYMSDGSDLDEEDNGGRSSEDSGDGRGGQGVADEGGEPQYQADPTQLYTAIRKEHGGETQNVSDMIPLDKTHSYSPLETQHGAGVFQPESAGRGGWDTERSSHPELTTEADEEDEASLSTHMATKGVSLSNAEGTASEEIRLVQGPDSTGILKAEDLENVSPEISPSSDNIVRSEAELGGGASEDGHLSFTGSDRDQQGPGRGLVKGRDGQSDKLVDETSIREMGFQKEGVLMSSPEEGGEEERDLEPFPNGSATESLNMGKSQVPPLLTHTEELSHRGAPHTTTMTTTMTLEGEAKNVQTGLTESPVLLETLAEIFDTPASKVTRADLTSAVTASEMKSQVKEDSLTGGPEKETGPCTSLGHCDKCIHVDMLEPNEHTPSCALVAPPTVKDNLCSVNNAGEKSVRPQEDWPPAAEVRLSDACVEESISEGKAGILQFTPENSDSTLSRLPHQSVAGWGKSADSVQARLPVSGVRHTSADTLDVGCPQLESSREKASAEEEPHRERALSLKPQEREHHMLGFVEDGRSILKSSLDKVHMNLQEVGDPSAGTGTKISIQNLIRRAILSELPNEVSNVPSHGISPISNSSEVRAESGGDPFCITSFLHLLKQNQPPQETPGISELAKVLTQMDCDPEQRGLGSELLPPQLKNAFYKLLFDGYATEKDQAEALGQTSCAVPKMAEEKPHVCSDLRNKEGHHCPLNPQAVGEAEVEPFSVHIAALPGGEKLGELCSEPPEHSESTSGSKERSSDSSSKEKCSNGLQQCLQHTEKMHEYLVLLQDMKPPLDNQASVESSLEALKSQLKQLEAFELGLAPIAVFLRKDLKLAEEFLKSFPSDLPRRHHEELSKSHQRLQNAFSSLSSVSSERMKLIKLAINSEMSKLAVRHEDFLHKLTSYSDWVSEKSRSVKAIQTVNVQDTELVKNSVKFLKNVLADLSHTKMQLETTAFDVQSFISDYAQDLSPSQSRQLLRLLNTTQKGFLDLQELVTTEADRLEALLQLEQELGHQKVVAERQQEYREKLQGLCDLLTQTENRLISNQEAFVIGDGTVELQKYQSKQEELQRDMQGSTQAMEEIVRNTELFLKESGDELSQADRALIEQKLNEVKMKCAQLNLKAEQSRKELDKAVTTALKEETEKVAAVRQLEESKTKIENLLNWLSNVEEDSEGVWTKHTQPMEQNGTYLHEGDSKLGAGEEDEVNGNLLETDAEGHSEATKGNLNQQYEKVKAQHGKIMAQHQAVLLATQSAQVLLEKQGHYLSPEEKEKLQKNTQELKVHYEKVLAECEKKVKLTHSLQEELEKFDTDYSEFEHWLQQSEQELANLEAGADDLSGLMDKLTRQKSFSEDVISHKGDLRYITISGNRVIDAAKSCSKRDSDRIGKDSVETSATHREVQTKLDQVTDRFRSLYSKCSVLGNNLKDLVDQYQQYEDASCGLLSGLQACEAKASKHLREPIALDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDAKGSLLPAKNDIQKTLDDIVGRYDDLSKCVNERNEKLQITLTRSLSVQDALDEMLDWMGSVESSLVKPGQVPLNSTALQDLISKDTMLEQDITGRQSSINAMNEKVKTFIETTDPSTASSLQAKMKDLSARFSEASQKHKEKLAKMVELKAKVEQFEKLSDKLQTFLETQSQALTEVAMPGKDVPELSQHMQESTAKFLEHRKDLEALHSLLKEISSHGLPGDKALVFEKTNNLSRKFKEMEDTIQEKKDALSSCQEQLSAFQTLAQSLKTWIKETTKQVPVVKPSLGTEDLRKSLEETKKLQEKWNLKAPEIHKANNSGVSLCNLLSALISPAKAIAAAKSGGVILNGEGTDTNTQDFLANKGLTSIKKDMTDISHSYEDLGLLLKDKIVELNTKLSKLQKAQEESSAMMQWLEKMNKTASRWRQTPTPADTESVKLQVEQNKSFEAELKQNVNKVQELKDKLSELLEENPEAPEAQSWKQALAEMDTKWQELNQLTMDRQQKLEESSNNLTQFQTTEAQLKQWLMEKELMVSVLGPLSIDPNMLNTQKQQVQILLQEFDTRKPQYEQLTAAGQGILSRPGEDPSLHGIVNEQLEAVTQKWDNLTGQLRDRCDWIDQAIVKSTQYQSLLRSLSGTLTELDDKLSSGLTSGALPDAVNQQLEAAQRLKQEIEQQAPKIKEAQEVCEDLSALVKEEYLKAELSRQLEGILKSFKDIEQKTENHVQHLQSACASSHQFQQMSKDFQAWLDAKKEEQRDSPPISAKLDVLESLLNSQKDFGKTFTEQSNIYEKTISEGENLLLKTQGAEKAALQLQLNTMKTDWDRFRKQVKEREEKLKDSLEKALKYREQVETLRPWIDRCQHSLDGVTFSLDPTESESSIAELKSLQKEMDHHFGMLELLNNTANSLLSVCEVDKEAVTEENQSLMEKVNRVTEQLQSKTVSLENMAQKFKEFQEVSRDTQRQLQDTKEQLEVHHSLGPQAYSNKHLSVLQAQQKSLQTLKQQVDEAKRLAQDLVVEAADSKGTSDVLLQAETLAEEHSELSQQVDEKCSFLETKLQGLGHFQNTIREMFSQFTECDDELDGMAPVGRDAETLRKQKACMQTFLKKLEALMASNDSANRTCKMMLATEETSPDLIGVKRDLEALSKQCNKLLDRAKTREEQVDGATEKLEEFHRKLEEFSTLLQKAEEHEESQGPVGTETETINQQLDVFKVFQKEEIEPLQVKQQDVNWLGQGLIQSAAANTCTQGLEHDLDSVNSRWKTLNKKVAQRTSQLQEALLHCGRFQDALESLLSWMADTEELVANQKPPSAEFKVVKAQIQEQKLLQRLLEDRKSTVEVIKREGEKIAASAEPADRVKLTRQLSLLDSRWEALLSRAEARNRQLEGISVVAQEFHETLEPLNEWLTAVEKKLANSEPIGTQAPKLEEQISQHKALQEDILLRKQSVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSADVAKTLEHALQLAGQLQSMHKELCNWLDKVEVELLSYETQGLKGEAASQVQERQKELKNEVRSNKALVDSLNEVSSALLELVPWRAREGLEKTIAEDNERYRLVSDTITQKVEEIDAAILRSQQFEQAADAELSWITETQKKLMSLGDIRLEQDQTSAQLQVQKAFTMDILRHKDIIDELVTSGHKIMTTSSEEEKQSMKKKLDKVLKKYDAVCQINSERHLQLERAQSLVSQFWETYEELWPWLTETQRIISQLPAPALEYETLRRQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPKEGIYIQEKYVAADTLYSQIKEDVKKRAVVLDEAISQSTQFHDKIDQILESLERIAERLRQPPSISAEVEKIKEQIGENKSVSVDMEKLQPLYETLRQRGEEMIARSEGTEKDVSARAVQDKLDQMVFIWGSIHTLVEEREAKLLDVMELAEKFWCDHMSLVVTIKDTQDFIRDLEDPGIDPSVVKQQQEAAEAIREEIDGLQEELDMVITLGSELIAACGEPDKPIVKKSIDELNSAWDSLNKAWKDRVDRLEEAMQAAVQYQDGLQGIFDWVDIAGNKLATMSPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEEADKHTVQDPLMELKLIWDSLDERIVSRQHKLEGALLALGQFQHALDELLAWLTHTKGLLSEQKPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSEGEEASNLQYKLRILNQRWQDILEKTDQRKQQLDSALRQAKGFHGEIEDLQQWLTDTERHLLASKPLGGLPETAKEQLNAHMEVCTAFAIKEETYKSLMLRGQQMLARCPRSAETNIDQDITNLKEKWESVKSKLNEKKTKLEEALHLAMNFHNSLQDFINWLTQAEQTLNVASRPSLILDTILFQIDEHKVFANEVNSHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDEARKRAKQFHEAWSKLMEWLEESEKSLDSELEIANDPDKIKAQLVQHKEFQKSLGGKHSVYDTTNRTGRSLKEKTSLADDNLKLDNMLSELRDKWDTICGKSVERQNKLEEALLFSGQFTDALQALIDWLYRVEPQLAEDQPVHGDIDLVMNLIDNHKVFQKELGKRTSSVQALKRSARELIEGSRDDSSWVRVQMQELSTRWETVCALSISKQTRLESALQQAEEFHSVVHTLLEWLAEAEQTLRFHGALPDDEDALRTLIEQHKEFMKRLEEKRAELSKATGMGDALLAVCHPDSITTIKHWITIIQARFEEVLAWAKQHQQRLAGALAGLIAKQELLETLLAWLQWAETTLTEKDKEVIPQEIEEVKTLIAEHQTFMEEMTRKQPDVDKVTKTYKRRATDPPSLQSHIPVLDKGRAGRKRFPASGFYPSGSQTQIETKNPRVNLLVSKWQQVWLLALERRRKLNDALDRLEELREFANFDFDIWRKKYMRWMNHKKSRVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAYKPITDADKIEDEVTRQVAKCKCAKRFQVEQIGDNKYRFFLGNQFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRVHHHGSKMLRSESNSSITATQPTLAKGRTNMELREKFILADGASQGMAAFRPRGRRSRPSSRGASPNRSTSASSHACQAASPPVPAAASTPKGTPIQGSKLRLPGYLSGKGFHSGEDSALITTAAARVRTQFAESRKTPSRPGSRAGSKAGSRASSRRGSDASDFDISEIQSVCSDVETVPQTHRPVPRAGSRPSTAKPSKIPTPQRRSPASKLDKSSKR 7393 P03247 E1B E1B 10515 None SL-0415 SL-0416 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}. UNIPROT P03247 Pfam PF01691 PROSITE PS50062 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}. O60238 EBI-849900 0.65 P02545 EBI-849870 0.37 Q16611 EBI-849884 0.37 Q12982 EBI-849887 0.37 Q12983 EBI-849890 0.49 GO:0044165 GO:0044199 GO:0044203 GO:0020002 GO:0016020 GO:0019050 Unknown UniProt Sequence Analysis MEAWECLEDFSAVRNLLEQSSNSTSWFWRFLWGSSQAKLVCRIKEDYKWEFEELLKSCGELFDSLNLGHQALFQEKVIKTLDFSTPGRAAAAVAFLSFIKDKWSEETHLSGGYLLDFLAMHLWRAVVRHKNRLLLLSSVRPAIIPTEEQQQEEARRRRRQEQSPWNPRAGLDPRE 175 P10406 E1B E1BS 28280 None SL-0415 SL-0416 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}. UNIPROT P10406 Pfam PF01691 PROSITE PS50062 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}. GO:0044203 GO:0020002 GO:0016020 GO:0019050 Unknown UniProt Sequence Analysis MEIWTVLEDFHKTRQLLENASNGVSHLWRFCFGGDLAKLVYRAKQDYREQFEDILRECPSLFDALNLGHQSHFNQRISRALDFTTPGRTTAAVAFFAFIFDKWSQETHFSRDYQLDFLAVALWRTWKCQRLNAIPATCRYSR 142 P03246 E1B E1BS 28285 None SL-0415 SL-0416 Host cell membrane. Host nucleus envelope. Host nucleus lamina. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. UNIPROT P03246 Pfam PF01691 PROSITE PS50062 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. O15173 EBI-11722343 0.35 Q9H2V7 EBI-11722343 0.35 P62834 EBI-11722343 0.35 P35813 EBI-11722343 0.35 Q9NZM1 EBI-11722343 0.35 O95297 EBI-11722343 0.35 P50281 EBI-11722343 0.35 O75695 EBI-11722343 0.35 Q9Y6C9 EBI-11722343 0.35 Q9BQB6 EBI-11722343 0.35 Q9P0L0 EBI-11722343 0.35 Q96IX5 EBI-11722343 0.35 O14773 EBI-11722343 0.35 Q96JJ7 EBI-11722343 0.35 P42166 EBI-11722343 0.35 Q8N4L2 EBI-11722343 0.35 Q9BTV4 EBI-11722343 0.35 Q9NV96 EBI-11722343 0.35 Q9HC07 EBI-11722343 0.35 O15533 EBI-11722343 0.35 P46977 EBI-11722343 0.35 Q13586 EBI-11722343 0.35 Q9Y5M8 EBI-11722343 0.35 P08240 EBI-11722343 0.35 Q9Y6N5 EBI-11722343 0.35 Q99523 EBI-11722343 0.35 Q15599 EBI-11722343 0.35 P11166 EBI-11722343 0.35 P60468 EBI-11722343 0.35 O75396 EBI-11722343 0.35 P31040 EBI-11722343 0.35 Q14108 EBI-11722343 0.35 Q969E2 EBI-11722343 0.35 Q9NTJ5 EBI-11722343 0.35 P06703 EBI-11722343 0.35 Q9NQC3 EBI-11722343 0.35 Q14699 EBI-11722343 0.35 Q9HBH5 EBI-11722343 0.35 P51148 EBI-11722343 0.35 Q9BZG1 EBI-11722343 0.35 Q9NP72 EBI-11722343 0.35 P53801 EBI-11722343 0.35 Q13308 EBI-11722343 0.35 Q9HCU5 EBI-11722343 0.35 O60831 EBI-11722343 0.35 O75688 EBI-11722343 0.35 O00264 EBI-11722343 0.35 P50479 EBI-11722343 0.35 P09619 EBI-11722343 0.35 Q96AQ6 EBI-11722343 0.35 Q9Y639 EBI-11722343 0.35 O00483 EBI-11722343 0.35 Q6PIU2 EBI-11722343 0.35 Q9BRK3 EBI-11722343 0.35 Q13724 EBI-11722343 0.35 Q14165 EBI-11722343 0.35 Q96N66 EBI-11722343 0.35 P29966 EBI-11722343 0.35 Q6IAA8 EBI-11722343 0.35 P05556 EBI-11722343 0.35 P26006 EBI-11722343 0.35 Q16891 EBI-11722343 0.35 Q70UQ0 EBI-11722343 0.35 P11717 EBI-11722343 0.35 Q8TED1 EBI-11722343 0.35 P59768 EBI-11722343 0.35 P62873 EBI-11722343 0.35 Q9H4G4 EBI-11722343 0.35 P48060 EBI-11722343 0.35 P17302 EBI-11722343 0.35 P25445 EBI-11722343 0.35 A0FGR8 EBI-11722343 0.35 Q969X5 EBI-11722343 0.35 P17813 EBI-11722343 0.35 P50402 EBI-11722343 0.35 A4FU69 EBI-11722343 0.35 Q96KC8 EBI-11722343 0.35 O00273 EBI-11722343 0.35 P39656 EBI-11722343 0.35 Q16527 EBI-11722343 0.35 Q1MSJ5 EBI-11722343 0.35 Q6UVK1 EBI-11722343 0.35 P09543 EBI-11722343 0.35 Q9H5V8 EBI-11722343 0.35 P16070 EBI-11722343 0.35 Q9BWT7 EBI-11722343 0.35 P35613 EBI-11722343 0.35 Q07812 EBI-11722343 0.35 Q16611 EBI-11722343 0.35 P16615 EBI-11722343 0.35 P05023 EBI-11722343 0.35 Q8IZ07 EBI-11722343 0.35 Q8N2K0 EBI-11722343 0.35 P80404 EBI-11722343 0.35 Q13323 EBI-11735775 0.37 GO:0044203 GO:0020002 GO:0016020 GO:0019050 Unknown UniProt Sequence Analysis MEAWECLEDFSAVRNLLEQSSNSTSWFWRFLWGSSQAKLVCRIKEDYKWEFEELLKSCGELFDSLNLGHQALFQEKVIKTLDFSTPGRAAAAVAFLSFIKDKWSEETHLSGGYLLDFLAMHLWRAVVRHKNRLLLLSSVRPAIIPTEEQQQQQEEARRRRQEQSPWNPRAGLDPRE 176 P03248 E1B E1BS 10519 None SL-0415 SL-0416 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}. UNIPROT P03248 Pfam PF01691 PROSITE PS50062 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}. GO:0044203 GO:0020002 GO:0016020 GO:0019050 Unknown UniProt Sequence Analysis MEVWAILEDLRQTRLLLENASDGVSGLWRFWFGGDLARLVFRIKQDYREEFEKLLDDIPGLFEALNLGHQAHFKEKVLSVLDFSTPGRTAAAVAFLTFILDKWIRQTHFSKGYVLDFIAAALWRTWKARRMRTILDYWPVQPLGVAGILRHPPTMPAVLQEEQQEDNPRAGLDPPVEE 178 P04492 E1B E1BS 28282 None SL-0415 SL-0416 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}. UNIPROT P04492 Pfam PF01691 PROSITE PS50062 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}. GO:0044203 GO:0020002 GO:0016020 GO:0019050 Unknown UniProt Sequence Analysis MELETVLQSFQSVRQLLQYTSKNTSGFWRYLFGSTLSKVVNRVKEDYREEFENILADCPGLLASLDLCYHLVFQEKVVRSLDFSSVGRTVASIAFLATILDKWSEKSHLSWDYMLDYMSMQLWRAWLKRRVCIYSLARPLTMPPLPTLQEEKEEERNPAVVEK 163 P10543 E1B E1BS 28284 None SL-0415 SL-0416 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}. UNIPROT P10543 Pfam PF01691 PROSITE PS50062 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}. GO:0044203 GO:0020002 GO:0016020 GO:0019050 Unknown UniProt Sequence Analysis MELWSELQSYQNLRRLLELASARTSSCWRILFGSTLTNVIYRAKEEYSSRFADLLSHNPGIFASLNLGHHSFFQEIVIRNLDFSSPGRTVSGLAFICFILDQWSAQTHLSQGYTLDYMAMALWRTLLRRKRVLGCLPAQRPHGLDPVQEEEEEEENLRAGLDPSTEL 167 P10544 E1B E1BS 10524 None SL-0415 SL-0416 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}. UNIPROT P10544 Pfam PF01691 PROSITE PS50062 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}. GO:0044203 GO:0020002 GO:0016020 GO:0019050 Unknown UniProt Sequence Analysis MEFWSELQSYQSLRRLLELASARTSSCWRFIFGSTLTNVIYRAKEDYSSRFAELLSFNPGIFASLNLGHHSFFQEIVIKNLDFSSPGRTVSGLAFICFILDQWSAQTHLSEGYTLDYMTMALWRTLLRRKRVLGCSPAQPPHGLDPVREEEEEEEEEENLRAGLDPQTEL 170 P12827 Protein DA26 46015 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P12827 Pfam PF11050 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}. GO:0030430 GO:0044201 GO:0016020 GO:0044423 Unknown UniProt Sequence Analysis MESVQTRLCASSNQFAPFKKRQLAVPVGSVNSLTHTITSTTVTSVIPKNYQEKRQKICHIISSLRNTHLNFNKIQSVHKKKLRHLQNLLRKKNEIIAELVRKLESAQKKTTHRNISKPAHWKYFGVVRCDNTIRTIIGNEKFVRRRLAELCTLYNAEYVFCQARADGDKDRQALASLLTAAFGSRVIVYENSRRFEFINPDEIASGKRLIIKHLQDESQSDINAY 225 P19525 Interferon-induced, EIF2AK2 9606 None SL-0198 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}. UNIPROT P19525 UNIPROT A8K3P0 UNIPROT D6W584 UNIPROT E9PC80 UNIPROT Q52M43 UNIPROT Q7Z6F6 UNIPROT Q9UIR4 PDB 1QU6 PDB 2A19 PDB 2A1A PDB 3UIU PDB 6D3K PDB 6D3L Pfam PF00035 Pfam PF00069 PROSITE PS50137 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 OMIM 176871 OMIM 618877 OMIM 619687 DisGeNET 5610 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}. 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. O75569 EBI-6116026 0.80 O92972 EBI-6918687 0.40 P60953 EBI-8612632 0.44 P62999 EBI-8612643 0.44 Q27968 EBI-640789 0.59 P06748 EBI-6958371 0.46 Q9UJU6 EBI-1080906 0.00 P05198 EBI-1226418 0.78 P20639 EBI-8674959 0.67 P35570 EBI-2603511 0.44 P06493 EBI-7909622 0.44 P60520 EBI-3046676 0.35 Q96C10 EBI-6115711 0.50 Q8IY81 EBI-6116026 0.62 P05455 EBI-6116026 0.35 P46087 EBI-6116026 0.35 Q9HCE1 EBI-6116026 0.62 O00458 EBI-6116026 0.35 Q99848 EBI-6116026 0.53 P07910 EBI-6116026 0.35 P56537 EBI-6116026 0.50 Q13310 EBI-6116026 0.35 Q9NUL3 EBI-6116026 0.62 Q9NZM5 EBI-6116026 0.53 Q9BZE4 EBI-6116026 0.53 Q9H0E2 EBI-6116026 0.50 Q7L2E3 EBI-6116026 0.71 Q9H0D6 EBI-6116026 0.35 P20248 EBI-6116026 0.35 Q9NSD9 EBI-6116026 0.35 O95793 EBI-6116026 0.35 O60812 EBI-6116026 0.35 Q8WTT2 EBI-6116026 0.53 Q9UPY3 EBI-6116026 0.50 Q9NX58 EBI-6116026 0.53 Q8N5Z5 EBI-6116026 0.35 Q96CT7 EBI-6116026 0.35 Q00577 EBI-6116026 0.53 P36873 EBI-6116026 0.35 Q15633 EBI-6116026 0.50 Q6P2E9 EBI-6116026 0.50 Q9Y285 EBI-6116026 0.35 Q9UL40 EBI-6116026 0.62 P16403 EBI-6116026 0.35 Q00526 EBI-6116026 0.35 P11387 EBI-6116026 0.35 Q9BVP2 EBI-6116026 0.35 Q08211 EBI-6116026 0.50 P04591 EBI-6178285 0.40 O00425 EBI-6255714 0.35 Q9Y6M1 EBI-6255714 0.35 P08238 EBI-6424177 0.40 Q86VP6 EBI-21322532 0.35 Q13618 EBI-21329068 0.35 P04487 EBI-6880922 0.59 P27958 EBI-8765629 0.70 Q16543 EBI-8770673 0.35 Q2HR71 EBI-8876191 0.40 P05412 EBI-11324725 0.35 Q96FF9 EBI-11027063 0.35 P27635 EBI-11035646 0.35 Q99PL5 EBI-11066888 0.35 Q14108 EBI-11072280 0.35 Q6PFD6 EBI-11093571 0.35 Q6PJG2 EBI-11106137 0.35 Q9H444 EBI-11151252 0.35 P78563 EBI-25249266 0.56 P51608 EBI-21532962 0.35 Q96SL4 EBI-21714987 0.35 Q8N6M8 EBI-21771054 0.35 P04798 EBI-21774067 0.35 Q60803 EBI-15560282 0.40 P53235 EBI-15561786 0.44 P19525 EBI-15561809 0.56 Q96P20 EBI-15999105 0.60 O14862 EBI-15999033 0.40 Q9C000 EBI-15999201 0.40 Q9NPP4 EBI-15999262 0.40 Q14684 EBI-16686997 0.53 Q7KZN9 EBI-20304305 0.35 P09622 EBI-20304669 0.35 P36957 EBI-20305285 0.35 P10636 EBI-20798291 0.35 Q15628 EBI-20936084 0.40 Q5S007 EBI-21360986 0.35 P03372 EBI-21301141 0.35 Q9UN86 EBI-26877955 0.40 Q13283 EBI-26877944 0.53 P0DTC9 EBI-26948583 0.82 P59595 EBI-26984718 0.40 K9N4V7 EBI-26984727 0.40 Q9BY44 EBI-26989881 0.40 P35226 EBI-27109494 0.35 Q9Y4W2 EBI-28934478 0.35 Q9Y3T9 EBI-28934478 0.35 Q9Y3C1 EBI-28934478 0.35 Q9Y3B9 EBI-28934478 0.35 Q9UKM9 EBI-28934478 0.35 Q9UKD2 EBI-28934478 0.35 Q9NW13 EBI-28934478 0.35 Q9NVP1 EBI-28934478 0.35 Q9NQ55 EBI-28934478 0.35 Q9H7B2 EBI-28934478 0.35 Q9H0A0 EBI-28934478 0.35 Q9GZR7 EBI-28934478 0.35 Q9BYG3 EBI-28934478 0.35 Q9BU76 EBI-28934478 0.35 Q9BRT6 EBI-28934478 0.35 Q99459 EBI-28934478 0.35 Q96SI9 EBI-28934478 0.35 Q96SB4 EBI-28934478 0.35 Q96KR1 EBI-28934478 0.35 Q96GQ7 EBI-28934478 0.35 Q96B26 EBI-28934478 0.35 Q8WTW3 EBI-28934478 0.35 Q8TDD1 EBI-28934478 0.35 Q8N9T8 EBI-28934478 0.35 Q8IZL8 EBI-28934478 0.35 Q1KMD3 EBI-28934478 0.35 Q15024 EBI-28934478 0.35 Q14690 EBI-28934478 0.35 Q14146 EBI-28934478 0.35 Q14137 EBI-28934478 0.35 Q13823 EBI-28934478 0.35 Q13523 EBI-28934478 0.35 Q12906 EBI-28934478 0.35 Q03701 EBI-28934478 0.35 Q01780 EBI-28934478 0.35 P55265 EBI-28934478 0.35 P51116 EBI-28934478 0.35 P30048 EBI-28934478 0.35 O95478 EBI-28934478 0.35 O75683 EBI-28934478 0.35 O60832 EBI-28934478 0.35 O60287 EBI-28934478 0.35 O43159 EBI-28934478 0.35 O15226 EBI-28934478 0.35 GO:0005737 GO:0005829 GO:0016020 GO:0005634 GO:0048471 GO:0005840 GO:0005524 GO:0003725 GO:0004694 GO:0042802 GO:0004715 GO:0004672 GO:0019888 GO:0106310 GO:0004674 GO:0003723 GO:0034198 GO:0051607 GO:0030968 GO:0045087 GO:0043066 GO:0008285 GO:0033689 GO:0017148 GO:0045071 GO:0032722 GO:0001819 GO:0043410 GO:0051092 GO:1901224 GO:0032874 GO:0046777 GO:0006468 GO:1901532 GO:1902036 GO:1902033 GO:1900225 GO:0035455 GO:0009615 GO:0006412 Unknown UniProt Sequence Analysis MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKKAVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAKRSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC 551 Q03963 Interferon-induced, Eif2ak2 10090 None SL-0198 Cytoplasm {ECO:0000250|UniProtKB:P19525}. Nucleus {ECO:0000250|UniProtKB:P19525}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P19525}. UNIPROT Q03963 UNIPROT Q61742 UNIPROT Q62026 PDB 1X48 PDB 1X49 Pfam PF00035 Pfam PF00069 PROSITE PS50137 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. P35569 EBI-2603482 0.40 P35570 EBI-2603524 0.44 Q8R4B8 EBI-15999088 0.52 Q9EPB4 EBI-15999182 0.40 GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0005524 GO:0003725 GO:0004694 GO:0042802 GO:0004715 GO:0004672 GO:0106310 GO:0034198 GO:0051607 GO:0030968 GO:0045087 GO:0043066 GO:0033689 GO:0017148 GO:0045071 GO:0043065 GO:0032722 GO:0001819 GO:0043410 GO:0051092 GO:1901224 GO:0032874 GO:0046777 GO:0006468 GO:1901532 GO:1902036 GO:1902033 GO:1900225 GO:0035455 GO:0032496 GO:0009636 GO:0009615 GO:0033197 GO:0006412 Unknown UniProt Sequence Analysis MASDTPGFYMDKLNKYRQMHGVAITYKELSTSGPPHDRRFTFQVLIDEKEFPEAKGRSKQEARNAAAKLAVDILDNENKVDCHTSASEQGLFVGNYIGLVNSFAQKKKLSVNYEQCEPNSELPQRFICKCKIGQTMYGTGSGVTKQEAKQLAAKEAYQKLLKSPPKTAGTSSSVVTSTFSGFSSSSSMTSNGVSQSAPGSFSSENVFTNGLGENKRKSGVKVSPDDVQRNKYTLDARFNSDFEDIEEIGLGGFGQVFKAKHRIDGKRYAIKRVKYNTEKAEHEVQALAELNHVNIVQYHSCWEGVDYDPEHSMSDTSRYKTRCLFIQMEFCDKGTLEQWMRNRNQSKVDKALILDLYEQIVTGVEYIHSKGLIHRDLKPGNIFLVDERHIKIGDFGLATALENDGKSRTRRTGTLQYMSPEQLFLKHYGKEVDIFALGLILAELLHTCFTESEKIKFFESLRKGDFSNDIFDNKEKSLLKKLLSEKPKDRPETSEILKTLAEWRNISEKKKRNTC 515 Q63184 Interferon-induced, Eif2ak2 10116 None SL-0198 Cytoplasm {ECO:0000250|UniProtKB:P19525}. Nucleus {ECO:0000250|UniProtKB:P19525}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P19525}. UNIPROT Q63184 Pfam PF00035 Pfam PF00069 PROSITE PS50137 PROSITE PS00107 PROSITE PS50011 PROSITE PS00108 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}. GO:0005737 GO:0005829 GO:0005634 GO:0048471 GO:0005524 GO:0003725 GO:0004694 GO:0042802 GO:0004715 GO:0004672 GO:0106310 GO:0034198 GO:0051607 GO:0030968 GO:0045087 GO:0043066 GO:0033689 GO:0017148 GO:0045071 GO:0043065 GO:0032722 GO:0001819 GO:0043410 GO:0051092 GO:1901224 GO:0032874 GO:0046777 GO:0006468 GO:1901532 GO:1902036 GO:1902033 GO:1900225 GO:0043330 GO:0035455 GO:0032496 GO:0009612 GO:0010033 GO:0009636 GO:0009615 GO:0033197 GO:0006412 Unknown UniProt Sequence Analysis MASDTPGFYVDKLNKYSQIHKVKIIYKEISVTGPPHDRRFTFQVIIEEREFPEGEGRSKQEAKNNAAKLAVEILDNENKVDSHTDASEQGLIEGNYIGLVNSFAQKENLPVNFELCDPDSQLPHRFICKCKIGQTTYGTGFGANKKEAKQLAAKNAYQKLSEKSPSKTGFVTSLSSDFSSSSSITSNSASQSASGRDFEDIFMNGLREKRKSGVKVPSDDVLRNKYTLDDRFSKDFEDIEEIGSGGFGQVFKAKHRIDGKTYAIKRITYNTKKAKREVQALAELNHANIVQYRVCWEGEDYDYDPENSTNGDTSRYKTRCLFIQMEFCDKGTLQQWLEKRNRSQEDKALVLELFEQIVTGVDYIHSKGLIHRDLKPGNIFLVDEKHIKIGDFGLATALENDGNPRTKYTGTPQYMSPEQKSSLVEYGKEVDIFALGLILAELLHICKTDSEKIEFFQLLRNGIFSDDIFDNKEKSLLQKLLSSKPRERPNTSEILKTLAEWKNISEKKKRNTC 513 P11317 Early E311 45659 None SL-0415 SL-0418 Host nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT P11317 GO:0044200 GO:0016021 Transmembrane UniProt Sequence Analysis {ECO:0000255} MILFQSNTTTSYAYTNIQPKYAMQLEITILIVIGILILSVILYFIFCRQIPNVHRNSKRRPIYSPMISRPHMALNEI 77 P17590 Early E311 28285 None SL-0415 SL-0418 Host nucleus membrane; Single-pass membrane protein. UNIPROT P17590 Pfam PF05393 GO:0044200 GO:0016021 Transmembrane UniProt Sequence Analysis {ECO:0000255} MTNTTNAAAATGLTSTTNTPQVSAFVNNWDNLGMWWFSIALMFVCLIIMWLICCLKRKRARPPIYSPIIVLHPNNDGIHRLDGLKHMFFSLTV 93 O55653 Early E311 10534 None SL-0415 SL-0418 Host nucleus membrane; Single-pass membrane protein. UNIPROT O55653 Pfam PF05393 GO:0044200 GO:0016021 Transmembrane UniProt Sequence Analysis {ECO:0000255} MTGSTIAPTTDYRNTTATGLKSALNLPQVHAFVNDWASLGMWWFSIALMFVCLIIMWLICCLKRRRARPPIYRPIIVLNPHNEKIHRLDGLKPCSLLLQYD 101 P17592 Early E311 10519 None SL-0415 SL-0418 Host nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. UNIPROT P17592 GO:0044200 GO:0016021 Transmembrane UniProt Sequence Analysis {ECO:0000255} MILFQSNTTNTINVQTTLNHDMENHTTSYAYINIQPKYAMHLKITILIVIGILILSVILYFLFSYD 66 Q60490 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase EBP 10141 None SL-0178 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}. UNIPROT Q60490 UNIPROT Q9QV23 PROSITE PS51751 Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000250|UniProtKB:Q15125}. GO:0031410 GO:0005783 GO:0005789 GO:0016021 GO:0043231 GO:0005635 GO:0000247 GO:0047750 GO:0042802 GO:0004769 GO:0006695 GO:0030097 GO:0043931 Transmembrane UniProt Sequence Analysis {ECO:0000255} MATTSTGPLHPYWPRHLRLDHFVPNDLSAWYIVTVLFTVFGALVVTMWLLSSRASVVPLGTWRRLSVCWFAVCAFVHLVIEGWFVLYQKAILGDQAFLSQLWKEYAKGDSRYIIEDNFIICMESITVVLWGPLSLWAVIAFLRQHPSRYVLQFVISLGQIYGDLLYFLTEYRDGFQHGEMGHPIYFWFYFFFMNVLWLVIPGVLFFDSVKQFYGAQNALDTKVMKSKGK 229 Q15125 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase EBP 9606 None SL-0178 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}. UNIPROT Q15125 UNIPROT Q6FGL3 UNIPROT Q6IBI9 PDB 6OHT PDB 6OHU PROSITE PS51751 OMIM 300205 OMIM 300960 OMIM 302960 DisGeNET 10682 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}. 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. A0A142I5B9 EBI-20626314 0.35 A0PK00 EBI-24669908 0.56 P0DTD1 EBI-25686067 0.35 Q05397 EBI-20903608 0.40 O75030 EBI-3915259 0.37 Q9WMX2 EBI-9083439 0.37 Q9Z1B5 EBI-10996176 0.35 P14625 EBI-11044830 0.35 Q92542 EBI-11046886 0.35 O75446 EBI-11060854 0.35 Q8BGH2 EBI-11097023 0.35 Q9R0Q3 EBI-11111571 0.35 Q8K1S6 EBI-11147685 0.35 Q6NUS6 EBI-11368748 0.27 Q96GX1 EBI-11375285 0.27 P49286 EBI-11576336 0.37 P27105 EBI-12452286 0.51 Q5T700 EBI-24310594 0.56 Q8WWP7 EBI-24268159 0.56 P02724 EBI-22752401 0.56 Q8IXM6 EBI-22753239 0.56 Q9BXJ8 EBI-22754310 0.56 Q8IWU4 EBI-22754620 0.56 Q9BWM7 EBI-22754569 0.56 Q6UX98 EBI-24270634 0.56 O95167 EBI-24271223 0.56 P23141 EBI-22757994 0.56 Q08426 EBI-22758661 0.56 Q9NVC3 EBI-22759787 0.56 Q6P1K1 EBI-22760233 0.56 Q9H2L4 EBI-24272883 0.56 Q96G79 EBI-22760053 0.56 Q96BA8 EBI-24631155 0.56 Q96GQ5 EBI-24659828 0.56 Q9NRX6 EBI-24660186 0.56 Q3SXY8 EBI-23669642 0.56 Q9BU79 EBI-24661627 0.56 Q9NZG7 EBI-24663072 0.56 P23763 EBI-24664214 0.56 P63027 EBI-24667622 0.56 Q9Y385 EBI-24670704 0.56 P01031 EBI-23688881 0.56 A5PKU2 EBI-24671905 0.56 Q13190 EBI-24673341 0.56 Q96CP7 EBI-24673683 0.56 O75396 EBI-24674462 0.56 B2RUZ4 EBI-24675325 0.56 O43759 EBI-24676164 0.56 P81534 EBI-24677503 0.56 Q8TBM7 EBI-24681654 0.56 O14653 EBI-24684144 0.56 P07204 EBI-24684847 0.56 Q8N2H4 EBI-24685442 0.56 Q9Y342 EBI-24686559 0.56 Q7Z4F1 EBI-23718808 0.56 P43378 EBI-24688841 0.56 P17152 EBI-24690030 0.56 O95870 EBI-24690968 0.56 Q8N6S5 EBI-24694418 0.56 Q9NV29 EBI-24695294 0.56 Q16873 EBI-23732251 0.56 Q96BZ9 EBI-24696326 0.56 P30519 EBI-23733774 0.56 Q9NW97 EBI-24698352 0.56 Q9Y6X1 EBI-24698993 0.56 Q96LL9 EBI-24699507 0.56 Q86Y82 EBI-24702845 0.56 Q92982 EBI-24703744 0.56 P49447 EBI-24704221 0.56 Q8N2M4 EBI-24706015 0.56 Q8N8N0 EBI-24705925 0.56 Q8NBD8 EBI-24706316 0.56 Q8TD22 EBI-24707774 0.56 Q9UGM5 EBI-24708280 0.56 O75379 EBI-24711580 0.56 Q9HD20 EBI-24716721 0.56 Q8TDT2 EBI-24716697 0.56 Q969S6 EBI-24716998 0.56 O95452 EBI-24717966 0.56 Q6ZSS7 EBI-24719764 0.56 Q96F15 EBI-23774914 0.56 Q9Y282 EBI-24721575 0.56 Q969E2 EBI-24722338 0.56 Q9BZL3 EBI-24722570 0.56 Q15125 EBI-24723056 0.56 Q9Y5Z9 EBI-24725377 0.56 O15400 EBI-23784204 0.56 O43169 EBI-23784333 0.56 O14925 EBI-24728082 0.56 Q12983 EBI-24729517 0.56 Q15836 EBI-24730650 0.56 P50281 EBI-24732670 0.56 Q9BSR8 EBI-24732968 0.56 Q9UNK0 EBI-24732900 0.56 Q9P0L0 EBI-24733627 0.56 Q8N661 EBI-24733842 0.56 Q13520 EBI-23803453 0.56 Q9NUH8 EBI-24740093 0.56 Q5BJF2 EBI-24740501 0.56 Q9NV12 EBI-24747854 0.56 Q7Z5P4 EBI-23821019 0.56 Q9NRQ5 EBI-24750511 0.56 Q96EC8 EBI-24751251 0.56 Q6PI78 EBI-24752570 0.56 Q7L5A8 EBI-24753438 0.56 Q8NHS1 EBI-24753392 0.56 Q9NWH2 EBI-24756813 0.56 Q9NX14 EBI-24756945 0.56 Q9BTX3 EBI-24763251 0.56 P60033 EBI-24764608 0.56 Q9BVK8 EBI-24764734 0.56 Q9H1M4 EBI-24765471 0.56 Q9UHE5 EBI-24765482 0.56 Q9P0S3 EBI-24766077 0.56 Q9UKR5 EBI-24767459 0.56 A2RU14 EBI-24768914 0.56 Q68G75 EBI-24769184 0.56 Q86W74 EBI-24769830 0.56 Q9H2C2 EBI-24779387 0.56 Q04941 EBI-24781694 0.56 Q9H1C4 EBI-24782065 0.56 O95393 EBI-24782166 0.56 Q9Y5U4 EBI-24782454 0.56 Q9H0R3 EBI-24783086 0.56 O14523 EBI-24783925 0.56 Q9NTJ5 EBI-24784958 0.56 Q16617 EBI-24785619 0.56 Q8WW34 EBI-24786375 0.56 P61266 EBI-24787698 0.56 Q9P0B6 EBI-24795437 0.56 Q14318 EBI-24797367 0.56 Q96IV6 EBI-24797582 0.56 P25942 EBI-23911966 0.56 Q2M3R5 EBI-25279560 0.56 Q9BV81 EBI-25282644 0.56 P08195 EBI-25283560 0.56 Q9Y548 EBI-25283492 0.56 Q53HI1 EBI-23922913 0.56 Q9BWH2 EBI-25286529 0.56 Q96AG4 EBI-24548327 0.56 Q07108 EBI-24594671 0.56 Q8N138 EBI-24641145 0.56 Q8N511 EBI-25145474 0.56 Q53FV1 EBI-24641826 0.56 Q8NHW4 EBI-24642201 0.56 P15151 EBI-24644197 0.56 Q8WVV5 EBI-24646926 0.56 P54849 EBI-24647331 0.56 Q8IY26 EBI-24647840 0.56 Q9NSU2 EBI-24652174 0.56 Q99519 EBI-24652828 0.56 Q01453 EBI-24654227 0.56 P55061 EBI-24654827 0.56 Q8WVX3 EBI-24654804 0.56 Q9Y5U9 EBI-24656328 0.56 Q6UX34 EBI-24657064 0.56 P57105 EBI-24659444 0.56 Q96JW4 EBI-24746616 0.56 Q5JX71 EBI-24758742 0.56 Q5TGU0 EBI-24762253 0.56 Q14802 EBI-24774166 0.56 A0AVG3 EBI-24776609 0.56 Q9NZ43 EBI-24789687 0.56 Q7L5N7 EBI-24790934 0.56 Q0VAQ4 EBI-24790824 0.56 Q96MV1 EBI-25203477 0.56 Q5J8X5 EBI-24791226 0.56 Q8N6R1 EBI-25205775 0.56 O95070 EBI-24799738 0.56 P54315 EBI-24800746 0.56 Q69YG0 EBI-24801451 0.56 P29033 EBI-24803571 0.56 Q9P0S9 EBI-25216661 0.56 Q6UWT4 EBI-24806821 0.56 O95292 EBI-24808346 0.56 Q2M2E3 EBI-25223826 0.56 O14735 EBI-24810822 0.56 Q9H9P2 EBI-24810960 0.56 P06681 EBI-25266575 0.56 O43752 EBI-25266516 0.56 Q5QGT7 EBI-25268527 0.56 P78329 EBI-25269159 0.56 Q8N5M9 EBI-25270965 0.56 Q9H0Q3 EBI-25273560 0.56 O95159 EBI-25273227 0.56 Q9Y3D6 EBI-25274191 0.56 Q7RTS5 EBI-25274864 0.56 O43889 EBI-12701192 0.56 Q8IWL3 EBI-13943458 0.35 Q8IVT5 EBI-14035152 0.35 Q99679 EBI-21516430 0.35 P06028 EBI-21557067 0.35 P35414 EBI-21559824 0.35 Q8TD20 EBI-21562097 0.35 P41587 EBI-21567910 0.35 Q8NHX9 EBI-21578009 0.35 O95274 EBI-21607810 0.35 P32241 EBI-21613594 0.35 Q9H244 EBI-21614520 0.35 Q9H2J7 EBI-21614809 0.35 Q9ULW2 EBI-21704037 0.35 Q00765 EBI-21723128 0.35 P46098 EBI-21749232 0.35 Q96G97 EBI-21755399 0.35 P25101 EBI-21755472 0.35 Q9Y2T5 EBI-21760939 0.35 Q53R12 EBI-21829296 0.35 P04899 EBI-21830586 0.40 Q8NHS3 EBI-21887118 0.35 P05161 EBI-16720078 0.35 P05067 EBI-20769256 0.37 Q12816 EBI-20904848 0.40 Q5S007 EBI-21360986 0.35 P13569 EBI-25416349 0.35 Q5T9L3 EBI-22085230 0.49 GO:0031410 GO:0005783 GO:0005789 GO:0030176 GO:0005635 GO:0000247 GO:0047750 GO:0042802 GO:0004769 GO:0006695 GO:0033489 GO:0033490 GO:0008203 GO:0030097 GO:0043931 GO:0016126 Transmembrane UniProt Sequence Analysis {ECO:0000255} MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN 230 P70245 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase Ebp 10090 None SL-0178 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}. UNIPROT P70245 UNIPROT Q9CSP4 PROSITE PS51751 Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000269|PubMed:8798407}. 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. GO:0031410 GO:0005783 GO:0005789 GO:0016021 GO:0043231 GO:0005635 GO:0000247 GO:0047750 GO:0042802 GO:0004769 GO:0006695 GO:0008203 GO:0030097 GO:0043931 GO:0016126 Transmembrane UniProt Sequence Analysis {ECO:0000255} MTTNTVPLHPYWPRHLKLDNFVPNDLPTSHILVGLFSISGGLIVITWLLSSRASVVPLGAGRRLALCWFAVCTFIHLVIEGWFSLYNGILLEDQAFLSQLWKEYSKGDSRYILSDSFVVCMETVTACLWGPLSLWVVIAFLRQQPFRFVLQLVVSMGQIYGDVLYFLTELHEGLQHGEIGHPVYFWFYFVFLNAVWLVIPSILVLDAIKHLTSAQSVLDSKVMKIKSKHN 230 Q9JJ46 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase Ebp 10116 None SL-0178 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}. UNIPROT Q9JJ46 UNIPROT Q548M8 PROSITE PS51751 Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000269|PubMed:11171067}. GO:0031410 GO:0005783 GO:0005789 GO:0016021 GO:0043231 GO:0005635 GO:0000247 GO:0047750 GO:0042802 GO:0004769 GO:0006695 GO:0008203 GO:0030097 GO:0043931 GO:0016126 Transmembrane UniProt Sequence Analysis {ECO:0000255} MTTNMLPLHPYWPRHLRLDNFVPNDLPTWHILVGLFSFSGVLIVITWLLSSRVSVVPLGTGRRLALCWFAVCTFIHLVIEGWFSFYHEILLEDQAFLSQLWKEYSKGDSRYILSDGFIVCMESVTACLWGPLSLWVVIAFLRHQPFRFVLQLVVSVGQIYGDVLYFLTELRDGFQHGELGHPLYFWFYFVIMNAIWLVIPGILVFDAIKHLTNAQSMLDNKVMKIKSKHN 230 Q8GTY0 Elongation A4 3702 None SL-0198 Cytoplasm {ECO:0000269|PubMed:21245040}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21245040}. UNIPROT Q8GTY0 UNIPROT P13905 UNIPROT Q0WSD5 UNIPROT Q39093 UNIPROT Q9C5L4 Pfam PF00009 Pfam PF03144 Pfam PF03143 PROSITE PS00301 PROSITE PS51722 This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. Q03250 EBI-8801785 0.35 GO:0005737 GO:0005739 GO:0005634 GO:0048471 GO:0000325 GO:0005886 GO:0009506 GO:0005525 GO:0003924 GO:0003729 GO:0003746 GO:0006412 GO:0006414 Unknown UniProt Sequence Analysis MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKDPTGAKVTKAAVKKGAK 449 Q17902 Egalitarian egal 6239 None SL-0178 Nucleus envelope {ECO:0000305|PubMed:20005871}. Note=Probably recruited to the nuclear envelope by unc-83. {ECO:0000305|PubMed:20005871}. UNIPROT Q17902 UNIPROT Q65ZH5 Pfam PF01612 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}. Q22799 EBI-2413132 0.75 V6CJ04 EBI-2903351 0.51 GO:0005875 GO:0005635 GO:1990923 GO:0008408 GO:0003676 GO:0031047 GO:0030473 GO:0034587 Unknown UniProt Sequence Analysis MEEAKNMALLFFMDHLMQKNGRRTIHDLSCQFGARGFSEEMRNAVGTTQEGLTEFLQGHPSLFTVEGDQVILNGHNDLNAKNNPLLQSGIRSRNYEKEAVDFFVTKLTKFGPELQIKSLLGHRSQAAPEVRLVSGRHLKEFCEFLQSQVDYFVVEGDRVRLKNMPEPDENAIEMDDEGRPLAGVKAKQAAVEYLKSVLEQNEDQPIPLDQFYQNFCQRFSHTIRQDVATNPKELLQFLKLNRGLFFIRSNKVSLVKNRLNEDGSENGSDEGEETNNNGMFPLDQSALTRIHFVKALKPAQDLISRLWQDINNMEKKVVGLDLKTVTVGVDGEIFLSLGVIATTSQIGIFDLASSDVIILESGFKGILESEKVVKVIHDARRVASLLAHKYAVHMRNVFDTQVAHSLLQHEKFNKSLNEMRPISFINLQRVYYPQSIMLSDVTPRKMSMCPNWGVRPITEEFQLTIVEEAHCLLSALYQSLSNLIPVHLRGVFEDKCIEVNHPEVLLASPNRPPPQPFISSPYRASTRRDVRNGGSIMQSFSPAPYAAAPRPQMSDACTQTFSTGDIEVLNVFYE 574 P13387 Epidermal EGFR 9031 None SL-0178 SL-0182 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}. UNIPROT P13387 Pfam PF00757 Pfam PF14843 Pfam PF01030 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}. GO:0005789 GO:0010008 GO:0000139 GO:0016021 GO:0031965 GO:0005634 GO:0005886 GO:0005524 GO:0004713 GO:0004714 GO:0071364 GO:0007173 GO:0007611 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGVRSPLSASGPRGAAVLVLLLLGVALCSAVEEKKVCQGTNNKLTQLGHVEDHFTSLQRMYNNCEVVLSNLEITYVEHNRDLTFLKTIQEVAGYVLIALNMVDVIPLENLQIIRGNVLYDNSFALAVLSNYHMNKTQGLRELPMKRLSEILNGGVKISNNPKLCNMDTVLWNDIIDTSRKPLTVLDFASNLSSCPKCHPNCTEDHCWGAGEQNCQTLTKVICAQQCSGRCRGKVPSDCCHNQCAAGCTGPRESDCLACRKFRDDATCKDTCPPLVLYNPTTYQMDVNPEGKYSFGATCVRECPHNYVVTDHGSCVRSCNTDTYEVEENGVRKCKKCDGLCSKVCNGIGIGELKGILSINATNIDSFKNCTKINGDVSILPVAFLGDAFTKTLPLDPKKLDVFRTVKEISGFLLIQAWPDNATDLYAFENLEIIRGRTKQHGQYSLAVVNLKIQSLGLRSLKEISDGDIAIMKNKNLCYADTMNWRSLFATQSQKTKIIQNRNKNDCTADRHVCDPLCSDVGCWGPGPFHCFSCRFFSRQKECVKQCNILQGEPREFERDSKCLPCHSECLVQNSTAYNTTCSGPGPDHCMKCAHFIDGPHCVKACPAGVLGENDTLVWKYADANAVCQLCHPNCTRGCKGPGLEGCPNGSKTPSIAAGVVGGLLCLVVVGLGIGLYLRRRHIVRKRTLRRLLQERELVEPLTP 703 P00533 Epidermal EGFR 9606 None SL-0178 SL-0182 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. UNIPROT P00533 UNIPROT O00688 UNIPROT O00732 UNIPROT P06268 UNIPROT Q14225 UNIPROT Q68GS5 UNIPROT Q92795 UNIPROT Q9BZS2 UNIPROT Q9GZX1 UNIPROT Q9H2C9 UNIPROT Q9H3C9 UNIPROT Q9UMD7 UNIPROT Q9UMD8 UNIPROT Q9UMG5 PDB 1IVO PDB 1M14 PDB 1M17 PDB 1MOX PDB 1NQL PDB 1XKK PDB 1YY9 PDB 1Z9I PDB 2EB2 PDB 2EB3 PDB 2GS2 PDB 2GS6 PDB 2GS7 PDB 2ITN PDB 2ITO PDB 2ITP PDB 2ITQ PDB 2ITT PDB 2ITU PDB 2ITV PDB 2ITW PDB 2ITX PDB 2ITY PDB 2ITZ PDB 2J5E PDB 2J5F PDB 2J6M PDB 2JIT PDB 2JIU PDB 2JIV PDB 2KS1 PDB 2M0B PDB 2M20 PDB 2N5S PDB 2RF9 PDB 2RFD PDB 2RFE PDB 2RGP PDB 3B2U PDB 3B2V PDB 3BEL PDB 3BUO PDB 3C09 PDB 3G5V PDB 3G5Y PDB 3GOP PDB 3GT8 PDB 3IKA PDB 3LZB PDB 3NJP PDB 3OB2 PDB 3OP0 PDB 3P0Y PDB 3PFV PDB 3POZ PDB 3QWQ PDB 3UG1 PDB 3UG2 PDB 3VJN PDB 3VJO PDB 3VRP PDB 3VRR PDB 3W2O PDB 3W2P PDB 3W2Q PDB 3W2R PDB 3W2S PDB 3W32 PDB 3W33 PDB 4G5J PDB 4G5P PDB 4HJO PDB 4I1Z PDB 4I20 PDB 4I21 PDB 4I22 PDB 4I23 PDB 4I24 PDB 4JQ7 PDB 4JQ8 PDB 4JR3 PDB 4JRV PDB 4KRL PDB 4KRM PDB 4KRO PDB 4KRP PDB 4LI5 PDB 4LL0 PDB 4LQM PDB 4LRM PDB 4R3P PDB 4R3R PDB 4R5S PDB 4RIW PDB 4RIX PDB 4RIY PDB 4RJ4 PDB 4RJ5 PDB 4RJ6 PDB 4RJ7 PDB 4RJ8 PDB 4TKS PDB 4UIP PDB 4UV7 PDB 4WD5 PDB 4WKQ PDB 4WRG PDB 4ZAU PDB 4ZJV PDB 4ZSE PDB 5C8K PDB 5C8M PDB 5C8N PDB 5CAL PDB 5CAN PDB 5CAO PDB 5CAP PDB 5CAQ PDB 5CAS PDB 5CAU PDB 5CAV PDB 5CNN PDB 5CNO PDB 5CZH PDB 5CZI PDB 5D41 PDB 5EDP PDB 5EDQ PDB 5EDR PDB 5EM5 PDB 5EM6 PDB 5EM7 PDB 5EM8 PDB 5FED PDB 5FEE PDB 5FEQ PDB 5GMP PDB 5GNK PDB 5GTY PDB 5GTZ PDB 5HCX PDB 5HCY PDB 5HCZ PDB 5HG5 PDB 5HG7 PDB 5HG8 PDB 5HG9 PDB 5HIB PDB 5HIC PDB 5J9Y PDB 5J9Z PDB 5JEB PDB 5LV6 PDB 5SX4 PDB 5SX5 PDB 5U8L PDB 5UG8 PDB 5UG9 PDB 5UGA PDB 5UGB PDB 5UGC PDB 5UWD PDB 5WB7 PDB 5WB8 PDB 5X26 PDB 5X27 PDB 5X28 PDB 5X2A PDB 5X2C PDB 5X2F PDB 5X2K PDB 5XDK PDB 5XDL PDB 5XGM PDB 5XGN PDB 5XWD PDB 5Y25 PDB 5Y9T PDB 5YU9 PDB 5ZTO PDB 5ZWJ PDB 6ARU PDB 6B3S PDB 6D8E PDB 6DUK PDB 6JRJ PDB 6JRK PDB 6JRX PDB 6JWL PDB 6JX0 PDB 6JX4 PDB 6JXT PDB 6JZ0 PDB 6LUB PDB 6LUD PDB 6P1D PDB 6P1L PDB 6P8Q PDB 6S89 PDB 6S8A PDB 6S9B PDB 6S9C PDB 6S9D PDB 6TFU PDB 6TFV PDB 6TFW PDB 6TFY PDB 6TFZ PDB 6TG0 PDB 6TG1 PDB 6V5N PDB 6V5P PDB 6V66 PDB 6V6K PDB 6V6O PDB 6VH4 PDB 6VHN PDB 6VHP PDB 6WA2 PDB 6WAK PDB 6WXN PDB 6XL4 PDB 6Z4B PDB 6Z4D PDB 7A2A PDB 7A6I PDB 7A6J PDB 7A6K PDB 7AEI PDB 7AEM PDB 7B85 PDB 7JXI PDB 7JXK PDB 7JXL PDB 7JXM PDB 7JXP PDB 7JXQ PDB 7JXW PDB 7K1H PDB 7K1I PDB 7KXZ PDB 7KY0 PDB 7LEN PDB 7LFR PDB 7LFS PDB 7LG8 PDB 7LGS PDB 7LTX PDB 7OM4 PDB 7OXB PDB 7SYD PDB 7SYE PDB 7SZ0 PDB 7SZ1 PDB 7SZ5 PDB 7SZ7 PDB 7TVD Pfam PF00757 Pfam PF14843 Pfam PF07714 Pfam PF01030 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 OMIM 131550 OMIM 211980 OMIM 616069 DisGeNET 1956 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}. 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. D4A631 EBI-22084260 0.35 O43707 EBI-9689686 0.55 O60645 EBI-10764491 0.40 O75694 EBI-32720286 0.27 O94875 EBI-4397010 0.55 O96018 EBI-7877395 0.44 P00519 EBI-7887814 0.69 P22681 EBI-8682709 0.96 P29353 EBI-8682733 0.98 P27986 EBI-8682765 0.81 P16333 EBI-8682777 0.82 P62994 EBI-8682799 0.56 P15941 EBI-7913778 0.82 Q99962 EBI-8173591 0.68 Q96B97 EBI-8173605 0.69 Q13322 EBI-8679878 0.73 P62993 EBI-297464 0.98 P68431 EBI-298046 0.27 P13987 EBI-298103 0.44 P98083 EBI-370958 0.40 P63104 EBI-446460 0.77 Q17R13 EBI-457635 0.35 P04083 EBI-7411482 0.77 P25098 EBI-7436130 0.46 Q06124 EBI-8533094 0.82 O75368 EBI-8533072 0.68 P51692 EBI-8533286 0.40 P46109 EBI-8533556 0.75 P41240 EBI-8533610 0.68 P01133 EBI-640874 0.97 P22682 EBI-640915 0.50 O00750 EBI-641139 0.81 O00443 EBI-641139 0.35 O43147 EBI-733199 0.00 P36542 EBI-733962 0.00 Q8WUM4 EBI-7397470 0.68 P02533 EBI-702075 0.35 Q03135 EBI-702075 0.81 P10809 EBI-702075 0.35 P31689 EBI-702075 0.35 P68104 EBI-702075 0.35 P08238 EBI-702075 0.89 Q99959 EBI-702075 0.48 P38646 EBI-702075 0.75 Q04695 EBI-702075 0.35 P11021 EBI-702075 0.53 P13647 EBI-702075 0.35 P05141 EBI-702075 0.35 P10412 EBI-702075 0.35 P31943 EBI-702075 0.53 P11142 EBI-702075 0.80 Q14289 EBI-702075 0.35 P29317 EBI-702075 0.48 Q9NR50 EBI-702075 0.35 Q96EY1 EBI-702075 0.35 P40855 EBI-702075 0.35 P61978 EBI-702075 0.35 Q05397 EBI-702075 0.75 Q71U36 EBI-702075 0.75 P02538 EBI-702075 0.35 P10599 EBI-702075 0.79 P49023 EBI-702075 0.35 P62807 EBI-702075 0.35 P52597 EBI-702075 0.35 P04264 EBI-702075 0.35 Q14974 EBI-702075 0.35 P98172 EBI-702075 0.35 Q13191 EBI-702075 0.35 P06493 EBI-702075 0.67 P16615 EBI-702075 0.64 P35221 EBI-702075 0.68 P40763 EBI-702075 0.92 P04792 EBI-702075 0.61 P62258 EBI-702075 0.35 O60716 EBI-702075 0.75 P27348 EBI-702075 0.85 Q14192 EBI-702075 0.35 P04626 EBI-702075 0.95 P31947 EBI-702075 0.83 P31949 EBI-702075 0.35 P07947 EBI-702075 0.56 Q07065 EBI-702075 0.35 Q9UBB4 EBI-702075 0.35 Q14134 EBI-702075 0.35 P08195 EBI-702075 0.64 Q96AG4 EBI-702075 0.35 Q9H5V8 EBI-702075 0.35 Q07912 EBI-702075 0.35 O75815 EBI-702075 0.35 Q969Z0 EBI-702075 0.35 P06576 EBI-702075 0.35 O43592 EBI-702075 0.53 P54760 EBI-702075 0.35 P0CG47 EBI-702075 0.35 P08107 EBI-702075 0.80 O60884 EBI-702075 0.53 Q00325 EBI-702075 0.53 P55060 EBI-702075 0.53 P56945 EBI-702075 0.35 P07437 EBI-702075 0.35 Q8IZV2 EBI-7868933 0.56 P42684 EBI-7874891 0.69 Q96D37 EBI-7875378 0.44 Q9Y490 EBI-7875422 0.44 P43405 EBI-7875448 0.44 Q92529 EBI-7875536 0.44 P20936 EBI-7875605 0.44 P19174 EBI-7875736 0.85 Q92569 EBI-7875764 0.76 O00459 EBI-7875895 0.76 P49757 EBI-7876086 0.57 Q13387 EBI-7876156 0.69 Q9UQF2 EBI-7876199 0.44 O60674 EBI-7876243 0.44 O14654 EBI-7876269 0.44 Q7Z6G8 EBI-7876386 0.44 P98077 EBI-7876430 0.44 Q6PKX4 EBI-7876474 0.44 Q9P104 EBI-7876593 0.44 Q8TEW6 EBI-7876742 0.44 Q8IZW8 EBI-7876785 0.44 P46108 EBI-7876865 0.69 Q9UKG1 EBI-7876909 0.57 O95704 EBI-7877048 0.44 Q92870 EBI-7877108 0.74 Q92625 EBI-7877154 0.79 O00213 EBI-7877304 0.44 Q9NP31 EBI-7879463 0.44 O60880 EBI-7879502 0.44 Q9NRF2 EBI-7879524 0.77 Q13882 EBI-7879563 0.44 P16885 EBI-7879602 0.79 Q7Z7G1 EBI-7879641 0.44 Q9UQQ2 EBI-7879742 0.44 P51451 EBI-7883080 0.69 Q13239 EBI-7887945 0.69 Q8WYP3 EBI-7888049 0.44 Q9Y6R0 EBI-7888501 0.57 P35568 EBI-7888870 0.44 P07332 EBI-7888914 0.44 Q9NSE2 EBI-7889043 0.74 P43403 EBI-7889327 0.69 P51813 EBI-7890778 0.44 P21860 EBI-875451 0.91 Q15303 EBI-875456 0.56 P42566 EBI-921718 0.35 Q9UJ41 EBI-921718 0.60 P00533 EBI-970714 0.98 Q9UQC2 EBI-975219 0.67 P01135 EBI-1034394 0.78 O60603 EBI-7127435 0.68 O00206 EBI-7127511 0.40 P09496 EBI-1188138 0.35 P05026 EBI-1188138 0.35 P68366 EBI-1188138 0.53 P53675 EBI-1188138 0.35 Q13740 EBI-1188138 0.35 P04406 EBI-1188138 0.79 Q9NYD6 EBI-1188138 0.35 P51636 EBI-1188138 0.67 P05362 EBI-1188138 0.35 P55735 EBI-1188138 0.35 P06702 EBI-1188138 0.35 P05023 EBI-1188138 0.35 P07948 EBI-1188138 0.82 P62158 EBI-1188138 0.83 P0A0I7 EBI-7213556 0.46 P62157 EBI-1256868 0.40 Q29376 EBI-1256888 0.44 P62161 EBI-1256912 0.52 P62204 EBI-1256994 0.40 P03372 EBI-4309290 0.52 P12931 EBI-7248693 0.90 Q62245 EBI-8661857 0.40 Q60631 EBI-8664380 0.35 P13866 EBI-1772419 0.52 P20417 EBI-8608593 0.80 P18031 EBI-8629259 0.90 O75886 EBI-2119941 0.58 Q13671 EBI-2119957 0.46 P08575 EBI-25369712 0.59 P23467 EBI-20976986 0.69 Q12913 EBI-2264953 0.00 Q8K424 EBI-2650756 0.40 Q5NEB4 EBI-2807083 0.00 A0A6L7H280 EBI-2834648 0.00 Q8ZE20 EBI-2870787 0.00 O75674 EBI-7270434 0.56 P52294 EBI-8109298 0.40 P08581 EBI-2927740 0.80 P42224 EBI-8478938 0.77 P06240 EBI-8638762 0.35 P52735 EBI-8565016 0.35 P29350 EBI-8683880 0.55 O75165 EBI-8631408 0.27 P11279 EBI-8631521 0.43 Q00944 EBI-3953289 0.44 Q05209 EBI-3952087 0.81 P17931 EBI-3989365 0.40 P13693 EBI-4303426 0.40 Q13480 EBI-4303473 0.74 P06396 EBI-5235004 0.55 O15511 EBI-5234978 0.55 Q9H299 EBI-5234886 0.55 Q15819 EBI-4397413 0.55 Q15005 EBI-4397397 0.55 Q14204 EBI-4397381 0.55 Q12852 EBI-4397329 0.62 Q06830 EBI-4397313 0.55 Q02952 EBI-4397297 0.63 Q02790 EBI-4397289 0.55 Q02246 EBI-4397281 0.55 P60520 EBI-4397232 0.63 P60174 EBI-4397224 0.55 P54368 EBI-4397208 0.55 P43243 EBI-4397192 0.55 P40925 EBI-4397176 0.55 P34932 EBI-4397168 0.67 P31948 EBI-4397160 0.63 P31939 EBI-4397152 0.55 P26641 EBI-4397136 0.55 P23528 EBI-4397128 0.67 P20336 EBI-4397112 0.55 P17174 EBI-4397104 0.55 P16930 EBI-4397074 0.55 P14625 EBI-4397058 0.55 P06132 EBI-4397042 0.55 P04075 EBI-4397034 0.55 O95433 EBI-4397026 0.55 O94992 EBI-4397018 0.55 O00170 EBI-5324173 0.55 Q9Y2H9 EBI-4397860 0.63 Q9UNE7 EBI-4397844 0.72 Q9P0L0 EBI-4397828 0.71 Q99784 EBI-4397783 0.55 Q96CW1 EBI-4397767 0.77 Q92733 EBI-4397759 0.55 Q8N4S1 EBI-4397712 0.37 Q8N111 EBI-4397696 0.55 A4FU49 EBI-4397659 0.55 P17600 EBI-4397603 0.55 Q59GR8 EBI-4397580 0.55 Q6UWJ1 EBI-4397688 0.55 Q59EJ3 EBI-4397553 0.55 P53041 EBI-4397535 0.55 Q16186 EBI-4397421 0.55 Q15120 EBI-4397405 0.55 Q14318 EBI-4397389 0.68 Q14050 EBI-4397373 0.55 Q13561 EBI-4397365 0.55 Q13491 EBI-4397337 0.55 Q09666 EBI-4397321 0.67 P62330 EBI-4397240 0.55 P55036 EBI-4397216 0.55 P49908 EBI-4397200 0.55 P41222 EBI-4397184 0.55 P31321 EBI-4397144 0.55 P16152 EBI-4397066 0.55 P21291 EBI-4397120 0.55 P09936 EBI-4397050 0.63 O14818 EBI-4396992 0.55 O75095 EBI-4397001 0.55 Q9Y3A3 EBI-4397868 0.55 Q9Y237 EBI-4397852 0.55 Q9UBN7 EBI-4397836 0.81 Q96AD5 EBI-4397820 0.55 Q9NNZ3 EBI-4397812 0.55 Q99608 EBI-4397775 0.55 Q8TDB4 EBI-4397733 0.55 Q8N2Y8 EBI-4397704 0.55 Q7L273 EBI-4397611 0.55 P07900 EBI-4397595 0.78 Q59G22 EBI-4397572 0.55 Q53GZ6 EBI-4397527 0.55 P60880 EBI-4397510 0.55 P52306 EBI-4397490 0.55 Q4KWH8 EBI-4397437 0.55 O95782 EBI-4397884 0.67 P02751 EBI-4398148 0.40 P46940 EBI-5465302 0.63 Q01973 EBI-6082648 0.58 Q9H267 EBI-7913457 0.27 Q15075 EBI-8051513 0.43 P12830 EBI-6592813 0.74 P01100 EBI-6593803 0.27 P08631 EBI-6599779 0.65 Q16539 EBI-6600298 0.27 P33992 EBI-6870068 0.35 P33993 EBI-6870068 0.35 P50281 EBI-8769968 0.35 P63010 EBI-8769968 0.57 Q8TF42 EBI-8769968 0.60 Q9UBS4 EBI-8769968 0.57 O75223 EBI-8769968 0.35 P62701 EBI-8769968 0.35 P62269 EBI-8769968 0.35 P34931 EBI-8769968 0.35 P54652 EBI-8769968 0.35 P01040 EBI-8769968 0.35 P62805 EBI-8769968 0.35 Q75V66 EBI-8769968 0.35 O95155 EBI-8769968 0.35 Q01469 EBI-8769968 0.35 Q92832 EBI-8769968 0.35 Q6UWL2 EBI-8769968 0.35 P25705 EBI-8769968 0.35 Q8N163 EBI-8769968 0.35 Q13098 EBI-8769968 0.35 Q9UJM3 EBI-8769968 0.87 P49411 EBI-8769968 0.35 Q8WV24 EBI-8770081 0.35 P10586 EBI-8770081 0.55 Q9BYJ9 EBI-8770081 0.35 Q92522 EBI-8770081 0.35 P53680 EBI-8770081 0.57 P62841 EBI-8770081 0.35 Q96JX3 EBI-8770081 0.35 P30711 EBI-8770081 0.35 P48594 EBI-8770081 0.35 Q96QV6 EBI-8770081 0.35 P23634 EBI-8770081 0.35 Q01650 EBI-8770081 0.35 P35321 EBI-8770081 0.35 P18621 EBI-8770081 0.35 P23246 EBI-8770081 0.35 P01892 EBI-8770081 0.35 Q5JNZ5 EBI-8770081 0.35 Q10567 EBI-8770081 0.65 P26232 EBI-8770081 0.35 O94973 EBI-8770081 0.57 Q9H0D6 EBI-8770081 0.53 P23468 EBI-8770081 0.55 Q9UMD9 EBI-8770081 0.35 Q8IUR7 EBI-8770081 0.35 P27824 EBI-8770081 0.35 P04114 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EBI-22085491 0.50 P50904 EBI-22179932 0.35 P32577 EBI-22179950 0.35 P41499 EBI-22179950 0.35 Q9WUD9 EBI-22179950 0.35 Q8CFN2 EBI-22180003 0.35 A0A0G2K3B0 EBI-22180003 0.35 A0A0G2JSR4 EBI-22180124 0.35 Q5XI26 EBI-22180124 0.35 F1M9D6 EBI-22180124 0.35 Q8K4S7 EBI-22237510 0.35 D3ZY64 EBI-22237510 0.35 B2GV15 EBI-22237510 0.35 D3ZV15 EBI-22237510 0.35 P24135 EBI-22237486 0.35 P10686 EBI-22237486 0.35 E9PT59 EBI-22237831 0.35 D4A3T0 EBI-22237831 0.35 P59622 EBI-22237831 0.35 Q8R424 EBI-22237831 0.35 F1M3E4 EBI-22237831 0.35 Q920L0 EBI-22237831 0.35 Q4KM68 EBI-22237831 0.35 D3ZG10 EBI-22237831 0.35 Q9EQH1 EBI-22237766 0.35 P97573 EBI-22237766 0.35 P85968 EBI-22237766 0.35 D4A5Q1 EBI-22237766 0.35 P52631 EBI-22237766 0.35 Q63788 EBI-22237766 0.35 P08461 EBI-22238066 0.35 P15651 EBI-22238080 0.35 A0A0R4J8U1 EBI-22238080 0.35 Q63065 EBI-22238008 0.35 Q5M824 EBI-22238008 0.35 Q32PX8 EBI-22238008 0.35 B5DFI9 EBI-22238008 0.35 F1M9C0 EBI-22238008 0.35 D3Z8I4 EBI-22238008 0.35 Q00972 EBI-22238008 0.35 P52632 EBI-22238008 0.35 Q5BK11 EBI-22238008 0.35 O55156 EBI-22238008 0.35 Q6AZ23 EBI-22241891 0.35 A0A0G2K064 EBI-22241891 0.35 P24155 EBI-22241891 0.35 P84083 EBI-22241891 0.35 Q7TT49 EBI-22241891 0.35 A9CMB8 EBI-22241875 0.35 P50116 EBI-22241875 0.35 F1MAF2 EBI-22266198 0.35 Q6ZWB6 EBI-25370031 0.37 Q14515 EBI-25370141 0.37 P0DMV8 EBI-25370295 0.37 P23469 EBI-25370790 0.37 Q58FF7 EBI-25380009 0.35 P09651 EBI-25380009 0.35 Q32P51 EBI-25380009 0.35 P17844 EBI-25380009 0.35 P61221 EBI-25380009 0.35 Q8IXB1 EBI-25380009 0.48 P60709 EBI-25391021 0.35 Q15208 EBI-25391021 0.35 Q16875 EBI-25391021 0.35 Q9UHB6 EBI-25391021 0.35 Q9ULV4 EBI-25391021 0.35 Q9Y383 EBI-25391021 0.35 P0DJI4 EBI-22303808 0.35 O94898 EBI-25414995 0.46 Q96JA1 EBI-25467913 0.74 O14944 EBI-25434733 0.62 Q6UW88 EBI-25434749 0.62 P35070 EBI-25434882 0.44 P15514 EBI-25434902 0.44 Q9BXH1 EBI-25466126 0.40 O43752 EBI-25466975 0.46 Q63635 EBI-25467027 0.27 P69479 EBI-25568044 0.35 Q5EP34 EBI-25772822 0.35 P0DTC2 EBI-26592776 0.54 P01116 EBI-27041844 0.27 P01111 EBI-27042293 0.27 P01112 EBI-27045317 0.27 F1PAA9 EBI-27079701 0.27 P63252 EBI-28956270 0.27 O15194 EBI-27115784 0.27 P0DTD8 EBI-27127141 0.35 Q96ST3 EBI-30836929 0.44 Q13885 EBI-32717697 0.50 Q9NVI1 EBI-32717697 0.35 O14980 EBI-32717697 0.35 Q14257 EBI-32717697 0.35 P50402 EBI-32717697 0.42 Q9UBV2 EBI-32717697 0.50 Q8TEM1 EBI-32717697 0.35 Q7Z3U7 EBI-32717697 0.35 Q9Y4L1 EBI-32717697 0.53 Q5SRE5 EBI-32717697 0.35 Q5T9A4 EBI-32717697 0.35 P01893 EBI-32717697 0.35 P19823 EBI-32717697 0.35 Q00059 EBI-32717697 0.35 O94822 EBI-32717697 0.35 P51571 EBI-32717697 0.35 Q9BXW9 EBI-32717697 0.50 Q13438 EBI-32717697 0.50 P52926 EBI-32717697 0.35 Q6ZNB6 EBI-32717697 0.35 O75843 EBI-32717697 0.35 Q9BSD7 EBI-32717697 0.35 P61619 EBI-32717697 0.50 Q9H583 EBI-32717697 0.35 O43819 EBI-32717697 0.35 P47869 EBI-32717697 0.50 Q15653 EBI-32717697 0.35 Q92504 EBI-32717697 0.35 Q8WVX9 EBI-32717697 0.35 Q9NZ01 EBI-32717697 0.35 O15438 EBI-32717697 0.35 O94933 EBI-32717697 0.35 O75155 EBI-32717697 0.35 Q92973 EBI-32717697 0.35 Q2M3M2 EBI-32717697 0.35 Q9Y2A7 EBI-32720286 0.27 Q01484 EBI-32720286 0.27 P52594 EBI-32720286 0.27 Q96RU3 EBI-32720286 0.27 P09012 EBI-32720286 0.27 Q92738 EBI-32720286 0.27 Q8IYB1 EBI-32720286 0.27 Q16625 EBI-32720286 0.27 Q12955 EBI-32720286 0.27 Q15811 EBI-32720286 0.27 Q96RT1 EBI-32720286 0.27 Q7Z2K8 EBI-32720286 0.27 Q12923 EBI-32720286 0.27 Q7L576 EBI-32720286 0.27 Q9UHD8 EBI-32720286 0.27 Q9P0K7 EBI-32720286 0.27 Q14126 EBI-32720286 0.27 Q7Z3T8 EBI-32720286 0.27 Q9HAU0 EBI-32720286 0.27 Q92598 EBI-32720286 0.47 Q96AC1 EBI-32720286 0.27 Q9UGP4 EBI-32720286 0.27 A8MVW0 EBI-32720286 0.27 Q9BSJ8 EBI-32720286 0.27 O95487 EBI-32720286 0.27 Q96F07 EBI-32720286 0.27 O95757 EBI-32720286 0.27 Q15334 EBI-32720286 0.27 Q9H3P7 EBI-32720286 0.27 Q9HB21 EBI-32720286 0.27 Q7Z2W4 EBI-32720286 0.27 Q5T2T1 EBI-32720286 0.27 O43865 EBI-32720286 0.27 Q8NDI1 EBI-32720286 0.27 Q5JSH3 EBI-32720286 0.27 P35241 EBI-32720286 0.27 Q0JRZ9 EBI-32720286 0.27 Q9ULH0 EBI-32720286 0.27 Q15437 EBI-32720286 0.27 P35612 EBI-32720286 0.27 Q96TA1 EBI-32720286 0.27 Q92599 EBI-32720286 0.27 O95486 EBI-32720286 0.27 Q86YQ8 EBI-32720286 0.27 Q15654 EBI-32720286 0.27 Q96HN2 EBI-32720286 0.27 Q14141 EBI-32720286 0.27 Q9UHR4 EBI-32720286 0.27 Q9P265 EBI-32720286 0.27 O95819 EBI-32720286 0.27 Q9H4G0 EBI-32720286 0.27 Q9UKE5 EBI-32720286 0.27 Q15436 EBI-32720286 0.27 Q8IY81 EBI-32720286 0.27 Q8IZP0 EBI-32720286 0.27 Q01968 EBI-32720286 0.27 Q9UGI8 EBI-32720286 0.27 Q9Y217 EBI-32720286 0.27 Q9NNW5 EBI-32720286 0.27 P35240 EBI-32720286 0.27 Q02487 EBI-32720286 0.27 Q04721 EBI-32720286 0.27 Q13425 EBI-32720286 0.27 Q9P0V9 EBI-32720286 0.27 Q6WCQ1 EBI-32720286 0.27 Q7KZI7 EBI-32720286 0.27 Q9Y4K4 EBI-32720286 0.27 Q8IYB5 EBI-32720286 0.27 Q13492 EBI-32720286 0.27 Q99618 EBI-32720286 0.27 Q9NUP9 EBI-32720286 0.27 O95405 EBI-32720286 0.27 Q5VUB5 EBI-32720286 0.27 P41743 EBI-32720286 0.27 Q86X29 EBI-32720286 0.27 O14639 EBI-32720286 0.27 Q96JB5 EBI-32720286 0.27 O95721 EBI-32720286 0.27 Q9NZ52 EBI-32720286 0.27 Q8TEW0 EBI-32720286 0.27 Q13642 EBI-32720286 0.27 Q9H2D6 EBI-32720286 0.27 Q9P2D6 EBI-32720286 0.27 Q8WU79 EBI-32720286 0.27 P51648 EBI-32720286 0.27 Q9UNF0 EBI-32720286 0.27 Q9H2J7 EBI-32720286 0.27 Q15311 EBI-32720286 0.27 Q96S66 EBI-32720286 0.27 Q9NYB9 EBI-32720286 0.27 P61081 EBI-32720286 0.27 Q07960 EBI-32720286 0.27 Q7Z6J0 EBI-32720286 0.27 Q96Q05 EBI-32720286 0.27 Q9H425 EBI-32720286 0.27 Q9GZT9 EBI-32720286 0.27 Q8WUW1 EBI-32720286 0.27 Q9Y2I1 EBI-32720286 0.27 Q9C0B5 EBI-32720286 0.27 Q9NRW7 EBI-32720286 0.27 Q9H792 EBI-32720286 0.27 Q96QG7 EBI-32720286 0.27 O43318 EBI-32720286 0.27 Q8NEU8 EBI-32720286 0.27 P98082 EBI-32720286 0.27 Q9H939 EBI-32720286 0.27 Q13586 EBI-32720286 0.27 Q12792 EBI-32720286 0.27 Q9HDC5 EBI-32720286 0.27 O95292 EBI-32720286 0.27 Q92734 EBI-32720286 0.27 Q6WKZ4 EBI-32720286 0.27 Q9HD26 EBI-32720286 0.27 Q9H8Y8 EBI-32720286 0.27 O60858 EBI-32720286 0.27 Q9UH03 EBI-32720286 0.27 Q9UKD2 EBI-32720286 0.27 Q00013 EBI-32720286 0.27 Q9Y4J8 EBI-32720286 0.27 Q13177 EBI-32720286 0.27 Q9H1K0 EBI-32720286 0.27 P48553 EBI-32720286 0.27 Q8NI08 EBI-32720286 0.27 O75116 EBI-32720286 0.27 P08240 EBI-32720286 0.27 P61088 EBI-32720286 0.27 Q8TAA9 EBI-32720286 0.27 Q14254 EBI-32720286 0.27 Q86WR0 EBI-32720286 0.27 Q9UQN3 EBI-32720286 0.27 O60869 EBI-32720286 0.27 Q96KQ4 EBI-32720286 0.27 Q53SF7 EBI-32720286 0.27 O95208 EBI-32720286 0.27 Q13610 EBI-32720286 0.27 Q6ZVF9 EBI-32720286 0.27 Q8WU20 EBI-32720286 0.27 P15170 EBI-32720286 0.27 Q9UH65 EBI-32720286 0.27 O60493 EBI-32720286 0.27 O43617 EBI-32720286 0.27 Q8NBS9 EBI-32720286 0.27 C4AMC7 EBI-32720286 0.27 Q8TDM6 EBI-32720286 0.27 Q8IXS6 EBI-32720286 0.27 Q5HYI8 EBI-32720286 0.27 O60925 EBI-32720286 0.27 Q12774 EBI-32720286 0.27 Q13541 EBI-32720286 0.27 Q5HYK7 EBI-32720286 0.27 Q9UQ80 EBI-34582286 0.35 P36776 EBI-34582286 0.35 P06733 EBI-34582286 0.35 Q9NYU2 EBI-34582286 0.35 P36952 EBI-34582286 0.35 Q9NSE4 EBI-34582286 0.35 P80723 EBI-34582286 0.35 Q99798 EBI-34582286 0.35 P50995 EBI-34582286 0.35 P08865 EBI-34582286 0.35 Q9Y696 EBI-34582286 0.35 P08758 EBI-34582286 0.35 P29144 EBI-34582286 0.35 GO:0009925 GO:0016323 GO:0030054 GO:0009986 GO:0030669 GO:0005737 GO:0031901 GO:0005789 GO:0005768 GO:0010008 GO:0005615 GO:0005925 GO:0000139 GO:0005887 GO:0097708 GO:0016020 GO:0045121 GO:0097489 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:0032991 GO:0043235 GO:0032587 GO:0070435 GO:0044214 GO:0051015 GO:0005524 GO:0051117 GO:0045296 GO:0003682 GO:0003690 GO:0019899 GO:0048408 GO:0005006 GO:0042802 GO:0019900 GO:0004709 GO:0019903 GO:0030296 GO:0004713 GO:0030297 GO:0004714 GO:0004888 GO:0031625 GO:0001618 GO:0007202 GO:0030154 GO:0000902 GO:0007166 GO:0098609 GO:0071230 GO:0071276 GO:0071364 GO:0071392 GO:0034614 GO:0021795 GO:0048546 GO:0001892 GO:0007173 GO:0050673 GO:0038134 GO:0061029 GO:0001942 GO:0007611 GO:0060571 GO:0043066 GO:1905208 GO:0042059 GO:0042177 GO:0001503 GO:0038083 GO:0018108 GO:0090263 GO:0030307 GO:0030335 GO:0008284 GO:0045737 GO:0045739 GO:0045740 GO:0045893 GO:0050679 GO:0070374 GO:0048146 GO:1900087 GO:0033674 GO:0043406 GO:1903800 GO:1901224 GO:0010750 GO:0033138 GO:0042327 GO:0051897 GO:1900020 GO:1903078 GO:0001934 GO:0045944 GO:0046777 GO:0051205 GO:0070372 GO:0046328 GO:0050999 GO:0050730 GO:0014066 GO:0070141 GO:0007435 GO:0007165 GO:0007169 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA 1210 P55245 Epidermal EGFR 9544 None SL-0178 SL-0182 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}. UNIPROT P55245 UNIPROT F6YXS7 UNIPROT G7ML99 UNIPROT H9FAB2 Pfam PF00757 Pfam PF14843 Pfam PF07714 Pfam PF01030 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. GO:0009925 GO:0005737 GO:0005789 GO:0005768 GO:0010008 GO:0000139 GO:0005887 GO:0031965 GO:0005634 GO:0005886 GO:0043235 GO:0005524 GO:0003682 GO:0048408 GO:0005006 GO:0004713 GO:0004714 GO:0030154 GO:0071364 GO:0071392 GO:0007173 GO:0007611 GO:0043066 GO:0030307 GO:0008284 GO:0050679 GO:0070374 GO:0033674 GO:1902966 GO:0001934 GO:0045944 GO:0046777 GO:0007169 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSEFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDTLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSSQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCQNVSRGRECVDKCNVLEGEPREFVENSECIQCHPECLPQVMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCARNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA 1210 Q01279 Epidermal Egfr 10090 None SL-0178 SL-0182 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}. UNIPROT Q01279 Pfam PF00757 Pfam PF14843 Pfam PF07714 Pfam PF01030 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. P42567 EBI-7373206 0.44 O70469 EBI-7588761 0.40 O54928 EBI-7477248 0.40 P01132 EBI-7853849 0.40 P18031 EBI-7945363 0.40 P01133 EBI-8618729 0.44 P35831 EBI-8614373 0.40 P32883 EBI-6296299 0.46 P22682 EBI-8846800 0.50 Q60631 EBI-8846800 0.35 Q15109 EBI-15599433 0.52 O54890 EBI-15645972 0.40 Q9D1T0 EBI-15654918 0.40 P62991 EBI-15844305 0.40 Q91XA9 EBI-16880617 0.27 P70193 EBI-25424163 0.40 Q9JKY5 EBI-27088765 0.40 GO:0016324 GO:0009925 GO:0016323 GO:0030054 GO:0009986 GO:0005737 GO:0031901 GO:0030139 GO:0005789 GO:0005768 GO:0010008 GO:0000139 GO:0005887 GO:0097708 GO:0016020 GO:0045121 GO:0097489 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:0032991 GO:0043235 GO:0032587 GO:0044214 GO:0045202 GO:0051015 GO:0005524 GO:0005516 GO:0003682 GO:0019899 GO:0048408 GO:0005006 GO:0042802 GO:0005178 GO:0016301 GO:0019900 GO:0030235 GO:0019901 GO:0019903 GO:0030296 GO:0004713 GO:0044877 GO:0005102 GO:0030297 GO:0004714 GO:0004888 GO:0031625 GO:0048143 GO:0030154 GO:0000902 GO:0008283 GO:0007166 GO:0098609 GO:0071230 GO:0071276 GO:0071549 GO:0071364 GO:0071392 GO:0071363 GO:0071260 GO:0034614 GO:0071466 GO:0021795 GO:0007623 GO:0048546 GO:0016101 GO:0001892 GO:0007173 GO:0008544 GO:0050673 GO:0038134 GO:0061029 GO:0001942 GO:0042743 GO:0035556 GO:0007611 GO:0097421 GO:0030324 GO:0010960 GO:0007494 GO:0060571 GO:0043066 GO:1905208 GO:0045930 GO:0042177 GO:0048812 GO:0042698 GO:0038083 GO:0018108 GO:0045780 GO:0090263 GO:0030307 GO:0030335 GO:0008284 GO:0045737 GO:0045739 GO:0045740 GO:0045893 GO:0050679 GO:0070374 GO:0048146 GO:1900087 GO:0060252 GO:0050729 GO:0033674 GO:0043406 GO:0043410 GO:1903800 GO:0070257 GO:1901224 GO:0010750 GO:0033138 GO:0042327 GO:1902722 GO:0051897 GO:1900020 GO:1902966 GO:1903078 GO:0001934 GO:0048661 GO:0032930 GO:0051968 GO:0045944 GO:0045907 GO:0046777 GO:0042127 GO:0070372 GO:0046328 GO:0050999 GO:0050730 GO:0014066 GO:0051592 GO:0033590 GO:0033594 GO:0006970 GO:0070141 GO:0007435 GO:0007165 GO:0043586 GO:0006412 GO:0007169 GO:0042311 GO:0042060 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRPSGTARTTLLVLLTALCAAGGALEEKKVCQGTSNRLTQLGTFEDHFLSLQRMYNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNALYENTYALAILSNYGTNRTGLRELPMRNLQEILIGAVRFSNNPILCNMDTIQWRDIVQNVFMSNMSMDLQSHPSSCPKCDPSCPNGSCWGGGEENCQKLTKIICAQQCSHRCRGRSPSDCCHNQCAAGCTGPRESDCLVCQKFQDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGPDYYEVEEDGIRKCKKCDGPCRKVCNGIGIGEFKDTLSINATNIKHFKYCTAISGDLHILPVAFKGDSFTRTPPLDPRELEILKTVKEITGFLLIQAWPDNWTDLHAFENLEIIRGRTKQHGQFSLAVVGLNITSLGLRSLKEISDGDVIISGNRNLCYANTINWKKLFGTPNQKTKIMNNRAEKDCKAVNHVCNPLCSSEGCWGPEPRDCVSCQNVSRGRECVEKCNILEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGIMGENNTLVWKYADANNVCHLCHANCTYGCAGPGLQGCEVWPSGPKIPSIATGIVGGLLFIVVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQAHLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPYGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASDISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELILEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMEDVVDADEYLIPQQGFFNSPSTSRTPLLSSLSATSNNSTVACINRNGSCRVKEDAFLQRYSSDPTGAVTEDNIDDAFLPVPEYVNQSVPKRPAGSVQNPVYHNQPLHPAPGRDLHYQNPHSNAVGNPEYLNTAQPTCLSSGFNSPALWIQKGSHQMSLDNPDYQQDFFPKETKPNGIFKGPTAENAEYLRVAPPSSEFIGA 1210 Q18250 Early egrh 6239 None SL-0198 Nucleus {ECO:0000269|PubMed:20736289}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20736289}. Note=Perinuclear localization only observed in sperm. {ECO:0000269|PubMed:20736289}. UNIPROT Q18250 Pfam PF00096 PROSITE PS00028 PROSITE PS50157 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}. GO:0005634 GO:0048471 GO:0000981 GO:0046872 GO:0000978 GO:0043407 GO:1900194 GO:0060280 GO:0006357 Unknown UniProt Sequence Analysis MALHEPPSKLNRHSHSNLLKPPSLNKPILTFADNDCLKTPTMNDMLKTPTVNSPRHTPMNIDGTPKVNGFSGFTPQTDQKFFGEHEPLFNQMHTTTLMPAPSSSYKEPAYSSEQPSSSSDEAKPKELLGSNSFGVPRMTNGNSKQKPEELTLKDIEISSTGPGGVDSPGLSAAMFQFSPMVEHFLQNLTNKAGLPELVVDSKTAGLNHQEPSDLIKSVQVRRSSIEDQKFSDVLHVPTLPRKTSEPSHLGSSLQNEHPQSNSRPSTVIPRVQRTNTSASLTRSMDHSSMSPISAHDDPYSNSASYSSLSTHTSFSDSASLAHFEPKTEPMDDYSYNFSDNDFNSFEFSSTSEELKNIGCQKMKSSKMPLQDRPYKCPRDGCDRRFSRSDELTRHIRIHTGQKPFQCRICMRAFSRSDHLTTHVRTHTGEKPFSCDICGRKFARSDERKRHTKVHKTSRSGS 461 O14681 Etoposide-induced EI24 9606 None SL-0178 SL-0182 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}. UNIPROT O14681 UNIPROT A8K7D6 UNIPROT B4DKL6 UNIPROT Q9BUQ1 OMIM 605170 DisGeNET 9538 Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250}. 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. A0A142I5B9 EBI-20626169 0.35 P51668 EBI-2339419 0.37 P62837 EBI-2339474 0.37 P06460 EBI-11723082 0.35 P0C739 EBI-11725101 0.35 Q6NUS6 EBI-11368748 0.27 Q9WMX2 EBI-11513187 0.35 P11234 EBI-12451925 0.51 P27105 EBI-12452286 0.51 Q8N4P2 EBI-12452567 0.51 Q9NUH8 EBI-24698409 0.56 O15173 EBI-24712104 0.56 Q12982 EBI-24742623 0.56 Q9UI14 EBI-24743382 0.56 Q6PL24 EBI-25225021 0.56 Q8IWL3 EBI-13943458 0.35 P51685 EBI-20804904 0.37 F5H1C8 EBI-21264930 0.35 Q9H1C4 EBI-21266770 0.35 P01116 EBI-27041844 0.27 P01111 EBI-27042293 0.27 P01112 EBI-27045317 0.27 Q9H5K3 EBI-28948637 0.35 Q8NCK7 EBI-27103180 0.35 GO:0005829 GO:0005783 GO:0005789 GO:0005794 GO:0016021 GO:0016020 GO:0031965 GO:0061676 GO:0006915 GO:0016236 GO:0030308 Transmembrane UniProt Sequence Analysis {ECO:0000255} MADSVKTFLQDLARGIKDSIWGICTISKLDARIQQKREEQRRRRASSVLAQRRAQSIERKQESEPRIVSRIFQCCAWNGGVFWFSLLLFYRVFIPVLQSVTARIIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRKPHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWPYYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSTSAEKFPSPHPSPAKLKATAGH 340 Q61070 Etoposide-induced Ei24 10090 None SL-0178 SL-0182 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}. UNIPROT Q61070 UNIPROT Q3T9X1 UNIPROT Q3TVX9 UNIPROT Q3UGS7 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}. GO:0005829 GO:0005783 GO:0005789 GO:0005794 GO:0016021 GO:0031965 GO:0061676 GO:0006914 GO:0071494 GO:0008630 GO:0016236 GO:0030308 GO:0042308 GO:0050885 GO:2001244 GO:0009410 Transmembrane UniProt Sequence Analysis {ECO:0000255} MADSVKTFLQDLGRGIKDSIWGICTISKLDARIQQKREEQRRRRASSLLAQRRPQSVERKQESEPRIVSRIFQCCAWNGGVFWFSLLLFYRVFIPVLQSVTARIIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRKPHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWPYYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSSSAEKFPSPHPSPAKLKAAAGH 340 Q4KM77 Etoposide-induced Ei24 10116 None SL-0178 SL-0182 Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q4KM77 Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy. {ECO:0000269|PubMed:20550938}. GO:0005829 GO:0005783 GO:0005789 GO:0005794 GO:0016021 GO:0031965 GO:0061676 GO:0006914 GO:0071494 GO:0008630 GO:0016236 GO:0030308 GO:0042308 GO:0050885 GO:2001244 GO:0009410 Transmembrane UniProt Sequence Analysis {ECO:0000255} MADSVKTFLQDLGRGIKDSIWGICTISKLDARIQQKREEQRRRRASSLLAQRRAQSVERKQESEPRIVSRIFQCCAWNGGVFWFSLLLFYRVFIPVLQSVTARVIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRKPHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWPYYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSSSAEKFPSPHPSPAKLKAAAGH 340 Q3ZC12 Eukaryotic EIF3G 9913 None SL-0198 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}. UNIPROT Q3ZC12 Pfam PF12353 Pfam PF00076 PROSITE PS50102 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}. GO:0016282 GO:0033290 GO:0005852 GO:0005634 GO:0048471 GO:0003723 GO:0003743 GO:0001732 GO:0006413 Unknown UniProt Sequence Analysis MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSLEPELLPGAPLPPPKEVINGNIKTVTEYRIDEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN 320 O75821 Eukaryotic EIF3G 9606 None SL-0198 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. UNIPROT O75821 UNIPROT O14801 UNIPROT Q969U5 PDB 2CQ0 PDB 2MJC PDB 5K0Y PDB 6YBS PDB 6ZMW Pfam PF12353 Pfam PF00076 PROSITE PS50102 OMIM 603913 DisGeNET 8666 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}. P55884 EBI-366642 0.86 O75822 EBI-366663 0.35 Q99547 EBI-373791 0.00 O60739 EBI-1059553 0.00 P62330 EBI-1068233 0.00 O95831 EBI-7083391 0.60 Q13347 EBI-7083418 0.69 O15372 EBI-2510472 0.56 Q9Y6I4 EBI-2512627 0.40 Q9Z0R6 EBI-2557425 0.40 P23116 EBI-2559355 0.56 Q5NEC0 EBI-2807069 0.00 A0A5P8YFD8 EBI-2870697 0.00 Q13573 EBI-7950968 0.35 Q99459 EBI-7954144 0.35 Q9P2Y5 EBI-3622729 0.35 P54619 EBI-8638625 0.37 O95257 EBI-7156156 0.37 Q13526 EBI-7302217 0.37 Q16513 EBI-7308665 0.37 Q16637 EBI-7388997 0.37 P37840 EBI-7391140 0.37 P04183 EBI-7397222 0.37 B2BUF1 EBI-6110503 0.35 P03366 EBI-6174791 0.46 O00571 EBI-6261906 0.35 Q13618 EBI-21329068 0.35 Q08379 EBI-10189737 0.56 Q8IZU0 EBI-10189751 0.56 Q9H074 EBI-10766330 0.35 Q99613 EBI-10766374 0.67 Q14152 EBI-10766374 0.67 Q6ZWV7 EBI-10997876 0.35 E9QNG1 EBI-11017017 0.35 P27635 EBI-11035646 0.35 P60229 EBI-11148789 0.35 Q9QZD9 EBI-11149349 0.35 Q96AP0 EBI-11307293 0.51 Q9NUX5 EBI-11307303 0.37 P40217 EBI-11530486 0.56 Q6FHY5 EBI-24331428 0.56 A9UHW6 EBI-25261639 0.56 Q6IQ23 EBI-16398399 0.35 Q9Y262 EBI-21660564 0.35 Q7L2H7 EBI-21660564 0.35 P60228 EBI-21660564 0.35 O15371 EBI-21660564 0.35 O00303 EBI-21660564 0.35 Q49MI3 EBI-21731388 0.35 O95714 EBI-16811721 0.35 P09622 EBI-20304669 0.35 Q9BRX2 EBI-20567709 0.65 P10636 EBI-20799058 0.35 Q9UMQ6 EBI-20900672 0.40 P13693 EBI-20992046 0.35 Q5S007 EBI-21360986 0.35 P42858 EBI-21132926 0.67 P03372 EBI-21301141 0.35 P20339 EBI-25391898 0.35 Q8K337 EBI-25409748 0.35 Q6ZR37 EBI-25411486 0.35 P0DOF2 EBI-25603126 0.35 P06730 EBI-25478272 0.35 P0C6X7 EBI-26377128 0.35 P35226 EBI-27108918 0.35 P0DTC9 EBI-27102375 0.35 P0DTD1 EBI-27128043 0.27 P46108 EBI-30819739 0.44 Q9UIH9 EBI-29019642 0.35 Q9BXK1 EBI-29019783 0.35 O95600 EBI-29020196 0.35 GO:0005737 GO:0005829 GO:0016282 GO:0033290 GO:0005852 GO:0048471 GO:0003723 GO:0003743 GO:0001732 GO:0006413 GO:0075525 Unknown UniProt Sequence Analysis MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSPEPELLPGAPLPPPKEVINGNIKTVTEYKIDEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN 320 Q9Z1D1 Eukaryotic Eif3g 10090 None SL-0198 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}. UNIPROT Q9Z1D1 UNIPROT Q9R079 Pfam PF12353 Pfam PF00076 PROSITE PS50102 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}. Q3TBT3 EBI-10729637 0.35 Q9QWV4 EBI-767142 0.37 Q9JL25 EBI-649611 0.37 P23116 EBI-7466744 0.46 Q9H074 EBI-10766353 0.35 Q9EPK7 EBI-17171503 0.35 P97414 EBI-20564572 0.35 GO:0005737 GO:0005829 GO:0016282 GO:0033290 GO:0005852 GO:0005634 GO:0048471 GO:0003723 GO:0003743 GO:0001732 GO:0006413 GO:0075525 Unknown UniProt Sequence Analysis MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLPTGDTSPEPELLPGDPLPPPKEVINGNIKTVTEYKIEEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQAAQSKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN 320 Q5RK09 Eukaryotic Eif3g 10116 None SL-0198 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}. UNIPROT Q5RK09 Pfam PF12353 Pfam PF00076 PROSITE PS50102 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}. P09619 EBI-22247316 0.35 Q9H5Y7 EBI-22259307 0.35 GO:0005737 GO:0016282 GO:0033290 GO:0005852 GO:0048471 GO:0003723 GO:0003743 GO:0001732 GO:0006413 GO:0075525 Unknown UniProt Sequence Analysis MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLPTGDTSPEPELLPGDPLPPPKEVINGNIKTVTEYKVEEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQAAQNKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN 320 G0S2G1 Protein ELYS 759272 None SL-0178 SL-0185 Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8WYP5}. UNIPROT G0S2G1 UNIPROT G0ZGV2 Pfam PF13934 Required for the assembly of a functional nuclear pore complex (NPC). {ECO:0000250|UniProtKB:Q8WYP5}. G0S0E7 EBI-16069427 0.62 G0S2X1 EBI-16069404 0.56 G0SDQ4 EBI-16069488 0.62 G0S9A7 EBI-16069540 0.49 G0SAK3 EBI-16069540 0.58 G0SER9 EBI-16069540 0.49 G0SA60 EBI-16069540 0.49 GO:0005643 GO:0051028 GO:0015031 Unknown UniProt Sequence Analysis MLDFTHFPEVFPTDGPRPYDQHFVRQTETFRKSLDGVLFIDRVLGALGLPDAAKAYPPRGDAGLRALHQQVCSAKVSAHAKLSVLYYLLLDHDEHRGSRSQLADALAEEVGLPANYQILMRGLWHMDRKEFKFALEHLAHPSLPAEFADEIITVLVRDGHTTGDYSLPLAYYHAVRPVLQTSSALENLFAALARTSVTDALAFSRTYPDHGARQLLFERLVASVLEEHGSGQVAGRSASRAKELVSLPLTGVEEKWLNDYLSTGEGRKSRSAKAVVQMRQVVTGRQKELGAVVGVRAGR 299 Q9VWE6 Protein Elys 7227 None SL-0178 SL-0185 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}. UNIPROT Q9VWE6 UNIPROT Q95TR2 Pfam PF13934 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}. Q24568 EBI-9919289 0.35 Q9VHC7 EBI-235409 0.00 Q24276 EBI-469514 0.00 Q961V9 EBI-469517 0.00 Q9V470 EBI-471896 0.00 P49657 EBI-471899 0.00 P92177 EBI-8283416 0.35 Q9VUH7 EBI-9961648 0.35 P31007 EBI-9965763 0.35 Q9VF82 EBI-26819136 0.49 GO:0005694 GO:0005643 GO:0003682 GO:0031490 GO:0051028 GO:0015031 Unknown UniProt Sequence Analysis MEWHEVELDGSRTIAFPERIVPGFGREPSAHLDAAEYLGGIIRDGQWGWVTWRYGSDATLLVCSMSTGDYLSWHCFWSESDDLGPRKSIRCVEELFPGEHERPAMLAICLESWNSGDQRPIDCPLSTQVLIYAIRNSQVLRRFDLHGITCSALTFLDKRIYGLTRLRRFKGCLAVATEEGTVLLVDLNSDSLQASTQRRSLCSPSSKDEPSDGNLYFVSSEESKRQLSSKLTHCRSKGAHLAVRMDVASIGISCLMGISMAPGYAAGLEDGRILIYDLINFDVTTDLNSPVKRKGVNRAVKRMCLIMPPDDPKPCFYICALYQNIDVLQMMLHSVCYRGSYRDRETHTIRFKDYRSRTVRNRQILDGGICSVIGCATASTFSFAGDNGTLLIVISWHSSADKKNKLVLFDINQWYKDEMPTSVHKNEVPNYMSGYILSGLQTGLALDLRSTTILHFVSLQRYDEHFYPNSLTFDCSLLTPTGKRYYAQDGVQHRFLNALRCDRATLFLRPQIYHEDIVRLRLLPQFCELNPNATFSKIAMYELILSVALEHNCGALLNDCARSWMDGSFLCNMIDNTQLSLSTLTNWILKRAGQIKTRCSELCHGIFDYGGYPLDQRERREFQVLSGQLRELVRLQSYIVEQGRRRLTSSILDDCRANERALKTVLEYQRVLLWFIDHGLLPEGQHMDNLVPGEQAFVRLQHEYSEKRAQGKILYIDSLGKRASFPEPYPPDSLHAYIHLMLSPDIELCHKHALILYLLMDLNQQLVGRFQIAFQLDKDLATSLRCFWYLDHGDYERGVEELYKEPAPAKNLKSWQMRLLIDKLLAEGAVKAAKKVVSRPPGPLSSALHMKVLLANENITEAFQIARLDDDEDGQPLLERFFRHCIEIRRFKVLAELYLREPEERLLYSLLRQCRSRQTDCVQLIMLLQKSKFIEAVSFMDEVAAERERDESSNTILPAYSATMGPVTQNIAGTYLRIRDTLEPYQKTGPLEPFSCQLVKQNASGQLGGIFQSSAVSAHWATQCESPPKMTPVSIQSKIGYTNVPFLRHAQYGHSELPLPRRIVKPVPHQVVEKRQRELEDQRTNLQDQRQLGTERPNKRPCLMVERMVEDVKDYVRSIREKSSNQMEQEEVKQNEATNLLQPPNFLQARQSTTIRQSSSSPQPIPPILKGSGAVDAVKRAPPVATFTALAGPKRFRFVPPIPLRTDKSDKSTEMGSEGAAEGEEETDEIIVEIESRSEPRSACSYESDEEDEFLSPLVSANVSLVDPVPSRNSPHYFAPPAGPQPRNSLLHGGNGSGSKIGTATGSESSSGFGSFSTVQPAQTSSHSQFVPTVCSSKMGETQSQVFSSGSCGIKISERTTICGEMESTDLGAELTAAPSAQWSLPSARPAIQGHHQMMDTTLGMSTYDVASLEQQDTQDVENEEELKLGDTKSLEEQQNPQDEQKPEQEQDQDEDQAQEPLATGGQLAFLSNSEGTAQEPLSSPIYSLSSEDSNVSSAGIRNPMLPTLHTDDPMYSIVVESPGSITTSRSVTHTPTSFLPSDTNVSQTSSPQAPHGEDGDGTPISLYRANSLETVDDLDTTKGSLEEEEEYDDDDCVIALDGTEVRGYVARPQQSAASSSAELFAFKDECQEEAAGVPSPFLSLGATVNSDSDVADTIVLDSDEETAKEKDTQPEQRKDWPMEEETPSNESVATVEFSEQKQPRADMDIGMEVDAVPDVLEVLEVPEMEPLPVLSDVDIEMAVDEVPNVLEVLEVPELEPLPAGQATQSSGLGEIPEEDVDAEAEEQVVVKVEHVADEQPKEGDKTESKEASEEETQHNPEPLLPEEEDSRHSLKLIFSGDEDEEEQDVPTRAIHTLRPRRSFTEHQDSPRTLRPRRVSQEHRDSPTPVAGRTMSLRSTDAPTLSPASNPPVSTPKRRGLQHKYLLEVIDEHSPSDLSLPRTRSRTRLSVDSEATSSRPGTPTMTKARGKRATSQAPPTASPSVRRSLRGHSEPPAALSAQLVRKPKTARAGVRSRKTSSGVQSPVAVSPTPIDAPIDVPDSTAPEEEQPRLRRTARRRISELSDQSANGTGDLRSEASSSRTGSKSNSAASTQNRELRPRLRRTSKSEH 2111 Q8WYP5 Protein AHCTF1 9606 None SL-0178 SL-0185 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}. UNIPROT Q8WYP5 UNIPROT A6NGM0 UNIPROT A8MSG9 UNIPROT A8MZ86 UNIPROT Q7Z4E3 UNIPROT Q8IZA4 UNIPROT Q96EH9 UNIPROT Q9Y4Q6 Pfam PF13934 Pfam PF16687 OMIM 610853 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}. O75694 EBI-9050350 0.40 P02545 EBI-16795756 0.27 P05783 EBI-20924394 0.40 P37198 EBI-9050350 0.40 P49792 EBI-9050350 0.40 P52948 EBI-9050503 0.49 P55735 EBI-9050503 0.32 P57740 EBI-9050503 0.49 Q12769 EBI-9050503 0.49 Q5SRE5 EBI-9050350 0.40 Q6PFD9 EBI-2563676 0.56 Q8BH74 EBI-10997196 0.35 Q8N1F7 EBI-9050350 0.40 Q8NFH3 EBI-9050503 0.49 Q8NFH4 EBI-9050503 0.62 Q8NFH5 EBI-9050350 0.40 Q8WUM0 EBI-9050503 0.49 A0JLT2 EBI-394580 0.35 Q80Z64 EBI-2312516 0.35 P35222 EBI-2686783 0.00 Q8D0N9 EBI-2876232 0.00 O00716 EBI-7600105 0.35 Q9BW27 EBI-9050503 0.57 Q96EE3 EBI-9050503 0.49 Q92621 EBI-9050350 0.40 Q99567 EBI-9050350 0.40 Q96HA1 EBI-9050350 0.40 P06748 EBI-11145880 0.35 Q9P0L0 EBI-21550773 0.35 Q14627 EBI-21561326 0.35 P51957 EBI-20721387 0.35 P08670 EBI-20924386 0.40 P05787 EBI-20924378 0.40 Q15149 EBI-20924370 0.40 Q15651 EBI-20928904 0.40 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 P03372 EBI-21301141 0.35 P30530 EBI-32719959 0.27 P36888 EBI-32722567 0.27 Q02763 EBI-32732012 0.35 GO:0005829 GO:0070062 GO:0000776 GO:0005635 GO:0016363 GO:0031965 GO:0005643 GO:0005654 GO:0005634 GO:0003677 GO:0007049 GO:0051301 GO:0051028 GO:0051292 GO:0006913 GO:0015031 GO:0032465 Unknown UniProt Sequence Analysis MRDLRAQVTSGLLPFPEVTLQALGEDEITLESVLRGKFAAGKNGLACLACGPQLEVVNSITGERLSAYRFSGVNEQPPVVLAVKEFSWQKRTGLLIGLEETEGSVLCLYDLGISKVVKAVVLPGRVTAIEPIINHGGASASTQHLHPSLRWLFGVAAVVTDVGQILLVDLCLDDLSCNQNEVEASDLEVLTGIPAEVPHIRESVMRQGRHLCFQLVSPTGTAVSTLSYISRTNQLAVGFSDGYLALWNMKSMKREYYIQLESGQVPVYAVTFQEPENDPRNCCYLWAVQSTQDSEGDVLSLHLLQLAFGNRKCLASGQILYEGLEYCEERYTLDLTGGMFPLRGQTSNTKLLGCQSIEKFRSHGDREEGVNEALSPDTSVSVFTWQVNIYGQGKPSVYLGLFDINRWYHAQMPDSLRSGEYLHNCSYFALWSLESVVSRTSPHGILDILVHERSLNRGVPPSYPPPEQFFNPSTYNFDATCLLNSGVVHLTCTGFQKETLTFLKKSGPSLNELIPDGYNRCLVAGLLSPRFVDVQPSSLSQEEQLEAILSAAIQTSSLGLLTGYIRRWITEEQPNSATNLRFVLEWTWNKVVLTKEEFDRLCVPLFDGSCHFMDPQTIQSIQQCYLLLSNLNIVLSCFASEAREITERGLIDLSNKFVVSHLICQYAQVVLWFSHSGLLPEGIDDSVQLSRLCYNYPVIQNYYTSRRQKFERLSRGKWNPDCLMIDGLVSQLGERIEKLWKRDEGGTGKYPPASLHAVLDMYLLDGVTEAAKHSITIYLLLDIMYSFPNKTDTPIESFPTVFAISWGQVKLIQGFWLIDHNDYESGLDLLFHPATAKPLSWQHSKIIQAFMSQGEHRQALRYIQTMKPTVSSGNDVILHLTVLLFNRCMVEAWNFLRQHCNRLNIEELLKHMYEVCQEMGLMEDLLKLPFTDTEQECLVKFLQSSASVQNHEFLLVHHLQRANYVPALKLNQTLKINVMNDRDPRLRERSLARNSILDQYGKILPRVHRKLAIERAKPYHLSTSSVFRLVSRPKPLSAVPKQVVTGTVLTRSVFINNVLSKIGEVWASKEPINSTTPFNSSKIEEPSPIVYSLPAPELPEAFFGTPISKASQKISRLLDLVVQPVPRPSQCSEFIQQSSMKSPLYLVSRSLPSSSQLKGSPQAISRASELHLLETPLVVKKAKSLAMSVTTSGFSEFTPQSILRSTLRSTPLASPSPSPGRSPQRLKETRISFVEEDVHPKWIPGAADDSKLEVFTTPKKCAVPVETEWLKSKDRTTSFFLNSPEKEHQEMDEGSQSLEKLDVSKGNSSVSITSDETTLEYQDAPSPEDLEETVFTASKPKSSSTALTTNVTEQTEKDGDKDVFASEVTPSDLQKQMGNLEDAETKDLLVAAEAFSELNHLSPVQGTEASLCAPSVYEGKIFTQKSKVPVLDEGLTSVETYTPAIRANDNKSMADVLGDGGNSSLTISEGPIVSERRLNQEVALNLKEDHEVEVGVLKESVDLPEEKLPISDSPPDTQEIHVIEQEKLEAQDSGEEARNLSFNELYPSGTLKLQYNFDTIDQQFCDLADNKDTAECDIAEVDGELFVAQSNFTLILEGEEGEVEPGDFASSDVLPKAANTATEEKLVCSGENDNHGQIANLPSAVTSDQKSQKVDTLPYVPEPIKVAIAENLLDVIKDTRSKEITSDTMEQSIHETIPLVSQNIMCPTKLVKSAFKTAQETSTMTMNVSQVDDVVSSKTRTRGQRIQNVNVKSAQQEASADVATPKMPGQSVRKKTRKAKEISEASENIYSDVRGLSQNQQIPQNSVTPRRGRRKKEVNQDILENTSSVEQELQITTGRESKRLKSSQLLEPAVEETTKKEVKVSSVTKRTPRRIKRSVENQESVEIINDLKVSTVTSPSRMIRKLRSTNLDASENTGNKQDDKSSDKQLRIKHVRRVRGREVSPSDVREDSNLESSQLTVQAEFDMSAIPRKRGRPRKINPSEDVGSKAVKEERSPKKKEAPSIRRRSTRNTPAKSENVDVGKPALGKSILVPNEELSMVMSSKKKLTKKTESQSQKRSLHSVSEERTDEMTHKETNEQEERLLATASFTKSSRSSRTRSSKAILLPDLSEPNNEPLFSPASEVPRKAKAKKIEVPAQLKELVSDLSSQFVISPPALRSRQKNTSNKNKLEDELKDDAQSVETLGKPKAKRIRTSKTKQASKNTEKESAWSPPPIEIRLISPLASPADGVKSKPRKTTEVTGTGLGRNRKKLSSYPKQILRRKML 2266 Q8CJF7 Protein Ahctf1 10090 None SL-0178 SL-0185 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}. UNIPROT Q8CJF7 UNIPROT B2RRC8 UNIPROT Q8BVJ5 UNIPROT Q8VD55 PDB 4I0O Pfam PF13934 Pfam PF16687 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}. P52927 EBI-9986179 0.35 GO:0000785 GO:0005737 GO:0000776 GO:0005635 GO:0016363 GO:0031965 GO:0005643 GO:0031080 GO:0005654 GO:0005634 GO:0003677 GO:0007049 GO:0051301 GO:0030097 GO:0051028 GO:0051292 GO:0006913 GO:0015031 GO:0032465 Unknown UniProt Sequence Analysis MQDLTAQVTSDLLHFPEVTIEALGEDEITLESVLRGKFAAGKNGLACLACGPQLEVVNSLTGERLSAYRFSGVNEQPPVVLAVKEFSWHKRTGLLIGLEEADGSVLCLYDLGISRVVKAVVLPGRVTAIEPIINHGGASASTQHLHPSLRWLFGVAAVVTDVGQILLIDLCLDDLSCSQNEVEASDLEVITGIPAEVPHIRERVMREGRHLCFQLVSPLGVAISTLSYINRTNQLAVGFSDGYLALWNMKSMKREYYTQLEGGRVPVHAVAFQEPENDPRNCCYLWAVQSTQDSEGDVLSLHLLQLAFGDRKCLASGQILYEGLEYCEERYTLDLAGGTFPLRGQTSNTKLLGCQSIERFPSHGDREESMREALSPDTSVSVFTWQVNIYGQGKPSVYLGLFDINRWYHAQMPDSLRSGESLHNCSYFALWSLDSVVSRTSPHHILDILVHERSLNRGVPPSYPPPEQFFNPSTFNFDATCLLDSGVIHVTCAGFQKETLTFLKKSGPTLNEVIPDSYNRCLVAGLLSPRLIDIQPSSLSQEEQLEAILSAAIQTSSLGLLTGYIRTWIIEEQPNSAANLRFVLEWTWNKVVLTKEEFDRLCVPLFDGSCRFIDPQTIQSIQQCHLLLSNLSTVLSCFAMEAQGITERGLVDLSNKHMVTQLLCQYAHMVLWFCHSGLLPEGLDDALQLSRLRYNYPVIQNYYTSRRQKSERSPRGKWNHDCLMIDGLVSQLGDEVEKLWKRDEGGTGRYPPASIHALLDIYLLDNITEASKHAITIYLLLDIMYSFPNKTDTPIESFPTAFAISWGQVKLVQGFWLLDHNDYENGLDLLFHPVTAKPASWQHSKIIEAFMSQGEHKQALRYLQTMKPTVSSSNEVILHLTVLLFNRCMVEAWNLLRQNSNRVNIEELLKHAYEVCQEMGLMEDLLKLPFTNTEQECLVKFLQSSTSVENHEFLLVHHLQRANYISALKLNQILKNNLMSDRDPRLRERSVTRNSILDQYGKILPRVQRKLAVERAKPYHLSTSSVFHEVSRPKPLSAFPKKAITGTVLTRSTFISNVLSKIGEVWASHEPRNGVSLFNSPKTEQPSPVVHSFPHPELPEAFVGTPISNTSQRISRLLDLVVHPVPQPSQCLEFIQQSPTRSPLCLLSSSLPLSSQFKRPHQNTSRPSELLLLETPLIVKKAKSLALSATSSGFAEFTPPSILRSGFRTTPLASPSLSPGRSLTPPFRVKETRISFMEEGMNTHWTDRATDDRNTKAFVSTSFHKCGLPAETEWMKTSDKNTYFPLDVPAKGPQKVVAESLATHSGRLEKLDVSKEDSTASTRSDQTSLEYHDAPSPEDLEGAVFVSPKPASSSTELTTNSTLQTERDNDKDAFKSEGAPSPVKKQIGTGDAAVEAFSELSRLDPVERAEASFAVSSVCEGETSTSNSKTSVLDGIVPIESRTSILTADHKESVANTVADVESSGSTSSKCPVTSERSLGQKLTLNLKEDEIEAHVPKENVGLPEESPRISAAPSDTHEIHLIGCENLEVQNSEEEAKNLSFDELYPLGAEKLEYNLSTIEQQFCDLPDDKDSAECDAAEVDGELFVAQSNFTLILEGEEGEAEASDSAAPNMLPKATKEKPVCHREPHNQERVTDLPSAVTADQESHKVETLPYVPEPVKVAIAENLLDVIKDTRSKEATPVAAGEAGDEDGAVIVSKAAHSSRLTNSTPKTVKEPHAETVNTSQNDDMVSSRTLTRRQHALSLNVTSEQEPSAVATPKKRTRKIKETPESSERTCSDLKVAPENQLTAQSPPAPRRGKKKDVSQGTLPSSGAVEPEPEPQGTPGRLRLRTQPPEPAAEETPSRTKVRLSSVRKGTPRRLKKSVENGQSTEILDDLKGSEAASHDGTVTELRNANLEDTQNMEYKQDEHSDQQLPLKRKRVREREVSVSSVTEEPKLDSSQLPLQTGLDVPATPRKRGRPRKVVPLEADGGTTGKEQTSPQKKDVPVVRRSTRNTPARNVSTLEKSVLVPNKEAALVVTSKRRPTKKSAEESSKDPSAAVSDLAGGAAHTESADRRDGLLAAAALTPSAQGTRTRSRRTMLLTDISEPKTEPLFPPPSVKVPKKKSKAENMEAAAQLKELVSDLSSQFVVSPPALRTRQKSISNTSKLLGELESDPKPLEIIEQKPKRSRTVKTRASRNTGKGSSWSPPPVEIKLVSPLASPVDEIKTGKPRKTAEIAGKTLGRGRKKPSSFPKQILRRKML 2243 Q5U249 Protein ahctf1 8355 None SL-0178 SL-0185 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}. UNIPROT Q5U249 PDB 7VCI PDB 7WB4 Pfam PF13934 Pfam PF16687 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}. Q6P5F9 EBI-11606853 0.35 GO:0005737 GO:0005643 GO:0005654 GO:0003677 GO:0051028 GO:0015031 Unknown UniProt Sequence Analysis MQNLEAQVTGSLVAFPDVTQKALKEDEINLDSVLRGKFSTGRTSLAWLACGPQLEITNSVTGERISAYHFSGLTERPPVVVAVKEFTWQKKTGLLVGLVEAEGSVLCLYDIGISKVVKAVVLPGSVTAVEPIINHGGASASTQHLHQSLRWFFGVTAVVTDVGHVLLIDLCLDEVSSNQDELDASDLEVMSVIPTKIPKLREAATRERRHLCLQLAAPTGTTVSCLSYISRTNQLAVGYSDGYFSLWNMKTLRRDYHVQIEGGRVPVCAVAFQEPENDPRNCCYLWAVQSSESGGDVSLHLLQLAFSDRKCLASGQIMYELLEYCEERYSLDLSGSTLSLRGQSNNTKLLGCQTIEKFRVHGEREDGVHEVTSPDTSVSVFSWQVNTYGQGKPSVYLGVFDINRWYQAQMPDSLRSGQFLRNCSYFAFWSLEAVVNITTQDIIFDILVHERSLSRGIPPSYPPPEQFYYPSTYNFDATCLLNSGLIHFACTGFQKETLHFLKKSGSSLNEAIPDGYNRCLAAGLLAPKFTDVQASSLSQEEQLQAILAAAVETSSLGLLTSCIKRWTAEEQPRSAANLRFVLEWTWKKVTLTKQEFDRLCFRLFDGSCNFIDPHTLQSLQQCHLYFSNLTAVLNCFIAQAKEVTQQGAVDLTNKQSVTRLLTLYASVVLWFCRSGMLPDSSDETVQLTRPFYNYQVIQQYYSDQRKKLERLARGKWDTSSLMIDGLINQFGDRIQQLWSRDDNGTGKYPPANLHALLDVYLLENADEMSKHAITIYFLLDIMYSFPDKPDSSIESFPTAFFVPGSLIKLIQGFWLLDHNDYQNSVDCILNPASSRVMSWQHSQIIENLLCHGDSRQALRYLQVMKPVATTSKEVKLHMTVLLANRSILEAWNLQRLHSSRLNVEELLKHMYEMCQEMGLIEELLKLTFTDFEQGYLHKFLQTTGVQNQELLLVHHLQRANYISALQLNQSLKTNHLNDCDRRLRERSGARNAILDQYGKILPRVQRTLASERAKPYSLPSLVWREVARPKPLSTTAKQAAPGSIITKANFICNVLSKIKEVSTANEKREEYSPYQSMVSEEPTAPPLQDIDVPDAFFGTPINKSRRVSRLLDSVVHPVLMEPTPLTSSDTDNNQTPHKSPLLKTSSPLHSSLRRIAHMRSFAKASEFSLLETPLVVRKAKALAANTASSGYTSITPQSILRSSVRTTPLVSPSVSPGRSLTPPLRPKETKISFMELSFTRHAKAAHSSEGNLLAISPVLRSSPDAVWSVKGKVASFTQNTPVKKLDEIDASSSGIQEESQDEMEVSKEISNISVRSEQASLEYHDAPTPEDLENDEISGTTNSQPQVNEVHHQMEDGQLTEKPAELALTEMQEEFIDSEEREIEYISAPLNGPNALECMTAVPDIYLEDASQCILETPEGSSVSVTGEQECVSSAKDSESVISIHDSDDAHSNLSENDQDSEEIEENNLRVPTTVTRCEEFDLIETKDLEVELEEADSEKTNYKDIYPDATVQLGFTVESIEQRYTCELADRRETPSETDEIEGEHFETENNFSLVLEGDVTEEEILEPSSSKTDLELTRPPIAHQKLISENRENIENCETTEKIPANMSPLVDSDHESKTLETLPSEADLSVAEKVLKGTEEKDVPPEVHSEVVLESKLVGNAMMSLDSSESQEVIISQYDNVISIEKLEMTQEKMYGEKTEQINEGQVSPNRDQSTLVKPLTPRRSIRKSSKPADSSTDIIGNITLPTTPKRGLKKAKENVDTLKNSISVVPEEELTLGTRRITRKATLTALDNPEPLQIKEPPSGEDLQVQPSTPTRGRRGKVITSDDLKEPPSGEDLQVQPSTPTRGRRGRVITSDDLREPPPGEDLQVQPSTPTRGRRGRVITSDDIKESPSVEDLQVQPSTPTRGRRGKVITSDDIKEPPSVEDLQVQPSTPTRGRKGKVITSDDIKEPLSGEDLQVQPSTPTRGRKGKVITSDDIKEPLSEEVLQEQPSTPTRGRRGRVITSDGKGYECVEEKNALPLTPTRITRSKNILEPEKGISQIEPEKGISQIEPDKGLSQIEDTGETEHEVVTPRRGRRGKRVVNELVKHFERNSSQPNIKADTSPPVSPKKVSLRWTRTRSENQRINATEEQASKIQEDLSDTPRKRYKKSSNKMGFEETTDTVTEGAIVEDVQESLIISHLGKNPNTSIVRSARKTALPPVTEDHSEQPLLPPESHSKVHSSLAIADEENKTNTRTRSGNKSSVDVSAITFEFSTPKARTKKTAKGSAVPTELIPSTQYVFSPPSTRTRRATRANVSEAVIEPQLQFQESCEIAETEVPEVPASKPRGRPPKHKAKAVTRVLKKPSWSTPPVEIKLISPPESPAVSETNTKTDSTEAKGAEKISVRRTRRRIIAKPVTRRKMR 2408 O00423 Echinoderm EML1 9606 None SL-0198 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}. UNIPROT O00423 UNIPROT Q86U15 UNIPROT Q8N536 UNIPROT Q8N5C4 UNIPROT Q8WWL6 PDB 4CI8 Pfam PF03451 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 OMIM 600348 OMIM 602033 DisGeNET 2009 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}. 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. Q9H9L3 EBI-759235 0.62 Q96GG9 EBI-21325177 0.35 Q9Y266 EBI-9482705 0.40 Q14203 EBI-11366138 0.27 Q13509 EBI-21665394 0.35 Q9NVF7 EBI-21835198 0.35 Q9HC35 EBI-21835198 0.35 Q9BVA1 EBI-21835198 0.35 Q13885 EBI-21835198 0.35 P07437 EBI-21835198 0.35 P55212 EBI-25834583 0.56 P13473 EBI-25872768 0.56 P31948 EBI-25913540 0.56 P51114 EBI-26508437 0.51 P60484 EBI-26513677 0.37 Q05086 EBI-26516191 0.37 GO:0005829 GO:0005874 GO:0005875 GO:1990023 GO:0097431 GO:0048471 GO:0005509 GO:0008017 GO:0015631 GO:0007420 GO:0002244 GO:0000226 GO:0007052 GO:0007405 Unknown UniProt Sequence Analysis MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKGPTKARPLMQTLPLRTTVNNGTVLPKKPTGSLPSPSGVRKETAVPATKSNIKRTSSSERVSPGGRRESNGDSRGNRNRTGSTSSSSSGKKNSESKPKEPVFSAEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGFFDRAVTCIAFSKSNGGTNLCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTEIPEQFGPIRTVAEGKGDVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYGGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRVI 815 Q05BC3 Echinoderm Eml1 10090 None SL-0198 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}. UNIPROT Q05BC3 UNIPROT Q05AF8 UNIPROT Q0P5V3 Pfam PF03451 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. 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. P35922 EBI-16728828 0.35 GO:0005829 GO:0005874 GO:0015630 GO:0048471 GO:0008017 GO:0015631 GO:0007420 GO:0002244 GO:0000226 GO:0007052 GO:0007405 Unknown UniProt Sequence Analysis MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKGPTKARPLGQTLPLRTTVNNGTVLPKKPSASLPAPSGARKEVVVPVTKSINRTSSSERVSPGGRRESSGDSKGSRNRTGSTSSSSSGKKNSESKPKEPAFSPEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGFFDRAVTCIAFSKSNGGGHLCAVDDSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGNSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKLHKAEIPEQFGPIRTVAEGKGNVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRAPSHIYSGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRVI 814 Q4V8C3 Echinoderm Eml1 10116 None SL-0198 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}. UNIPROT Q4V8C3 Pfam PF03451 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. P54645 EBI-16399805 0.35 GO:0005829 GO:0005874 GO:0048471 GO:0008017 GO:0015631 GO:0007420 GO:0002244 GO:0000226 GO:0007052 GO:0007405 Unknown UniProt Sequence Analysis MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEISDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKGPTKARPLGQTLPLRTTVNNGTVLPKKPSASLPSPSGSRKEMVVPVTKSINRTSSSERVSPGGRRESSGDSKGSRNRTGSTSSSSSGKKNSESKPKEPTFSPEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGFFDRAVTCIAFSKSNGGSHLCAVDDSNDHVLSVWDWQREERLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGNSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKLHKAEIPEQFGPIRTVAEGKGNVILIGTTRNFVLQGTLTGDFTPITQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYSGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRVI 814 P50402 Emerin EMD 9606 None SL-0178 SL-0179 SL-0182 SL-0183 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. UNIPROT P50402 UNIPROT Q6FI02 PDB 1JEI PDB 2ODC PDB 2ODG PDB 6GHD PDB 6RPR PDB 7NDY Pfam PF03020 PROSITE PS50954 OMIM 300384 OMIM 310300 DisGeNET 2010 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}. 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. A1L3G9 EBI-12595918 0.40 O75531 EBI-10759397 0.94 O94901 EBI-22057164 0.46 P00533 EBI-32717697 0.42 P01112 EBI-27045317 0.27 P02545 EBI-16795756 0.80 P03246 EBI-11722343 0.35 P04626 EBI-32718334 0.35 P0DTC7 EBI-25510184 0.35 P13285 EBI-11733017 0.35 P35240 EBI-23824818 0.56 Q9NYF8 EBI-489904 0.59 Q7L5N1 EBI-731797 0.00 Q7L190 EBI-731800 0.00 Q99962 EBI-710249 0.51 Q99963 EBI-731806 0.00 Q969F0 EBI-753397 0.85 O43889 EBI-12701204 0.56 Q8N7W2 EBI-10211848 0.81 P35222 EBI-8577506 0.59 P13569 EBI-1171716 0.53 Q9UKV8 EBI-7642406 0.35 P04296 EBI-9631489 0.35 Q9HCK5 EBI-2269711 0.35 O70126 EBI-2557780 0.40 P03372 EBI-2877710 0.35 Q9BQS8 EBI-3242919 0.35 Q15051 EBI-4286917 0.35 P51858 EBI-4409719 0.35 Q16659 EBI-7207761 0.37 P0DOE9 EBI-6138583 0.35 P19320 EBI-6191076 0.53 Q77M19 EBI-6270503 0.35 Q13617 EBI-21327106 0.35 Q13618 EBI-21329068 0.35 P22893 EBI-6506418 0.35 Q5S007 EBI-6515609 0.53 Q9UH99 EBI-6753091 0.64 Q9D666 EBI-6752609 0.52 P57078 EBI-12503575 0.35 Q8IWZ5 EBI-10211808 0.72 Q53Z40 EBI-10211828 0.56 Q5JST6 EBI-10211838 0.56 Q8NEC5 EBI-10211860 0.81 Q9P286 EBI-10211880 0.56 Q8NHQ1 EBI-10211870 0.72 Q9P127 EBI-10211900 0.81 Q9UNY5 EBI-10211910 0.56 Q9Y228 EBI-10211920 0.81 Q13895 EBI-10230959 0.72 Q8N8X9 EBI-10268015 0.56 Q8WTP8 EBI-10275770 0.56 Q9ULW3 EBI-10323933 0.72 P50402 EBI-10484783 0.37 O14862 EBI-9995694 0.35 P10398 EBI-10101587 0.35 Q13418 EBI-10103376 0.35 P51617 EBI-10103481 0.53 O60674 EBI-10103554 0.35 P53671 EBI-10103591 0.35 P04049 EBI-10104226 0.53 Q9H0K1 EBI-10104403 0.35 Q8NF91 EBI-10759458 0.52 Q8WXH0 EBI-10760372 0.58 P03177 EBI-11721652 0.35 P03179 EBI-11721697 0.35 P03182 EBI-11721938 0.35 P03225 EBI-11722220 0.35 P06460 EBI-11723082 0.35 P06461 EBI-11723785 0.35 P06792 EBI-11724527 0.35 P06927 EBI-11724813 0.35 P0C739 EBI-11725101 0.35 P0CK56 EBI-11725466 0.35 P0CK58 EBI-11732874 0.35 P30119 EBI-11733103 0.35 P69901 EBI-11733364 0.35 Q2MG95 EBI-11733653 0.35 Q2MG96 EBI-11733890 0.35 Q8AZK7 EBI-11734159 0.35 Q8AZJ3 EBI-11734105 0.35 E9QKK1 EBI-10995761 0.35 Q9Z1B5 EBI-10996176 0.35 P36895 EBI-11008521 0.35 P31150 EBI-11035437 0.35 Q9Z2X1 EBI-11066678 0.35 F8VQC7 EBI-11104527 0.35 Q6ZNC8 EBI-11121915 0.35 Q5T3F8 EBI-11155257 0.35 Q6NUS6 EBI-11368748 0.27 Q86UK5 EBI-11372136 0.27 Q86X19 EBI-11372615 0.27 Q96GX1 EBI-11375285 0.27 Q9P0N5 EBI-11378021 0.27 Q96Q45 EBI-11396533 0.27 P48039 EBI-11575834 0.37 Q8N6L0 EBI-11774371 0.79 Q71U36 EBI-11897791 0.53 Q6FHY5 EBI-24279203 0.56 Q9BYN7 EBI-24339377 0.56 Q04864 EBI-24344788 0.56 Q16623 EBI-24487831 0.56 Q6P2D0 EBI-24525478 0.56 P20138 EBI-24662714 0.56 Q5JRM2 EBI-23676624 0.56 Q8N5K1 EBI-23679672 0.56 Q96HE8 EBI-24667793 0.56 Q6NX45 EBI-24670601 0.56 B7U540 EBI-24672111 0.56 A6NEL2 EBI-23696046 0.56 Q15842 EBI-24689183 0.56 Q9NQX5 EBI-24699630 0.56 Q8N4V1 EBI-24709706 0.56 Q7RTU1 EBI-23756438 0.56 O60930 EBI-23758332 0.56 Q0VD86 EBI-24717955 0.56 Q7Z6M4 EBI-23772605 0.56 Q9Y320 EBI-23795943 0.56 P16157 EBI-24733419 0.56 Q9HA82 EBI-23800001 0.56 P43628 EBI-24742152 0.56 Q9BSJ6 EBI-24763001 0.56 Q5JX71 EBI-24763501 0.56 Q6IBW4 EBI-23853144 0.56 Q86VY9 EBI-24778276 0.56 Q8TDT2 EBI-25275476 0.56 Q5T7V8 EBI-23923221 0.56 Q8IUY3 EBI-24390287 0.56 P50221 EBI-24397223 0.56 O75031 EBI-24417083 0.56 Q9HAQ2 EBI-24439983 0.56 Q8TD17 EBI-24447341 0.56 Q5SNT2 EBI-24476865 0.68 Q96S94 EBI-24556880 0.56 Q6P9A3 EBI-24557406 0.56 Q9NU63 EBI-24580547 0.56 Q5T686 EBI-24599743 0.56 P21964 EBI-24641360 0.56 Q86UD4 EBI-24646904 0.56 Q96PL5 EBI-25169259 0.56 Q4KMG9 EBI-24747207 0.56 Q68DC2 EBI-25195191 0.56 Q9BRJ2 EBI-24789200 0.56 Q14500 EBI-24790299 0.56 Q7Z7G2 EBI-25207978 0.56 Q9H400 EBI-24799476 0.56 Q8WWF3 EBI-24800633 0.56 Q9UGI6 EBI-24807534 0.56 Q86T13 EBI-25224374 0.56 Q8WUU8 EBI-25273036 0.56 P49910 EBI-12696914 0.56 O95292 EBI-12698321 0.56 Q9NTW7 EBI-12700590 0.56 Q12846 EBI-12702158 0.56 P50222 EBI-12702328 0.56 Q8N5R6 EBI-12702476 0.56 O14829 EBI-14024386 0.35 P56180 EBI-14025693 0.57 Q6IQ23 EBI-16398399 0.35 Q05322 EBI-15481401 0.35 P60709 EBI-15531451 0.52 P68135 EBI-15531470 0.60 Q14684 EBI-16686997 0.35 O15155 EBI-16788067 0.27 P27824 EBI-16788621 0.27 P68431 EBI-16793336 0.27 P11279 EBI-16794808 0.27 Q9HBL7 EBI-16797780 0.27 P62491 EBI-16797971 0.27 P20339 EBI-16798221 0.27 P51151 EBI-16798325 0.27 P62753 EBI-16798663 0.27 O43493 EBI-16800265 0.42 Q9NS69 EBI-16802054 0.27 Q7KZN9 EBI-20304305 0.35 P36957 EBI-20305285 0.35 P08559 EBI-20306509 0.35 P35610 EBI-20307233 0.35 P21796 EBI-20307902 0.35 Q9HCE5 EBI-20595531 0.35 P51957 EBI-20721387 0.35 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 Q5T7N2 EBI-20993270 0.35 P14316 EBI-21260627 0.35 Q15077 EBI-21262943 0.35 F5H1C8 EBI-21264930 0.35 Q03518 EBI-21265865 0.35 Q9NQB0 EBI-21265942 0.35 Q9H1C4 EBI-21266770 0.35 Q9BTV4 EBI-22085077 0.54 Q13163 EBI-25374437 0.35 Q15311 EBI-25375541 0.35 Q92934 EBI-25378368 0.35 P19419 EBI-25378580 0.35 P0DOF2 EBI-25603126 0.35 Q9H9V9 EBI-25479633 0.35 Q8N5Y8 EBI-25482187 0.35 P69479 EBI-25568044 0.35 P0DTC4 EBI-25509966 0.35 P0DTC8 EBI-25510273 0.35 P0DTD3 EBI-25510342 0.35 Q96CS3 EBI-25770166 0.35 Q8IWF2 EBI-25770736 0.35 Q8NBM4 EBI-25771384 0.35 Q5U458 EBI-26450034 0.35 O60303 EBI-26582514 0.35 P34972 EBI-26880846 0.35 P01116 EBI-27041844 0.27 P01111 EBI-27042293 0.27 F1PAA9 EBI-27079701 0.27 A0A0H3NFP4 EBI-27055788 0.27 A0A0H3NG92 EBI-27055968 0.27 A0A0H3NF08 EBI-27055973 0.27 A0A0H3NB75 EBI-27055983 0.27 P35226 EBI-27108918 0.35 Q99592 EBI-27093179 0.35 Q6P5Z2 EBI-28941754 0.35 Q86UX6 EBI-28942129 0.35 Q99986 EBI-28944934 0.35 Q9UJY1 EBI-28946841 0.35 Q8NCK7 EBI-27103180 0.35 Q93009 EBI-30841862 0.44 Q05925 EBI-29000369 0.35 P23769 EBI-29000495 0.35 P23771 EBI-29000509 0.35 Q8TDD2 EBI-29000537 0.35 P57682 EBI-29000670 0.35 P43694 EBI-29011567 0.35 Q9UIH9 EBI-29019642 0.35 Q9BXK1 EBI-29019783 0.35 O95600 EBI-29020196 0.35 P48431 EBI-29373058 0.35 P35712 EBI-29384845 0.35 P08047 EBI-29385496 0.35 P31314 EBI-29607649 0.35 O43763 EBI-29612789 0.35 O43711 EBI-29624592 0.35 P52952 EBI-29653951 0.35 Q9Y4X4 EBI-29017631 0.27 P21709 EBI-32717758 0.35 P29322 EBI-32718189 0.42 P22455 EBI-32718547 0.35 P35916 EBI-32718614 0.35 P08069 EBI-32718669 0.42 P06213 EBI-32718777 0.42 P08581 EBI-32719056 0.42 P04629 EBI-32719115 0.35 Q16288 EBI-32719212 0.35 Q01974 EBI-32719482 0.42 Q6J9G0 EBI-32719662 0.42 Q06418 EBI-32719716 0.35 Q9UM73 EBI-32719830 0.27 P30530 EBI-32719959 0.27 P21860 EBI-32721529 0.27 P22607 EBI-32721979 0.27 P17948 EBI-32722433 0.27 P36888 EBI-32722567 0.27 P14616 EBI-32723232 0.27 P35968 EBI-32723270 0.27 Q8IWU2 EBI-32723604 0.27 Q12866 EBI-32723870 0.27 O15146 EBI-32724025 0.27 P07949 EBI-32725031 0.27 P08922 EBI-32731758 0.27 Q02763 EBI-32732012 0.35 Q8N612 EBI-34574737 0.27 Q5W0V3 EBI-34574999 0.27 GO:0005737 GO:0005829 GO:0005783 GO:0016021 GO:0016020 GO:0005874 GO:0005635 GO:0005637 GO:0031965 GO:0005640 GO:0005654 GO:0005819 GO:0003779 GO:0048487 GO:0045296 GO:0071363 GO:0006936 GO:0007517 GO:0090090 GO:0048147 GO:0071763 GO:0046827 GO:0060828 GO:0035914 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDNYADLSDTELTTLLRRYNIPHGPVVGSTRRLYEKKIFEYETQRRRLSPPSSSAASSYSFSDLNSTRGDADMYDLPKKEDALLYQSKGYNDDYYEESYFTTRTYGEPESAGPSRAVRQSVTSFPDADAFHHQVHDDDLLSSSEEECKDRERPMYGRDSAYQSITHYRPVSASRSSLDLSYYPTSSSTSFMSSSSSSSSWLTRRAIRPENRAPGAGLGQDRQVPLWGQLLLFLVFVIVLFFIYHFMQAEEGNPF 254 O08579 Emerin Emd 10090 None SL-0178 SL-0179 SL-0182 SL-0183 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}. UNIPROT O08579 UNIPROT Q3TIH6 UNIPROT Q3UJP3 Pfam PF03020 PROSITE PS50954 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}. P20263 EBI-3043810 0.35 P52927 EBI-9986179 0.35 Q8NF91 EBI-10760599 0.27 Q8WXH0 EBI-10760623 0.27 Q9NRI5 EBI-26612017 0.35 GO:0032541 GO:0005737 GO:0005783 GO:0016021 GO:0005874 GO:0005635 GO:0005637 GO:0005652 GO:0031965 GO:0005640 GO:0005654 GO:0005634 GO:0005819 GO:0031616 GO:0003779 GO:0048487 GO:0071363 GO:0090090 GO:0048147 GO:0071763 GO:0046827 GO:0060828 GO:0035914 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDDYAVLSDTELAAVLRQYNIPHGPIVGSTRKLYEKKIFEYETQRRRLLPPNSSSSSFSYQFSDLDSAAVDSDMYDLPKKEDALLYQSKDYNDDYYEESYLTTKTYGEPESVGMSKSFRQPGTSLVDADTFHHQVRDDIFSSLEEEGKDRERLIYGQDSAYQSIAHYRPISNVSRSSLGLSYYPTSSTSSVSSSSSSPSSWLTRRAIRPEKQAPAAALGQDRQVPLWGQLLLFLVFAAFLLFVYYSIQAEEGNPFWMDP 259 Q63190 Emerin Emd 10116 None SL-0178 SL-0179 SL-0182 SL-0183 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}. UNIPROT Q63190 Pfam PF03020 PROSITE PS50954 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}. GO:0005737 GO:0016021 GO:0005874 GO:0005635 GO:0005637 GO:0031965 GO:0005640 GO:0005654 GO:0005634 GO:0005819 GO:0003779 GO:0048487 GO:0071363 GO:0090090 GO:0048147 GO:0071763 GO:0031468 GO:0046827 GO:0060828 GO:0035914 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDDYAVLSDTELAAVLRQYNIPHGPILGSTRKLYEKKIFEYETQRRRLSPPSSSSSSFSYRFSDLDSASVDSDMYDLPKKEDALLYQSKDYNDDYYEESYLTTRTYGEPESVGMSKSFRRPGTSLVDADDTFHHQVRDDIFSSSEEEGKDRERPIYGRDSAYQSIAEYRPISNVSRSSLGLSYYPRSSTSSVSSSSSSPSSWLTRRAIRPEKQAPTAALGQDRQVPLWGQLLLFLAFATFLLFVYYSIQAQEGNPFWMDP 260 Q2NKU9 Epithelial EMP2 9913 None SL-0198 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}. UNIPROT Q2NKU9 Pfam PF00822 PROSITE PS01221 PROSITE PS01222 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}. GO:0045177 GO:0016324 GO:0009986 GO:0005737 GO:0005829 GO:0005794 GO:0000139 GO:0016021 GO:0045121 GO:0005634 GO:0005886 GO:0019901 GO:0007015 GO:0070252 GO:0032147 GO:0032060 GO:0043534 GO:0007155 GO:0008219 GO:0016477 GO:0007160 GO:0045022 GO:0007566 GO:0060136 GO:0060914 GO:0001765 GO:0001787 GO:1990266 GO:0044854 GO:0045766 GO:0062043 GO:0008284 GO:2001046 GO:0034394 GO:0072659 GO:0045765 GO:0001952 GO:0010594 GO:0003093 GO:0043549 GO:2001212 GO:0001913 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLVLLAFIIVFHITSAALLLVATIDNAWWVGEEFFADIWKVCVNNTNCTELNDSVQDFSTVQAVQATMILSTILCCIAFLIFLLQLFRLKQGERFVLTSIIQLMACLCVMIAASIYTDRRKDIHEKNEELYAQTSGGSFGYSFILAWVAFAFTFISGLMYLILRKRK 167 F1QIK8 Epithelial emp2 7955 None SL-0198 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}. UNIPROT F1QIK8 Pfam PF00822 PROSITE PS01221 PROSITE PS01222 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}. GO:0016324 GO:0005737 GO:0005794 GO:0000139 GO:0016021 GO:0045121 GO:0005634 GO:0005886 GO:0008284 GO:0003093 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLVILAFIILFHITSAILLFIATINNAWRIKGDFSMDLWYNCNTTACYDIPKSATYDAAYLQAVQATMILATILCCVGFFVFILQLFRLKQGERFVFTAIIQLLSAFCVMTGASIYTAEGLTFNGQEFKNAEYGYSFVVAWVAFPMTLLSGLMYLVLRKRK 161 P54851 Epithelial EMP2 9606 None SL-0198 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}. UNIPROT P54851 UNIPROT B2R7V6 UNIPROT D3DUF8 Pfam PF00822 PROSITE PS01221 PROSITE PS01222 OMIM 602334 OMIM 615861 DisGeNET 2013 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}. 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. Q9WMX2 EBI-9083575 0.37 Q6IQ23 EBI-16398399 0.35 GO:0045177 GO:0016324 GO:0009986 GO:0005737 GO:0031410 GO:0005829 GO:0005794 GO:0000139 GO:0016021 GO:0045121 GO:0005634 GO:0005886 GO:0005178 GO:0019900 GO:0019901 GO:0007015 GO:0070252 GO:0032147 GO:0032060 GO:0043534 GO:0007155 GO:0008219 GO:0016477 GO:0007160 GO:0045022 GO:0007566 GO:0060136 GO:0060914 GO:0001765 GO:0001787 GO:1990266 GO:0044854 GO:0045766 GO:0062043 GO:0008284 GO:0001954 GO:2001046 GO:0034394 GO:0072659 GO:0045765 GO:0001952 GO:0010594 GO:0003093 GO:0043549 GO:2001212 GO:0001913 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLVLLAFIIAFHITSAALLFIATVDNAWWVGDEFFADVWRICTNNTNCTVINDSFQEYSTLQAVQATMILSTILCCIAFFIFVLQLFRLKQGERFVLTSIIQLMSCLCVMIAASIYTDRREDIHDKNAKFYPVTREGSYGYSYILAWVAFACTFISGMMYLILRKRK 167 O88662 Epithelial Emp2 10090 None SL-0198 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}. UNIPROT O88662 Pfam PF00822 PROSITE PS01221 PROSITE PS01222 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}. GO:0045177 GO:0016324 GO:0009986 GO:0005737 GO:0005829 GO:0005794 GO:0000139 GO:0016021 GO:0045121 GO:0005634 GO:0005886 GO:0005178 GO:0019900 GO:0019901 GO:0007015 GO:0070252 GO:0032147 GO:0032060 GO:0043534 GO:0007155 GO:0008219 GO:0016477 GO:0007160 GO:0045022 GO:0007566 GO:0060136 GO:0060914 GO:0001765 GO:0001787 GO:1990266 GO:0044854 GO:0045766 GO:0062043 GO:0008284 GO:0001954 GO:2001046 GO:0034394 GO:0072659 GO:0045765 GO:0001952 GO:0010594 GO:0003093 GO:0043549 GO:2001212 GO:0001913 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLVILAFIIVFHIVSTALLFISTIDNAWWVGDSFSADLWRVCTNSTNCTEINELTGPEAFEGYSVMQAVQATMILSTILSCISFLIFLLQLFRLKQGERFVLTSIIQLMSCLCVMIGASIYTDRRQDLHQQNRKLYYLLQEGSYGYSFILAWVAFAFTFISGLMYMILRKRK 172 A5A6N6 Epithelial EMP2 9598 None SL-0198 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}. UNIPROT A5A6N6 Pfam PF00822 PROSITE PS01221 PROSITE PS01222 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}. GO:0045177 GO:0016324 GO:0009986 GO:0005737 GO:0031410 GO:0005829 GO:0005794 GO:0000139 GO:0016021 GO:0045121 GO:0005634 GO:0005886 GO:0005178 GO:0019901 GO:0007015 GO:0070252 GO:0032147 GO:0032060 GO:0043534 GO:0007155 GO:0008219 GO:0016477 GO:0007160 GO:0045022 GO:0007566 GO:0060136 GO:0060914 GO:0001765 GO:0001787 GO:1990266 GO:0044854 GO:0045766 GO:0062043 GO:0008284 GO:0001954 GO:2001046 GO:0034394 GO:0072659 GO:0045765 GO:0001952 GO:0010594 GO:0003093 GO:0043549 GO:2001212 GO:0001913 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLVLLAFIIAFHITSAALLFIATIDNAWWVGDEFFADVWRICTNNTNCTVINDSFQEYSTLQAVQATMILSTILCCIAFFIFVLQLFRLKQGERFVLTSIIQLMSCLCVMIAASIYTDRREDIHHKNAKFYPVTREGSYGYSYILAWVAFACTFISGMMYLILRKRK 167 Q66HH2 Epithelial Emp2 10116 None SL-0198 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}. UNIPROT Q66HH2 Pfam PF00822 PROSITE PS01221 PROSITE PS01222 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}. GO:0045177 GO:0016324 GO:0009986 GO:0005737 GO:0031410 GO:0005829 GO:0005794 GO:0000139 GO:0016021 GO:0045121 GO:0005634 GO:0005886 GO:0005178 GO:0019900 GO:0019901 GO:0007015 GO:0070252 GO:0032147 GO:0032060 GO:0043534 GO:0007155 GO:0008219 GO:0016477 GO:0007160 GO:0045022 GO:0007566 GO:0060136 GO:0060914 GO:0001765 GO:0001787 GO:1990266 GO:0044854 GO:0045766 GO:0062043 GO:0008284 GO:0001954 GO:2001046 GO:0034394 GO:0072659 GO:0045765 GO:0001952 GO:0010594 GO:0003093 GO:0043549 GO:2001212 GO:0001913 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLVILAFIIVFHIVSTALLFISTIDNAWWVGDGFSADIWRVCTNSTNCTEINDLSSTEEFSGYSVMQAVQATMILSTILSCISFLIFLLQLFRLKQGERFVLTAIIQLMSCLCVMIGASVYTDRRQDLHHQNSQLYYLLQEGSYGYSFILAWVAFAFTFISGLMYMILRKRK 172 O01971 Emerin emr 6239 None SL-0178 SL-0179 SL-0182 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}. UNIPROT O01971 Pfam PF03020 PROSITE PS50954 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}. Q9XTB5 EBI-6260324 0.27 GO:0005639 GO:0005635 GO:0005521 GO:0007059 GO:0000281 GO:0006998 GO:0010165 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDVSQLTDAELRDSLKSHGVSVGPIVATTRKLYEKKLIKLSDGSINNQSNLNDSQFNEDSLIISSSPKKSPPQRVFQNVSAATAAATTSPESDSDDCEESMRYLTEEEMAADRASARQAQSNKGGFLGSTITFTILFVFIAVFAYFLIENAEQLKLVAETNPEDTI 166 Q9VYX1 Enhancer e 7227 None SL-0178 SL-0182 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}. UNIPROT Q9VYX1 Pfam PF10163 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}. Q7JXF5 EBI-2550835 0.46 Q9U3V9 EBI-2550885 0.54 Q9U5W9 EBI-2550010 0.35 Q8I8U7 EBI-2550010 0.35 O76216 EBI-2550010 0.43 Q8I8V0 EBI-2550010 0.35 Q9VZJ9 EBI-15145789 0.67 Q9U6R9 EBI-15171898 0.49 Q9VI64 EBI-15172342 0.49 Q9VVR6 EBI-15172118 0.49 Q9VRY7 EBI-15172566 0.67 P98149 EBI-26728176 0.49 P49905 EBI-26751710 0.49 Q9VGG3 EBI-26795784 0.49 Q9VE51 EBI-26806623 0.49 Q8IP15 EBI-26838266 0.49 GO:0000785 GO:0005737 GO:0071819 GO:0034399 GO:0005643 GO:0005634 GO:0000124 GO:0070390 GO:0070742 GO:0003682 GO:0043035 GO:0030374 GO:0001094 GO:0003713 GO:0033696 GO:0016578 GO:0006406 GO:0016973 GO:0045893 GO:0045944 GO:0015031 GO:0006357 GO:0006368 Peripheral UniProt Sequence Analysis MSTSGAVDQYTVLTGDRSKIKDLLCSRLTECGWRDEVRLMCRNILMEKGTNNSFTVEQLIAEVTPKARTLVPDAVKKELLMKIRTILTEIEEEPDEPEDES 101 Q9VE34 Ectopic Epg5 7227 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HCE0}. Lysosome {ECO:0000250|UniProtKB:Q9HCE0}. UNIPROT Q9VE34 UNIPROT Q8MT53 Involved in autophagy. Plays a role in late steps of autophagy. {ECO:0000269|PubMed:26917586}. Q24568 EBI-9944837 0.35 O61307 EBI-9946542 0.35 M9NFI9 EBI-9959939 0.35 GO:0005737 GO:0005764 GO:0048471 GO:0097352 GO:0006914 Unknown UniProt Sequence Analysis MATLEKPKKEKSKKSRNRVPIEKEEEEPAELSTSEEQRPAENVSLLEEFERVATLASSSSGEAIISHECCISSDVGVTSQEPEGTQEPTETEAQPSAPSAPPSTTVHVVQYPNLQPMQLSNAQVEEHSAKIVYRQAESPTGFALARSHIKLLSTEELRQIYDCPELELAKQFELEFLMNSLLETSEADPLYAAVMEYYELQGKITSNLHDVEKLRKGCAESQKQIWVRQPVTRTFSGTCGDGNVVQECVTYDVIQVDPIKLEVAKTSLTGLYDLVCHAYTNNSITAKITKVKVDQIINDLLTYPNLDGHSVVSLHHTQSGEALQCVSQLRRAISILFSFVRRPSPNANFDKDLKEWLRKLIALQLLLATREDHWFLLFNILRCPNGVGSWAAQFLQLPGTRAVRRGSQQNELPLDLNSPELNHCMAVLQILLMPVKKRNEYLKSQAQAHRELSDTPGATDRWIVVDSDGEDSHTPAGECVGLKESDLVALLNQMPFEKIFTSALRIEKFLDDYIIEPDMITAQQMLAVVVFFSQLVKTIGEGLLTYNNERYKQLAKRLGRLVRHTLQYVFDYNELFINNNLYKSSEMYERIQVELQALLVRACGYIYRTRNLGTWQYFSTLPFGTLDAEVIWHLFYYLNVGFPTDLANDLVSNAEAAFQAEDFWRKFDLANADVAPEDMYYLLQTFFEMANERNRSKDGSLVKAICLHIFHIGYIHKSTREICYKTARDMLANLMDEDLFGCVLVQLKMRYGEVDQAAYLFKALPLENWHPSMDTFEVLSNWLLHFDYQSSESQLARLIISHLNWGLDCEGRLFLPHNIHVRMAHLVNEALNKYAPEVIGASGISESVRQVSSLIDSTQSSREQFTNWCWRMVSVLRLHLMDQGVESVRRTLQHPTEPLLFIPELERMEMIFQGVNENRPLALYVGMLVSLHGHSIPLICQHGFILLQQLLLDHRHAATIRCLELIVPLFLETPETLANCESFQRLITTLLNADRTYLKLAKDMVYANSIGPILELLDNMLHHQIISYTSYGLCSPLNLLNIWLNCFTTLPGWSQNSNLLYLLDRMLRISYQFPDCRAQAVEFFYNYYKDCTEWKSAPKGSALKAFFGGQSVSRIPLISPQNCWLNLVILEIEFRLVDTRIFPELLRQISAQPVEAALKKTISLSKTSAFPASQLVIFKYAQLLASMESTHALFPIVCQKFFELYLWRVPTENESLNFSHNFGVSDKFYEYNVPLMKSIKSQLKSAESYYSALATKNANDDAMAHFYRNCCKLMQNCALWLEDTQINRFTSDAEHLPAQYNSEKLRELLSGHVNHWTEFLCLASLRKEQRHQADQWGRKVMRLSNQKAPRTPVQPKQRQPPAQHIKSLLKSYEKIVENPLHIRVEPIKTPPIDGVIVAQIQKKMTTLNSTANNYHYKTSELNSLDLNYLERVPTLYSMIPYEETRRKECTSLLFKRNCTAPAQIKLTPEHIRINDVISRKQAQNRERHDKIIEDILLAMSVESFAQAIEELGVCIGALLVAPLESSVTQIGVRVFYDIVDNLNEVTMKFQPTHDLYFQVLEKLGVFLEADQAAQGLAILRLALKRPDLLELLAGVFVPSRTDVDHFLSMYEFLIDSHLKHCDTQTLFVLFSKFDLLGWMEAYQPKLSEINRLLLLVLQGLEAWSQPDSSLLQDLFRRHLVHIFGYDFPQHYGEVMQLVLDRTSDQKLMPVVLLDLLNALFVRSNCAELSLQQSEVRVHELALDFARRQKLFTLKAATDTLLLLSRHFQKERLHHGLHGLYPKHKDYCQALVLWFTSFGHTLLASAICSYQELLADQISDIVFGSIVETYSPWLIPYTEETVSGVAHWIRQLTPGQSKVLLPWSEQHVSSCKLMIRSFVATIIQVLQYLPSSNKILEHVFAWYVHHFAQSSTTGHVLAPIHEGLAQLPWERFLPPAQHVELLYDSLQKFLPESHAMLGHIFIRIEWNNWFAQMPQPVSILSRLFTIFVKIAFEPNIHIHPNTSKILEDAIRYPWHLVECSELEQLLKWFVASVEPAIALKIPAESNYADRAVLELLRLACAMLPERSAQDAVVLGTAKRMLYTRSMVRMQRACGAKHQKLLATKEGERAFSNAFLELLDSIDGAISSCSEHRTMEEQRREALNLMLELVAPTQTQSQEVSNIHIKALVWWQQRCSPGNLVMCSTLPAIGHLNTYIASIYSLLEASIENYFRTSPEIASWHAPSWQGLMEALSMSLPKLDLMPIMQGSYFFSLHVFVLYKMEEIATDGDKVTFLQDLSQLLENLKTSPQTEPRMALVWGVIIARGCQIAQVNQQVKKPLHMLARHLQIASTKAEGWGDGLLGVIGLKSEVITNRRKVLTRCLACVIFSLFPANRDLRIPSEEYESALRELSMLLANKKFTDIKPLIVRAVSLLKESTFPDIRAVPHMVCRLISIFYEESYLTTIPEVWDFEFKLMAT 2455 Q9HCE0 Ectopic EPG5 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:29130391}. Lysosome {ECO:0000269|PubMed:29130391}. UNIPROT Q9HCE0 UNIPROT A2BDF3 UNIPROT Q9H8C8 PDB 7JHX OMIM 242840 OMIM 615068 DisGeNET 57724 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}. 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}. Q6VMQ6 EBI-7244636 0.37 O55234 EBI-11049538 0.35 P19739 EBI-25685423 0.35 GO:0005737 GO:0005764 GO:0048471 GO:0097352 GO:1990786 GO:0032456 GO:0008333 GO:0006862 GO:0034162 Unknown UniProt Sequence Analysis MAEAVKPQRRAKAKASRTKTKEKKKYETPQREESSEVSLPKTSREQEIPSLACEFKGDHLKVVTDSQLQDDASGQNESEMFDVPLTSLTISNEESLTCNTEPPKEGGEARPCVGDSAVTPKVHPGDNVGTKVETPKNFTEVEENMSVQGGLSESAPQSNFSYTQPAMENIQVRETQNSKEDKQGLVCSSEVPQNVGLQSSCPAKHGFQTPRVKKLYPQLPAEIAGEAPALVAVKPLLRSERLYPELPSQLELVPFTKEQLKILEPGSWLENVESYLEEFDSMAHQDRHEFYELLLNYSRCRKQLLLAEAELLTLTSDCQNAKSRLWQFKEEQMSVQGICADQVKVFSYHRYQRVEMNENALVELKKLFDAKSEHLHQTLALHSYTSVLSRLQVESYIYALLSSSAVLRSSAIHQQGRASKQTESIPSDLCQLKECISVLFMFTRRVNEDTQFHDDILLWLQKLVSVLQRVGCPGDHLFLLNHILRCPAGVSKWAVPFIQIKVLHNPSGVFHFMQSLALLMSPVKNRAEFMCHMKPSERKPSSSGPGSGTWTLVDEGGEEDEDPETSWILLNEDDLVTILAQFPFHELFQHLLGFKAKGDYLPETTRPQEMMKIFAFANSLVELLAVGLETFNRARYRQFVKRIGYMIRMTLGYVSDHWAQYVSHNQGSGLAQQPYSMEKLQVEFDELFLRAVLHVLKAKRLGIWLFMSEMPFGTLSVQMLWKLFYLMHQVESENLQQLSSSLQPAQCKQQLQDPEHFTNFEKCLSSMNSSEEICLLTTFAQMAQARRTNVDEDFIKIIVLEIYEVSYVTLSTRETFSKVGRELLGTITAVHPEIISVLLDRVQETIDQVGMVSLYLFKELPLYLWQPSASEIAVIRDWLLNYNLTVVKNKLACVILEGLNWGFAKQATLHLDQAVHAEVALMVLEAYQKYLAQKPYAGILSESMKQVSYLASIVRYGETPETSFNQWAWNLILRLKLHKNDYGIQPNCPAVPFSVTVPDMTESPTFHPLLKAVKAGMPIGCYLALSMTAVGHSIEKFCAEGIPLLGILVQSRHLRTVVHVLDKILPLFYPCQYYLLKNEQFLSHLLLFLHLDSGVPQGVTQQVTHKVAQHLTGASHGDNVKLLNSMIQAHISVSTQPNEVGPVAVLEFWVQALISQHLWYREQPILFLMDHLCKAAFQLMQEDCIQKLLYQQHKNALGYHCDRSLLSSLVSWIVAGNITPSFVEGLATPTQVWFAWTVLNMESIFEEDSQLRRVIEGELVINSAFTPDQALKKAQTQLKLPIVPSLQRLLIYRWAHQALVTPSDHPLLPLIWQKFFLLYLHRPGPQYGLPIDGCIGRRFFQSPAHINLLKEMKRRLTEVADFHHAASKALRVPAEGSEGLPESHSGTPGYLTSPELHKELVRLFNVYILWLEDENFQKGDTYIPSLPKHYDIHRLAKVMQNQQDLWMEYLNMERIYHEFQETVGLWTQAKLESHSTPCSLSVQLDFTDPLLAKERVLSNLRKHEAPQPPLALHPTKPPVPVISSAVLLSQKDATQLVCTDLNLLQQQARTAALRESQQVALDGELLDTMPKQYVNREEQTTLHLECRGSSGKKCQGAAVVTVQFEGMHKNEAISQQLHVLRKEVKQLQAEAAKPPSLNIVEAAVHAENLITALVNAYKLQPTPGIQKVGISLFFTIVDYVSDETQRHPPTRQFFTSCIEILGQVFISGIKSECRKVLETILKNSRLCSLLSPFFTPNAAPAEFIQLYEQVVKFLSEDNSDMIFMLLTKFDLKQWLSATKPPLSDRTRLLESIHLALTAWGLEPDEDILMPFNLFCKHWTYLLLYQFPDQYSDILRLLMQSSAEQLLSPECWKATLRALGCCAPSCQQGAASTEGAVLPSSSDALLSDKQVMETIQWLSDFFYKLRLSKMDFKSFGLFSKWSPYMADVKTFLGYLVKRLIDLEMTCLAQDPTASRKTVLKSLHSVIIQLFKPWILVLEDNESSQQRHYPWLESDTVVASSIVQLFTDCIDSLHESFKDKLLPGDAGALWLHLMHYCEACTAPKMPEFILYAFHSTYRKLPWKDLHPDQMLMEAFFKVERGSPKSCFLFLGSVLCEVNWVSVLSDAWNSSPHPETRSMIVCLLFMMILLAKEVQLVDQTDSPLLSLLGQTSSLSWHLVDIVSYQSVLSYFSSHYPPSIILAKESYAELIMKLLKVSAGLSIPTDSQKHLDAVPKCQAFTHQMVQFLSTLEQNGKITLAVLEQEMSKLLDDIIVFNPPDMDSQTRHMALSSLFMEVLMMMNNATIPTAEFLRGSIRTWIGQKMHGLVVLPLLTAACQSLASVRHMAETTEACITAYFKESPLNQNSGWGPILVSLQVPELTMEEFLQECLTLGSYLTLYVYLLQCLNSEQTLRNEMKVLLILSKWLEQVYPSSVEEEAKLFLWWHQVLQLSLIQTEQNDSVLTESVIRILLLVQSRQNLVAEERLSSGILGAIGFGRKSPLSNRFRVVARSMAAFLSVQVPMEDQIRLRPGSELHLTPKAQQALNALESMASSKQYVEYQDQILQATQFIRHPGHCLQDGKSFLALLVNCLYPEVHYLDHIR 2579 Q80TA9 Ectopic Epg5 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HCE0}. Lysosome {ECO:0000250|UniProtKB:Q9HCE0}. UNIPROT Q80TA9 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}. GO:0005737 GO:0005764 GO:0048471 GO:0097352 GO:0006914 GO:1990786 GO:0032456 GO:0008333 GO:0006862 GO:0034162 Unknown UniProt Sequence Analysis MAEAVKPRRAKAKASRTKGKEKKKHEALQTCDAGPLPETCREQESPCPASELKGDDLKSSADPQLHSDVCGWNESEMFDIPLTSLTIGDEGPPVQDTEDLKERGEVTAGDGDDEMELKVDPGDNVIAKGEPCKNFPEVEDHTLIQCGPPESTLQPDFPCTQQAVEGSHAREHPTRKQDEAALGCSKVFQNVSLHSSYEAKEVSQPPRVKKLYPELPAEIAEVPALVAVKPLLRSERLYPELPSQPEVTPFTKEQLKLLEPGSWLENVASYVEEFDNIAHQDRHEFYELLLNYSRCRKQLLLAEAELLTLMSDCHSAKSRLWHFKDEQMAVQGICADQVKVYGHHHYQRVEMNENVLGELKKLFDAKSEHLHQTLTLHSYTSVLSRLQVESYIFTLLNSSAALRSLAVYQADQVPKLTESIPSDVCQLKECISVLFMFTRRVSEDAQFHEDILLWLQKLVSVLQRVGCPGDHFFLLNHVLRCPAGIRKWAVPFIQIKVLNNPSGVFHFMQSLALLMSPVKNRAEFMCHMKPSEWKPSSSGPASGNWTLVDEAGEEDEDPETSWILLNEDDLVTLLSQFPFQELFQHLLGFKAKGDYLPETTRPQEMMKIFAFANSLVELLAVGLDTFNRARYRQFVKRIGYLIRMTLGYVSDHWAQYVSHSTGAGLTPQPYSMEKLQVEFDELFLRAVLHVLKAKRLGIWLFMSEMPFGTLSVQMLWKLLYLMHQVESGDLQQLCASLQPAECKRRLQDPEHFASFEKCLSSINSSEEICLLTAFAQMARARRTNVDEDFIKIIVLEIYEVSYVTLSTRETFSKVGRELLGAIAAVHPEIISVLLDRVQETIDQVGMVSLYLFKELPLYLWRPSAPEIAVIRDWLLNNNLTAVKNKLACVILEGLNWGFTEQGTLHLDQALHTEVALLVLEAYQKYLAQKPYTGLISESMKQVSYLASIVRYGETPETSFNQWAWNLILRLKLHKNDFGRQNFPVIPFCSTVPDMTESSMFHPLLKAVKSGLPIGCYLALAVTAVGHSLEKFCAEGIPLLGVLVQSRHLRAVVHALDKILPVFYPYQCYLLKNEQFLSNLLLFLQLDSGVPQGVTQQVTHRVAQHLTGAVHGDNVKLLSSMIQAHICVSTQPDGVGPVAVLEFWVQALISQHLWYREQPILFLMDHLCKTAFHLMQEDCVQKLLYQQHKNALGYHCDRSLLSSLVNWIVAGNITPSFVEGLSTSTQVWFAWTVLNMESIFEEDSQLRRVVERELVINAFSPDQALKKAQVQLKLPIVPSLQRLLIYRWAHQALVTPSDHPLLPLIWQKFFLLYLHRPGPQYGLPVDGCIGRRFFQSPSHVNLLKDMKRRLTEVADFHYAASKALRVPAEGSEGTPEGQAGTPGFLTSPELHRELVRLFNVYVLWLEDENFQKGDTYIPSLPKHYDVHRLAKVMQNQQDLWMEYVNMERIQHEFQETVALWTQAKLESHAAPCSSSAQLDFTDPLLAKARVLSNLEKHEAPHPPLLLHPVRPPVPLIPSAALLTQKDSTQLMCTDLNLLQQQARSATLRESQQVALDGELLETMPKQYVNREDQATLHLECRGSSGKKCQGAAVVTVQFEGMNKNEAVSQQIHVLQKEVRQLQAEAAQPPALNVVEAAVHAENLITALVNTYKLQPTPGVQKLGISLFFTVVDHVSDETQRHPPTRQFFTSCIEILGQVFVSGTKSECRKLLQTILKNRRLCSLLAPFFTPNAAPAEFIQLYERVVTCLREDNSDVIFMLLTKFDIQQWLNSTKPPLSDRTRLLESIHLALTAWGLEPEEDILMPFNLFCKHWTHLLLYQFPDQYSDVLRLLVQSSAEQLLSPECWKATLRALGCYAPSSQQGAASVESSGLHSASRVLLSDKQVMETVQWLSDFFYKLRLSKLDFKSFGLFSKWSPYMADVKTFLGYLVKRLTDLEIASLSQDPTASSKEVLRSLHAQIIQLFKPWILVLEDAESSHQRHYPWLESDTAVASSIVQLFSDCVGSLHTSFKDRLLPGDEGALRLHLLHYCETCTAPKMPEFILYAFHSAYQRLEWKDLHPDQRLMEAFFKVERGSPKSCFLFLGSVLCRVNWVSVLSDAWNPSPLPETQSMAVCLLFMMVLLAKEAQLVDEPDSPLLSLLGQTSSLSWHLVDLVSYQSVLGYFSSHYPPSVVLANDCSSELIVKLLKVSAGLSAHADGRKHVDIVPKCQAFTHQMVQFLSALEQTGKITFPALEREISKLLDDIIIFNPPDMDSQTRHMALSSFFVEVLMMMNNAAVPTAEFLAVSIRTWIGQRVHGLIVLPLLTAACQSLASVRHMAEITEACIMAYFKESSLDQNLGWGPVLVSLQVPQLTARDFLEECLALGSCLTLYVYLLQCLNSEQTVKNDMKMLLVVSGWLEQVYPSSAQEEAKLFLWWHQILQLSLIQLEQNDSVLTESVIRILLMLQSRQSLMAEERLSSGILGAIGLGRRSPLSNRFRVAARSMAAFLLVQVPAEDQIRLKPSSELHLAPKAQQVLTALESMTLSKQYVEYQDQILHALQFIRHPGHCLQNGKSFLALLVNRLYPEVHYLDNIR 2572 Q9H201 Epsin-3 EPN3 9606 None SL-0198 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. UNIPROT Q9H201 UNIPROT A8K6J3 UNIPROT A8KAB2 UNIPROT Q9BVN6 UNIPROT Q9NWK2 Pfam PF01417 Pfam PF02809 PROSITE PS50942 PROSITE PS50330 OMIM 607264 DisGeNET 55040 O95271 EBI-21644009 0.35 Q9Y3C5 EBI-7221338 0.37 Q13571 EBI-7265708 0.37 Q6IQ23 EBI-16398399 0.35 Q9Y6I3 EBI-21644009 0.35 Q9Y597 EBI-21644009 0.35 Q9Y4X5 EBI-21644009 0.35 Q9UK73 EBI-21644009 0.35 Q9UJV3 EBI-21644009 0.35 Q9HCE7 EBI-21644009 0.35 Q9H3F6 EBI-21644009 0.35 Q9H2K2 EBI-21644009 0.35 Q9H0C5 EBI-21644009 0.35 Q96JC1 EBI-21644009 0.35 Q8TBC3 EBI-21644009 0.35 Q8IWV7 EBI-21644009 0.35 Q86YT6 EBI-21644009 0.35 P42575 EBI-21644009 0.35 P0CG47 EBI-21644009 0.35 O95208 EBI-21644009 0.35 O43175 EBI-21644009 0.35 O15344 EBI-21644009 0.35 E9PJD7 EBI-21644009 0.35 P14625 EBI-20908912 0.40 P62258 EBI-25384933 0.35 F1PAA9 EBI-27079701 0.27 P42566 EBI-30823506 0.44 GO:0030125 GO:0005905 GO:0030136 GO:0005768 GO:0070062 GO:0019897 GO:0043231 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0030276 GO:1990175 GO:0005543 GO:0006897 Unknown UniProt Sequence Analysis MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGIGIGSGQLGFSRRYGEDYSRSRGSPSSYNSSSSSPRYTSDLEQARPQTSGEEELQLQLALAMSREEAEKPVPPASHRDEDLQLQLALRLSRQEHEKEVRSWQGDGSPMANGAGAVVHHQRDREPEREERKEEEKLKTSQSSILDLADIFVPALAPPSTHCSADPWDIPGFRPNTEASGSSWGPSADPWSPIPSGTVLSRSQPWDLTPMLSSSEPWGRTPVLPAGPPTTDPWALNSPHHKLPSTGADPWGASLETSDTPGGASTFDPFAKPPESTETKEGLEQALPSGKPSSPVELDLFGDPSPSSKQNGTKEPDALDLGILGEALTQPSKEARACRTPESFLGPSASSLVNLDSLVKAPQVAKTRNPFLTGLSAPSPTNPFGAGEPGRPTLNQMRTGSPALGLAGGPVGAPLGSMTYSASLPLPLSSVPAGLTLPASVSVFPQAGAFAPQPLLPTPSSAGPRPPPPQTGTNPFL 632 Q91W69 Epsin-3 Epn3 10090 None SL-0198 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}. UNIPROT Q91W69 UNIPROT Q9CV55 Pfam PF01417 Pfam PF02809 PROSITE PS50942 PROSITE PS50330 Q9WVK4 EBI-15895272 0.35 P42566 EBI-15895302 0.35 Q8BH64 EBI-15895326 0.35 GO:0005938 GO:0030125 GO:0005905 GO:0030136 GO:0005768 GO:0019897 GO:0043231 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0030276 GO:1990175 GO:0005543 GO:0006897 Unknown UniProt Sequence Analysis MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFAEVMGMVWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGMGIGSGQLGYSRRSRGSPSSYTSASSSPRYASDLEQARPQTSGEEELQLQLALAMSREEAERPVPPASHRDEDLQLQLALSLSRQEHEKGVRSWKGDDSPVANGAEPAGQRRQRDREPEREERKEEEKLKTSQSSILDLADIFAPAPALPSTHCSADPWDIPGLRPNTEPSGSSWGPSADPWSPVPSGNALSRSQPWDLLPTLSSSEPWGRTPVLPSGPPIADPWAPSSPTRKLPSTGADPWGASMETSDTSALGGASPFDPFAKPLESTEPKESRDSAQALPTGKSPSTVELDPFGDSSPSCKQNGMKEPEALDLGVLGEALPQQPGKEARPCRTPESFLGPSASSLVNLDSLVKAPLAARTRNPFLTGLGVPSPTNPFGAGDQGRPTLNQMRTGSPALGLPPGGPVGAPVGSMTYSASLPLPLSSVPVGATLPASVSVFPQAGAFAPPPASLPQPLLPTSGPMGPLPPQAGTNPFL 636 Q4V882 Epsin-3 Epn3 10116 None SL-0198 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}. UNIPROT Q4V882 Pfam PF01417 PROSITE PS50942 PROSITE PS50330 GO:0005938 GO:0030125 GO:0005905 GO:0030136 GO:0005768 GO:0019897 GO:0005634 GO:0048471 GO:0005886 GO:0030276 GO:1990175 GO:0005543 GO:0006897 Unknown UniProt Sequence Analysis MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFAEVMGMVWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGMGIGSGQLGFSRRSRGSPSSYTSASSSPRYASDLEQARPQTSGEEELQLQLALAMSREEAEKGGRSWKGDDFPVANGAEPAGQRRRDREPEREERKEEEKLKTSQSSILDLADVFAPAPALPSTHCSADPWDIPGLRPNTEPSGSSWGPSADPWSPVPSGNALSRSQPWDLLPTLSSSEPWGRTPVLPSGPPITDPWAPSSPTPKLPSTGVDPWGASVETSNTSALGGASPFDPFAKPLESTEPMESRDSAQALPKGKSPSPVELDPFGDSSPSCKQNGVKETEALDLGVLGEALTQQPGKEARPCRTPESFLGPSASSLVNLDSLVKAPLAARTRNPFLTGLSAPSPTNPFGAGEQGRPTLNQMRTGSPALGLPPGGPVGVPLGSMTYSASLPLPLSSVPVGATLPASVSVFPQAGAFAPPPASLPQPLLPTSDPVGPLPPQAGTNPFL 608 A7Z035 Clathrin CLINT1 9913 None SL-0198 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}. UNIPROT A7Z035 Pfam PF01417 PROSITE PS50942 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}. GO:0030125 GO:0005768 GO:0005798 GO:0005654 GO:0048471 GO:0005886 GO:0005802 GO:0030276 GO:0005543 GO:0006897 Peripheral UniProt By Similarity {ECO:0000250} MLNMWKVRELVDKATNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYVGVSSDSVGGFRYSERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKARRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSLKTSVPSSKSSGDLVDLFDGTSQSTGGSADLFGGFADFGSAAASGNFPSQVTATSGNGDFGDWSAFNQAPSVPVAASGELFGSASQPAVELVSSSQPALGPPPAASNSSDLFDLMGSSQATMTSSQSMNFSMMSTNTVGLGLPMSRSQPLQNVSTVLQKPNPLYNQNTDMVQKSVSKTLPSTWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPMNMMTQSFGAVNLSSPSNMLPVRPQTNPLMGGPMPMSMPNVMTGTMGMAPLGNSPMMNQSMMGMNMNIGMSTTGMGLTGTMGMGMPNLAMTSGTMQPKQDAFANFANFSK 643 Q14677 Clathrin CLINT1 9606 None SL-0198 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. UNIPROT Q14677 UNIPROT B7Z6F8 UNIPROT D3DQJ6 UNIPROT Q8NAF1 UNIPROT Q96E05 PDB 1XGW PDB 2QY7 PDB 2V8S Pfam PF01417 PROSITE PS50942 OMIM 607265 DisGeNET 9685 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}. O14976 EBI-11150908 0.35 O15027 EBI-11083608 0.35 P22892 EBI-7071326 0.54 P13569 EBI-1171360 0.35 Q68FD5 EBI-7071372 0.40 Q96FJ0 EBI-2511015 0.40 O95630 EBI-2511053 0.40 Q9BXB5 EBI-2514827 0.40 Q9JLQ0 EBI-2563436 0.40 A0A5P8YCG4 EBI-2847836 0.00 A0A5P8YJZ1 EBI-2870530 0.00 Q8CKM1 EBI-2870523 0.00 Q8ZD27 EBI-2870516 0.00 A0A5P8YBI5 EBI-2870542 0.00 Q8ZDX4 EBI-2870549 0.00 Q99459 EBI-7954144 0.35 O95166 EBI-2946896 0.44 Q9H0R8 EBI-2947275 0.52 P60520 EBI-2947563 0.44 Q9GZQ8 EBI-2947914 0.52 Q9BXW4 EBI-2948265 0.44 Q9H492 EBI-3044058 0.35 Q13618 EBI-21329068 0.35 Q9NQW6 EBI-11009421 0.35 Q91X51 EBI-11015786 0.35 Q99JI4 EBI-11026623 0.35 Q92734 EBI-11029015 0.35 Q92614 EBI-11030093 0.35 Q96H55 EBI-11031416 0.35 O75787 EBI-11037152 0.35 P56377 EBI-11037753 0.35 P21333 EBI-11038784 0.35 Q61879 EBI-11041929 0.35 P60710 EBI-11045267 0.35 P51148 EBI-11046231 0.35 P63167 EBI-12449761 0.51 Q91YN9 EBI-11052510 0.35 Q9UHB6 EBI-11058729 0.35 Q9D6P8 EBI-11062262 0.35 G3X972 EBI-11079358 0.35 Q91VZ6 EBI-11079957 0.35 Q16643 EBI-11080402 0.35 P09497 EBI-11081190 0.35 Q9NYZ3 EBI-11081743 0.35 Q13492 EBI-11082344 0.35 Q00610 EBI-11082478 0.35 Q8N3V7 EBI-11086992 0.35 P13541 EBI-11092646 0.35 Q8VDD5 EBI-11092730 0.35 Q9WTI7 EBI-11093786 0.35 P12883 EBI-11098156 0.35 P35579 EBI-11098811 0.35 Q96QS3 EBI-11107478 0.35 P16333 EBI-11108107 0.35 Q9Z1Z0 EBI-11110688 0.35 P47755 EBI-11117728 0.35 Q6ZNC8 EBI-11121915 0.35 P46940 EBI-11132927 0.35 Q99615 EBI-11136121 0.35 P62140 EBI-11142496 0.35 Q5BJF6 EBI-11367291 0.27 Q86X19 EBI-11372615 0.27 Q9P0N5 EBI-11398030 0.27 Q6P5F9 EBI-11603310 0.35 Q8WTR4 EBI-16430940 0.56 Q96FJ2 EBI-12449804 0.51 P03431 EBI-12579531 0.35 P03428 EBI-12579909 0.35 I6T1Z2 EBI-12581451 0.35 Q5EP37 EBI-12582677 0.35 C5E526 EBI-12584689 0.35 Q1K9H5 EBI-12588354 0.35 B4URF7 EBI-12588729 0.35 Q6IQ23 EBI-16398399 0.35 Q96CW1 EBI-21520588 0.35 O75379 EBI-21524155 0.35 Q9UEU0 EBI-21525256 0.35 Q9UNK0 EBI-21615189 0.35 Q9NSY1 EBI-21615189 0.35 Q9H0L4 EBI-21615189 0.35 Q96D71 EBI-21615189 0.35 Q8WXE9 EBI-21615189 0.35 Q8WU79 EBI-21615189 0.35 Q15311 EBI-21615189 0.35 Q10567 EBI-21615189 0.35 P53675 EBI-21615189 0.35 O95782 EBI-21615189 0.35 O94973 EBI-21615189 0.35 O00443 EBI-21615189 0.35 B9A025 EBI-21615189 0.35 Q9UJ41 EBI-21644136 0.35 Q96T17 EBI-21796065 0.35 Q9UJY4 EBI-21886169 0.35 O88384 EBI-15671994 0.65 Q01968 EBI-16412089 0.35 Q14684 EBI-16686997 0.35 O15155 EBI-16788067 0.27 P11279 EBI-16794808 0.27 O43493 EBI-16800265 0.42 P14404 EBI-21026252 0.35 Q5T7N2 EBI-20993270 0.35 Q9NPJ6 EBI-25472202 0.27 Q9Y586 EBI-21261050 0.35 G3V2R1 EBI-21264254 0.35 O84226 EBI-22302652 0.40 Q9C0B5 EBI-25636144 0.35 O76024 EBI-25897869 0.56 O60333 EBI-25915115 0.56 O43464 EBI-27050249 0.35 Q96LU5 EBI-27050332 0.35 Q96T52 EBI-27050444 0.35 F1PAA9 EBI-27079701 0.27 A0A0H3NFP4 EBI-27055788 0.27 A0A0H3NB75 EBI-27055983 0.27 P35226 EBI-27108918 0.35 Q99592 EBI-27093179 0.35 P80192 EBI-28938802 0.35 Q5TCX8 EBI-28941668 0.35 Q9BYP7 EBI-28946054 0.35 Q9H3S7 EBI-27114830 0.35 Q9Y6R9 EBI-27132749 0.35 P63010 EBI-30816421 0.44 P54756 EBI-32720907 0.27 Q15375 EBI-32721052 0.27 P11362 EBI-32721578 0.27 P21802 EBI-32721907 0.27 P22455 EBI-32722168 0.27 Q16288 EBI-32724526 0.27 P07949 EBI-32725031 0.27 P03372 EBI-34581889 0.35 GO:0030125 GO:0005829 GO:0005768 GO:0005794 GO:0043231 GO:0016020 GO:0005654 GO:0048471 GO:0005886 GO:0045296 GO:0030276 GO:0005543 GO:0006897 Peripheral UniProt Sequence Analysis MLNMWKVRELVDKATNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYVGVSSDSVGGFRYSERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKARRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSVKTSVPSSKSSGDLVDLFDGTSQSTGGSADLFGGFADFGSAAASGSFPSQVTATSGNGDFGDWSAFNQAPSGPVASSGEFFGSASQPAVELVSGSQSALGPPPAASNSSDLFDLMGSSQATMTSSQSMNFSMMSTNTVGLGLPMSRSQNTDMVQKSVSKTLPSTWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPMNVMTQSFGAVNLSSPSNMLPVRPQTNALIGGPMPMSMPNVMTGTMGMAPLGNTPMMNQSMMGMNMNIGMSAAGMGLTGTMGMGMPNIAMTSGTVQPKQDAFANFANFSK 625 Q99KN9 Clathrin Clint1 10090 None SL-0198 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}. UNIPROT Q99KN9 UNIPROT Q8CFH4 Pfam PF01417 PROSITE PS50942 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}. GO:0030125 GO:0030136 GO:0005768 GO:0005794 GO:0043231 GO:0005654 GO:0048471 GO:0005886 GO:0030276 GO:0005543 GO:0048268 GO:0006897 Peripheral UniProt By Similarity {ECO:0000250} MLIFMYLYVCVCTCTCAFSLCSTNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYVGVSSDSVGGFRYNERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKARRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSAKPSVPSSKSSGDLVDLFDGSSQSAGGSADLFGGFADFGSAAASGNFPSQATSGNGDFGDWSAFNQAPSGPVASGGELFGSAPQSAVELISASQPALGPPPAASNSADLFDLMGSSQATMTSSQSMNFSLMSTNTVGLGLPMSRSQNTDMVQKSASKTLPSTWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPLNVMTQSFGAVNLSSPSNMLPVRPQTNPLLGGPMPMNMPGVMTGTMGMAPLGNSAGMSQGMVGMNMNMGMSASGMGLSGTMGMGMPSMAMPSGTVQPKQDAFANFANFSK 631 O18735 Receptor ERBB2 9615 None SL-0198 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}. UNIPROT O18735 Pfam PF00757 Pfam PF14843 Pfam PF07714 Pfam PF01030 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. GO:0009925 GO:0005769 GO:0005887 GO:0005634 GO:0048471 GO:0005886 GO:0043235 GO:0005524 GO:0001042 GO:0004714 GO:0071364 GO:0071363 GO:0035556 GO:0030182 GO:0030307 GO:0008284 GO:0033674 GO:0043410 GO:0090314 GO:0045943 GO:0045727 GO:0070372 GO:0032886 GO:0007169 Transmembrane UniProt Sequence Analysis {ECO:0000255} MELAAWCRWGLLLALLPSGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPANASLSFLQDIQEVQGYVLIAHSQVRQIPLQRLRIVRGTQLFEDNYALAVLDNGDPLEGGIPAPGAAQGGLRELQLRSLTEILKGGVLIQRSPQLCHQDTILWKDVFHKNNQLALTLIDTNRFSACPPCSPACKDAHCWGASSGDCQSLTRTVCAGGCARCKGPQPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTSCPYNYLSTDVGSCTLVCPLNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLRVFEALEEITGYLYISAWPDSLPNLSVFQNLRVIRGRVLHDGAYSLTLQGLGISWLGLRSLRELGSGLALIHRNARLCFVHTVPWDQLFRNPHQALLHSANRPEEECVGEGLACYPCAHGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVKDRYCLPCHSECQPQNGSVTCFGSEADQCVACAHYKDPPFCVARCPSGVKPDLSFMPIWKFADEEGTCQPCPINCTHSCADLDEKGCPAEQRASPVTSIIAAVVGILLAVVVGLVLGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESIPPRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVAEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPEPTPGAGGTAHRRHRSSSTRNGGGELTLGLEPSEEEPPKSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPSQDPSPLQRYSEDPTVPLPPETDGKVAPLTCSPQPEYVNQPEVWPQPPLALEGPLPPSRPAGATLERPKTLSPKTLSPGKNGVVKDVFAFGSAVENPEYLAPRGRAAPQPHPPPAFSPAFDNLYYWDQDPSERGSPPSTFEGTPTAENPEYLGLDVPV 1259 P04626 Receptor ERBB2 9606 None SL-0198 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. UNIPROT P04626 UNIPROT B2RZG3 UNIPROT B4DHN3 UNIPROT Q14256 UNIPROT Q6LDV1 UNIPROT Q9UMK4 UNIPROT X5D2V5 PDB 1MFG PDB 1MFL PDB 1MW4 PDB 1N8Z PDB 1QR1 PDB 1S78 PDB 2A91 PDB 2JWA PDB 2KS1 PDB 2L4K PDB 2N2A PDB 3BE1 PDB 3H3B PDB 3MZW PDB 3N85 PDB 3PP0 PDB 3RCD PDB 3WLW PDB 3WSQ PDB 4GFU PDB 4HRL PDB 4HRM PDB 4HRN PDB 4NND PDB 5K33 PDB 5KWG PDB 5MY6 PDB 5O4G PDB 5OB4 PDB 5TQS PDB 6ATT PDB 6BGT PDB 6J71 PDB 6LBX PDB 6OGE PDB 7JXH PDB 7MN5 PDB 7MN6 PDB 7MN8 Pfam PF00757 Pfam PF14843 Pfam PF07714 Pfam PF01030 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 OMIM 137800 OMIM 164870 OMIM 167000 OMIM 211980 OMIM 613659 OMIM 619465 DisGeNET 2064 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}. 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. O00165 EBI-32718334 0.35 O70248 EBI-22242478 0.35 O75190 EBI-8770853 0.35 O75694 EBI-32721465 0.27 P00519 EBI-7881352 0.44 P00533 EBI-702075 0.95 P04406 EBI-9687897 0.55 Q9H299 EBI-8533023 0.40 P29353 EBI-8533045 0.82 O00459 EBI-8533204 0.70 P62993 EBI-8533665 0.92 O00443 EBI-641125 0.35 O00750 EBI-641125 0.52 P23727 EBI-7472363 0.40 P43405 EBI-7872191 0.44 P20936 EBI-7872273 0.59 P19174 EBI-7872323 0.44 Q92569 EBI-7872366 0.59 P27986 EBI-7872561 0.76 P23458 EBI-7872614 0.44 Q9Y490 EBI-7872742 0.44 Q7KZ85 EBI-7872692 0.44 Q63HR2 EBI-7872814 0.44 Q9UQF2 EBI-7873480 0.59 Q13387 EBI-7873391 0.44 P09769 EBI-7873560 0.44 O14796 EBI-7873641 0.44 P98077 EBI-7873711 0.44 Q8TEW6 EBI-7873800 0.44 P46109 EBI-7873890 0.44 P46108 EBI-7873995 0.44 P42684 EBI-7874156 0.44 Q9NSE2 EBI-7874052 0.44 P42681 EBI-7877479 0.44 P42224 EBI-7877610 0.57 O15524 EBI-7877654 0.44 Q9H6Q3 EBI-7877680 0.44 Q13239 EBI-7877723 0.44 Q8WYP3 EBI-7877809 0.44 Q13671 EBI-7877852 0.44 Q7Z7G1 EBI-7878187 0.44 Q08881 EBI-7878322 0.44 O14654 EBI-7878365 0.44 P35568 EBI-7878450 0.44 Q14451 EBI-7878494 0.78 Q7Z6G8 EBI-7878520 0.44 Q6PKX4 EBI-7878747 0.44 Q99704 EBI-7878971 0.44 Q8WV28 EBI-7879040 0.44 P51451 EBI-7879084 0.44 O95704 EBI-7879155 0.44 O00213 EBI-7879203 0.44 Q92625 EBI-7879248 0.44 Q9UKW4 EBI-7879334 0.44 P52735 EBI-7879377 0.44 Q96D37 EBI-7879875 0.44 Q68CZ2 EBI-7879918 0.44 P78314 EBI-7880141 0.44 Q9NP31 EBI-7880184 0.44 Q06124 EBI-7880270 0.59 P16885 EBI-7880409 0.57 O43639 EBI-7880962 0.44 O75791 EBI-7881093 0.57 O75553 EBI-7881180 0.44 P51813 EBI-7881223 0.44 O75815 EBI-7881266 0.44 P40763 EBI-7883743 0.78 Q92529 EBI-7883839 0.44 P42679 EBI-7884171 0.59 Q9UQQ2 EBI-7884193 0.44 P16591 EBI-7884310 0.44 Q6ZV89 EBI-7884338 0.44 P15882 EBI-7884418 0.44 P42680 EBI-7891341 0.44 Q9BRG2 EBI-7892184 0.44 O14492 EBI-7893084 0.44 P21860 EBI-875459 0.97 Q15303 EBI-875465 0.82 Q80TH2 EBI-7806162 0.37 P04626 EBI-1000502 0.93 P62157 EBI-1257031 0.40 P62161 EBI-1257044 0.44 P16070 EBI-1774582 0.35 P08575 EBI-2256762 0.00 Q15262 EBI-2257483 0.00 P23470 EBI-2258522 0.00 P23471 EBI-2263296 0.00 P23467 EBI-2264176 0.00 Q12913 EBI-2264587 0.00 Q16827 EBI-2265156 0.00 P26045 EBI-2266001 0.00 Q05209 EBI-3952071 0.59 Q9Y2R2 EBI-2266470 0.00 Q02297 EBI-2460992 0.44 P12931 EBI-8289901 0.71 P41240 EBI-8677066 0.35 Q05397 EBI-2942138 0.54 O95980 EBI-8569595 0.56 Q9Y316 EBI-7072663 0.40 Q14974 EBI-4373084 0.57 P49792 EBI-4373195 0.46 O14980 EBI-4373229 0.56 Q00610 EBI-4373234 0.35 Q15075 EBI-4373273 0.57 P50570 EBI-4373368 0.35 P42566 EBI-4373373 0.43 P60709 EBI-4373715 0.54 O95602 EBI-4373923 0.57 Q9UBN7 EBI-4398276 0.55 P15309 EBI-8681281 0.47 P98172 EBI-5451673 0.46 P46940 EBI-5458762 0.60 O43157 EBI-6092574 0.40 O75367 EBI-6249307 0.56 P06401 EBI-6255956 0.35 Q96SB4 EBI-6659552 0.44 P08238 EBI-6424213 0.79 Q14289 EBI-6589791 0.27 P35070 EBI-6590054 0.27 P14923 EBI-6592604 0.27 P01135 EBI-6593605 0.27 Q99650 EBI-6595538 0.27 Q16543 EBI-8770673 0.69 Q03169 EBI-8770853 0.35 P25686 EBI-8770853 0.35 P33947 EBI-8770853 0.35 Q9HCY8 EBI-8770853 0.35 Q3ZCQ8 EBI-8770853 0.53 P42704 EBI-8770853 0.53 P36542 EBI-8770853 0.53 P08195 EBI-8770853 0.35 P07355 EBI-8770853 0.35 Q9NVI7 EBI-8770853 0.53 P07900 EBI-8770853 0.86 O60884 EBI-8770853 0.57 P15880 EBI-8770853 0.35 O00483 EBI-8770853 0.53 P02786 EBI-8770853 0.67 P27348 EBI-8770853 0.35 P55795 EBI-8770853 0.35 Q00325 EBI-8770853 0.53 P62714 EBI-8770853 0.35 Q9H254 EBI-8770853 0.35 P11021 EBI-8770853 0.66 P49411 EBI-8770853 0.35 P61619 EBI-8770853 0.53 P30153 EBI-8770853 0.35 Q99959 EBI-8770853 0.35 P67775 EBI-8770853 0.35 Q9BVV7 EBI-8770853 0.53 Q9P035 EBI-8770853 0.35 Q92504 EBI-8770853 0.53 Q93084 EBI-8770853 0.35 Q8TF42 EBI-8770853 0.35 P62879 EBI-8770853 0.35 Q9UJM3 EBI-8770853 0.66 O95292 EBI-8770853 0.67 Q9HAV0 EBI-8770853 0.35 P43307 EBI-8770853 0.35 Q8WUY1 EBI-8770853 0.53 P35232 EBI-8770853 0.35 Q8NHS0 EBI-8770853 0.35 Q99623 EBI-8770853 0.35 Q9UBM7 EBI-8770853 0.35 P53007 EBI-8770853 0.35 P27824 EBI-8770853 0.57 Q9NTG1 EBI-8770853 0.35 P05023 EBI-8770853 0.64 P62873 EBI-8770853 0.35 Q9P0L0 EBI-8770853 0.55 P10620 EBI-8770853 0.35 P16520 EBI-8770853 0.35 Q9GZT3 EBI-8770853 0.35 O95470 EBI-8770853 0.35 P31689 EBI-8770853 0.53 Q96FQ6 EBI-8770853 0.35 P57088 EBI-8770853 0.35 Q8IXB1 EBI-8770853 0.35 O95573 EBI-8770853 0.53 P16615 EBI-8770853 0.35 Q14032 EBI-8997691 0.37 Q9BU70 EBI-8997704 0.37 P49336 EBI-8997717 0.37 Q14093 EBI-8997730 0.37 O75474 EBI-8997756 0.37 P09467 EBI-8997743 0.37 P37058 EBI-8997769 0.37 Q9P1Z9 EBI-8997782 0.37 Q02750 EBI-8997795 0.37 Q6FHJ7 EBI-8997821 0.37 Q15797 EBI-8997834 0.37 O75820 EBI-8997860 0.37 P01137 EBI-8997847 0.37 O94812 EBI-9064260 0.37 P08133 EBI-9064247 0.37 P41252 EBI-9064312 0.37 P51797 EBI-9064273 0.37 Q9P2T1 EBI-9064286 0.55 Q00341 EBI-9064299 0.37 Q9BUL5 EBI-9064351 0.37 Q8IW90 EBI-9064325 0.37 Q96DR8 EBI-9064338 0.37 Q9H3H9 EBI-9064403 0.37 P49005 EBI-9064364 0.37 P07602 EBI-9064377 0.37 Q9Y6E0 EBI-9064390 0.37 Q9Y5J1 EBI-9064442 0.37 Q15904 EBI-9064416 0.37 Q8N6N2 EBI-9064429 0.37 P05093 EBI-9067433 0.37 Q14627 EBI-9067472 0.37 O94923 EBI-9067459 0.37 Q9Y337 EBI-9067485 0.37 O95274 EBI-9067498 0.37 P11245 EBI-9067511 0.37 Q9P2W1 EBI-9067537 0.37 Q9GZV8 EBI-9067524 0.37 Q9BYZ6 EBI-9067550 0.37 Q92748 EBI-9067563 0.37 Q13451 EBI-9363176 0.40 Q3UJD6 EBI-9363211 0.40 Q6PK50 EBI-9363230 0.40 Q9BPW0 EBI-9363250 0.40 P58340 EBI-9363270 0.40 Q9BTE6 EBI-9363294 0.40 Q9Y266 EBI-9363318 0.40 Q13200 EBI-9363339 0.40 Q8IWX7 EBI-9363369 0.40 P31948 EBI-9363393 0.57 Q8IVD9 EBI-9363414 0.40 B4DYC6 EBI-9363439 0.40 Q96BE0 EBI-9363465 0.40 Q9HB71 EBI-9363493 0.57 Q15773 EBI-9363541 0.40 Q53FC7 EBI-9363565 0.40 Q13882 EBI-9293590 0.63 P14618 EBI-9353947 0.44 P06241 EBI-9396596 0.56 P15311 EBI-9690211 0.37 P06461 EBI-11723785 0.35 P0C739 EBI-11725101 0.35 P0CK58 EBI-11732874 0.35 P48651 EBI-11145552 0.35 P26641 EBI-11145552 0.35 O15260 EBI-11145552 0.35 Q9H9Y6 EBI-11145552 0.35 Q92973 EBI-11145552 0.35 Q3V6T2 EBI-11145552 0.35 P11498 EBI-11145552 0.35 Q8ND82 EBI-11145552 0.35 Q9Y251 EBI-11145552 0.35 Q969S3 EBI-11145552 0.35 Q99952 EBI-12739796 0.56 P22681 EBI-13637258 0.40 P04201 EBI-21538834 0.35 Q8TDQ0 EBI-21556046 0.35 P43115 EBI-21607127 0.35 P37173 EBI-21668347 0.35 P40259 EBI-21668943 0.35 Q58DX5 EBI-21782845 0.35 P24394 EBI-21800565 0.35 Q8NBA8 EBI-21829890 0.35 P14625 EBI-16072470 0.40 Q93034 EBI-16247158 0.40 O14522 EBI-20977013 0.37 Q92729 EBI-20977022 0.37 Q15256 EBI-20977323 0.51 Q9H0C8 EBI-20980596 0.37 O95147 EBI-20980636 0.37 Q8NEJ0 EBI-20980646 0.37 Q8WTR2 EBI-20980656 0.37 Q8WUJ0 EBI-20980666 0.37 P29350 EBI-20980616 0.37 P35813 EBI-20980576 0.37 P49593 EBI-20980586 0.37 Q96LT7 EBI-20938756 0.35 B4F779 EBI-22242273 0.35 P62078 EBI-22242273 0.35 A0A0G2K064 EBI-22242273 0.35 Q64537 EBI-22242273 0.35 Q6AZ23 EBI-22242273 0.35 Q62985 EBI-22242478 0.35 P41499 EBI-22242478 0.35 F1LM93 EBI-22242478 0.35 A0A0G2JVN4 EBI-22242478 0.35 P68101 EBI-22242478 0.35 M0R6T4 EBI-22242478 0.35 Q3KRF2 EBI-22242478 0.35 Q5M963 EBI-22242478 0.35 D3ZT90 EBI-22242478 0.35 Q8K1Q0 EBI-22242478 0.35 Q6AYD5 EBI-22242478 0.35 Q9QZC5 EBI-22242478 0.35 P62083 EBI-22242478 0.35 B2GV09 EBI-22242478 0.35 B2RZ33 EBI-22242478 0.35 D3ZD73 EBI-22242478 0.35 M0R7K1 EBI-22242478 0.35 P62703 EBI-22242478 0.35 G3V8S2 EBI-22242478 0.35 Q9Z2M4 EBI-22242478 0.35 Q66X93 EBI-22242478 0.35 Q9WVK3 EBI-22242478 0.35 Q8VID1 EBI-22242478 0.35 P10860 EBI-22242478 0.35 P15651 EBI-22242478 0.35 P24666 EBI-25367578 0.37 P25098 EBI-25367534 0.37 P26038 EBI-25367457 0.37 P63104 EBI-25367490 0.37 Q15654 EBI-25367468 0.37 Q96NW7 EBI-25367523 0.37 P04075 EBI-25367688 0.37 O00170 EBI-25367666 0.37 Q6ZMQ8 EBI-25367655 0.37 P09972 EBI-25367699 0.37 Q13367 EBI-25367710 0.37 Q02952 EBI-25367677 0.37 P84085 EBI-25367743 0.37 P84077 EBI-25367732 0.37 P51693 EBI-25367721 0.37 Q7L266 EBI-25367754 0.37 P27449 EBI-25367765 0.37 Q12981 EBI-25367776 0.37 Q96D05 EBI-25367787 0.37 Q9UKR5 EBI-25367798 0.37 Q96A57 EBI-25367809 0.37 P57076 EBI-25367820 0.37 Q8N5G0 EBI-25367831 0.37 P16152 EBI-25367842 0.37 Q9Y2S6 EBI-25367853 0.37 P12277 EBI-25367897 0.37 O75122 EBI-25367908 0.37 Q14055 EBI-25367919 0.37 Q14050 EBI-25367930 0.37 P52943 EBI-25367941 0.37 O75534 EBI-25367952 0.37 P23528 EBI-25367886 0.37 Q9NYZ1 EBI-25367974 0.37 P62942 EBI-25367985 0.37 Q00688 EBI-25367996 0.37 P49368 EBI-25367864 0.37 Q8N111 EBI-25367875 0.37 Q03001 EBI-25367963 0.37 P23677 EBI-25368128 0.37 Q7Z5L9 EBI-25368117 0.37 Q12906 EBI-25368106 0.37 P10809 EBI-25368095 0.37 P38646 EBI-25368084 0.37 P06396 EBI-25368073 0.37 Q13491 EBI-25368062 0.37 O76003 EBI-25368051 0.37 P60520 EBI-25368040 0.37 Q9H0R8 EBI-25368029 0.37 Q14643 EBI-25368139 0.37 O75369 EBI-25368018 0.37 Q14318 EBI-25368007 0.55 Q9H9V9 EBI-25368150 0.37 Q07866 EBI-25368172 0.37 Q8NC69 EBI-25368161 0.37 Q9BRJ7 EBI-25368260 0.37 Q9Y2I6 EBI-25368249 0.37 Q643R3 EBI-25368194 0.37 B2RTY4 EBI-25368227 0.37 Q7L2J0 EBI-25368216 0.37 P40925 EBI-25368205 0.37 O00214 EBI-25368183 0.37 Q14690 EBI-25368293 0.37 P11940 EBI-25368282 0.37 Q9ULJ1 EBI-25368271 0.37 P12036 EBI-25368238 0.37 P30086 EBI-25368304 0.37 P18669 EBI-25368315 0.37 Q9Y237 EBI-25368326 0.37 Q14863 EBI-25368337 0.37 P30044 EBI-25368359 0.37 P25786 EBI-25368370 0.37 P17980 EBI-25368381 0.37 P51148 EBI-25368392 0.37 Q8NDT2 EBI-25368403 0.37 Q6NTF9 EBI-25368414 0.37 Q8N4K4 EBI-25368425 0.37 Q15181 EBI-25368348 0.37 P31949 EBI-25368447 0.37 Q14151 EBI-25368458 0.37 Q9Y6D0 EBI-25368469 0.37 O43246 EBI-25368480 0.37 Q9NQC3 EBI-25368436 0.37 O60641 EBI-25368502 0.37 P10451 EBI-25368513 0.37 P16949 EBI-25368524 0.37 Q93045 EBI-25368535 0.37 Q9NXE4 EBI-25368491 0.37 Q9HCE3 EBI-25368634 0.37 Q9ULU4 EBI-25368623 0.37 Q96NC0 EBI-25368612 0.37 Q8TCF1 EBI-25368601 0.37 P19971 EBI-25368590 0.37 P10599 EBI-25368579 0.37 Q8WW01 EBI-25368568 0.37 Q9H6X4 EBI-25368557 0.37 O15061 EBI-25368546 0.37 P0DOF2 EBI-25603126 0.35 Q96JA1 EBI-25424141 0.75 Q6UXM1 EBI-25424266 0.35 P0DTD8 EBI-25687199 0.53 Q7TFA1 EBI-25688644 0.35 F1PAA9 EBI-27079701 0.27 P63252 EBI-28956128 0.27 Q9BUF5 EBI-32718334 0.35 Q58FF8 EBI-32718334 0.35 Q01813 EBI-32718334 0.35 Q9NNW5 EBI-32718334 0.35 P05141 EBI-32718334 0.35 Q53GQ0 EBI-32718334 0.35 P00367 EBI-32718334 0.42 Q5T9A4 EBI-32718334 0.35 P50402 EBI-32718334 0.35 P17858 EBI-32718334 0.35 A1L0T0 EBI-32718334 0.35 Q15293 EBI-32718334 0.35 Q96EY1 EBI-32718334 0.35 Q9BSD7 EBI-32718334 0.42 P13674 EBI-32718334 0.42 P13667 EBI-32718334 0.35 Q9H936 EBI-32718334 0.35 P42338 EBI-32718334 0.35 Q9UBS4 EBI-32718334 0.35 Q9Y6K0 EBI-32718334 0.35 Q9Y4W6 EBI-32718334 0.42 O14967 EBI-32718334 0.35 Q9UBX3 EBI-32718334 0.35 Q5VV42 EBI-32718334 0.35 P05067 EBI-32718334 0.35 Q9H0U4 EBI-32718334 0.35 Q8IV08 EBI-32718334 0.35 Q9UET6 EBI-32718334 0.35 O43819 EBI-32718334 0.35 Q9Y4L1 EBI-32718334 0.42 O94905 EBI-32718334 0.35 Q9NXW2 EBI-32718334 0.35 Q5XKP0 EBI-32718334 0.35 P62158 EBI-32718334 0.42 Q9NZ01 EBI-32718334 0.35 Q04837 EBI-32718334 0.35 Q5K4L6 EBI-32718334 0.35 Q15072 EBI-32718334 0.35 O15269 EBI-32718334 0.35 Q13308 EBI-32718334 0.35 P54709 EBI-32718334 0.35 Q9H3P7 EBI-32721465 0.27 O95487 EBI-32721465 0.27 Q14141 EBI-32721465 0.27 Q96B97 EBI-32721465 0.27 O95757 EBI-32721465 0.27 O75410 EBI-32721465 0.27 P05198 EBI-32721465 0.27 Q15437 EBI-32721465 0.27 P35241 EBI-32721465 0.27 Q13643 EBI-32721465 0.27 Q92599 EBI-32721465 0.27 Q9NSK0 EBI-32721465 0.27 O60282 EBI-32721465 0.27 P16333 EBI-32721465 0.27 Q12774 EBI-32721465 0.27 P63244 EBI-32721465 0.27 Q96JB5 EBI-32721465 0.27 O95486 EBI-32721465 0.27 Q13586 EBI-32721465 0.27 P43034 EBI-32721465 0.27 P18085 EBI-32721465 0.27 P51648 EBI-32721465 0.27 Q9GZT9 EBI-32721465 0.27 Q9UKD2 EBI-32721465 0.27 Q93008 EBI-32721465 0.27 P09543 EBI-32721465 0.27 Q96PK6 EBI-32721465 0.27 Q5JRA6 EBI-32721465 0.27 Q8N1F7 EBI-32721465 0.27 P51659 EBI-32721465 0.27 O95433 EBI-32721465 0.27 Q9Y5M8 EBI-32721465 0.27 Q15717 EBI-32721465 0.27 Q96S66 EBI-32721465 0.27 Q9H939 EBI-32721465 0.27 P61088 EBI-32721465 0.27 Q92974 EBI-32721465 0.27 Q5VUB5 EBI-32721465 0.27 O94979 EBI-32721465 0.27 Q9H9A6 EBI-32721465 0.27 O14745 EBI-32721465 0.27 Q13541 EBI-32721465 0.27 Q14126 EBI-34582386 0.40 GO:0016324 GO:0009925 GO:0016323 GO:0005829 GO:0005769 GO:0010008 GO:0038143 GO:0016021 GO:0005887 GO:0043209 GO:0005634 GO:0048471 GO:0005886 GO:0043235 GO:0044214 GO:0005524 GO:0043125 GO:0042802 GO:0008022 GO:0046982 GO:0019903 GO:0004713 GO:0001042 GO:0004714 GO:0004888 GO:0007166 GO:0071364 GO:0071363 GO:0007167 GO:0038134 GO:0038133 GO:0038135 GO:0007507 GO:0033080 GO:0035556 GO:0008045 GO:0042552 GO:0033088 GO:0007528 GO:0030182 GO:0048709 GO:0018108 GO:0007422 GO:0014065 GO:0045785 GO:0030307 GO:0008284 GO:0050679 GO:0043547 GO:0033674 GO:0043406 GO:0043410 GO:0001934 GO:0090314 GO:0045943 GO:0045727 GO:0046777 GO:0006468 GO:0045765 GO:0070372 GO:0032886 GO:0007165 GO:0007169 GO:0042060 Transmembrane UniProt Sequence Analysis {ECO:0000255} MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV 1255 Q60553 Receptor ERBB2 10036 None SL-0198 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}. UNIPROT Q60553 Pfam PF00757 Pfam PF14843 Pfam PF07714 Pfam PF01030 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. GO:0005769 GO:0016021 GO:0005634 GO:0048471 GO:0005886 GO:0098590 GO:0005524 GO:0001042 GO:0004714 GO:0048513 GO:0071364 GO:0071363 GO:0007417 GO:0035556 GO:0030307 GO:0090314 GO:0045943 GO:0045727 GO:0042127 GO:0070372 GO:0032886 GO:0007169 Transmembrane UniProt Sequence Analysis {ECO:0000255} MELAAWCGWGLLLALLSPGASGTQVCTGTDMKLRLPASPETHLDIVRHLYQGCQVVQGNLELTYLPANATLSFLQDIQEVQGYMLIAHSQVRHVPLQRLRIVRGTQLFEDKYALAVLDNRDPLDNVTTATGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDTVLWKDVFRKNNQLAPVDIDTNRSRACPPCAPACKDNHCWGASPEDCQTLTGTIAPRAVPAARARLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTTCPYNYLSTEVGSCTLVCPLNNQEVTAEDGTQRCEKCSKSCARVCYGLGMEHLRGARAITSANIQEFAGCKKIFGSLAFLPESFDGNPSSGIAPLTPEQLQVFETLEEITGYLYISAWPDSLHDLSVFQNLRVIRGRVLHDGAYSLALQGLGIRWLGLRSLRELGSGLVLIHRNTHLCFVHTVPWDQLFRNPHQALLHSGNPSEEECGLKDFACYPLCAHGHCWGPGPTQCVNCSHFLRGQECVKECRVWKGLPREYVNGKHCLPCHPECQPQNSTETCTGSEADQCTACPHYKDSPFCVARCPSGVKPDLSYMPIWKYPDEEGMCQPCPINCTHSCVDLDERGCPAEQRASPATSIIATVVGILLFLVIGVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGLGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWIALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFFPDPAPGAGSTAHRRHRSSSTRSGGGELTLGMEPSGEEPPRSPLAPSEGAGSDVFEGELGMGATKGPQSISPRDLSPLQRYSEDPTLPLPTETDGYVAPLACSPQPEYVNQPEVRPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFTFGGAVENPEYLVPRGGSASQPHPPALCPAFDNLYYWDQDPSERGSPPNTFEGTPTAENPEYLGLDVPV 1254 P70424 Receptor Erbb2 10090 None SL-0198 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}. UNIPROT P70424 UNIPROT Q61525 UNIPROT Q6ZPE0 Pfam PF00757 Pfam PF14843 Pfam PF07714 Pfam PF01030 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. P12931 EBI-5451946 0.40 Q80TH2 EBI-7320494 0.67 Q61526 EBI-2945516 0.40 P98172 EBI-5451919 0.46 P42227 EBI-6255143 0.54 Q60748 EBI-15606164 0.40 P18762 EBI-15606183 0.52 GO:0016324 GO:0009925 GO:0016323 GO:0005737 GO:0031410 GO:0005829 GO:0005769 GO:0010008 GO:0038143 GO:0016021 GO:0005887 GO:0043219 GO:0045121 GO:0005902 GO:0043209 GO:0005634 GO:0048471 GO:0005886 GO:0045211 GO:0043235 GO:0044214 GO:0005524 GO:0043125 GO:0019838 GO:0051879 GO:0042802 GO:0008022 GO:0046982 GO:0019903 GO:0004713 GO:0044877 GO:0001042 GO:0004714 GO:0004888 GO:0031625 GO:0007166 GO:0071364 GO:0071363 GO:0038134 GO:0038133 GO:0038135 GO:0044849 GO:0010001 GO:0007507 GO:0033080 GO:0035556 GO:0008045 GO:0042552 GO:0043066 GO:0033088 GO:0007399 GO:0007528 GO:0030182 GO:0048709 GO:0018108 GO:0007422 GO:0014065 GO:0045785 GO:0030307 GO:0008284 GO:0050679 GO:0010628 GO:0043547 GO:0033674 GO:0043406 GO:0043410 GO:0014068 GO:0001934 GO:0090314 GO:0046579 GO:0045943 GO:0045727 GO:0046777 GO:0070372 GO:0032886 GO:0048678 GO:0007165 GO:0048485 GO:0007169 GO:0042060 Transmembrane UniProt Sequence Analysis {ECO:0000255} MELAAWCRWGFLLALLSPGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPANASLSFLQDIQEVQGYMLIAHNRVKHVPLQRLRIVRGTQLFEDKYALAVLDNRDPLDNVTTAAPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVLRKNNQLAPVDMDTNRSRACPPCAPTCKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALITYNTDTFESMLNPEGRYTFGASCVTTCPYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCAGVCYGLGMEHLRGARAITSDNIQEFAGCKKIFGSLAFLPESFDGNPSSGVAPLKPEHLQVFETLEEITGYLYISAWPESFQDLSVFQNLRVIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNTHLCFVNTVPWDQLFRNPHQALLHSGNRPEEACGLEGLVCNSLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVWKGLPREYVRGKHCLPCHPECQPQNSSETCYGSEADQCEACAHYKDSSSCVARCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATVVGVLLFLIIVVVIGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAVPNQAQMRILKETELRKLKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGELVDAEEYLVPQQGFFSPDPALGTGSTAHRRHRSSSARSGGGELTLGLEPSEEEPPRSPLAPSEGAGSDVFDGDLAVGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPEYVNQPEVRPQSPLTPEGPPPPIRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLAPRAGTASQPHPSPAFSPAFDNLYYWDQNSSEQGPPPSTFEGTPTAENPEYLGLDVPV 1256 P06494 Receptor Erbb2 10116 None SL-0198 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}. UNIPROT P06494 UNIPROT Q6P732 PDB 1IIJ PDB 1N8Y Pfam PF00757 Pfam PF14843 Pfam PF07714 Pfam PF01030 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. GO:0016324 GO:0009925 GO:0016323 GO:0005737 GO:0031410 GO:0005769 GO:0010008 GO:0038143 GO:0005887 GO:0043219 GO:0045121 GO:0005902 GO:0043209 GO:0005634 GO:0048471 GO:0005886 GO:0045211 GO:0043235 GO:0044214 GO:0005524 GO:0060724 GO:0003677 GO:0043125 GO:0051879 GO:0042802 GO:0008022 GO:0046982 GO:0019903 GO:0030296 GO:0004713 GO:0044877 GO:0001042 GO:0030297 GO:0004714 GO:0004888 GO:0031625 GO:0007166 GO:0071364 GO:0071363 GO:0007417 GO:0038134 GO:0038133 GO:0038135 GO:0044849 GO:0010001 GO:0007507 GO:0033080 GO:0035556 GO:0001889 GO:0060056 GO:0008045 GO:0042552 GO:0043066 GO:0033088 GO:0007399 GO:0007528 GO:0030182 GO:0048709 GO:0018108 GO:0007422 GO:0014065 GO:0045785 GO:0030307 GO:0008284 GO:0050679 GO:0010628 GO:0043547 GO:0033674 GO:0043406 GO:0043410 GO:0014068 GO:0001934 GO:0090314 GO:0046579 GO:0045943 GO:0045727 GO:0046777 GO:0045595 GO:0042127 GO:0070372 GO:0032886 GO:0048678 GO:0032570 GO:0009410 GO:0007165 GO:0007519 GO:0048485 GO:0043586 GO:0007169 GO:0042060 Transmembrane UniProt Sequence Analysis {ECO:0000255} MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNRDPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQLAPVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTCPYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSDNVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSLRDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHTVPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVARCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATVVGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPSEGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPEYVNQSEVQPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLVPREGTASPPHPSPAFSPAFDNLYYWDQNSSEQGPPPSNFEGTPTAENPEYLGLDVPV 1257 Q96RT1 Erbin ERBIN 9606 None SL-0178 SL-0182 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}. UNIPROT Q96RT1 UNIPROT A0AVR1 UNIPROT B4E3F1 UNIPROT B7ZLV9 UNIPROT E7EQW9 UNIPROT E9PCR8 UNIPROT Q1RMD0 UNIPROT Q86W38 UNIPROT Q9NR18 UNIPROT Q9NW48 UNIPROT Q9ULJ5 PDB 1MFG PDB 1MFL PDB 1N7T PDB 2H3L PDB 2QBW PDB 3CH8 PDB 6Q0M PDB 6Q0N PDB 6Q0U PDB 6UBH PDB 7LUL Pfam PF13855 Pfam PF00595 PROSITE PS51450 PROSITE PS50106 OMIM 606944 DisGeNET 55914 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}. O43542 EBI-11129266 0.35 P00533 EBI-32720286 0.27 Q16620 EBI-32724423 0.27 Q5XI72 EBI-22258042 0.35 Q6AXS5 EBI-22258042 0.35 O95405 EBI-7255424 0.37 Q99569 EBI-8449263 0.63 P35222 EBI-8449492 0.27 Q9UQ13 EBI-993893 0.62 Q15796 EBI-2695978 0.40 P84022 EBI-2696171 0.40 Q5NID9 EBI-2805400 0.00 Q8CZZ5 EBI-2841600 0.00 Q8CZQ2 EBI-2865700 0.00 P25054 EBI-3436880 0.00 P01106 EBI-3893063 0.35 P25791 EBI-3939532 0.37 P40763 EBI-3940529 0.37 B1AYL1 EBI-8068438 0.44 P36873 EBI-6911905 0.57 P57078 EBI-12503575 0.35 A2AUM9 EBI-10994361 0.35 Q96H55 EBI-11031416 0.35 Q8C767 EBI-11064501 0.35 Q5HZK1 EBI-11074242 0.35 G3X972 EBI-11079358 0.35 Q16643 EBI-11080402 0.35 Q9NYZ3 EBI-11081743 0.35 Q00610 EBI-11082478 0.35 Q8BGH2 EBI-11097023 0.35 P53667 EBI-11101207 0.35 P09803 EBI-11106849 0.35 Q86X19 EBI-11390509 0.27 Q9HC29 EBI-11420226 0.66 Q6P5F9 EBI-11603310 0.35 P03496 EBI-11519918 0.37 Q2PJP0 EBI-11520503 0.37 Q6DP93 EBI-11520678 0.37 P03508 EBI-11520965 0.37 Q20MH4 EBI-11521170 0.37 Q9UQB3 EBI-11793333 0.40 O00192 EBI-11793379 0.40 Q9BY21 EBI-11793409 0.40 Q96DL1 EBI-11793419 0.40 Q8NHY3 EBI-11793429 0.40 A3EX99 EBI-11794147 0.40 A3EXD5 EBI-11794185 0.40 P06427 EBI-11794195 0.40 Q9IDV3 EBI-11794220 0.40 Q1A244 EBI-11794243 0.40 P03126 EBI-11794253 0.40 P50804 EBI-11794263 0.40 P0C9G5 EBI-11794280 0.40 A3EXD4 EBI-11794297 0.40 P89432 EBI-11794318 0.40 P0C213 EBI-11794328 0.40 Q18LE1 EBI-11794586 0.40 Q8IWL3 EBI-13943458 0.35 P62136 EBI-14025896 0.42 Q96H86 EBI-21521634 0.35 Q7Z398 EBI-21528160 0.35 A8K8V0 EBI-21612043 0.35 P09017 EBI-21634836 0.35 Q8IZ69 EBI-21636338 0.35 Q8WV44 EBI-21636495 0.35 Q96IQ9 EBI-21636586 0.35 Q9H9D4 EBI-21642543 0.35 O43296 EBI-21725229 0.35 Q49MI3 EBI-21731388 0.35 P43235 EBI-21781359 0.35 Q8TA94 EBI-21783979 0.35 Q9NY56 EBI-21795463 0.35 Q6ZMY9 EBI-21818150 0.35 P20160 EBI-21867396 0.35 Q14CB8 EBI-21871748 0.35 Q9P0T4 EBI-21882203 0.35 P15311 EBI-16791848 0.27 P49841 EBI-16793176 0.27 P11279 EBI-16795491 0.27 Q9NPJ6 EBI-25472202 0.27 P03372 EBI-21301141 0.35 Q2LC84 EBI-22258042 0.35 Q04970 EBI-22258042 0.35 P60868 EBI-22258042 0.35 A0A0G2K8Z9 EBI-22258042 0.35 G3V7V7 EBI-22258042 0.35 D4A9L2 EBI-22258042 0.35 A0A0G2K654 EBI-22258042 0.35 Q27W01 EBI-22258042 0.35 B2RYP6 EBI-22258042 0.35 G3V6S1 EBI-22258042 0.35 P62890 EBI-22258042 0.35 P35427 EBI-22258042 0.35 Q8K1Q0 EBI-22258042 0.35 B5DFM8 EBI-22258042 0.35 Q6AYK8 EBI-22258042 0.35 Q4V8C8 EBI-22258042 0.35 Q920F5 EBI-22258042 0.35 D4A3K5 EBI-22258042 0.35 E9PT65 EBI-22258042 0.35 P62850 EBI-22258042 0.35 G3V9L1 EBI-22258042 0.35 M0R6J0 EBI-22258042 0.35 P62278 EBI-22258042 0.35 Q6IMY8 EBI-22258042 0.35 Q62780 EBI-22258042 0.35 P24368 EBI-22258042 0.35 A0A0G2K719 EBI-22258042 0.35 Q7TT49 EBI-22258042 0.35 P09875 EBI-22258042 0.35 P09895 EBI-22258042 0.35 P62893 EBI-22258042 0.35 Q9R0T3 EBI-22258042 0.35 A0A0G2JW88 EBI-22258042 0.35 M0R9L3 EBI-22258042 0.35 Q5RK00 EBI-22258042 0.35 E9PU01 EBI-22258042 0.35 Q3KRF2 EBI-22258042 0.35 F1M124 EBI-22258042 0.35 D3ZZT9 EBI-22258042 0.35 Q9JJ31 EBI-22258042 0.35 Q63186 EBI-22258042 0.35 P17078 EBI-22258042 0.35 P13471 EBI-22258042 0.35 F1MAF2 EBI-22258042 0.35 Q6AYE2 EBI-22258042 0.35 D4AD15 EBI-22258042 0.35 P50904 EBI-22258042 0.35 B2GV09 EBI-22258042 0.35 P05197 EBI-22258042 0.35 G3V9N7 EBI-22258042 0.35 Q9Z1W6 EBI-22258042 0.35 P62961 EBI-22258042 0.35 A0A096MK30 EBI-22258042 0.35 D4A4R1 EBI-22258042 0.35 P30009 EBI-22258042 0.35 Q5M7V8 EBI-22258042 0.35 P47198 EBI-22258042 0.35 P31000 EBI-22258042 0.35 P61314 EBI-22258042 0.35 D3Z898 EBI-22258042 0.35 Q5U2Q7 EBI-22258042 0.35 Q5XIM5 EBI-22258042 0.35 P13086 EBI-22258042 0.35 Q5M963 EBI-22258042 0.35 P81795 EBI-22258042 0.35 M0R9T2 EBI-22258042 0.35 P41743 EBI-25380638 0.35 P0DOF2 EBI-25603126 0.35 K9N5R3 EBI-26973414 0.40 F1PAA9 EBI-27079701 0.27 A0A0H3NFP4 EBI-27055788 0.27 P13569 EBI-27087549 0.35 Q99592 EBI-27093179 0.35 Q92630 EBI-28952324 0.27 Q13886 EBI-29000705 0.35 P30530 EBI-32717503 0.35 P29317 EBI-32720711 0.27 P29320 EBI-32720767 0.27 P54764 EBI-32720816 0.27 P54756 EBI-32720907 0.27 Q15375 EBI-32721052 0.27 P21802 EBI-32721907 0.27 P22455 EBI-32722168 0.27 Q06124 EBI-32723738 0.27 Q16288 EBI-32724526 0.27 P16234 EBI-32724889 0.27 Q01973 EBI-32725295 0.27 Q6J9G0 EBI-32731895 0.27 P12830 EBI-34580821 0.35 GO:0009925 GO:0005604 GO:0016323 GO:0030054 GO:0005737 GO:0098978 GO:0030056 GO:0031965 GO:0016607 GO:0005634 GO:0005886 GO:0098794 GO:0005176 GO:0005102 GO:0005200 GO:0045175 GO:0007155 GO:0071356 GO:0007173 GO:0045197 GO:0007229 GO:0045104 GO:0071638 GO:0032088 GO:0070433 GO:0046579 GO:0006605 GO:0099072 GO:0032496 GO:0032495 GO:0007165 Unknown UniProt Sequence Analysis MTTKRSLFVRLVPCRCLRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRLTKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLKEFWMDANRLTFIPGFIGSLKQLTYLDVSKNNIEMVEEGISTCENLQDLLLSSNSLQQLPETIGSLKNITTLKIDENQLMYLPDSIGGLISVEELDCSFNEVEALPSSIGQLTNLRTFAADHNYLQQLPPEIGSWKNITVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSDNQSKPLIPLQKETDSETQKMVLTNYMFPQQPRTEDVMFISDNESFNPSLWEEQRKQRAQVAFECDEDKDEREAPPREGNLKRYPTPYPDELKNMVKTVQTIVHRLKDEETNEDSGRDLKPHEDQQDINKDVGVKTSESTTTVKSKVDEREKYMIGNSVQKISEPEAEISPGSLPVTANMKASENLKHIVNHDDVFEESEELSSDEEMKMAEMRPPLIETSINQPKVVALSNNKKDDTKETDSLSDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTSLCSPVKQTHIDINSKIRQEDENFNSLLQNGDILNSSTEEKFKAHDKKDFNLPEYDLNVEERLVLIEKSVDSTATADDTHKLDHINMNLNKLITNDTFQPEIMERSKTQDIVLGTSFLSINSKEETEHLENGNKYPNLESVNKVNGHSEETSQSPNRTEPHDSDCSVDLGISKSTEDLSPQKSGPVGSVVKSHSITNMEIGGLKIYDILSDNGPQQPSTTVKITSAVDGKNIVRSKSATLLYDQPLQVFTGSSSSSDLISGTKAIFKFDSNHNPEEPNIIRGPTSGPQSAPQIYGPPQYNIQYSSSAAVKDTLWHSKQNPQIDHASFPPQLLPRSESTENQSYAKHSANMNFSNHNNVRANTAYHLHQRLGPARHGEMWAISPNDRLIPAVTRSTIQRQSSVSSTASVNLGDPGSTRRAQIPEGDYLSYREFHSAGRTPPMMPGSQRPLSARTYSIDGPNASRPQSARPSINEIPERTMSVSDFNYSRTSPSKRPNARVGSEHSLLDPPGKSKVPRDWREQVLRHIEAKKLEKKHPQTSSSGDPCQDGIFISGQQNYSSATLSHKDVPPDSLMKMPLSNGQMGQPLRPQANYSQIHHPPQASVARHPSREQLIDYLMLKVAHQPPYTQPHCSPRQGHELAKQEIRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVREVSS 1412 Q80TH2 Erbin Erbin 10090 None SL-0178 SL-0182 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}. UNIPROT Q80TH2 UNIPROT E9QND6 UNIPROT Q8BQ14 UNIPROT Q8CE41 UNIPROT Q8K171 UNIPROT Q99JU3 UNIPROT Q9JI47 Pfam PF13855 Pfam PF00595 PROSITE PS51450 PROSITE PS50106 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}. P04626 EBI-7806162 0.37 P70424 EBI-7320494 0.67 Q8BUN5 EBI-8626978 0.40 Q62432 EBI-8627018 0.44 P70340 EBI-8627088 0.44 P97471 EBI-8627224 0.44 O35253 EBI-8627324 0.44 P84022 EBI-8627354 0.37 P52927 EBI-9986179 0.35 Q9D415 EBI-16725590 0.35 Q8VI24 EBI-26885104 0.35 Q9QWI6 EBI-27100778 0.35 GO:0016323 GO:0030054 GO:0005737 GO:0098978 GO:0030056 GO:0031594 GO:0031965 GO:0016607 GO:0005634 GO:0005886 GO:0098794 GO:0099572 GO:0005176 GO:0005102 GO:0071356 GO:0071638 GO:0032088 GO:0070433 GO:0046579 GO:0006605 GO:0099072 GO:0032496 GO:0032495 GO:0007165 Unknown UniProt Sequence Analysis MTTKRSLFVRLVPCRCLRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRLTKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLREFWMDGNRLTFIPGFIGSLRQLTYLDVSKNNIEMVEEGISTCENLQDFLLSSNSLQQLPETIGSLKNVTTLKIDENQLMYLPDSIGGLRSIEELDCSFNEIEALPSSIGQLTNMRTFAADHNYLQQLPPEIGNWKNITVLFLHCNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSDNQSKPLIPLQKETDTETQKMVLTNYMFPQQPRTEDVMFISDNESFNPALWEEQRKQRAQVAFECDEDKDEREAPPREGNLKRYPTPYPDELKNMVKTVQTIVHRLKDEETNEESGRDLKQHEDQQVVNKDKCVKTSESTTTKSKLDEREKYMNSVQKMSEPEAETNGGNLPVTASMKLSGNLKHIVNHDDVFEESEELSSDEEMKMAEMRPPLIESSINQPKVVALSNNKKDDAKDADSLSDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTSLCSPVKQTPVDSNSKVRQEDENFNSLLQNGVNLNNSPEEKFKINDKKDFKLPEYDLNIEEQLVLIEKDIDSKATSDDSRQLDHINMNINKLVTNNIFQPEVMERSKMQDIVLGTGFLSIHPKNEAEHIENGAKFPNLESINKVNGLCEDTAPSPGRVEPQKASSSADVGISKSTEDLSPQRSGPTGAVVKSHSITNMETGGLKIYDILGDDGPQPPSAAVKIASAVDGKNIVRSKSATLLYDQPLQVFTAASSSSELLSGTKAVFKFDSNHNPEEPDIIRAATVSGPQSTPHLYGPPQYNVQYSGSATVKDTLWHPKQNPQIDPVSFPPQRLPRSESAENHSYAKHSANMNFSNHNNVRANTGYHLQQRLAPARHGEMWAISPNDRLVPAVTRTTIQRQSSVSSTASVNLGDPTRRTEGDYLSYRELHSMGRTPVMSGSQRPLSARAYSIDGPNTSRPQSARPSINEIPERTMSVSDFNYSRTSPSKRPNTRVGSEHSLLDPPGKSKVPHDWREQVLRHIEAKKLEKHPQTSSPGECCQDDRFMSEEQNHPSGALSHRGLPDSLMKMPLSNGQMGQPLRPQAHYSQTHHPPQASVARHPSREQLIDYLMLKVAHQPPYTHPHCSPRQGHELAKQEIRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFHNAVDLIIVREVSS 1402 Q20057 Enhancer erh 6239 None SL-0198 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}. UNIPROT Q20057 PDB 7EJO PDB 7EJS PDB 7O6L PDB 7O6N Pfam PF01133 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}. O61955 EBI-21449069 0.35 O76616 EBI-21449031 0.48 Q09293 EBI-21449069 0.35 Q19541 EBI-21448974 0.55 Q17698 EBI-21449069 0.35 Q8T3B7 EBI-21449069 0.35 Q9BL06 EBI-21449069 0.35 Q20140 EBI-21449069 0.35 Q20848 EBI-21449069 0.35 Q22537 EBI-21449069 0.35 Q18490 EBI-21449069 0.48 Q20057 EBI-21449848 0.37 GO:0005737 GO:0005634 GO:0048471 GO:0034518 GO:0034585 GO:0007049 GO:0051301 GO:0007059 GO:0009792 GO:0031047 GO:1990511 GO:0051781 GO:0051984 Unknown UniProt Sequence Analysis MSTSSHTVLLIQTSPRLDSRTWGDYESVTDALDALCKMFEDFLSKKSAAPVTYDVSQVYEFLDKLSDVSMMIFNRETGQYIGRTRAWIKQQVYEMMRGRCQHPEGGEKVIVGY 113 Q94F30 Ubiquitin-like-specific ESD4 3702 None SL-0178 SL-0182 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. UNIPROT Q94F30 UNIPROT B9DFG4 UNIPROT O23439 UNIPROT Q70G10 UNIPROT Q7DLT0 Pfam PF02902 PROSITE PS50600 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}. A4GSN8 EBI-1545682 0.37 GO:0031965 GO:0005634 GO:0016929 GO:0019900 GO:0070139 GO:0009911 GO:0016926 GO:0009909 Peripheral UniProt Sequence Analysis MGAVAINRKRSDESFNFINQQSTNPLRNSPYFQASKKRRFSFAMSEDSGKPASSNPTISRISRYPDAKAPLRREIHAPSRGILRYGKAKSNDYCEKDANFFVRKYDDAKRSALEALRFVNKGKDFVDLGDEVEKEEVVSDDSSVQAIEVIDCDDDEEKKNLQPSFSSGVTDVKKGENFRVEDTSMMLDSLSLDRDVDNDASSLEAYRKLMQSAEKRNSKLEALGFEIVLNEKKLSLLRQSRPKTVEKRVEVPREPFIPLTEDEEAEVYRAFSGRNRRKVLATHENSNIDITGEVLQCLTPSAWLNDEVINVYLELLKERETREPKKYLKCHYFNTFFYKKLVSDSGYNFKAVRRWTTQRKLGYALIDCDMIFVPIHRGVHWTLAVINNRESKLLYLDSLNGVDPMILNALAKYMGDEANEKSGKKIDANSWDMEFVEDLPQQKNGYDCGMFMLKYIDFFSRGLGLCFSQEHMPYFRLRTAKEILRLRAD 489 Q9LTB0 Exocyst EXO84B 3702 None SL-0198 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}. UNIPROT Q9LTB0 Pfam PF16528 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}. GO:0005856 GO:0005829 GO:0000145 GO:0005576 GO:0048471 GO:0009524 GO:0005886 GO:0006887 GO:0006893 GO:0008104 GO:0015031 Unknown UniProt Sequence Analysis MAAKTARSKATPTKENGVRVEEGLSLFKSDKFDADAYVQSKCSINEKDIKQLCSYLLDLKRASAEEMRRSVYANYPAFIRTSKEISDLEGELSSIRNLLSTQATLIHGLADGVNIDDDKVSDESLANGLLNFEDNGLSDLEKWATEFPDHLDALLAERRVDEALAAFDEGEILVSQANEKHTLSSSVLSSLQFAIAERKQKLADQLAKAACQPSTRGGELRSAIAALKRLGDGPRAHTVLLDAHFQRYQYNMQSLRPSSTSYGGAYTAALSQLVFSAISQASSDSLGIFGKEPAYSSELVTWATKQTEAFSLLVKRHALASSAAAGGLRAAAECAQIALGHCSLLEARGLSLCPVLLKHFKPIVEQALEANLKRIEENTAAMAAADDWVLTSPPAGSRHASTAFQNKLTSSAHRFNLMVQDFFEDVGPLLSMQLGSKALEGLFRVFNSYVDVLVRALPGSIEEEDPNFESSCNKIVQMAETEANQLALLANASLLADELLPRAAMKLSLDQTGQRTDDLRRPLDRQNRNPEQREWKRRLLSTVDKLKDAFCRQHALDLIFTEEGDSHLSADMYVNIDENGEDVDFFPSLIFQELFAKLNRMASLAADMFVGRERFAISLLMRLTETVILWLSGDQSFWDDIEEGPRPLGPLGLRQLYLDMKFVICFASQGRYLSRNLHRGTNEIISKALAAFTATGIDPYSELPEDDWFNDICVDAMERLSGKTKGNNGDVHSPTASVSAQSVSSARSHGSY 752 Q9NV70 Exocyst EXOC1 9606 None SL-0198 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}. UNIPROT Q9NV70 UNIPROT Q504V4 UNIPROT Q8WUE7 UNIPROT Q96T15 UNIPROT Q9NZE4 Pfam PF15277 Pfam PF09763 OMIM 607879 DisGeNET 55763 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}. O60645 EBI-12449995 0.51 O95295 EBI-21673234 0.35 Q03001 EBI-1105725 0.00 Q12840 EBI-21673234 0.35 Q7Z3B4 EBI-24426768 0.67 Q8IX03 EBI-15812551 0.41 Q8IYI6 EBI-12450194 0.51 Q8NF91 EBI-21375821 0.00 Q8TAG9 EBI-12449995 0.51 Q8WXH0 EBI-21375239 0.00 P01106 EBI-1062888 0.00 Q9BZD4 EBI-21673234 0.35 Q5KU26 EBI-1105596 0.00 Q9HCM1 EBI-1105801 0.00 Q13439 EBI-21673234 0.35 Q9H7U1 EBI-1105914 0.00 Q9C0D2 EBI-1105940 0.00 Q9UPN3 EBI-1106060 0.00 Q9NRI5 EBI-1106277 0.00 Q96A65 EBI-12449995 0.80 O60239 EBI-1106308 0.00 Q13813 EBI-1106390 0.00 Q9C026 EBI-1106505 0.00 O75962 EBI-1106525 0.00 Q5NH32 EBI-2806981 0.00 Q13573 EBI-7950968 0.35 Q80U62 EBI-3506571 0.40 Q8CDJ3 EBI-3506695 0.40 Q15051 EBI-4286917 0.64 A8K0Z3 EBI-9075674 0.51 Q6P5D4 EBI-10991106 0.35 P48039 EBI-11578238 0.00 Q96KP1 EBI-12449995 0.80 O95721 EBI-12449995 0.51 Q13445 EBI-12449995 0.51 Q9UEU0 EBI-12449995 0.51 Q9UPT5 EBI-12449995 0.51 Q53HC9 EBI-12449995 0.51 Q13049 EBI-12449995 0.51 O00471 EBI-12449995 0.51 Q9H5N1 EBI-12449995 0.51 Q9Y2D4 EBI-12450145 0.51 Q8TD31 EBI-24359951 0.56 P18848 EBI-22734600 0.56 P11234 EBI-11934086 0.00 O36551 EBI-14062552 0.35 P35414 EBI-21559824 0.35 Q96EV8 EBI-21651992 0.35 P27930 EBI-21662122 0.35 P24530 EBI-21672284 0.35 O95229 EBI-21673234 0.35 Q9UJ41 EBI-21673234 0.35 Q9Y2X7 EBI-21673234 0.35 Q9UID3 EBI-21673234 0.35 Q9NUP1 EBI-21673234 0.35 Q9NNX1 EBI-21673234 0.35 Q9BRV8 EBI-21673234 0.35 Q9BQD3 EBI-21673234 0.35 Q96JG6 EBI-21673234 0.35 Q96EK4 EBI-21673234 0.35 Q96BD5 EBI-21673234 0.35 Q8TBA6 EBI-21673234 0.35 Q6S8J3 EBI-21673234 0.35 Q6QNY1 EBI-21673234 0.35 Q6NZI2 EBI-21673234 0.35 Q5VIR6 EBI-21673234 0.35 Q5T1M5 EBI-21673234 0.35 Q5T0U0 EBI-21673234 0.35 Q5R372 EBI-21673234 0.35 Q4V328 EBI-21673234 0.35 Q16204 EBI-21673234 0.35 Q15276 EBI-21673234 0.35 Q15025 EBI-21673234 0.35 Q14161 EBI-21673234 0.35 Q14155 EBI-21673234 0.35 Q13107 EBI-21673234 0.35 Q13033 EBI-21673234 0.35 P33176 EBI-21673234 0.35 P05412 EBI-21673234 0.35 O95613 EBI-21673234 0.35 O60282 EBI-21673234 0.35 O43815 EBI-21673234 0.35 O15516 EBI-21673234 0.35 O14777 EBI-21673234 0.35 Q9Y2V7 EBI-21673529 0.35 Q9UJT2 EBI-21696311 0.35 P28908 EBI-21750180 0.35 Q70UQ0 EBI-21813594 0.35 Q9BT49 EBI-21869056 0.35 Q9NPJ6 EBI-25472377 0.35 Q9Y275 EBI-21266480 0.35 Q9H1C4 EBI-21266770 0.35 Q9UP83 EBI-21370112 0.00 O14795 EBI-21370190 0.00 Q96RF0 EBI-21371429 0.00 Q86XK3 EBI-21371888 0.00 Q8TAB5 EBI-21372100 0.00 A0AUZ9 EBI-21372770 0.00 Q7Z6K1 EBI-21373121 0.00 O60341 EBI-21374572 0.00 Q9NYJ8 EBI-21374944 0.00 Q08AD1 EBI-21375463 0.00 O75044 EBI-21376088 0.00 O94822 EBI-21377108 0.00 Q9UIF3 EBI-21377680 0.00 Q96JM3 EBI-21378253 0.00 Q8WYA0 EBI-21378706 0.00 P28330 EBI-21379260 0.00 Q14197 EBI-21379436 0.00 Q14571 EBI-21379754 0.00 Q6ZTA4 EBI-21380545 0.00 O15230 EBI-21380204 0.00 Q14980 EBI-21380995 0.00 Q9ULH1 EBI-21381430 0.00 Q9NR80 EBI-21381244 0.00 Q9Y383 EBI-21381969 0.00 Q567U6 EBI-21382571 0.00 Q5T0N5 EBI-21382805 0.00 Q9NX95 EBI-21383531 0.00 Q7Z4S6 EBI-21383490 0.00 Q3V6T2 EBI-21383689 0.00 Q8WXA3 EBI-21383580 0.00 Q99459 EBI-21383874 0.00 Q8TDR0 EBI-21383847 0.00 Q96SN8 EBI-21383834 0.00 Q8N2N9 EBI-21385250 0.00 Q8IYE0 EBI-21385113 0.00 Q7Z6B7 EBI-21384976 0.00 Q49A88 EBI-21386371 0.00 P53804 EBI-21388051 0.00 Q8IYT3 EBI-21389251 0.00 P55197 EBI-21389515 0.00 Q9H2F5 EBI-21389541 0.00 Q9ULU8 EBI-21390808 0.00 O43490 EBI-21391143 0.00 P35609 EBI-21391067 0.00 Q8NEY1 EBI-21391441 0.00 O15066 EBI-21392232 0.00 Q5NHH2 EBI-22298200 0.37 Q5NGE3 EBI-22298210 0.37 O84008 EBI-22302433 0.35 GO:0005737 GO:0098592 GO:0005829 GO:0000145 GO:0090543 GO:0016020 GO:0048471 GO:0005886 GO:0005546 GO:0051607 GO:0006887 GO:0006893 GO:0090148 GO:0000281 GO:0048015 GO:0050714 GO:0015031 GO:0016241 GO:0006904 GO:0090522 Unknown UniProt Sequence Analysis MTAIKHALQRDIFTPNDERLLSIVNVCKAGKKKKNCFLCATVTTERPVQVKVVKVKKSDKGDFYKRQIAWALRDLAVVDAKDAIKENPEFDLHFEKIYKWVASSTAEKNAFISCIWKLNQRYLRKKIDFVNVSSQLLEESVPSGENQSVTGGDEEVVDEYQELNAREEQDIEIMMEGCEYAISNAEAFAEKLSRELQVLDGANIQSIMASEKQVNILMKLLDEALKEVDQIELKLSSYEEMLQSVKEQMDQISESNHLIHLSNTNNVKLLSEIEFLVNHMDLAKGHIKALQEGDLASSRGIEACTNAADALLQCMNVALRPGHDLLLAVKQQQQRFSDLRELFARRLASHLNNVFVQQGHDQSSTLAQHSVELTLPNHHPFHRDLLRYAKLMEWLKSTDYGKYEGLTKNYMDYLSRLYEREIKDFFEVAKIKMTGTTKESKKFATLPRKESAVKQETESLHGSSGKLTGSTSSLNKLSVQSSGNRRSQSSSLLDMGNMSASDLDVADRTKFDKIFEQVLSELEPLCLAEQDFISKFFKLQQHQSMPGTMAEAEDLDGGTLSRQHNCGTPLPVSSEKDMIRQMMIKIFRCIEPELNNLIALGDKIDSFNSLYMLVKMSHHVWTAQNVDPASFLSTTLGNVLVTVKRNFDKCISNQIRQMEEVKISKKSKVGILPFVAEFEEFAGLAESIFKNAERRGDLDKAYTKLIRGVFVNVEKVANESQKTPRDVVMMENFHHIFATLSRLKISCLEAEKKEAKQKYTDHLQSYVIYSLGQPLEKLNHFFEGVEARVAQGIREEEVSYQLAFNKQELRKVIKEYPGKEVKKGLDNLYKKVDKHLCEEENLLQVVWHSMQDEFIRQYKHFEGLIARCYPGSGVTMEFTIQDILDYCSSIAQSH 894 Q8R3S6 Exocyst Exoc1 10090 None SL-0198 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}. UNIPROT Q8R3S6 UNIPROT E9QQ24 Pfam PF15277 Pfam PF09763 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0005737 GO:0098592 GO:0000145 GO:0090543 GO:0005886 GO:0005546 GO:0007566 GO:0006887 GO:0006893 GO:0090148 GO:0000281 GO:0048015 GO:0050714 GO:0015031 GO:0006904 GO:0090522 Unknown UniProt Sequence Analysis MTAIKHALQRDIFTPNDERLLSIVNVCKAGKKKKNCFLCATVTTERPVQVKVVKVKKSDKGDFYKRQIAWALRDLAVVDAKDAIKENPEFDLHFEKVYKWVASSTAEKNAFISCIWKLNQRYLRKKIDFVNVSSQLLEESVPSGENQSVAGGDEEAVDEYQELNAREEQDIEIMMEGCECAISNAEAFAEKLSRELQVLDGANIQSIMASEKQVNTLMQLLDEALTEVDQIELKLSSYEEMLQSVKEQMDQISESNHLIHLSNTNNVKLLSEIEFLVNHMDLAKGHIKALQEGDLVSSRGIEACTNAADALLQCMNVALRPGHDMLLAVKQQQQRFSDLREHFARRLASHLNNVFVQQGHDQSSTLAQHSVELTLPNHHPFHRDLLRYAKLMEWLKSTDYGKYEGLTKNYMDYLSRLYEREIKDFFEVAKMKMTGTSKESKKFATLPRKESAVKQETESLHGSSGKLTGSTSSLNKLSVQSSGSRRSQSSSLLDMGNMSASDLDVADRTKFDKIFEQVLSELEPLCLAEQDFISKFFKLQQHQNMSASMTEAEDLDGGSLLRQHSSGTLLPVSSEKDMIRQMMIKIFRCIEPELNNLIALGDKVDSFNSLYMLVKMSHHVWTAQNVDPASFLSTTLGNVLVTVKRNFDKCISNQIRQMEEVKISKKSKVGILPFVAEFEEFAGLAESIFKNAERRGDLDKAYTKLIRGVFINVEKVANESQKTPRDVVMMENFHHIFATLSRLKISCLEAEKKEAKQKYTDHLQSYVIYSLGQPLEKLNHFFEGVEARVAQGIREEEVSYQLAFNKQELRKVIKEYPGKEVKKGLDNLYKKVDKHLCEEENLLQVVWHSMQDEFIRQYKHFEGLIARCYPGSGVTMEFTIQDILDYCSSIAQSH 894 Q0V8C2 Exocyst EXOC3 9913 None SL-0198 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}. UNIPROT Q0V8C2 Pfam PF06046 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0000145 GO:0005794 GO:0030426 GO:0030496 GO:0048471 GO:0000149 GO:0051601 GO:0006887 GO:0015031 Unknown UniProt Sequence Analysis MKETDREAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVRHSQLAAAVENLKNIFSVPEIVRETQDLIEHGELLQAHRKLMDLECSRDGLMYEQYRMDSGNTRDMTLIHSYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGRPKNWKEKMFTILDRTVTTRIEGTQADTRESDRMWLVRHLEIIRKYVLDDLIVAKNLLAQCFPPHYEIFRSLLRTYHQALSARMQDLAAEDLEANEIVSLLTWVLNTYTSVEMMGNAELAPEVDVALLEPLLSADVVSALLDTYMSTLTSNIIAWLRKALETDKKDWMKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKEEAQLYRDEHLRDRQHPHCYVQYMVAVVNNCQTFKESIVSLKRKYLKHEAEEGVSLSQPSMDGVLDAIAKEGCGSLLEEVFLDLEQHLNELMTKKWLLGSNAVDIICVTVEDYFNDFAKIKKPYRKRMIAEAHRRAVQEYLRAVMQKRISFRSAEERKDGAERMVREAEQLRFLFRKLASGFGEEMDSYCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLAMRGDASRDMKQTIIETLEQGPAQASPDYVPIFKDIVVPSLNVAKLLK 745 Q54BP6 Exocyst exoc3 44689 None SL-0198 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}. UNIPROT Q54BP6 Pfam PF06046 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0000145 GO:0005794 GO:0030426 GO:0030496 GO:0048471 GO:0000149 GO:0051601 GO:0006887 GO:0015031 Unknown UniProt Sequence Analysis METVSLVPLEGLDDLSAQSAAIKKIEQNFSNIDSLASVTNHKISLIQQKKTIEAQIKNEVHSELEKSKKGLETLYKSYNRINRMDESFSDTVELCSETSNLIGHYQLIKKVNTVRVNLINILKEVDRLLTIPEKAAEIEQLLSDDLNLLEIHSKLRELERLHQKALKQFESNFEELEAIKEMFSSVPELSHRFENKIWNIVSNSIDIAQIKPAVLVKVAQIIEREKLHEQKQKEKKSQNSLISSEGIHDDDDDDDDTEVNLNNSNKQQNNENENSSSNNNNNYDINNEDEGYDRNRSNYGDRFLEVLIQSISGKFEPMFLNSHNDLVQTLKDVNKMVDELFIVMDIVQECYPPSYDLFNFYVDQYHTKFYSLFGSFSNLMESSHVNNNYQVVVTKNIPSAHILMLVEWVVKNYSRDLSRLGIQDISPPLLDSLDPLIKIYKMHIKQLMREWCDNIINNDNQNKPEVVDGQYCSLAPIQLFESVASQLDIAAATKCQKLVVGVMEEVVSALMYFQVQSITLLQERNHEIKLENVIAYVNNNSKCYDHTQTIVDKVSNILDSEHMGYLDFDPVLEGFLNVSKVATQAISSVIFRDLDECIHKFYTVEWYQEDLMQPIINTFEDYVTNDIQKYILENYLKRLALLLLDTLIEQLLAQLIGGKNKFNENTYKILSNDCDKLLDFFKKYLRLSVVTAKVQILEDFKQMITSSIDMVPVYFRSVINFHKDINERVVELVLYQRTDISKSEITEVLGQIKTIVETVHTDPTNPPTGIFSRMNIYQRGWFS 783 O60645 Exocyst EXOC3 9606 None SL-0198 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}. UNIPROT O60645 UNIPROT Q6P2E8 UNIPROT Q8TEN6 UNIPROT Q8WUW0 UNIPROT Q96DI4 Pfam PF06046 OMIM 608186 DisGeNET 11336 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. A1L4K1 EBI-25258050 0.56 P01106 EBI-1074529 0.00 O88738 EBI-1765706 0.35 Q8BHD1 EBI-2557128 0.40 A0A2U2H1F8 EBI-2870328 0.00 Q13573 EBI-7950968 0.35 P40692 EBI-2932395 0.37 O43684 EBI-3916000 0.37 Q86VI4 EBI-10764290 0.40 P00533 EBI-10764491 0.40 Q8CAQ8 EBI-11096643 0.35 Q9HBH9 EBI-11139967 0.35 O00139 EBI-11140263 0.35 Q9Z172 EBI-11157923 0.35 Q86X19 EBI-11372615 0.27 Q9NV70 EBI-12449995 0.51 Q96KP1 EBI-12450028 0.64 Q9UPT5 EBI-12450043 0.51 Q13445 EBI-12450043 0.51 Q96A65 EBI-12450043 0.64 O00471 EBI-12450093 0.64 Q9BZL4 EBI-24371831 0.56 Q96IK5 EBI-24472724 0.56 Q13049 EBI-11902318 0.00 P11234 EBI-11902309 0.00 O75386 EBI-11902300 0.00 Q9Y2D4 EBI-21672799 0.35 Q8IYI6 EBI-21672932 0.51 Q8TAG9 EBI-21673041 0.51 P35613 EBI-21560440 0.35 P34741 EBI-21628438 0.35 Q96EV8 EBI-21651992 0.35 P27930 EBI-21662122 0.35 Q13563 EBI-21672799 0.35 Q9Y496 EBI-21672799 0.35 Q9H0B6 EBI-21672799 0.35 Q9BQD3 EBI-21672799 0.35 Q9BQ69 EBI-21672799 0.35 Q99666 EBI-21672799 0.35 Q96NL6 EBI-21672799 0.35 Q96JN2 EBI-21672799 0.35 Q8WXW3 EBI-21672799 0.35 Q8IY31 EBI-21672799 0.35 Q8IWJ2 EBI-21672799 0.35 P0DJD1 EBI-21672799 0.35 Q2M2Z5 EBI-21672799 0.35 Q15643 EBI-21672799 0.35 Q07866 EBI-21672799 0.35 Q32P51 EBI-20938684 0.40 P12004 EBI-21238234 0.37 Q96T52 EBI-27050444 0.35 F1PAA9 EBI-27079701 0.27 P18433 EBI-27116377 0.27 Q9HD43 EBI-27116527 0.27 GO:0005829 GO:0000145 GO:0005794 GO:0030426 GO:0030496 GO:0048471 GO:0042734 GO:0030667 GO:0045296 GO:0000149 GO:0051601 GO:0006887 GO:0090148 GO:0000281 GO:0015031 GO:0006904 GO:0090522 Unknown UniProt Sequence Analysis MKETDREAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLECSRDGLMYEQYRMDSGNTRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGRPKNWKEKMFTILERTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLIVAKNLMVQCFPPHYEIFKNLLNMYHQALSTRMQDLASEDLEANEIVSLLTWVLNTYTSTEMMRNVELAPEVDVGTLEPLLSPHVVSELLDTYMSTLTSNIIAWLRKALETDKKDWVKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKDEAQLYKEEHLRNRQHPHCYVQYMIAIINNCQTFKESIVSLKRKYLKNEVEEGVSPSQPSMDGILDAIAKEGCSGLLEEVFLDLEQHLNELMTKKWLLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSPEERKEGAEKMVREAEQLRFLFRKLASGFGEDVDGYCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLAVRGDASRDMKQTIMETLEQGPAQASPSYVPLFKDIVVPSLNVAKLLK 745 Q6KAR6 Exocyst Exoc3 10090 None SL-0198 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}. UNIPROT Q6KAR6 Pfam PF06046 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. P25322 EBI-3956307 0.46 O35382 EBI-8299949 0.40 P23819 EBI-8300089 0.40 P35438 EBI-8300130 0.40 P11234 EBI-3956345 0.27 GO:0000145 GO:0005794 GO:0030426 GO:0030496 GO:0048471 GO:0042734 GO:0030667 GO:0000149 GO:0051601 GO:0006887 GO:0090148 GO:0000281 GO:0015031 GO:0006904 GO:0090522 Unknown UniProt Sequence Analysis MCKDSACFLTMKETDLEAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLECSRDGLMCEQYRMDSGNKRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGRPKNWKEKMFAILDRTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLIVAKNLMVQCFPPHYEIFKNLLSMYHQALSTRMQDLASEDLEANEIVSLLTWVLNTYTSAEMMGNVELAPEVDVSALEPLLSPNIVSELLDTYMSTLTSNIIAWLRKALETDKKDWSKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKDEAQLYKEEHLRNRQHPHCYVQYMIAIINNCQTFKESIISLKRKYLKTEAEEGLCLSQPSMDGILDAIAKEGCSSLLEEVFLDLEQHLNELMTKKWLLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSAEERKEGAEKMVREAEQLRFLFRKLASGFGEDADGHCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLALRGDASRDMKQTIMETLEQGPMQASPNYVPIFKEIVVPSLNVAKLLK 755 Q62825 Exocyst Exoc3 10116 None SL-0198 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}. UNIPROT Q62825 UNIPROT Q4QQU2 Pfam PF06046 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. P97879 EBI-15885274 0.35 P07949 EBI-22248789 0.35 GO:0000145 GO:0005794 GO:0030426 GO:0030496 GO:0048471 GO:0042734 GO:0000149 GO:0051601 GO:0006887 GO:0015031 Unknown UniProt Sequence Analysis MCKDSACFSTMKETDLEAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLECSRDGLMCEQYRMDSGNKRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGRPKNWKEKMFAVLDRTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLVIAKNLLVQCFPPHYDIFKNLLSMYHQALSIRMQDLASEDLEANEIVSLLTWVLNTYTSAEMMGNVELAPEVDVNALEPLLSPNVVSELLDTYMSTLTSNIIAWLRKALETDKKDWSKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKEEAQLYKEEHLRNRQHPHCYVQYMVAIINNCQTFKESIISLKRKYLKPETEESLCQSQPSMDGILDAIAKEGCSSLLEEVFLDLEQHLNELMTKKWMLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSAEERKEGAEKMVREAEQLRFLFRKLASGFGEDADGHCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLALRGDASRDMKQTIMETLEQGPMQASPNYVPIFQEIVVPSLNVAKLLK 755 E2R766 Exocyst EXOC6 9615 None SL-0198 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}. UNIPROT E2R766 Pfam PF04091 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}. GO:0000145 GO:0090543 GO:0030426 GO:0048471 GO:0006887 GO:0006893 GO:0006886 GO:0090522 Unknown UniProt Sequence Analysis MAENSEGLGTVPEHERILQEIESTDTACVGPTLRSVYDDQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITELLKVRTDAEKLKVQVTDTNRRFQDAGKEVIIQTEDIIRCRIQQRNITTVVENLQYAFPVLEMYSKLKEQMTAKRYYSALKTMEQLENVYFPRVSQYRFCQLMIENLPKLREDIKEISMSDLKDFLESIRKHSDKIGETAMKQAQQQKTFSVALQKQNNVKFGKNMYINDRIPEERKENELKQGFEEEDENEEEILTVQDLVDFSPVYRCLHIYSVLGDEETFENYYRKQRKKQARLVLQPQSNMHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRAYTDELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLIVIFADTLQGYGFPVNRLFDLLFEIRDQYNETLLKKWAGVFRDIFEEDNYSPIPIVNEEEYKAVISKFPFQDPDFEKQSFPKKFPMSQSVPHIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRTLSSCLLNLIRKPHIGLTELVQIIINTTHLEQACKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMSEPDGRASGYLMDLINFLRSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFIDLRQLLDLFMVWDWSTYLADYGQPASKYLRVNPNTALTLLEKMKDTSKKNNIFAQFRKNDRDKQKLIETVVKQLRSLVNGMSQHT 803 Q54B27 Exocyst exoc6 44689 None SL-0198 Cytoplasm {ECO:0000250|UniProtKB:O54923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}. UNIPROT Q54B27 Pfam PF04091 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0000145 GO:0090543 GO:0048471 GO:0031267 GO:0070177 GO:0006887 GO:0006893 GO:0006886 GO:0090522 Unknown UniProt Sequence Analysis MSNKKQKEEINTAGGSVILKTMVRDKDKEQKEEKREKKEKKRLEKKEAENVKKEKKKEKKELKKIGKAGRSGSITSDSSTHSGAQEFDSYGNDSNGGGGGLSASIDSNGLSSSGQPMQTRHLEKEVGEKQGIYSLSSQDRSSSLPHSSQDDQAKPLITESEIFSSESFLIAVSDTDHLGPAIKSVFENNKEKEVIKILNAYIAQKDLDIEKICGENHEGFINSVTAFLGLKGENLDLKQDVINLNYELQEIGRKYVTKAEELFAYKQIKDNIKRTKEVLNNCQYAILLGMKVDEYVQQKKYYQAIKNMDQLHNVYLKKLSDFQFARNMDYNIPVLKEKIKKLVKDEFNQWMVEIKEKSAVIGKLGMIQTSKKLLKEREINPLKIKTTFGENEQIWDKILDIPPIINSSSIGSLALYPTLNSPVTAPIYSPNSGKTPSSFGFNKQINEKDLKEDINQFSPFDESDIQFHPLYQCLFIHASIGQLEEFQAYYTLNRLLQFQLVIQPKESGQVWELFLQQILGYFMVESKVIDSTEPFLSKTTINDSWNSALVKVTSVLQELFTHCVDTQPLIAFKKFVLIFTNTMSFYSYHVQPLYYFLDTMKEKYCQFSIKEAVERFTIILERDSHCSLIIESLEEYKSLILANKLDILERQQLRQLQNSLNNNQFQFGDKNLNNNNNNDDDDDYFDEDENEDDKISKRLPKSFLFSKMVPQFYTLIKKFISEFYEFSDQLTENENFIIRSTDTLIKKINEVLYSYLTQSQAVPQVIQLVINLQHLISGCSFFKDYLNSLILGEDYQKNQSIVNETNKVILNSQNLLYTTKSHGEKLIIKLCEQKIEDLMSSAANIEWFPQNAIDDRPRDYIIDVCTFLEVTLPFISPLSQNLKEEFITKAFKNISESLFSLIYDDQLKKLNLQGVKSFDADLKYIETYVKEKANEKERTTTTSRNMVGYFVELRQLTNFLLSDNPEDFVDPKIKAKHYNLITNIPQLLNILNKYKEESKGFTTSKEIKDRNKKIADAIKKIKDSL 1025 Q8TAG9 Exocyst EXOC6 9606 None SL-0198 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}. UNIPROT Q8TAG9 UNIPROT E9PHI3 UNIPROT Q5VXH8 UNIPROT Q9NZ24 Pfam PF04091 OMIM 609672 DisGeNET 54536 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}. O43542 EBI-11129266 0.35 O60645 EBI-21673041 0.51 P0DTD1 EBI-26951880 0.49 P50148 EBI-21673041 0.35 P62834 EBI-21673041 0.35 Q53GS7 EBI-25859244 0.56 Q8IYI6 EBI-12450124 0.64 P02768 EBI-1223494 0.35 Q9BQ95 EBI-3385759 0.37 P32119 EBI-3385854 0.37 Q96JB6 EBI-3385849 0.37 Q92947 EBI-3385844 0.37 Q9Y3B2 EBI-3385839 0.37 P05067 EBI-3385834 0.37 P29474 EBI-3385829 0.37 Q8TAG9 EBI-3385859 0.37 Q9Y2H9 EBI-3385991 0.37 P49810 EBI-3386181 0.37 Q96A65 EBI-10764425 0.73 P0DOE7 EBI-11327042 0.40 Q9NV70 EBI-12449995 0.51 O00471 EBI-12450093 0.79 P61006 EBI-12450124 0.51 Q9UPT5 EBI-12450124 0.51 Q96KP1 EBI-12450124 0.64 Q16891 EBI-12450124 0.51 Q9Y2D4 EBI-11923380 0.00 P32970 EBI-21512742 0.35 P35414 EBI-21559824 0.35 P49146 EBI-21569349 0.35 Q8N7X8 EBI-21585341 0.35 O75558 EBI-21632742 0.35 Q96EV8 EBI-21651992 0.35 P27930 EBI-21662122 0.35 O60939 EBI-21671922 0.35 Q96LW7 EBI-21673041 0.35 Q5VIR6 EBI-21673041 0.35 Q9H410 EBI-21673116 0.35 P08173 EBI-21707586 0.35 P0DOF2 EBI-25603126 0.35 P0DTC5 EBI-26495256 0.35 O43572 EBI-26451580 0.35 Q7Z699 EBI-25932191 0.56 GO:0005829 GO:0000145 GO:0090543 GO:0030426 GO:0048471 GO:0005886 GO:0006887 GO:0006893 GO:0006886 GO:0090148 GO:0000281 GO:0006904 GO:0090522 Unknown UniProt Sequence Analysis MAENSESLGTVPEHERILQEIESTDTACVGPTLRSVYDDQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITELLKVRTDAEKLKVQVTDTNRRFQDAGKEVIVHTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSAKRYYSALKTMEQLENVYFPWVSQYRFCQLMIENLPKLREDIKEISMSDLKDFLESIRKHSDKIGETAMKQAQHQKTFSVSLQKQNKMKFGKNMYINRDRIPEERNETVLKHSLEEEDENEEEILTVQDLVDFSPVYRCLHIYSVLGDEETFENYYRKQRKKQARLVLQPQSNMHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRAYTDELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLTVIFADTLQGYGFPVNRLFDLLFEIRDQYNETLLKKWAGVFRDIFEEDNYSPIPVVNEEEYKIVISKFPFQDPDLEKQSFPKKFPMSQSVPHIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRTLSSCLLNLIRKPHIGLTELVQIIINTTHLEQACKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMSEPDGRASGYLMDLINFLRSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFIDLRQLLDLFMVWDWSTYLADYGQPASKYLRVNPNTALTLLEKMKDTSKKNNIFAQFRKNDRDKQKLIETVVKQLRSLVNGMSQHM 804 Q8R313 Exocyst Exoc6 10090 None SL-0198 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}. UNIPROT Q8R313 Pfam PF04091 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}. Q62739 EBI-9202177 0.52 GO:0000145 GO:0090543 GO:0030426 GO:0048471 GO:0005886 GO:0030218 GO:0006887 GO:0006893 GO:0006886 GO:0090148 GO:0000281 GO:0006904 GO:0090522 Unknown UniProt Sequence Analysis MAESCEALGTVPEHERILQEIESTDTACVGPTLRSVYDDQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITELLKVRADAEKLKVTDTNRRFQDAGKEVIIQTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSMKRYYSALKTMEQLENVYFPRVSQYRFCQLMMETLPKLREDMMNYCMSDLTYGLESIRKHSDKIGEAAMKQAQQQKSFSVALQKQNNMRFGKNMHVNNDRILEEKSDVIPKHALEEEAENDEEVLTVQDLVDFSPVYRCLHIYSALGDEETFENYYRKQRKKQARLVLQPQSSVHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRVYTEELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLIVIFADTLQGYGFPVNRLFDLLFEIRDQYNETLLKKWAGIFRDIFEEDNYSPIPIGSEEEYKVVISRFPFQDPDLEKQSFPKKFPMSQSVPLIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRILSSCLLNLIRKPHIGLTELVQIIINTTHLEQACKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMAESDGRASGYLMDLINFLRSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFIDLRQLLDLFMVWDWSTYLADYGQPASKYLRVNPHAALTLLEKMKDTSKKNNIFAQFRKNDRDRQKLIETVVRQLRGLVTGMSQHT 802 O54923 Exocyst Exoc6 10116 None SL-0198 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}. UNIPROT O54923 Pfam PF04091 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}. GO:0000145 GO:0090543 GO:0030426 GO:0048471 GO:0030218 GO:0006887 GO:0006893 GO:0006886 GO:0090522 Unknown UniProt Sequence Analysis MAESGEALGTVPEHERILQEIESTDTACVGPTLRSVYDGQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITELLKVRADAEKLKVQVTDTNRRFQDAGKEVIEQTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSMQRYYSALKTMEQLENVYFPRVSQYRFCQLMMDTLPKLREDIKDISMSDLKDFLESIRKHSDKIGETAMKQAQQQKSFSIAVQKQTNMRFGKNMHVNNDRTLEEKSDIILKHTLEEEAENDEEVLTVQDLVDFSPVYRCSHIYSALGDEETFENYYRKQRKKQARLVLQPQSSVHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRAYTDELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLIVIFADTLQGYGFSVNRLFDLLFEIRDQYNETLLKKWAGIFRDIFEEDNYSPIPIGSEEEYKMVISKFPFQDPDLEKQSFPKKFPMSQSVPLIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRILSSCLLNLIRKPHIGLTELVQIIINTTHLEQACKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMAESDGRASGYLMDLINFLRSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFIDLRQLLDLFMVWDWSTYLADYGQPASKYLRVNPHAALTLLEKMKDTSKKNNIFAQFRKNDRDRQKLIETVVKQLRGLVTGMSQHM 804 A4IF89 Exocyst EXOC8 9913 None SL-0198 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}. UNIPROT A4IF89 Pfam PF16528 PROSITE PS50003 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0000145 GO:0030426 GO:0005770 GO:0048471 GO:0035091 GO:0031267 GO:0007032 GO:0006887 GO:0022617 GO:0006893 GO:0008104 GO:0015031 Unknown UniProt Sequence Analysis MAMAMSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRIQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLTLLPAAAAAGAAAASGGEEGGGGAGGRDQLRGQTGFFPSPGGASRDGSGPGEEGKQRTLTTLLEKVEGCRHLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDGLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSEKRRREQEEAAAPRGPPQVTPKASNPFEDEDDDEPTVPEIEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRARVDERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVRVAKEHCQQLGDIGLDLTFIVHALLVKDIQGALHSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLIRVNPESTTSVV 725 Q5ZJ43 Exocyst EXOC8 9031 None SL-0198 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}. UNIPROT Q5ZJ43 Pfam PF16528 PROSITE PS50003 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0000145 GO:0030426 GO:0048471 GO:0006887 GO:0006893 GO:0008104 GO:0015031 Unknown UniProt Sequence Analysis MALALGEGGGGSRLRRQLESGGFAAAEYVKQLSQQSDGDRDLQEHRQRIQALQEETAQSLKRNVYQNYRQFIETAREISYLESEMYQLSHILTEQKGIMEAVTQALLLQADRDDPALGARRAAAADPFLPLSAKEAAASEEGRQRTLTTLLEKVEGCRDLLPESPGKYLVYNGDLLEYDADHMAQIQRVHAFLMNDCLLVATALPNRRGAYRYDALYPLEGLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKKEWLEVLEETKRNRALSEKRRLEQEALPRPAPTPPESTNPFEEEEEEEEEPSAEEEAVDLSLEWIQELPEDLDVCIAQRDFEGAVDLLDKLNEYLADKPVSQPVKELRAKVDERVRQLTDVLVFELSPDRSLRGGPRATRRAVSQLIRLGQSTKACELFLKNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGNNGCYSAFVVWARSSMRMFVDAFSKQVFDSKESLSTAAECVKVAKEHCKQLSDIGLDLTFIIHALLVKDIKGALQSYKDIIIEATKHRNSEEMWRRMNLMTPEALGKLREEMKSCGVGSFDQYTGDDCWVNLSYTVVAFTKQTMAFLEEALKLYFPELHMVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLMRINPESTTSVV 708 Q54VZ8 Exocyst exoc8 44689 None SL-0198 Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}. UNIPROT Q54VZ8 Pfam PF16528 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0042995 GO:0000145 GO:0048471 GO:0006887 GO:0006893 GO:0008104 GO:0015031 Unknown UniProt Sequence Analysis MKKGVTYPLKIDTNLSTVSSSVNYNDIECVDIKSNGHYIVKFMYREWVGPLNLMTTQKTSIKISIDLKEQTVTCTHTDKKKTVYRWGEFPNKKETEQNKKEDNPVQYETFLSSNFNSEKYVNDLFTHKTDQQATVHLQYLENRKLGCIDHLKKDVYKNHLIFIGASKEIANSEVDMLDFRNLISDYGNVMSSLQNISISWDHYKVKKSGKIDFEPLSPATEPIQWLTTAPNELSVSIEQREFEVAVGLVEKINKIYESNPKVEIVMQTHPLKDQIENKVKILTDKLMNELRSPLLKANQIKDTISLLVRLSQNDKAKSIFLESRSHSINQAIKKIVFSGDLNRFIGELARVIFNSINSTCNDFTNSFPSYMNSGLVSWIIEELVLISDIFNRQVFILDNFYSISQAIRIIESHCEMMDQTGLSIGFYWNLLLQPHVEQLIVNYEIKIRDSMLHQLMDEKWNGVSNWDYEVKSQLNSLPSSLKNSGTPNSGGSGISNNNSNNNNNYQSPIINNNFNSGGGNKKIGLTFQQMHQDNLNNMEDIDQGRLKLTSSTIFLNTIIQKFAIDICQIITIDLIPVISQSLGSIFKDYMSYLKNEIQKEYLSDTQCLAIISDSVYIVDDLVSRIATRFEDATGEKLNNLTQLSSLLYSYFESIRDQYSTRKALELVDNSMNWEEQEYQVEEELDPFPKNFIVLSEALDRLAESIQTNVNVESVLPIASRIISEIVNIISNRFESTSNLVFGYGGLQHFILEMKYLATFAGKYPVEDSTFELINTMIRNHKEIYLNNTSDPKPLKTEEYFTSIIDNLVYQKAVYN 815 Q8IYI6 Exocyst EXOC8 9606 None SL-0198 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}. UNIPROT Q8IYI6 UNIPROT B3KU33 UNIPROT Q5TE82 Pfam PF16528 PROSITE PS50003 OMIM 615283 OMIM 619076 DisGeNET 149371 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. 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. O60645 EBI-21672932 0.51 P00533 EBI-10764512 0.40 P05783 EBI-756712 0.37 Q7Z3B4 EBI-24565174 0.56 Q8N6Y0 EBI-760525 0.70 P35900 EBI-753154 0.37 O75478 EBI-753181 0.37 P19012 EBI-753475 0.37 O14964 EBI-754885 0.37 Q9UL45 EBI-756178 0.67 P08727 EBI-756208 0.67 Q15154 EBI-24482767 0.56 Q15834 EBI-758167 0.37 Q8TBN0 EBI-2349923 0.49 Q9NS73 EBI-10263400 0.56 Q5JST6 EBI-2349935 0.49 P46736 EBI-2510058 0.40 Q14457 EBI-3506822 0.60 Q8CDJ3 EBI-3506734 0.40 Q80U62 EBI-3506709 0.40 Q96A65 EBI-3509957 0.73 Q4R379 EBI-3509942 0.35 A8K0Z3 EBI-9075672 0.55 Q14247 EBI-9075593 0.27 Q8VDD8 EBI-9075562 0.27 Q15323 EBI-10263378 0.56 Q8IYX8 EBI-10263388 0.56 Q9UKT9 EBI-10263412 0.78 P06428 EBI-11738085 0.37 O00471 EBI-12450093 0.64 Q8TAG9 EBI-12450124 0.64 Q9Y2D4 EBI-12450145 0.51 Q9UPT5 EBI-12450194 0.51 Q9NV70 EBI-12450194 0.51 P11234 EBI-12451925 0.64 P14373 EBI-24274457 0.56 Q9UBB9 EBI-24277384 0.56 Q9Y250 EBI-24282357 0.56 P20807 EBI-24310203 0.56 P29084 EBI-24320917 0.56 Q8TD31 EBI-24326974 0.56 Q9H9H4 EBI-24338768 0.56 Q08379 EBI-24339832 0.56 P15884 EBI-24339961 0.56 Q15742 EBI-24480518 0.56 Q9H2G9 EBI-24488250 0.56 Q99081 EBI-24492403 0.56 Q13155 EBI-24501654 0.56 P19474 EBI-24506936 0.56 Q6AI39 EBI-24508160 0.56 Q9H992 EBI-24511640 0.56 O76013 EBI-24527203 0.60 Q9NU19 EBI-24617208 0.56 Q5EBL2 EBI-23729583 0.56 Q6GMQ7 EBI-23732828 0.56 Q6ZMJ2 EBI-24703615 0.56 O00472 EBI-24709958 0.56 Q9BRT2 EBI-23790765 0.56 Q969W8 EBI-23791595 0.56 Q9NTX9 EBI-23801072 0.56 Q9BVN2 EBI-24739968 0.56 Q9NZ72 EBI-24767700 0.56 Q16533 EBI-24771824 0.56 Q9NPF5 EBI-23881341 0.56 Q8NAM6 EBI-23889434 0.56 Q6QNY1 EBI-25276513 0.56 Q9ULR0 EBI-24803153 0.56 Q9BSW7 EBI-23914736 0.56 Q9BYV2 EBI-24396533 0.56 Q96GS4 EBI-24401384 0.56 Q8IYA8 EBI-24409360 0.56 Q5T5P2 EBI-24413377 0.56 P0CG20 EBI-24420156 0.56 Q9BVG8 EBI-24423104 0.56 Q8N0S2 EBI-24423729 0.56 Q01546 EBI-24425129 0.56 O14777 EBI-24431662 0.56 Q8TD10 EBI-24438784 0.56 Q70EL1 EBI-24446451 0.56 Q14142 EBI-24450438 0.56 O76011 EBI-24458571 0.56 Q5JR59 EBI-24470046 0.56 Q6NUQ1 EBI-24477001 0.56 Q9Y6H3 EBI-24545393 0.56 Q6IC98 EBI-24560187 0.56 Q96GY0 EBI-24575784 0.56 A0A1U9X8X8 EBI-24595565 0.56 Q8N2N9 EBI-24597123 0.56 Q9BYU1 EBI-24633510 0.56 Q9BXY8 EBI-25154342 0.56 Q8WWY6 EBI-24659479 0.56 Q2TBE0 EBI-25181664 0.56 Q8TDC0 EBI-24773710 0.56 P13682 EBI-24790242 0.56 Q96DF8 EBI-24799511 0.56 Q13360 EBI-25211267 0.56 P03427 EBI-14405248 0.35 P61006 EBI-11909914 0.00 Q96KP1 EBI-21672932 0.51 Q8N7X8 EBI-21585341 0.35 P21709 EBI-21595997 0.35 P27930 EBI-21662122 0.35 Q9Y3L3 EBI-21672932 0.35 Q9NX40 EBI-21672932 0.35 Q9H4M9 EBI-21672932 0.35 Q9H223 EBI-21672932 0.35 Q15345 EBI-21672932 0.35 Q13136 EBI-21672932 0.35 Q12981 EBI-21672932 0.35 O14975 EBI-21672932 0.35 O75131 EBI-20901088 0.40 P82914 EBI-20903504 0.40 P46781 EBI-20932336 0.40 P0DOF2 EBI-25603126 0.35 P19739 EBI-25685423 0.35 GO:0031252 GO:0005829 GO:0000145 GO:0030426 GO:0005770 GO:0016020 GO:0048471 GO:0005886 GO:0035091 GO:0031267 GO:0007032 GO:0006887 GO:0022617 GO:0006893 GO:0090148 GO:0000281 GO:0008104 GO:0015031 GO:0016241 GO:0006904 GO:0090522 Unknown UniProt Sequence Analysis MAMAMSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRIQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLTLLPAAAAAGAAAASGGEEGVGGAGGRDHLRGQAGFFSTPGGASRDGSGPGEEGKQRTLTTLLEKVEGCRHLLETPGQYLVYNGDLVEYDADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYSLDGLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEDTKRALSEKRRREQEEAAAPRGPPQVTSKATNPFEDDEEEEPAVPEVEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRAKVEERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFEIDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGDIGLDLTFIIHALLVKDIQGALHSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLIRVNPESTTSVV 725 Q6PGF7 Exocyst Exoc8 10090 None SL-0198 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}. UNIPROT Q6PGF7 Pfam PF16528 PROSITE PS50003 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. Q91VJ1 EBI-6253412 0.27 Q9EPB4 EBI-6253421 0.27 GO:0031252 GO:0000145 GO:0030426 GO:0005770 GO:0048471 GO:0005886 GO:0035091 GO:0031267 GO:0007032 GO:0006887 GO:0022617 GO:0006893 GO:0090148 GO:0000281 GO:0008104 GO:0015031 GO:0006904 GO:0090522 Unknown UniProt Sequence Analysis MSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRVQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLALLPAAAAGASAGEDTAGAGPRERGAVQAGFLPGPAGVPREGSGTGEEGKQRTLTTLLEKVEGCRDLLETPGQYLVYNGDLVEYDADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSDKRRREQEEAAAPRAPPPVTSKGSNPFEDEDDEELATPEAEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRAKVDERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGEIGLDLTFIIHALLVKDIQGALHSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVERRFEEGVGKPAKQLQDLRNASRLLRVNPESTTSVV 716 O54924 Exocyst Exoc8 10116 None SL-0198 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}. UNIPROT O54924 PDB 1ZC3 PDB 1ZC4 Pfam PF16528 PROSITE PS50003 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. GO:0031252 GO:0000145 GO:0030426 GO:0005770 GO:0048471 GO:0035091 GO:0031267 GO:0007032 GO:0006887 GO:0022617 GO:0006893 GO:0008104 GO:0015031 Unknown UniProt Sequence Analysis MSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRVQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLALLPAAAAGASTGEDTAGAGPRERGAAQAGFLPGPAGVPREGPGTGEEGKQRTLTTLLEKVEGCRDLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSDKRRREQEEAAALRAPPPVTSKGSNPFEDEAEEELATPEAEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPSVKELRAKVDERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGEIGLDLTFIIHALLVKDIQGALLSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMRSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEVILVAVQHVDYSLRCEQDPEKKTFIRQNASFLYDTVLPVVERRFEEGVGKPAKQLQDLRNASRLLRVNPESTTSVV 716 Q5U247 Exocyst exoc8 8355 None SL-0198 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}. UNIPROT Q5U247 Pfam PF16528 PROSITE PS50003 Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. GO:0000145 GO:0030426 GO:0048471 GO:0006887 GO:0015031 Unknown UniProt Sequence Analysis MAEGGGSVQRLRRQLESNSFQAEQYVKLLSQQSDGDRDLQEHRQRIQSLADETAQSLKRNVYQNYRQFIETAKEISYLEGEMYQLSHILTEQKSIMESVTQALLYTDRSEAARELQTAFPKEAEEGKVRNLTTLLEKVEGCKNLLETPGRYLVYNGDLTEFDVDNMALIQKVHAFLMNDCLLIATSVPNRRGIYKYNALHNLDDLAVVNVKENPPMKDMFKILMFPESRIFQAENAKIKKEWLEILEQTKKNKALNEKQKQEETTPQLPVVPEIPANPFIDEDGTFDEVEVDLTIDWIQELPEDLDVCIAQRNFEGAVDLLDKLNSYLEDKPLTHPVKELKSKVDERVRQLTDVLVFELSPDRSLRGGPKATRRAVSQLVRLGQSTKACELFLKNQAAAVQTAIRQLRIEGATLLYIHKLCNVFFTSLLETAKEFEMDFAENHGCYSAFIVWSRLALKMFVDAFSKQVFDSKESLSTVAECVKVAKEHCKQLSEIGLDLTFILHTLLVKDIKAALQSYKDIVIEATKHRNSEEMWRRMNLMTPEVLGKLREEMRNCGINNFDQYTGDDCWVNISYTIVAFTKQTMAFLEEALKLYFPELHMVLLECLMEIILVAIQHVDYSLRCEQESEKKAFIRQNASFLYENVLVVVEKRFEEGVGKPAKQLQELRNSSRLVRVNPESTTSVV 685 A8E639 Myelin-associated FAM168B 9913 None SL-0198 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}. UNIPROT A8E639 UNIPROT F1MAZ2 Pfam PF14944 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}. GO:0030424 GO:0016021 GO:0048471 GO:0005886 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYPGANPTFQAGYTSGTPYKVSCSPTSGAVPPYSSSPNPYQTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPLPPPRGNGVTMGMVAGTTMAMSAGTLLTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW 195 Q08BY2 Myelin-associated fam168b 7955 None SL-0198 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}. UNIPROT Q08BY2 Pfam PF14944 Inhibitor of neuronal axonal outgrowth. {ECO:0000250|UniProtKB:D4AEP3}. GO:0030424 GO:0016021 GO:0048471 GO:0005886 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNPVYSPASSGVPYANPKGIGYPAGFPVGYAAAAPAYSPSMYPGANPAFPSGYAPGTPFKMSCSPTTGAVPPYSSSPNPYPAAVYPVRSPYPQQNPYAQQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPAAMYAPPIPPPRPNGVTMGMVGGTTMAMSAGTLLTTHSPTPVAPHPSMPTYRQPATPTYSYVPPQW 195 A1KXE4 Myelin-associated FAM168B 9606 None SL-0198 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}. UNIPROT A1KXE4 UNIPROT Q2TAZ6 UNIPROT Q6NZ40 Pfam PF14944 DisGeNET 130074 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}. P0C762 EBI-2622097 0.37 Q9UGN5 EBI-7055170 0.44 Q9H6Z9 EBI-24622894 0.56 Q96A09 EBI-24509722 0.56 Q9BQY4 EBI-24509960 0.56 Q15915 EBI-24510851 0.56 Q9H0L4 EBI-24513225 0.56 O75593 EBI-24516068 0.56 Q6PEX3 EBI-24517441 0.56 O95231 EBI-24517283 0.56 P17482 EBI-24518222 0.56 Q96K80 EBI-24524781 0.56 Q9BZE0 EBI-24526759 0.56 Q08117 EBI-24528491 0.56 Q71SY5 EBI-24532543 0.56 Q13227 EBI-24609069 0.56 Q99932 EBI-24608889 0.56 Q7Z3H4 EBI-24616907 0.56 P78337 EBI-24621384 0.56 P32242 EBI-24631701 0.56 Q5T6F2 EBI-24714983 0.56 Q96HA1 EBI-24715141 0.56 P0CG20 EBI-24793729 0.56 P33240 EBI-25276276 0.56 Q9UQM7 EBI-24444859 0.56 P14678 EBI-24532872 0.56 A8MV65 EBI-24535723 0.56 Q64LD2 EBI-24535978 0.56 Q7Z5V6 EBI-24537270 0.56 A5D8V6 EBI-24543313 0.56 Q14119 EBI-24545906 0.56 Q8IXL7 EBI-24546845 0.56 Q01085 EBI-24552897 0.56 Q14847 EBI-24557301 0.56 O43251 EBI-24559610 0.56 Q9ULV5 EBI-24560739 0.56 Q7Z3K3 EBI-24561135 0.56 O43711 EBI-24564751 0.56 Q8TDC0 EBI-24570617 0.56 Q12951 EBI-24571134 0.56 O75909 EBI-24574824 0.56 Q9HBE1 EBI-24585617 0.56 Q01974 EBI-24590730 0.56 Q03989 EBI-24595017 0.56 P21549 EBI-24595339 0.56 Q9BTL3 EBI-24598895 0.56 Q14511 EBI-24633779 0.56 Q8WU58 EBI-24636945 0.56 Q9NQB0 EBI-24637975 0.56 Q92567 EBI-24639575 0.56 O95817 EBI-24640942 0.56 P09234 EBI-24758025 0.56 Q8IVT5 EBI-14035664 0.35 Q9BYX4 EBI-20206253 0.35 P17813 EBI-22197897 0.35 P22607 EBI-25855324 0.56 O14901 EBI-25906201 0.56 Q9BVL2 EBI-25908575 0.56 GO:0030424 GO:0070062 GO:0016021 GO:0048471 GO:0005886 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYPGANPTFQTGYTPGTPYKVSCSPTSGAVPPYSSSPNPYQTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPIPPPRGNGVTMGMVAGTTMAMSAGTLLTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW 195 Q80XQ8 Myelin-associated Fam168b 10090 None SL-0198 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}. UNIPROT Q80XQ8 UNIPROT Q3UNC7 UNIPROT Q5DTR7 Pfam PF14944 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}. GO:0030424 GO:0016021 GO:0048471 GO:0005886 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNPVYSPGSSGVPYANAKGIGYPAGFPVGYAAAPAYSPNMYPGANPTFQTGYTPGTPYKVSCSPTSGAVPPYSSSPNPYQTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPIPPPRGSGVTMGMVAGTTMAMSAGTLLTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW 194 D4AEP3 Myelin-associated Fam168b 10116 None SL-0198 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}. UNIPROT D4AEP3 Pfam PF14944 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}. Q92567 EBI-7957948 0.37 Q96QA6 EBI-7958149 0.37 Q15038 EBI-7958079 0.37 Q8IUR5 EBI-7958221 0.37 GO:0030424 GO:0016021 GO:0048471 GO:0005886 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNPVYSPGSSGVPYANAKGIGYPAGFPVGYAAAPAYSPNMYPGANPTFQTGYTPGTPYKVSCSPTSGAVPPYSSSPNPYQTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPIPPPRGSGVTMGMVAGTTMAMSAGTLLTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW 194 Q0IHC4 Myelin-associated fam168b 8355 None SL-0198 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}. UNIPROT Q0IHC4 Pfam PF14944 Inhibitor of neuronal axonal outgrowth. {ECO:0000250|UniProtKB:D4AEP3}. GO:0030424 GO:0016021 GO:0048471 GO:0005886 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYAGPNPAFQQELEHPAHVSSGVQMFMFGHAFSVARNGAIPSGYTPGTPYKVSCSPTSGTVPPYSSSPNPYQTAVYPVRSAYPQQNPYAQQGAYYTQPFYAAPPHVIHHTTVVQPNGMPATMYPAPIQSPRGNGVAMGMVAGTTMAMSAGTLLTSHYPSPVAPQVTMPTYRPPGTPTYSYVPPQW 225 Q0VFP2 Myelin-associated fam168b 8364 None SL-0198 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}. UNIPROT Q0VFP2 Pfam PF14944 Inhibitor of neuronal axonal outgrowth. {ECO:0000250|UniProtKB:D4AEP3}. GO:0030424 GO:0016021 GO:0048471 GO:0005886 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYAGPNPAFQPGYTPGTPYKVSCSPTSGTVPPYSSSPNPYQTAVYPVRSAYPQQNPYAQQGAYYTQPLYAAPPHVIHHTTVVQPNGMPATMYPAPIPQPRGNGVAMGMVAGTTMAMSAGTLLTSHYPTPVAPHQVTMPTYRPPGTPTYSYVPPQW 195 Q9Y6X4 Soluble FAM169A 9606 None SL-0178 SL-0179 SL-0182 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. UNIPROT Q9Y6X4 UNIPROT A8K1T9 UNIPROT Q6MZT0 UNIPROT Q9H989 OMIM 615769 P02545 EBI-16795756 0.27 P20700 EBI-24534698 0.56 Q96QG7 EBI-24348015 0.56 P02647 EBI-1220621 0.35 P58166 EBI-21648669 0.35 P27824 EBI-16788621 0.27 P62807 EBI-25471348 0.27 GO:0005637 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:22412018} MAFPVDMLENCSHEELENSAEDYMSDLRCGDPENPECFSLLNITIPISLSNVGFVPLYGGDQTQKILALFAPEDSLTAVALYLADQWWAIDDIVKTSVPSREGLKQVSTLGERVVLYVLNRIIYRKQEMERNEIPFLCHSSTDYAKILWKKGEAIGFYSVKPTGSICASFLTQSYQLPVLDTMFLRKKYRGKDFGLHMLEDFVDSFTEDALGLRYPLSSLMYTACKQYFEKYPGDHELLWEVEGVGHWYQRIPVTRALQREALKILALSQNEPKRPMSGEYGPASVPEYEARTEDNQSSEMQLTIDSLKDAFASTSEGHDKTSVSTHTRSGNLKRPKIGKRFQDSEFSSSQGEDEKTSQTSLTASINKLESTARPSESSEEFLEEEPEQRGIEFEDESSDRDARPALETQPQQEKQDGEKESELEPMNGEIMDDSLKTSLITEEEDSTSEVLDEELKLQPFNSSEDSTNLVPLVVESSKPPEVDAPDKTPRIPDSEMLMDEGTSDEKGHMEEKLSLLPRKKAHLGSSDNVATMSNEERSDGGFPNSVIAEFSEEPVSENLSPNTTSSLEDQGEEGVSEPQETSTALPQSSLIEVELEDVPFSQNAGQKNQSEEQSEASSEQLDQFTQSAEKAVDSSSEEIEVEVPVVDRRNLRRKAKGHKGPAKKKAKLT 670 Q5XG69 Soluble Fam169a 10090 None SL-0178 SL-0179 SL-0182 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}. UNIPROT Q5XG69 UNIPROT E9Q0D7 UNIPROT Q69ZW7 GO:0005637 Peripheral UniProt By Similarity {ECO:0000250} MAFPVDLLDNCTHEELENSSEDYLSSLRCGDPEHPECFSSLNITIPVSLSNVGFVPLYGGNQTQKILALFAPEDSLTAVALYLVGQWWAIDDIVKTSEPSREGLKQVSTLGERVVLYVLNRIIYRKQEMERNEIPFLCHSSTDYAKILWKKGEAVGFYSVKPTGSLCASFLTQNYQLPVLDTMFIRKKYRGKDLGLHMLEDFVDSFTEDALGLRYPLSSLMYTASKQYFEKYPGDHELLWEVEGVGHWHQRVPVTRALQREAIKATDVSQYEATRPVSGEYGLAAVPEHEPGLDDTQSSELQIHSLKDAFASTSEGPEKTPVSTRTRSSHLKRPKIGKHFQDSEFSSSQGEDENVAKTSPTASVNKIEYAARTSESSEEFLEEEPEQGVIDFEDESGDKDAQPALETQPRLQKQDGDKDSALEPVNGEVMDAALKPSLTTEDEDSTSEGLEEDLKVPPFNSSGEPGNPVPLVAESSKVPEATLAKTSPDTDSEMLIDQSPSDDKGHTEENLSPVSKKKTLLGSSDNVATVSNIEKSDGNFPNSVVPEFPEEPVSQNLSPNTTSSVEDQGEEGAPEAQEPSATQSSLIEVELEDAPFPQNAGQKSQSEEQSEASSEHLEQFTQSAEKAVDSSSEEIEVEVPVVDRRNLRRKAKGHKGPGKKKAKLT 665 Q5JX71 Protein FAM209A 9606 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:A2APA5}; Single-pass type I membrane protein {ECO:0000255}. UNIPROT Q5JX71 UNIPROT Q05C43 Pfam PF15206 May play a role in sperm acrosome biogenesis. {ECO:0000250|UniProtKB:A2APA5}. P50402 EBI-24763501 0.56 Q12982 EBI-25279273 0.56 Q15125 EBI-24758742 0.56 Q53HI1 EBI-24651712 0.56 Q5BJF2 EBI-24745243 0.56 P30519 EBI-24659762 0.56 Q9BXJ8 EBI-24660892 0.56 Q92482 EBI-24661914 0.56 P55061 EBI-24663858 0.56 Q6UXB4 EBI-24665193 0.56 Q96F05 EBI-24665171 0.56 P24593 EBI-24667567 0.56 Q8NBD8 EBI-24669580 0.56 Q7Z2K6 EBI-24669534 0.56 B2RUZ4 EBI-24670029 0.56 Q14508 EBI-24673017 0.56 Q7Z769 EBI-24674473 0.56 O14931 EBI-24674574 0.56 Q9BQB6 EBI-24675452 0.56 Q8NHY0 EBI-24675781 0.56 P43628 EBI-24677593 0.56 Q8WVV5 EBI-24677762 0.56 O60883 EBI-24678057 0.56 Q9GZX9 EBI-24678373 0.56 P01350 EBI-24680641 0.56 Q96FZ5 EBI-24681115 0.56 Q8WWP7 EBI-24683139 0.56 O75063 EBI-24683555 0.56 Q5VZY2 EBI-24686702 0.56 Q96LB9 EBI-24687412 0.56 Q92520 EBI-24688381 0.56 Q96GQ5 EBI-24692371 0.56 P23560 EBI-23726439 0.56 Q9UPQ8 EBI-24693724 0.56 Q8WVX3 EBI-24694786 0.56 Q9Y5U4 EBI-24696764 0.56 Q9HAB3 EBI-24696666 0.56 P57739 EBI-24697673 0.56 I3L0A0 EBI-24698635 0.56 O14653 EBI-24698512 0.56 Q969Y0 EBI-24699463 0.56 Q9NV29 EBI-24699387 0.56 P02724 EBI-24701121 0.56 Q9NUH8 EBI-24703342 0.56 Q9NPR9 EBI-24703316 0.56 P01375 EBI-24703711 0.56 P54315 EBI-24703665 0.56 Q8IY49 EBI-24703604 0.56 Q8TBB6 EBI-24704053 0.56 P30536 EBI-24704355 0.56 Q8IY26 EBI-24705960 0.56 Q9BQJ4 EBI-24706026 0.56 Q9Y6D0 EBI-24706768 0.56 Q8N2M4 EBI-24707299 0.56 Q5BJH2 EBI-24708034 0.56 Q8NHS1 EBI-24708497 0.56 Q1RMY5 EBI-24709934 0.56 Q9Y6X1 EBI-24711058 0.56 A5D903 EBI-24711648 0.56 Q71RG4 EBI-24711927 0.56 P60033 EBI-24716011 0.56 O14735 EBI-24717599 0.56 P02808 EBI-24718795 0.56 Q8TBE7 EBI-24719810 0.56 P37268 EBI-24720377 0.56 Q8NHW4 EBI-24720728 0.56 P41732 EBI-24721505 0.56 Q969S6 EBI-24723426 0.56 Q8WVQ1 EBI-24724764 0.56 Q9C0I4 EBI-24726005 0.56 Q04941 EBI-24726747 0.56 P29033 EBI-24727519 0.56 O75396 EBI-24727475 0.56 Q96EC8 EBI-24727308 0.56 Q8IXM6 EBI-24729136 0.56 Q9NZ01 EBI-24728923 0.56 P11836 EBI-24729270 0.56 Q96I45 EBI-24729879 0.56 Q96IW7 EBI-24731532 0.56 Q5W0B7 EBI-24732788 0.56 Q9NZG7 EBI-24733776 0.56 Q8TBM7 EBI-24734476 0.56 Q86WK9 EBI-24735695 0.56 P29972 EBI-24741655 0.56 P19397 EBI-24741916 0.56 O60636 EBI-24741870 0.56 Q9UHJ9 EBI-24743958 0.56 Q9H2L4 EBI-24744254 0.56 Q15848 EBI-24744581 0.56 A0A0C4DFN3 EBI-24748093 0.56 Q8TAF8 EBI-24748474 0.56 Q9UHX3 EBI-24750533 0.56 Q69YG0 EBI-24750810 0.56 Q9NS64 EBI-24755295 0.56 Q6PI78 EBI-24755815 0.56 Q9NS71 EBI-24755725 0.56 Q7Z7B8 EBI-24763350 0.56 Q8N912 EBI-24765153 0.56 O95183 EBI-24766009 0.56 Q96S97 EBI-24767098 0.56 Q4VAQ0 EBI-24768660 0.56 Q13635 EBI-24769357 0.56 P29034 EBI-24770320 0.56 Q5QGT7 EBI-24771029 0.56 Q9HCP6 EBI-24771241 0.56 O14493 EBI-24771780 0.56 P41181 EBI-24771883 0.56 Q9H3K2 EBI-24773001 0.56 P02656 EBI-24778709 0.56 Q9GZY8 EBI-24778858 0.56 Q9BVK2 EBI-24779310 0.56 Q8IWU4 EBI-24780535 0.56 Q92903 EBI-24780869 0.56 Q7L5A8 EBI-24781569 0.56 O75379 EBI-24782054 0.56 Q86W74 EBI-24782320 0.56 P05090 EBI-24782399 0.56 O14569 EBI-24783279 0.56 P26678 EBI-24784407 0.56 P02786 EBI-24784925 0.56 A6NDP7 EBI-24785107 0.56 O95674 EBI-24793784 0.56 Q7Z4F1 EBI-24793953 0.56 Q15546 EBI-24794093 0.56 Q9P0N8 EBI-24794270 0.56 Q8N609 EBI-24795904 0.56 O95393 EBI-24798213 0.56 P13987 EBI-25276491 0.56 P40313 EBI-25276423 0.56 Q59EV6 EBI-25276813 0.56 Q8N6F1 EBI-25277574 0.56 Q8N661 EBI-25278338 0.56 Q9HDC9 EBI-25279172 0.56 P21964 EBI-25279786 0.56 P29400 EBI-25280159 0.56 P56557 EBI-25280653 0.56 Q02094 EBI-25281444 0.56 Q9BQS2 EBI-25281434 0.56 Q9H2S6 EBI-25282993 0.56 O95968 EBI-25283181 0.56 Q9NRS4 EBI-25283685 0.56 Q8TDV0 EBI-25284292 0.56 Q9Y5Z9 EBI-25285255 0.56 Q4LDR2 EBI-25285389 0.56 Q9Y385 EBI-25285367 0.56 Q01453 EBI-25286025 0.56 Q9Y3D6 EBI-25287586 0.56 P09601 EBI-25287799 0.56 Q13190 EBI-25288503 0.56 Q86UF1 EBI-24641235 0.56 Q9UKR5 EBI-24641314 0.56 Q9BTX3 EBI-24641793 0.56 Q9BTV4 EBI-24641558 0.56 Q5J8X5 EBI-24642453 0.56 Q9NRQ5 EBI-24642874 0.56 Q96LL9 EBI-24643260 0.56 O75355 EBI-24643214 0.56 Q9BUP3 EBI-24643959 0.56 Q5NDL2 EBI-24645284 0.56 Q96G79 EBI-24646026 0.56 Q9BT09 EBI-24647320 0.56 Q5J5C9 EBI-24647994 0.56 Q9HD20 EBI-24648696 0.56 Q8N138 EBI-24649134 0.56 O43681 EBI-24650187 0.56 Q9H0R3 EBI-24650534 0.56 Q9H2C2 EBI-24650290 0.56 P17152 EBI-24650279 0.56 Q13323 EBI-24651167 0.56 Q15836 EBI-24651889 0.56 P60059 EBI-24652003 0.56 Q12983 EBI-24652350 0.56 A0PK05 EBI-24652273 0.56 Q9BZW4 EBI-24653078 0.56 P30301 EBI-24653337 0.56 O14798 EBI-24653654 0.56 P07306 EBI-24655518 0.56 Q6UX40 EBI-24656181 0.56 Q6RW13 EBI-24657303 0.56 Q5BVD1 EBI-24659602 0.56 Q14162 EBI-24659536 0.56 Q14802 EBI-24744695 0.56 O43169 EBI-24745059 0.56 Q9Y6I9 EBI-24758880 0.56 Q9BSE2 EBI-24759294 0.56 P06681 EBI-24759556 0.56 Q9NVC3 EBI-24759878 0.56 P43005 EBI-24761066 0.56 Q9BQE5 EBI-24773951 0.56 A2RU14 EBI-24774300 0.56 Q8WWT9 EBI-24774991 0.56 Q9NWW5 EBI-24775375 0.56 O76024 EBI-24776394 0.56 Q9UHE5 EBI-24776145 0.56 Q9BQA9 EBI-24776598 0.56 Q6UX06 EBI-24777357 0.56 Q9Y228 EBI-24787867 0.56 Q9BV81 EBI-24788001 0.56 Q9NRC9 EBI-24788293 0.56 Q13277 EBI-24788844 0.56 O43759 EBI-24789665 0.56 O95159 EBI-24790231 0.56 Q9BU79 EBI-24792203 0.56 Q9UBY5 EBI-24792539 0.56 O75711 EBI-24800001 0.56 P60201 EBI-24802443 0.56 Q969F0 EBI-24802386 0.56 P11686 EBI-24803127 0.56 Q969S0 EBI-24803316 0.56 O95406 EBI-24804040 0.56 Q9P0S9 EBI-24804775 0.56 Q8N5M9 EBI-24804922 0.56 O75841 EBI-24809719 0.56 Q96GC9 EBI-24810789 0.56 Q9NVV5 EBI-24810993 0.56 Q86XP6 EBI-25266404 0.56 Q6UX34 EBI-25267080 0.56 P21145 EBI-25267772 0.56 Q9H115 EBI-25269370 0.56 P78382 EBI-25269850 0.56 O15155 EBI-25270807 0.56 Q9NV12 EBI-25270546 0.56 P07204 EBI-25271156 0.56 Q9UNK0 EBI-25271982 0.56 Q6Y1H2 EBI-25273339 0.56 P61266 EBI-25273755 0.56 Q8TF42 EBI-21896717 0.40 GO:0070062 GO:0016021 GO:0005637 GO:0005634 GO:0030154 GO:0007283 Transmembrane UniProt Sequence Analysis {ECO:0000255} MWTLKSSLVLLLCLTCSYAFMFSSLRQKTSEPQGKVQYGEHFRIRQNLPEHTQGWLGSKWLWLLFVVVPFVILQCQRDSEKNKEQSPPGLRGGQLHSPLKKKRNASPNKDCAFNTLMELEVELMKFVSKVRNLKRAMATGSGSNLRLRKSEMPADPYHVTICEIWGEESSS 171 Q5JX69 Protein FAM209B 9606 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000250|UniProtKB:A2APA5}; Single-pass type I membrane protein {ECO:0000255}. UNIPROT Q5JX69 UNIPROT Q3KRB5 Pfam PF15206 May play a role in sperm acrosome biogenesis. {ECO:0000250|UniProtKB:A2APA5}. GO:0016021 GO:0005637 GO:0005634 GO:0030154 GO:0007283 Transmembrane UniProt Sequence Analysis {ECO:0000255} MWTLKSSLVLLLCLTCSYAFMFSSLRQKTSEPQGKVPCGEHFRIRQNLPEHTQGWLGSKWLWLLFAVVPFVILQCQRDSEKNKEQSPPGLRGFPFRTPLKKNQNASLYKDCVFNTLNELEVELLKFVSEVQNLKGAMATGSGSNLKLRRSEMPADPYHVTICKIWGEESSS 171 A2APA5 Protein Fam209 10090 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:34471926}; Single-pass type I membrane protein {ECO:0000255}. UNIPROT A2APA5 UNIPROT Q9D9T2 Pfam PF15206 Required for sperm acrosome biogenesis. {ECO:0000269|PubMed:34471926}. GO:0016021 GO:0005637 GO:0001675 GO:0007286 Transmembrane UniProt Sequence Analysis {ECO:0000255} MRTLLRWCLFLSLCVSCACAFMFSSMREKTKESPGKVPCGGHFRIRQNLPENAQGWLGNKWLWLFVAIMIYVMLKFRGDGENKEQHPPGLRGCQLRSPPKKAQNISPSKDFTFNTLTQLEMELVKFVSKVRNLKVSMATNSNSRQQVPESPTNLYNNVTIYEIWGEEDSE 170 O75844 CAAX ZMPSTE24 9606 None SL-0178 SL-0179 SL-0182 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}. UNIPROT O75844 UNIPROT B3KQI7 UNIPROT D3DPU7 UNIPROT Q8NDZ8 UNIPROT Q9UBQ2 PDB 2YPT PDB 4AW6 PDB 5SYT PDB 6BH8 Pfam PF01435 Pfam PF16491 OMIM 275210 OMIM 606480 OMIM 608612 DisGeNET 10269 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}. 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. Q9UET6 EBI-1069131 0.00 P08473 EBI-1389788 0.35 Q77M19 EBI-6270503 0.35 Q16666 EBI-9995438 0.35 Q6NUS6 EBI-11368748 0.27 Q96GX1 EBI-11375285 0.27 P06821 EBI-12590819 0.50 C5E519 EBI-12590830 0.50 Q6DPW5 EBI-12590841 0.40 Q20MH8 EBI-12590852 0.50 P29084 EBI-21499432 0.35 Q13503 EBI-21501670 0.35 Q99679 EBI-21516430 0.35 Q6PEY0 EBI-21551307 0.35 P22732 EBI-21554490 0.35 Q8WTR4 EBI-21566764 0.35 P54219 EBI-21609589 0.35 Q08AM6 EBI-21634069 0.35 O00624 EBI-21654627 0.35 Q9BVJ7 EBI-21667644 0.35 Q02223 EBI-21757502 0.35 Q86WS5 EBI-21771386 0.35 Q9BY78 EBI-21772313 0.35 P04798 EBI-21774067 0.35 O15263 EBI-21800402 0.40 P14324 EBI-21800273 0.35 P02545 EBI-16043055 0.56 P16401 EBI-20900343 0.40 A4D263 EBI-20905088 0.40 P47902 EBI-20906784 0.40 Q5S007 EBI-21360986 0.35 P0DTD8 EBI-25687199 0.35 Q7TFA1 EBI-25688644 0.35 Q2TAZ0 EBI-26443127 0.35 Q9BXK1 EBI-29019783 0.35 GO:0070062 GO:0030176 GO:0016020 GO:0005637 GO:0032991 GO:0003690 GO:0046872 GO:0004222 GO:0008235 GO:0007628 GO:0030282 GO:0071586 GO:1990036 GO:0061762 GO:0061337 GO:0055013 GO:0003231 GO:0044255 GO:0071480 GO:0006325 GO:0008340 GO:0006281 GO:0003417 GO:0001942 GO:0003007 GO:0043979 GO:0044029 GO:0006925 GO:0060993 GO:0001889 GO:0043007 GO:0035264 GO:1903799 GO:0050905 GO:0006998 GO:0030327 GO:0006508 GO:0010506 GO:0030500 GO:0008360 GO:2000772 GO:0050688 GO:0043516 GO:0048145 GO:0010906 GO:2000618 GO:0032350 GO:0019216 GO:1903463 GO:0040014 GO:1903025 GO:0070302 GO:2000730 GO:0032006 GO:0060307 GO:0072423 GO:0048538 GO:0003229 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGMWASLDALWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEEGNSEEIKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHYSHPPLLERLQALKTMKQH 475 Q80W54 CAAX Zmpste24 10090 None SL-0178 SL-0179 SL-0182 Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. UNIPROT Q80W54 UNIPROT Q8BJK4 UNIPROT Q8K569 Pfam PF01435 Pfam PF16491 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}. GO:0030176 GO:0016020 GO:0005635 GO:0005637 GO:0032991 GO:0003690 GO:0004175 GO:0046872 GO:0004222 GO:0007628 GO:0030282 GO:0071586 GO:1990036 GO:0061762 GO:0061337 GO:0055013 GO:0003231 GO:0044255 GO:0006974 GO:0071480 GO:0006325 GO:0051276 GO:0008340 GO:0006281 GO:0008544 GO:0003417 GO:0001942 GO:0003007 GO:0043969 GO:0043979 GO:0044029 GO:0006925 GO:0060993 GO:0001889 GO:0043007 GO:0035264 GO:0010629 GO:1903799 GO:0050905 GO:0006998 GO:0006997 GO:0010628 GO:0030327 GO:0016485 GO:0010506 GO:1903522 GO:0030500 GO:0008360 GO:2000772 GO:0050688 GO:0043516 GO:0044030 GO:0006355 GO:0048145 GO:0010906 GO:0008016 GO:0090239 GO:2000618 GO:0032350 GO:0019216 GO:0007346 GO:1903463 GO:0040014 GO:1903025 GO:0070302 GO:2000730 GO:0032006 GO:0060307 GO:0072423 GO:0048538 GO:0003229 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGMWASVDAMWDFPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTRVPAELEQIMDSDTFEKSRLYQLDKSTFSFWSGLYSEVEGTFILLFGGIPYLWRLSGQFCSSAGFGPEYEIIQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNHQTLEFFMKDAIKKFIVTQCILLPVSALLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKQEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVPNKDNQEESGMEARNEGEGDSEEVKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRRELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSTWHYSHPPLLERLQALKNAKQD 475 Q00944 Focal PTK2 9031 None SL-0198 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}. UNIPROT Q00944 PDB 1KTM PDB 1PV3 PDB 1QVX PDB 2AEH PDB 2AL6 PDB 2J0J PDB 2J0K PDB 2J0L PDB 2J0M PDB 2JKK PDB 2JKM PDB 2JKO PDB 2JKQ PDB 2L6F PDB 2L6G PDB 2L6H PDB 3ZDT PDB 4BRX PDB 4C7T PDB 4CYE PDB 4D4R PDB 4D4S PDB 4D4V PDB 4D4Y PDB 4D55 PDB 4D58 PDB 4D5H PDB 4D5K PDB 6CB0 PDB 6GCR PDB 6GCW PDB 6GCX PDB 6TY3 PDB 6TY4 Pfam PF00373 Pfam PF18038 Pfam PF03623 Pfam PF07714 PROSITE PS00661 PROSITE PS50057 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. P00523 EBI-6861774 0.59 P00533 EBI-3953289 0.44 P49024 EBI-2896453 0.61 P08581 EBI-3894385 0.60 P09619 EBI-3953300 0.44 Q00944 EBI-4305329 0.66 Q14451 EBI-4288386 0.40 P61157 EBI-6692630 0.61 A7MB62 EBI-6692672 0.35 G3GXX7 EBI-6899259 0.40 P62993 EBI-6899017 0.40 Q61140 EBI-6900257 0.40 GO:0036064 GO:0005737 GO:0043197 GO:0031234 GO:0005925 GO:0005634 GO:0048471 GO:0042383 GO:0005524 GO:0004198 GO:0042802 GO:0005178 GO:0140677 GO:0004715 GO:0002020 GO:0004713 GO:0005102 GO:0007015 GO:0001525 GO:0060055 GO:0030154 GO:0007173 GO:0045087 GO:2000811 GO:0010812 GO:0031953 GO:0030335 GO:0008284 GO:0051894 GO:0032092 GO:0061098 GO:1904237 GO:0046777 GO:0006468 GO:0140650 GO:0030155 GO:0035994 GO:0009268 GO:0007172 GO:0007169 GO:0044319 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:8423801} MAAAYLDPNLNHTPSSSAKTHLGTGMERSPGAMERVLKVFHYFENSSEPTTWASIIRHGDATDVRGIIQKIVDCHKVKNVACYGLRLSHLQSEEVHWLHLDMGVSNVREKFELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKNDYMLEIADQVDQEIALKLGCLEIRRSYGEMRGNALEKKSNYEVLEKDVGLRRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGANPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANNEKQGVRSHTVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAMAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKFSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSATDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKLQQEERMRMESRRQVTVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQPNHYQVSGYSGSHGIPAMAGSIYPGQASLLDQTDSWNHRPQEVSAWQPNMEDSGTLDVRGMGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLVMKPDVRLSRGSIEREDGGLQGPAGNQHIYQPVGKPDHAAPPKKPPRPGAPHLGSLASLNSPVDSYNEGVKIKPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDESLPVLPASTHREIEMAQKLLNSDLAELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMISQSRPH 1053 Q05397 Focal PTK2 9606 None SL-0198 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}. UNIPROT Q05397 UNIPROT B4E2N6 UNIPROT F5H4S4 UNIPROT J3QT16 UNIPROT Q14291 UNIPROT Q8IYN9 UNIPROT Q9UD85 PDB 1K04 PDB 1K05 PDB 1MP8 PDB 1OW6 PDB 1OW7 PDB 1OW8 PDB 2ETM PDB 2IJM PDB 3B71 PDB 3BZ3 PDB 3PXK PDB 3S9O PDB 4EBV PDB 4EBW PDB 4GU6 PDB 4GU9 PDB 4I4E PDB 4I4F PDB 4K8A PDB 4K9Y PDB 4KAB PDB 4KAO PDB 4NY0 PDB 4Q9S PDB 6I8Z PDB 6LES PDB 6PW8 PDB 6YOJ PDB 6YQ1 PDB 6YR9 PDB 6YT6 PDB 6YVS PDB 6YVY PDB 6YXV PDB 7PI4 Pfam PF00373 Pfam PF18038 Pfam PF03623 Pfam PF07714 PROSITE PS00661 PROSITE PS50057 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 OMIM 600758 DisGeNET 5747 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}. 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. O60711 EBI-7326264 0.55 P00533 EBI-702075 0.75 P04626 EBI-2942138 0.54 P05480 EBI-7976544 0.68 P07948 EBI-7859736 0.57 P12931 EBI-968957 0.92 P37198 EBI-30836789 0.44 P56945 EBI-8617929 0.59 P78396 EBI-6592527 0.54 P04637 EBI-1544471 0.75 Q80ZW7 EBI-7809276 0.46 P70372 EBI-7809400 0.40 Q7L0Q8 EBI-1792522 0.40 Q62219 EBI-1810942 0.52 P49023 EBI-1810961 0.94 O43294 EBI-1811097 0.77 Q62884 EBI-7505062 0.44 Q68CZ2 EBI-2607447 0.56 P54792 EBI-7848137 0.35 O14640 EBI-7848672 0.35 P43146 EBI-2678596 0.35 A0A5P8YHQ6 EBI-2870073 0.00 P62993 EBI-8590192 0.66 P63000 EBI-3449574 0.00 Q9BY76 EBI-3843710 0.35 P29317 EBI-3843951 0.49 Q9UBE0 EBI-3914256 0.37 Q8TAM1 EBI-7322989 0.37 O00148 EBI-7323069 0.37 P26641 EBI-7323654 0.37 Q9H6S3 EBI-7323997 0.37 P00488 EBI-7324567 0.37 P09467 EBI-7325203 0.37 Q14469 EBI-7325706 0.37 O15069 EBI-7326959 0.37 P49321 EBI-7327416 0.37 Q9NQX6 EBI-7328100 0.37 Q9H3S7 EBI-8423552 0.64 P46108 EBI-6181896 0.63 Q9Y3E5 EBI-6253054 0.40 P21145 EBI-6253719 0.35 O00459 EBI-6256910 0.35 P42336 EBI-6256910 0.35 Q92569 EBI-6256910 0.63 Q96SB4 EBI-6659921 0.59 P08238 EBI-6423484 0.40 O75925 EBI-6591889 0.27 P07949 EBI-6592681 0.27 P40763 EBI-6593385 0.27 P42224 EBI-6593396 0.54 P25054 EBI-6594490 0.27 P46109 EBI-6599743 0.27 P17948 EBI-6599815 0.27 P07947 EBI-6599941 0.57 P06756 EBI-6600280 0.27 P60484 EBI-6600406 0.27 P19174 EBI-6600388 0.27 P54939 EBI-6620512 0.40 P39052 EBI-8699700 0.40 Q05397 EBI-9256428 0.44 P14618 EBI-9355072 0.44 P29350 EBI-10691827 0.57 O60880 EBI-10691844 0.49 Q8TEW6 EBI-10691810 0.49 Q9NP31 EBI-10691878 0.57 Q14451 EBI-10691861 0.57 O14796 EBI-10697408 0.37 P08631 EBI-10697432 0.51 Q9H269 EBI-11047581 0.35 Q9QZB9 EBI-11074142 0.35 P16144 EBI-12599461 0.52 P16671 EBI-13940936 0.35 P05120 EBI-21713063 0.35 Q13976 EBI-21852154 0.35 Q15125 EBI-20903608 0.40 P07355 EBI-20913238 0.40 Q9NQ75 EBI-21384868 0.00 Q9NRI5 EBI-21384856 0.00 P06241 EBI-28938953 0.55 P13569 EBI-25416349 0.35 D4A3T0 EBI-22240287 0.35 F1M3E4 EBI-22240287 0.35 Q920L0 EBI-22240287 0.35 Q4KM68 EBI-22240287 0.35 P62994 EBI-22240287 0.35 D3ZG10 EBI-22240287 0.35 P20339 EBI-25381246 0.35 O84008 EBI-22302433 0.35 Q07889 EBI-25438153 0.35 Q06124 EBI-25438153 0.35 Q824H6 EBI-26494109 0.54 P49024 EBI-26498316 0.37 P25105 EBI-27099240 0.40 Q00535 EBI-28938854 0.35 P35251 EBI-28938953 0.35 P35249 EBI-28938953 0.35 Q9Y5J1 EBI-28938953 0.35 Q9Y3B2 EBI-28938953 0.35 Q9UQ35 EBI-28938953 0.35 Q9NXZ2 EBI-28938953 0.35 Q9NW13 EBI-28938953 0.35 Q9NQ55 EBI-28938953 0.35 Q9HCM4 EBI-28938953 0.35 Q9H7E9 EBI-28938953 0.35 Q9GZR7 EBI-28938953 0.35 Q9BZE4 EBI-28938953 0.35 Q9BRJ6 EBI-28938953 0.35 Q96B26 EBI-28938953 0.35 Q7L2E3 EBI-28938953 0.35 Q6DKI1 EBI-28938953 0.35 Q5TAQ9 EBI-28938953 0.35 Q2NL82 EBI-28938953 0.35 Q14978 EBI-28938953 0.35 Q14137 EBI-28938953 0.35 Q13868 EBI-28938953 0.35 Q13428 EBI-28938953 0.35 Q01780 EBI-28938953 0.35 Q00577 EBI-28938953 0.35 P68400 EBI-28938953 0.35 P67870 EBI-28938953 0.35 P61981 EBI-28938953 0.35 P56182 EBI-28938953 0.35 P49458 EBI-28938953 0.35 P49354 EBI-28938953 0.35 P42696 EBI-28938953 0.35 P31948 EBI-28938953 0.35 P13674 EBI-28938953 0.35 O75683 EBI-28938953 0.35 Q3SY52 EBI-30836811 0.44 Q504T8 EBI-30836822 0.44 O75038 EBI-30836778 0.44 Q08378 EBI-30836800 0.44 Q7Z478 EBI-30836833 0.44 Q8IYE1 EBI-30836844 0.44 Q8WZA0 EBI-30836855 0.44 Q92859 EBI-30836866 0.44 Q96BU1 EBI-30836877 0.44 Q9H0J4 EBI-30836888 0.44 GO:0005938 GO:0036064 GO:0005737 GO:0005856 GO:0005829 GO:0043197 GO:0031234 GO:0005925 GO:0043231 GO:0005634 GO:0005886 GO:0001725 GO:0003779 GO:0005524 GO:0005178 GO:0008432 GO:0140677 GO:0004715 GO:0019901 GO:0019903 GO:0004713 GO:0004725 GO:0042169 GO:0005102 GO:0001525 GO:0007411 GO:0030154 GO:0016477 GO:0048870 GO:0035995 GO:0048013 GO:0007173 GO:0030010 GO:0038096 GO:0060396 GO:0003007 GO:0045087 GO:0007229 GO:2000811 GO:0043066 GO:0022408 GO:0038007 GO:0018108 GO:0001890 GO:0030335 GO:0008284 GO:0010634 GO:0010718 GO:0010763 GO:0010759 GO:0120041 GO:0043552 GO:0014068 GO:0045860 GO:0051897 GO:0001934 GO:2000060 GO:0090303 GO:0046777 GO:0006468 GO:0065008 GO:0030155 GO:0033628 GO:0042127 GO:0008360 GO:0051493 GO:0010594 GO:0010632 GO:0051893 GO:0043087 GO:0045667 GO:0001932 GO:1900024 GO:0007172 GO:0007179 GO:0007169 GO:0048010 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q00944} MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH 1052 P34152 Focal Ptk2 10090 None SL-0198 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}. UNIPROT P34152 UNIPROT O08578 UNIPROT Q5DTH7 UNIPROT Q8C513 UNIPROT Q8CFH7 UNIPROT Q8CHM2 UNIPROT Q8K2S0 UNIPROT Q9DAW3 PDB 1K40 PDB 5F28 PDB 6BZ3 Pfam PF00373 Pfam PF18038 Pfam PF03623 Pfam PF07714 PROSITE PS00661 PROSITE PS50057 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. P05480 EBI-7361479 0.59 P12931 EBI-7921275 0.56 Q61140 EBI-77098 0.65 Q8VI36 EBI-7361489 0.78 P39688 EBI-653453 0.37 P54763 EBI-983197 0.46 Q60631 EBI-983357 0.51 Q03160 EBI-7281453 0.44 P18031 EBI-8672381 0.44 P97333 EBI-7921208 0.40 P11627 EBI-7921264 0.40 P35235 EBI-7186929 0.40 P54792 EBI-7848377 0.40 P62993 EBI-8633193 0.60 P56945 EBI-6569708 0.40 P49023 EBI-6569717 0.46 Q99JY9 EBI-6675060 0.46 Q91YD9 EBI-6675097 0.40 P39054 EBI-8699666 0.40 P39052 EBI-8699679 0.32 Q62108 EBI-16724752 0.35 Q9D415 EBI-16725590 0.35 Q3UHD9 EBI-16736255 0.35 Q6NZM9 EBI-26473528 0.35 GO:0016324 GO:0016323 GO:0036064 GO:0005737 GO:0005829 GO:0043197 GO:0031234 GO:0005925 GO:0098978 GO:0014704 GO:0043231 GO:0030027 GO:0016604 GO:0005730 GO:0005634 GO:0048471 GO:0005886 GO:0098794 GO:0042383 GO:0001725 GO:0003779 GO:0005524 GO:0042802 GO:0005178 GO:0008432 GO:0004715 GO:0019902 GO:0043548 GO:0019901 GO:0019903 GO:0004713 GO:0004725 GO:0044877 GO:0042169 GO:0005102 GO:0001525 GO:0007409 GO:0001568 GO:0030154 GO:0016477 GO:0030644 GO:0071560 GO:0021955 GO:0043542 GO:0048013 GO:0007173 GO:0030198 GO:0060396 GO:0045087 GO:0007229 GO:0007254 GO:0000165 GO:0000226 GO:2000811 GO:0043066 GO:0010507 GO:0050771 GO:0030336 GO:0022408 GO:0046621 GO:0051964 GO:0001764 GO:0007097 GO:0035265 GO:0038083 GO:0018108 GO:0010613 GO:0045785 GO:0030307 GO:0030335 GO:0008284 GO:0010763 GO:0060252 GO:0010759 GO:0120041 GO:0050766 GO:0014068 GO:0045860 GO:0051897 GO:0001934 GO:0014911 GO:0048661 GO:0050806 GO:2000060 GO:0090303 GO:0046777 GO:0006468 GO:0030155 GO:0033628 GO:0042127 GO:0008360 GO:0010632 GO:0051893 GO:0045667 GO:0001932 GO:1900024 GO:0007172 GO:0007179 GO:0007169 GO:0001570 GO:0042311 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q00944} MAAAYLDPNLNHTPSSSTKTHLGTGMERSPGAMERVLKVFHYFESSSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMQEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGVYLSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKVQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGIPAMAGSIYQGQASLLDQTELWNHRPQEMSMWQPSVEDSAALDLRGMGQVLPPHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSFQGPTGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLSNLSSISSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPALPASTHREIEMAQKLLNSDLGELISKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH 1052 O35346 Focal Ptk2 10116 None SL-0198 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}. UNIPROT O35346 UNIPROT Q62900 Pfam PF00373 Pfam PF18038 Pfam PF03623 Pfam PF07714 PROSITE PS00661 PROSITE PS50057 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. P62140 EBI-7935349 0.40 P41239 EBI-8594657 0.40 Q9BX66 EBI-8536646 0.35 Q5XI86 EBI-6253014 0.46 O70161 EBI-6614935 0.27 O35346 EBI-9256497 0.72 Q8VI36 EBI-9256513 0.38 Q6P6T5 EBI-15783756 0.59 F1M4A0 EBI-15783823 0.40 GO:0016324 GO:0016323 GO:0036064 GO:0005737 GO:0005829 GO:0043197 GO:0031234 GO:0005925 GO:0098978 GO:0014704 GO:0030027 GO:0016604 GO:0005730 GO:0005634 GO:0048471 GO:0005886 GO:0098794 GO:0042383 GO:0001725 GO:0003779 GO:0005524 GO:0042802 GO:0005178 GO:0008432 GO:0004715 GO:0019902 GO:0043548 GO:0019901 GO:0019903 GO:0004713 GO:0004725 GO:0044877 GO:0042169 GO:0005102 GO:0001525 GO:0007409 GO:0001568 GO:0030154 GO:0016477 GO:0030644 GO:0071560 GO:0021955 GO:0043542 GO:0048013 GO:0007173 GO:0030198 GO:0045444 GO:0060396 GO:0045087 GO:0007229 GO:0007254 GO:0000165 GO:0000226 GO:2000811 GO:0043066 GO:0010507 GO:0050771 GO:0030336 GO:0022408 GO:0046621 GO:0051964 GO:0001764 GO:0007097 GO:0035265 GO:0038083 GO:0018108 GO:0010613 GO:0045785 GO:0030307 GO:0030335 GO:0008284 GO:0010763 GO:0060252 GO:0010759 GO:0120041 GO:0050766 GO:0014068 GO:0045860 GO:0051897 GO:0001934 GO:0014911 GO:0048661 GO:0050806 GO:2000060 GO:0090303 GO:0046777 GO:0006468 GO:0030155 GO:0033628 GO:0042127 GO:0008360 GO:0010632 GO:0051893 GO:0045667 GO:0001932 GO:1900024 GO:0046685 GO:0032355 GO:0009749 GO:0009612 GO:0014070 GO:0010033 GO:0010243 GO:0009410 GO:0007172 GO:0007179 GO:0007169 GO:0001570 GO:0042311 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q00944} MAAAYLDPNLNHTPSSSTKTHLGTGTERSPGAMERVLKVFHYFESSNEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQDIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANNEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGVYLSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKVQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQISGYPGSHGIPAMAGSIYPGQASLLDQTELWNHRPQEMSMWQPSVEDSAALDLRGMGQVLPPHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSFQGPTGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLSNLSSISSPAESYNEGVKPWRLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPILPASTHREIEMAQKLLNSDLGELISKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH 1055 Q14289 Protein-tyrosine PTK2B 9606 None SL-0198 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. UNIPROT Q14289 UNIPROT D3DST0 UNIPROT Q13475 UNIPROT Q14290 UNIPROT Q16709 UNIPROT Q6PID4 PDB 2LK4 PDB 3CC6 PDB 3ET7 PDB 3FZO PDB 3FZP PDB 3FZR PDB 3FZS PDB 3FZT PDB 3GM1 PDB 3GM2 PDB 3GM3 PDB 3H3C PDB 3U3F PDB 4EKU PDB 4H1J PDB 4H1M PDB 4R32 PDB 4XEF PDB 4XEK PDB 4XEV PDB 5TO8 PDB 5TOB PDB 6LF3 Pfam PF00373 Pfam PF18038 Pfam PF03623 Pfam PF07714 PROSITE PS50057 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 OMIM 601212 DisGeNET 2185 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}. 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. A1A4S6 EBI-28941112 0.35 O60711 EBI-21392269 0.00 P00533 EBI-702075 0.35 P04626 EBI-6589791 0.27 P12931 EBI-7095687 0.64 Q02156 EBI-28938908 0.35 Q9Y6R4 EBI-7426200 0.46 Q8WUM4 EBI-7397527 0.40 Q00005 EBI-2210942 0.35 Q7L0Q8 EBI-1792396 0.58 P17778 EBI-2870052 0.00 Q8CKM0 EBI-2870059 0.00 Q8CKF8 EBI-2870066 0.00 P06241 EBI-7313404 0.70 P42679 EBI-8467868 0.46 P62993 EBI-8684794 0.35 Q99836 EBI-6390158 0.40 Q8NF50 EBI-6390162 0.35 P08238 EBI-6423496 0.40 O75161 EBI-11790516 0.40 P24830 EBI-16046716 0.37 P06921 EBI-16046979 0.00 P06422 EBI-16048727 0.00 P36780 EBI-16050118 0.00 P06790 EBI-16051603 0.00 P06423 EBI-16052167 0.00 P03118 EBI-16053185 0.00 P36778 EBI-16054551 0.00 O15259 EBI-21257674 0.40 Q00610 EBI-21371914 0.00 Q9NQ75 EBI-21373824 0.00 O60346 EBI-21375347 0.00 Q9Y2D4 EBI-21375334 0.00 P43121 EBI-21380363 0.00 P26367 EBI-21381329 0.00 Q9UQM7 EBI-21389795 0.00 O75563 EBI-21391374 0.00 Q9BUZ4 EBI-21980067 0.35 O43294 EBI-21980067 0.53 P14598 EBI-21980104 0.40 P49023 EBI-25376663 0.53 P05067 EBI-25938518 0.56 Q9H3G5 EBI-28941112 0.35 Q9C0A1 EBI-28941112 0.35 P24752 EBI-28941112 0.35 GO:0097440 GO:0044297 GO:0005938 GO:0005737 GO:0005856 GO:0005829 GO:0030425 GO:0043197 GO:0031234 GO:0005925 GO:0098978 GO:0030426 GO:0030027 GO:0045121 GO:0043025 GO:0017146 GO:0005634 GO:0048471 GO:0014069 GO:0043423 GO:0005524 GO:0004683 GO:0004972 GO:0004715 GO:0008022 GO:0043621 GO:0004713 GO:0044877 GO:0005102 GO:0031625 GO:0090630 GO:0042976 GO:0002250 GO:0006915 GO:0043534 GO:0045453 GO:0030154 GO:0007166 GO:0006968 GO:0071498 GO:0071300 GO:0070098 GO:0086100 GO:0007173 GO:0048041 GO:0014009 GO:0045087 GO:0007229 GO:0035235 GO:0060292 GO:0060291 GO:0000165 GO:0002315 GO:0043066 GO:0030502 GO:0008285 GO:0010656 GO:0045638 GO:0043524 GO:0043267 GO:0031175 GO:0001556 GO:0038083 GO:0018108 GO:0030838 GO:0045766 GO:2000538 GO:0030307 GO:0030335 GO:0008284 GO:0001954 GO:0007204 GO:2000573 GO:0010595 GO:0070374 GO:2000463 GO:0046330 GO:0043507 GO:0010976 GO:0045429 GO:0051000 GO:0050731 GO:0043552 GO:0045860 GO:2000379 GO:0051968 GO:0045727 GO:2000060 GO:0046777 GO:0006468 GO:0065003 GO:2000249 GO:0050848 GO:0030155 GO:0008360 GO:0010752 GO:2000114 GO:0032960 GO:0010758 GO:2000310 GO:0051279 GO:0048167 GO:2000058 GO:0051592 GO:0051591 GO:0043157 GO:0042220 GO:0045471 GO:0009749 GO:0009725 GO:0042542 GO:0001666 GO:0035902 GO:0002931 GO:0010226 GO:0009612 GO:0009410 GO:0007172 GO:0007165 GO:0002040 GO:0043149 GO:0007169 GO:0033209 GO:0048010 Peripheral UniProt Sequence Analysis MSGVSEPLSRVKLGTLRRPEGPAEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIREIITSILLSGRIGPNIRLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDAKPTCLAEFKQIRSIRCLPLEEGQAVLQLGIEGAPQALSIKTSSLAEAENMADLIDGYCRLQGEHQGSLIIHPRKDGEKRNSLPQIPMLNLEARRSHLSESCSIESDIYAEIPDETLRRPGGPQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAMEQERNARYRTPKILEPTAFQEPPPKPSRPKYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIQPSSREEAQQLWEAEKVKMRQILDKQQKQMVEDYQWLRQEEKSLDPMVYMNDKSPLTPEKEVGYLEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYLNVMELVRAVLELKNELCQLPPEGYVVVVKNVGLTLRKLIGSVDDLLPSLPSSSRTEIEGTQKLLNKDLAELINKMRLAQQNAVTSLSEECKRQMLTASHTLAVDAKNLLDAVDQAKVLANLAHPPAE 1009 Q9QVP9 Protein-tyrosine Ptk2b 10090 None SL-0198 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}. UNIPROT Q9QVP9 UNIPROT B2RQ16 UNIPROT G3X8V1 Pfam PF00373 Pfam PF18038 Pfam PF03623 Pfam PF07714 PROSITE PS50057 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. P16054 EBI-298523 0.35 P35438 EBI-396959 0.46 Q9QWY8 EBI-8651469 0.65 P59240 EBI-11790541 0.40 Q9EPK7 EBI-17171503 0.35 Q8BIZ1 EBI-26595802 0.35 Q8VI24 EBI-26885104 0.35 GO:0097440 GO:0030424 GO:0044297 GO:0005938 GO:0042995 GO:0005856 GO:0030425 GO:0043197 GO:0031234 GO:0005925 GO:0098978 GO:0030426 GO:0030027 GO:0045121 GO:0043025 GO:0017146 GO:0005634 GO:0048471 GO:0098794 GO:0014069 GO:0043423 GO:0005524 GO:0004683 GO:0019899 GO:0004972 GO:0004715 GO:0008022 GO:0004672 GO:0043621 GO:0004713 GO:0044877 GO:0005102 GO:0031625 GO:0007015 GO:0090630 GO:0042976 GO:0002250 GO:0001525 GO:0043534 GO:0045453 GO:0007155 GO:0030154 GO:0007166 GO:0006968 GO:0071498 GO:0071300 GO:0070098 GO:0086100 GO:0007173 GO:0048041 GO:0014009 GO:0045087 GO:0007229 GO:0035235 GO:0060292 GO:0060291 GO:0000165 GO:0002315 GO:0043066 GO:0030502 GO:0008285 GO:0010656 GO:0045638 GO:0043524 GO:0030279 GO:0043267 GO:0031175 GO:0001556 GO:0038083 GO:0018108 GO:0030838 GO:0045766 GO:2000538 GO:0030307 GO:0030335 GO:0008284 GO:0001954 GO:0007204 GO:2000573 GO:0010595 GO:0070374 GO:2000463 GO:0046330 GO:0043507 GO:0010976 GO:0045429 GO:0051000 GO:0050731 GO:0043552 GO:0045860 GO:0051247 GO:2000379 GO:0051968 GO:0045727 GO:2000060 GO:0006468 GO:2000249 GO:0050848 GO:0030155 GO:0008360 GO:0010752 GO:2000114 GO:0032960 GO:0010758 GO:0045428 GO:2000310 GO:0051279 GO:2000058 GO:0051592 GO:0051591 GO:0043157 GO:0042220 GO:0045471 GO:0009749 GO:0009725 GO:0042542 GO:0001666 GO:0035902 GO:0002931 GO:0010226 GO:0009612 GO:0009410 GO:0007172 GO:0002040 GO:0043149 GO:0007169 GO:0033209 GO:0048010 Peripheral UniProt Sequence Analysis MSGVSEPLSRVKVGTLRRPEGPPEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIQEIITSILLSGRIGPNIQLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDTKPTCLAEFKQIKSIRCLPLEETQAVLQLGIEGAPQSLSIKTSSLAEAENMADLIDGYCRLQGEHKGSLIMHAKKDGEKRNSLPQIPTLNLEARRSHLSESCSIESDIYAEIPDETLRRPGGPQYGVAREEVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTQDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVPTLVLYTLQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPELCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDIYQMEKDIAIEQERNARYRPPKILEPTTFQEPPPKPSRPKYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIRPSSREEAQQLWEAEKIKMKQVLERQQKQMVEDSQWLRREERCLDPMVYMNDKSPLTPEKEAGYTEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYHNVMTLVEAVLELKNKLGQLPPEDYVVVVKNVGLNLRKLIGSVDDLLPSLPASSRTEIEGTQKLLNKDLAELINKMKLAQQNAVTSLSEDCKRQMLTASHTLAVDAKNLLDAVDQAKVVANLAHPPAE 1009 P70600 Protein-tyrosine Ptk2b 10116 None SL-0198 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. UNIPROT P70600 UNIPROT O88489 UNIPROT Q3T1H4 UNIPROT Q63201 Pfam PF00373 Pfam PF18038 Pfam PF03623 Pfam PF07714 PROSITE PS50057 PROSITE PS00107 PROSITE PS50011 PROSITE PS00109 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}. Q62848 EBI-8651337 0.40 Q9WUD9 EBI-16803792 0.40 GO:0097440 GO:0030424 GO:0044297 GO:0005938 GO:0042995 GO:0005856 GO:0030425 GO:0043197 GO:0031234 GO:0005925 GO:0098978 GO:0030426 GO:0030027 GO:0045121 GO:0043025 GO:0017146 GO:0005634 GO:0048471 GO:0098794 GO:0014069 GO:0043423 GO:0005524 GO:0004683 GO:0019899 GO:0004715 GO:0008022 GO:0004672 GO:0043621 GO:0004713 GO:0044877 GO:0005102 GO:0031625 GO:0007015 GO:0090630 GO:0042976 GO:0002250 GO:0001525 GO:0043534 GO:0045453 GO:0007155 GO:0030154 GO:0007166 GO:0006968 GO:0071498 GO:0071300 GO:0070098 GO:0086100 GO:0007173 GO:0048041 GO:0014009 GO:0045087 GO:0007229 GO:0035235 GO:0060292 GO:0060291 GO:0000165 GO:0002315 GO:0043066 GO:0030502 GO:0008285 GO:0010656 GO:0045638 GO:0043524 GO:0030279 GO:0043267 GO:0031175 GO:0001556 GO:0038083 GO:0018108 GO:0030838 GO:0045766 GO:2000538 GO:0030307 GO:0030335 GO:0008284 GO:0001954 GO:0007204 GO:2000573 GO:0010595 GO:0070374 GO:2000463 GO:0046330 GO:0043507 GO:0010976 GO:0045429 GO:0051000 GO:0050731 GO:0043552 GO:0045860 GO:0051247 GO:2000379 GO:0051968 GO:0045727 GO:2000060 GO:0006468 GO:2000249 GO:0050848 GO:0030155 GO:0008360 GO:0010752 GO:2000114 GO:0032960 GO:0010758 GO:0045428 GO:2000310 GO:0051279 GO:2000058 GO:0051592 GO:0051591 GO:0043157 GO:0042220 GO:0045471 GO:0009749 GO:0009725 GO:0042542 GO:0001666 GO:0035902 GO:0002931 GO:0010226 GO:0009612 GO:0010243 GO:0006970 GO:0000302 GO:0009410 GO:0007172 GO:0002040 GO:0043149 GO:0007169 GO:0033209 GO:0048010 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:9645946} MSGVSEPLSRVKVGTLRPPEGPPEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIQEIITSILLSGRIGPNIQLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDTKPTCLAEFKQIRSIRCLPLEETQAVLQLGIEGAPQSLSIKTSSLAEAENMADLIDGYCRLQGEHKGSLIIHAKKDGEKRNSLPQIPTLNLESRRSHLSESCSIESDIYAEIPDETLRRPGGPQYGVAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIVMELYPYGELGHYLERNKNSLKVPTLVLYALQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPELCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDIYQMERDIAIEQERNARYRPPKILEPTAFQEPPPKPSRPKYKHPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIRPSSREEAQQLWEAEKIKMRQVLDRQQKQMVEDSQWLRREERCLDPMVYMNDKSPLTPEKEAGYTEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYHNVMTLVEAVLELKNKLSQLPPEEYVVVVKNVGLNLRKLIGSVDDLLPSLPASSRTEIEGTQKLLNKDLAELINKMRLAQQNAVTSLSEDCKRQMLTASHTLAVDAKNLLDAVDQAKVVANLAHPPAE 1009 A2VE78 F-box/LRR-repeat FBXL5 9913 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT A2VE78 Pfam PF12937 Pfam PF01814 Pfam PF13516 PROSITE PS50181 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}. GO:0048471 GO:0019005 GO:0005506 GO:0055072 GO:0045732 GO:0016567 GO:0031146 Unknown UniProt Sequence Analysis MAPFPEEVDVFTAPHWRMKQLVGLYCDKLSKTNFSNNNDFRALLQSLYATFKEFKMHEQIENEYIIGLLQQRSQTIYNVHSDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTKDFLPHMKEEEEVFQPMLMEYFTYEELKDIKKKVIAQHCSQKDTAELLRGLSLWNQAEERQKFFKYSVDEKSDKEAEVSEQSTGITHLPPEVMVSIFSYLNPQELCRCSQVSTKWSQLAKTGSLWKHLYPVHWARGDWYSGPAAELDTEPDEEWVKSRRDESRAFQEWDEDADIDESEESGEESIAISIAQMEKRLLHGLIHNVLPYVGTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTDISDSAFDSWSWLGCCQSLRHLDLSGCEKITDVALEKISRALGILTTHESGLLKTSTSKVTSTTWKNKDITMQSFKQSACLHDVTNKDIGEEVDNEHPWTKPISSDDFTSPYVWMLDAEDLADIEDAVEWRHRNVESLCVMETASNFSCPSSACYSKDIVGLRTSVCWQQHCASPAFAYCGHSYCCTGTALRTMSALPESSALCRKAPRTRLLREKDLIYSGSEKSDQETGRVLLFLSLSGCYQITDHGLRVLTLGGGLPYLEHLNLSGCLTVTGAGLQDLVSACPSLNDEYFYYCDNINGPHADTASGCQNLQCGFRACCRSGE 691 Q2YDQ5 F-box/LRR-repeat fbxl5 7955 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q2YDQ5 Pfam PF12937 Pfam PF01814 Pfam PF13516 PROSITE PS50181 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}. GO:0048471 GO:0019005 GO:0005506 GO:0055072 GO:0016567 GO:0031146 Unknown UniProt Sequence Analysis MAPFPDEVDVFTGPHWRMKQLVGLYSEKLSNTNFSNNRDFRSFLQSLLDTFTEFKKHEQIENECIMELLQERSHTVYHVHADNKLSDMLTLFQKGLRSVTSEFEQLNYAQQLKERLEAFTQDFIPHMKEEEEVYQPMLMEYFSYEELKAIKQQVMLQHCSSQCQSSCSDTHTLLKGLSLWSHAELQKAFKYSDHEKTGDERVLERVSVSSLPQELLLRIFRFLGPQDLCRCAQVCSVWTQVTRTGSLWRHLYPVRWARGEYYSGPPGDLDLEPDDDWIKSLQDDGRAYQEWDEDADVDESEEASAERSSISALQREKLLLNGIIQKLLPAVGSSVRSLSLAYSSTLSSKMVRQMLSLCPNLTHLDLTQTDVSDSAFDSWCALGACGTLQHLDLSGCDKITDRTLKILSVGLGDSSTPSPAHKLLQAPPSPIRIEEPRLQPMGRSCQDLIFKRRPGGRGSGCGPTHIWVLDPVKLADIEDAADWSRRGGVASQEIGCGGISEALSASCCCRRSQRRGFRTGLSSSPWQYGDALCGHSSCCSSDAAAIRTQSDLQATGGSAELRTKCWFEGQSCAEHHNRTDQSGAQRALRFLSLSGCHQITDLGLRCVCLRGGLPLLEHLNLSGCPLITGAGLQEVVSASPALNIEHFYYCDNINGPHADTASGCQNLQCGFRVCCRSGE 679 Q9UKA1 F-box/LRR-repeat FBXL5 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:17532294}. UNIPROT Q9UKA1 UNIPROT A8MSK4 UNIPROT B4DIB5 UNIPROT Q4W5A8 UNIPROT Q8NHP3 UNIPROT Q9NXN2 UNIPROT Q9P0I0 UNIPROT Q9P0X5 UNIPROT Q9UJT7 UNIPROT Q9UKC8 PDB 3U9J PDB 3U9M PDB 3V5X PDB 3V5Y PDB 3V5Z PDB 6VCD Pfam PF12937 Pfam PF01814 Pfam PF13516 PROSITE PS50181 OMIM 605655 DisGeNET 26234 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}. P49454 EBI-21796233 0.35 Q7L5N1 EBI-21796233 0.35 Q92905 EBI-21325777 0.53 P10242 EBI-2692353 0.00 Q5NID2 EBI-2806872 0.00 P63208 EBI-8636412 0.83 Q09472 EBI-3937381 0.37 O43929 EBI-3938477 0.44 P67870 EBI-7133308 0.37 P53350 EBI-7312743 0.37 Q9Y4X5 EBI-21796233 0.35 Q9Y3D0 EBI-21796233 0.35 Q9UNS2 EBI-21796233 0.35 Q9H2Y7 EBI-21796233 0.35 Q9BQ90 EBI-21796233 0.35 Q96T76 EBI-21796233 0.35 Q96JN8 EBI-21796233 0.35 Q92624 EBI-21796233 0.35 Q8N5M4 EBI-21796233 0.35 Q562R1 EBI-21796233 0.35 Q3KQU3 EBI-21796233 0.35 Q13616 EBI-21796233 0.35 P61201 EBI-21796233 0.35 P60709 EBI-21796233 0.35 P28676 EBI-21796233 0.35 P26232 EBI-21796233 0.35 O95714 EBI-21796233 0.35 O76071 EBI-21796233 0.35 O75521 EBI-21796233 0.35 Q13148 EBI-25985913 0.56 GO:0005829 GO:0048471 GO:0019005 GO:0000151 GO:0005506 GO:0004842 GO:0055072 GO:0045732 GO:0016567 GO:0031146 Unknown UniProt Sequence Analysis MAPFPEEVDVFTAPHWRMKQLVGLYCDKLSKTNFSNNNDFRALLQSLYATFKEFKMHEQIENEYIIGLLQQRSQTIYNVHSDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTRDFLPHMKEEEEVFQPMLMEYFTYEELKDIKKKVIAQHCSQKDTAELLRGLSLWNHAEERQKFFKYSVDEKSDKEAEVSEHSTGITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWKHLYPVHWARGDWYSGPATELDTEPDDEWVKNRKDESRAFHEWDEDADIDESEESAEESIAISIAQMEKRLLHGLIHNVLPYVGTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTDISDSAFDSWSWLGCCQSLRHLDLSGCEKITDVALEKISRALGILTSHQSGFLKTSTSKITSTAWKNKDITMQSTKQYACLHDLTNKGIGEEIDNEHPWTKPVSSENFTSPYVWMLDAEDLADIEDTVEWRHRNVESLCVMETASNFSCSTSGCFSKDIVGLRTSVCWQQHCASPAFAYCGHSFCCTGTALRTMSSLPESSAMCRKAARTRLPRGKDLIYFGSEKSDQETGRVLLFLSLSGCYQITDHGLRVLTLGGGLPYLEHLNLSGCLTITGAGLQDLVSACPSLNDEYFYYCDNINGPHADTASGCQNLQCGFRACCRSGE 691 Q8C2S5 F-box/LRR-repeat Fbxl5 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q8C2S5 UNIPROT Q14CG1 UNIPROT Q3TAK6 UNIPROT Q3TWC9 UNIPROT Q3UC66 UNIPROT Q80XI5 UNIPROT Q8BGF5 UNIPROT Q8BNL3 UNIPROT Q8C3Q8 Pfam PF12937 Pfam PF01814 Pfam PF13516 PROSITE PS50181 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}. GO:0048471 GO:0019005 GO:0005506 GO:0055072 GO:0045732 GO:0030163 GO:0016567 GO:0031146 Unknown UniProt Sequence Analysis MAPFPDEVDVFTAPHWRMKQLVGRYCDKLSKTNFSNNNDFRALLQSLYATFKEFKMHEQIENEYIIGLLQQRSQTIYNVHSDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTRDFLPHMKEEEEVFQPMLMEYFTYEELKDIKKKVIAQHCSQKDTAELLRGLSLWNQAEERQKVLKYSVDEKADTEAEVSEHSTGITHLPPEVMLSIFSYLNPQELCRCSQVSTKWSQLAKTGSLWKHLYPVHWARGDWYSGPATELDTEPDEEWVRNRKDESRAFQEWDEDADIDESEESAEESVAISIAQMEKRVLHGLIHNVLPYVGTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTDISDSAFDSWSWLGCCQSLRHLDLSGCEKITDMALEKISRALGVLTSHQSGFLKSAGKAASTPWTSKDITMPSTTQYACLHNLTDKGIGEEIDNEHSWTEPVSSESLTSPYVWMLDAEDLADIEDAVEWRHRNVESLCVMETASNFGCSSSGCYSKDIVGLRTSVCWQQHCASPAFAYCGHSFCCTGTALRTMTTLPATSAMCRKALRTTLPRGKDLIYFGSEKSDQETGRVLLFLSLSGCYQITDHGLRALTLGGGLPYLEHLNLSGCLTVTGAGLQDLVSACPSLNDEYFYYCDNINGPHADTASGCQNLQCGFRACCRSGE 690 Q5R6E1 F-box/LRR-repeat FBXL5 9601 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5R6E1 Pfam PF12937 Pfam PF01814 Pfam PF13516 PROSITE PS50181 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}. GO:0048471 GO:0019005 GO:0005506 GO:0055072 GO:0016567 GO:0031146 Unknown UniProt Sequence Analysis MAPFPEEVDVFTAPHWRTKQLVGLYCDKLSKTNFSNNNDFRALLQSLYATFKEFKMHEQIENEYIIGLLQQRSQTIYNVHSDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTRDFLPHMKEEEEVFQPMLMEYFTYEELKDIKKKVIAQHCSQKDTAELLRGLSLWNHAEERQKFFKYSVDEKSDKEAEVSEHSTGITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWKHLYPVHWARGDWYSGPATGLDTEPDEEWVKNRKDESRAFHEWDEDADIDESEESVEESIAISIAQMEKRLLHGLIHNVLPYVGTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTDISDSAFDSWSWLGCCQSLRHLDLSGCEKITDVALEKISRALGILTSHQSGFLKTSTSKITSTTWKNKDVTMQSTKQYAYLHDLTNKGIGEEIDNEHPWTKPVSSENFTSPYLWMLDAEDLADIEDTVEWRHRNVESLCVVETASNFSCSTSGCFSKDIVGLRTSVCWQQHCASPAFAYCGHSFCCTGTALRTMSALPESSAMCRKASRTRLPRGKDLIYFGSEKSDQETGRVLLFLSLSGCYQITDHGLRVLTLGGGLPYLEHLNLSGCLTITGAGLQDLVSACPSLNDEYFYYCDNINGPHADTASGCQNLQCGFRACCRSGE 691 C0HAC0 F-box/LRR-repeat fbxl5 8030 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT C0HAC0 Pfam PF12937 Pfam PF01814 Pfam PF13516 PROSITE PS50181 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}. GO:0048471 GO:0019005 GO:0005506 GO:0055072 GO:0016567 GO:0031146 Unknown UniProt Sequence Analysis MAPFPDEVDVFTGPHWRMKQLVGLYCEKLSQTNFSNNNDFRSFLQSLCATFKEFKMHEQIENEYIIGLLQQRSCNVYNVHSDNKLSEMLSLFEKGLRSVKSENEQLNYAQQLKERLEAFTQDFLPHMKEEEEVFQPMLMQYFTYEELKDIKKQVIAQHSSQQRWDCAAEVLKGLSLWSQAEELHKAFKYADHEKTDDELEKELCSTHISQLPTEILLCLFRYLGPEDLCHCGQVCSAWSDLAKTGSLWRHLYPVRWARGDYYRGPPDDVNQEPDEEWVKSLQDEGKAYQEWDEDADVDESDASCEDSLAISAAQREKKLLNGMIQNLLPAVGSSVRSIVLAYSSTVSSKMVRQILSLCPNLTHLDLTQTDVTDSAFDSWSSLWACLSLEHLDLSGCEKLTDRTLKKLSLGLGDLASPTCSEKRSDRRAKLLKSPPSPISLLDKRSLRPTGHSRQVLIFKQWPGKLGSAPCSPTRVWVLDASELADIEDAAEWNRRRGVSTPEVRGFVETQPGGLSCCCRRRRGGFRTGFSTSYWQQQYGLGEAGCGHSTCCTGETALRTLGGLQYESYTTRGSAGAEFRTKCSSGGQLCLECDNRTDPSDGRRSLRFLSLSGCYQVTDLGLRALSQRGGLPLLEHLNLSGCLLITEVGLQELVSACPALNDEHFYYCDNINGPHADTASGCQNLQCGFRVCCRSGE 696 Q6INS1 F-box/LRR-repeat fbxl5 8355 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q6INS1 Pfam PF12937 Pfam PF01814 Pfam PF13516 PROSITE PS50181 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}. GO:0048471 GO:0019005 GO:0005506 GO:0055072 GO:0016567 GO:0031146 Unknown UniProt Sequence Analysis MAPFPDEVDLFTGPHWRMKQLVGRYCEKLSNTNFSNNNDLLALLQSLYETFKEFKMHEQIENEYIIGLLQQRSHTVYNVHSDNKLSEMLVLFEKGMKNVKNEYKQLNYVQQLKERLEAFTSDFLPHMKEEEEVFQPMLMEYFTYDEMKDIKKKVIAQHCSQKDTTELLRGLSLWNKAEELQKVLKYSVDEKAERNSKTQKSSSSISSLPPEVMLNIFTYLNPQDLCRCSQVNTEWAQLAKTGSLWRHLYPVLWARGDWYSGSHAYLDNEPDEDWISRRKDESRAYQEWDEDADIDESEETGEEEDSSISMAQREKELLNSLVHYILPYVGHSVKTLVLAYSSATSSKVIRQMLEYCPNLEHLDLTQTDISDSAFNGWHFGACQTLHHIDLSGCDKITDLTLEKLSVALGIPSAHKKRLLKCYRNNRTLKDIRNQMRCSSLAQITGESTIYSDAFWANSDRSQDYTSPPIWILDSGNPGDIEDAADWKFRTTDGLCVLEMAPSVTCFSNGCCSRARPGRWTNVGWQEHCKAATVSYCGHTLCGNTLRTIHTLPEASALCNIGTRTLHSDITDCFPGSAKSDQQAARALQFLSLSGCHQITDHGLRALTIGGGLPKLEHLNLSGCLNVTGSGLQDLVATCPSLNDEHFYYCDNISGPHGATASGCQNLQCGFRMCCRSGE 678 Q5XGI3 F-box/LRR-repeat fbxl5 8364 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5XGI3 Pfam PF12937 Pfam PF01814 Pfam PF13516 PROSITE PS50181 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}. GO:0048471 GO:0019005 GO:0005506 GO:0055072 GO:0016567 GO:0031146 Unknown UniProt Sequence Analysis MAPFPDEVDLFTGPHWRMKQLVGRYCEKLSNTNFSSNTDFLALLQSLYETFKEFKMHEQIENEYIIGLLQQRSQTVFNVHSDNKLSEMLVLFEKGMKNNEYEQLNYAQQLKERLEAFTSDFLPHMKEEEEVFQPMLMEYFTYDELKDIKKKVIAQHCSQKDTAELLRGFSLWNKAEELQKVFKYSVDEKIERDSKNRKSSASICNLPPEVMLNIFSYLNPQDLCRCSQVNTKWAQLARTGSLWRHLYPVLWARGDWYSGPPTHLDNEPDEDWISRRKDESRAYQEWDEDADIDESEETGEDDPSISVAQREKELLNSLVHYILPYIGHSVKTLVLAYSSATSNKVIRQILEYCPNMEHLDLTQTDISDSAFNGWCFGACQTLRHIDLSGCEKITDSALEKLSVALGMPLAHKKRLLKCYRNNRTVKDIRNQMRCGSLAQITGESGIYSDYSSSQIWILNSGNLGDIEDAADWKFRTTDGLGVLEMTPNLTCFSNGCCSRAVPGRWTNVIRQEHCKAAPLNYCGHTLCGNTLRTIQALPGSNIGTKTLQSEIRDICPGSAKLDQQVARVLQFLSLSGCHQITDHGLRVLTIGGGLPNLEHLNLSGCLNVTGSGLQDLVSACPSLNDEHFYYCDNISGPHAATASGCQNLQCGFRACCRSGE 660 Q8N3Y1 F-box/WD FBXW8 9606 None SL-0198 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}. UNIPROT Q8N3Y1 UNIPROT Q9UK95 Pfam PF12937 PROSITE PS50181 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 OMIM 609073 DisGeNET 26259 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}. O75147 EBI-15927108 0.35 P0C6X4 EBI-27128759 0.35 P0C6X5 EBI-27128956 0.35 P0C6X6 EBI-27128688 0.35 Q14999 EBI-15927108 0.35 P63208 EBI-914791 0.56 P01106 EBI-1228329 0.57 Q13616 EBI-21323857 0.46 Q13620 EBI-21332061 0.35 P04637 EBI-7902921 0.64 Q6P5F9 EBI-11603310 0.35 Q12798 EBI-21576600 0.35 Q99832 EBI-21594461 0.35 P49368 EBI-21594293 0.35 Q8NA56 EBI-21620988 0.35 O14958 EBI-21622768 0.35 O60293 EBI-21634559 0.35 Q9H9D4 EBI-21642543 0.35 D6R9G5 EBI-21662389 0.35 O14978 EBI-21712468 0.35 Q16539 EBI-21766048 0.35 Q96BR6 EBI-21784034 0.35 O14737 EBI-15927108 0.35 Q15645 EBI-15927108 0.35 P84077 EBI-15927108 0.35 Q9H0W5 EBI-15927108 0.35 P61758 EBI-15927108 0.35 P40227 EBI-15927108 0.35 P78371 EBI-15927108 0.35 Q99471 EBI-15927108 0.35 Q92526 EBI-15927108 0.35 Q13617 EBI-15927108 0.35 B1WBR1 EBI-15927171 0.40 P0DOF2 EBI-25603126 0.35 Q13619 EBI-30863570 0.35 Q8WV16 EBI-30863977 0.35 GO:0031467 GO:0005829 GO:0005794 GO:0048471 GO:0019005 GO:0008283 GO:0007030 GO:0060716 GO:0050775 GO:1901485 GO:0016567 GO:0060712 Unknown UniProt Sequence Analysis MDDYSLDEFRRRWQEELAQAQAPKKRRRPEAAERRARRPEVGSGRGEQASGDPALAQRLLEGAGRPPAARATRAEGQDVASRSRSPLAREGAGGGEQLVDQLIRDLNEMNDVPFFDIQLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLCQQEGHLPDSSISDYSCWKLIFQECRAKEHMLRTNWKNRKGAVSELEHVPDTVLCDVHSHDGVVIAGYTSGDVRVWDTRTWDYVAPFLESEDEEDEPGMQPNVSFVRINSSLAVAAYEDGFLNIWDLRTGKYPVHRFEHDARIQALALSQDDATVATASAFDVVMLSPNEEGYWQIAAEFEVPKLVQYLEIVPETRRYPVAVAAAGDLMYLLKAEDSARTLLYAHGPPVTCLDVSANQVAFGVQGLGWVYEGSKILVYSLEAGRRLLKLGNVLRDFTCVNLSDSPPNLMVSGNMDGRVRIHDLRSGNIALSLSAHQLRVSAVQMDDWKIVSGGEEGLVSVWDYRMNQKLWEVYSGHPVQHISFSSHSLITANVPYQTVMRNADLDSFTTHRRHRGLIRAYEFAVDQLAFQSPLPVCRSSCDAMATHYYDLALAFPYNHV 598 Q8BIA4 F-box/WD Fbxw8 10090 None SL-0198 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}. UNIPROT Q8BIA4 UNIPROT Q8BI62 UNIPROT Q8BI75 UNIPROT Q8BI76 UNIPROT Q8CID8 UNIPROT Q921Z1 Pfam PF12937 PROSITE PS50181 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. GO:1990393 GO:0031467 GO:0005829 GO:0005794 GO:0048471 GO:0019005 GO:0004842 GO:0008283 GO:0007030 GO:0060716 GO:0050775 GO:1901485 GO:0016567 GO:0060712 GO:0006511 Unknown UniProt Sequence Analysis MDDHNLEEFRRHWQEELAQSQALRRRRRLEAGERRSPRRPEAGARGEPASGYLGLAQGLLEGAGRPPAPRPGRGGDRKDTSSRSRSPPDRDATEPEPLVDQLIRDLNELDDVPFFDVRLPYELAINIFQYLNRRELGLCAQVSKTWKVIAEDEVLWYRLCRQEGHLPHSRFSDYTCWKLILQECLAKEHTLRANWKNRKGAVSELEHVPDAVLCDVRSHDGVVIAGYTSGDVRVWDTRTWDYVAPFLESESEEEDPGMQPYVSFVRINSSLAVAAYEDGILNIWDLRTGRFPIFRFEHDARIQALALSQEKPIVATASAFDVVMLYPNEEGHWHVASEFEVQKLVDYLEIVPNTGRYPVAIATAGDLVYLLKADDSARTLHYVYGQPATCLDVSASQVAFGVKSLGWVYEGNKILVYSLEAERCLSKLGNALGDFTCVNIRDSPPNLMVSGNMDRRVRIHDLRSDKIALSLSAHQLGVSAVQMDDWKVVSGGEEGLVSVWDYRMNQKLWEVHSRHPVRYLSFNSHSLITANVPYEKVLRNSDLDNFACHRRHRGLIHAYEFAVDQLAFQSPLPVCRLPRDIMAGYSYDLALSFPHDSI 598 P0DL28 F-box/WD Fbxw8 10116 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:21572988}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. UNIPROT P0DL28 Pfam PF12937 PROSITE PS50181 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. D3ZEF4 EBI-15927289 0.40 O35254 EBI-15927211 0.40 GO:1990393 GO:0031467 GO:0005829 GO:0005794 GO:0048471 GO:0019005 GO:0004842 GO:0008283 GO:0007030 GO:0060716 GO:0050775 GO:1901485 GO:0016567 GO:0060712 Unknown UniProt Sequence Analysis MEDHNLEEFRQRWQEELAHSQVLRRRRRLEAGERRPRRPEAGARGEPASGYLGLAQGLLEGAGRPPAPRPGRTDRKDVSSRSRSPPDRDAAEPEPLVDQLIRDLNEMDDVPFFDVHLPYELAINIFQYLNRRELGLCAQVSKTWKVIAEDEVLWYRLCRQEGHLPHSRFSDYTCWKLILQECLAPVHLIRPSWMNRKGAVSELEHVPDAVLCDVRSHDGVVIAGYTSGEVRVWDTRTWDYVAPFLESESEEEDPGMQPYVSFVRINSSLAVAAYEDGILNVWDLRTGRFPIFRFEHDARIQALALSQEKPVVATASAFDVVMLYPNEEGNWHVASEFEVQKLVDYLEIVPNTGRYPVAIATAGDLVYLLKAEDSARTLHYVYGQPATCLDVSASQVAFGVKSLGWVYEGNKILVYSLEAERCLSKLGNALGDFTCVNIRDSPPNLMVSGNMDRRVRLHDLRTDKIALSLSAHQLGVSAVQMDDWKIVSGGEEGLVSVWDYRMNQKLWEVHSRHPVRYISFNSHSLITANVPYEKVLRNSDLDNFACHRRHRGLIHAYEFAVDQLAFQSPLPICRLPRDTVAGYSYDLALSFPYDSI 596 A8X181 Protein fic 6238 None SL-0178 SL-0182 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}. UNIPROT A8X181 Pfam PF02661 PROSITE PS51459 PROSITE PS50005 PROSITE PS50293 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}. GO:0005789 GO:0016021 GO:0031965 GO:0005524 GO:0016787 GO:0070733 GO:0050829 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSVRRRTHSDDFSFRLERTRRPSKLDVLRESPTLPVQQGYSLTTVVLVSLVVTLVCQNVAPPAFSYLNQLIKNSPKRKIPGQSNRLNIGFISTNSPEKFAPAVQKPTFLVDPIYDEKWKGVHTAVPVMTTEPEEKRDNNHAKVKEAILAAKAASRSRRDGNLERAVTIMEHAMALAPNNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTNPLVSAIDRKMLKTVHDLRNEFAHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLSKEHHEISIDDILEMHRRVLGNADPVEAGKIRTTQVYVGKFTPVAPEYVLEQLADMVDWLNDESTMAMDPIERAAIAHYKLVLVHPFTDGNGRTARLLLNLIMMRSGFPPVILPVETRAEYYASLHVANLGDLRPFVRYVAKHSEASIQRYIGAMKTSSGNVINGEEPNLTAEESKVSEKIETECRAGS 507 Q23544 Protein fic 6239 None SL-0178 SL-0182 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}. UNIPROT Q23544 PDB 5JJ6 PDB 5JJ7 Pfam PF02661 PROSITE PS51459 PROSITE PS50005 PROSITE PS50293 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}. GO:0005737 GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0005524 GO:0016787 GO:0070733 GO:0050829 GO:0018117 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSVRRRTHSDDFSYLLEKTRRPSKLNVVQEDPKSAPPQGYSLTTVIIISVLVSLICQHFVPYAVSTLHTVIKNSPKQKSSPPPSNRLNIGFISGNSPEKYAPAVQKPTFLVDPIYDEKWKGIQTAVPVMSTQTDEKRENDPAKVKEAILAAKAAGRSRKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTTPLVSAIDRKMLRSVHDLRDEFNHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLSKEHDEISIDDILEMHRRVLGNADPVEAGRIRTTQVYVGRFTPVSPEYVMEQLKDIVDWLNDESTLTIDPIERAAIAHYKLVLVHPFTDGNGRTARLLLNLIMMRSGFPPVILPVETRAEYYASLHVANLGDLRPFVRYVAKHSEASIQRYIGAMKTSSDNILNSGDSKLTPEESEVSEKIEAECRAGN 508 Q6PIW4 Fidgetin-like FIGNL1 9606 None SL-0198 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). UNIPROT Q6PIW4 UNIPROT D3DVM6 UNIPROT Q86V18 UNIPROT Q8ND59 UNIPROT Q9H8P1 UNIPROT Q9H917 PDB 3D8B Pfam PF00004 Pfam PF09336 PROSITE PS00674 OMIM 615383 DisGeNET 63979 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}. Q06609 EBI-21840775 0.35 O60341 EBI-8468384 0.37 Q9WMX2 EBI-9079662 0.37 O14713 EBI-10181340 0.56 P05412 EBI-11324725 0.35 Q9QWF0 EBI-11015136 0.35 Q99576 EBI-11128906 0.35 Q9NSG2 EBI-11128906 0.35 Q05682 EBI-11128906 0.35 Q9H7E2 EBI-11128906 0.35 Q96EK4 EBI-11128906 0.35 Q96CN9 EBI-24633661 0.56 P29401 EBI-21539637 0.35 O75366 EBI-21577101 0.35 P00740 EBI-21577264 0.35 Q9BQ31 EBI-21590203 0.35 Q9BTE6 EBI-21593012 0.35 Q6IBW4 EBI-21600868 0.35 Q6UWQ5 EBI-21641185 0.35 Q86YD3 EBI-21644294 0.35 Q7Z4W2 EBI-21670934 0.35 O15496 EBI-21699277 0.35 Q6ZWK4 EBI-21782601 0.35 O14593 EBI-21807186 0.35 Q96JH7 EBI-21840775 0.35 P0CG38 EBI-21840775 0.35 P20160 EBI-21867396 0.35 B7ZBD5 EBI-21871699 0.35 O94808 EBI-21881570 0.35 P22105 EBI-21892376 0.40 Q9H910 EBI-21892399 0.35 P10412 EBI-20924530 0.40 Q9H1C4 EBI-21266770 0.35 P09613 EBI-21497303 0.35 P69479 EBI-25568051 0.35 O75874 EBI-27039729 0.37 GO:0005737 GO:0070062 GO:0000228 GO:0005634 GO:0048471 GO:0005524 GO:0016887 GO:0016787 GO:0000287 GO:0008568 GO:0046034 GO:0071479 GO:0007140 GO:0043066 GO:2001243 GO:0001649 GO:0033687 GO:0051726 GO:0010569 Unknown UniProt Sequence Analysis MQTSSSRSVHLSEWQKNYFAITSGICTGPKADAYRAQILRIQYAWANSEISQVCATKLFKKYAEKYSAIIDSDNVESGLNNYAENILTLAGSQQTDSDKWQSGLSINNVFKMSSVQKMMQAGKKFKDSLLEPALASVVIHKEATVFDLPKFSVCGSSQESDSLPNSAHDRDRTQDFPESNRLKLLQNAQPPMVTNTARTCPTFSAPVGESATAKFHVTPLFGNVKKENHSSAKENIGLNVFLSNQSCFPAACENPQRKSFYGSGTIDALSNPILNKACSKTEDNGPKEDSSLPTFKTAKEQLWVDQQKKYHQPQRASGSSYGGVKKSLGASRSRGILGKFVPPIPKQDGGEQNGGMQCKPYGAGPTEPAHPVDERLKNLEPKMIELIMNEIMDHGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVINLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREASLGPIRSLQTADIATITPDQVRPIAYIDFENAFRTVRPSVSPKDLELYENWNKTFGCGK 674 Q8BPY9 Fidgetin-like Fignl1 10090 None SL-0198 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}. UNIPROT Q8BPY9 UNIPROT Q3UF48 UNIPROT Q8C2I6 UNIPROT Q9ERZ5 Pfam PF00004 Pfam PF09336 PROSITE PS00674 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}. GO:0005737 GO:0000228 GO:0005634 GO:0048471 GO:0005524 GO:0016887 GO:0016787 GO:0000287 GO:0008568 GO:0046034 GO:0071479 GO:0007140 GO:0043066 GO:2001243 GO:0001649 GO:0033687 GO:0051726 GO:0010569 Unknown UniProt Sequence Analysis METSSSMSVETTRSVQVDEWQKNYCVVTSSICTPKQKADAYRALLLHIQYAYANSEISQVFATNLFKRYTEKYSAIIDSDNVVTGLNNYAESIFALAGSRQADSNKWQSGLSIDNVFKMSCVQEMMQAGKKFEESLLEPADASVVLCKEPTAFEVPQLSVCGGSEDADILSSSGHDTDKTQAIPGSSLRCSPFQSARLPKETNTTKTCLTSSTSLGESATAAFHMTPLFGNTEKDTQSFPKTSTGLNMFLSNLSCVPSGCENPQERKAFNDSDIIDILSNPTLNKAPSKTEDRGRREDNSLPTFKTAKEQLWVDQKKKGHQSQHTSKSSNGVMKKSLGAGRSRGIFGKFVPPVSNKQDGSEQHAKKHKSSRAGSAEPAHLTDDCLKNVEPRMVELIMNEIMDHGPPVHWDDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVGNLMSKEQCCLSDEETDLVVQQSDGFSGADMTQLCREASLGPIRSLHAADIATISPDQVRPIAYIDFENAFKTVRPTVSPKDLELYENWNETFGCGK 683 Q6GX84 Fidgetin-like Fignl1 10116 None SL-0198 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}. UNIPROT Q6GX84 Pfam PF00004 Pfam PF09336 PROSITE PS00674 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}. GO:0005737 GO:0000228 GO:0005634 GO:0048471 GO:0005524 GO:0016887 GO:0016787 GO:0000287 GO:0008568 GO:0046034 GO:0071479 GO:0007140 GO:0043066 GO:2001243 GO:0001649 GO:0033687 GO:0051726 GO:0010569 Unknown UniProt Sequence Analysis METSSSRSVQVDDWQKNYSVVASSICTPKQKADAYRALLLHIQDAYANSEISQVFATNLFKRYTEKYSAIIDSDNVVTGLNNYAESIFALAGSQQADSDKWQSGLSINNVFKMSTVQEMMQAGQKFKESLLEPADASVVMCKEPTIFEVPQLGVCGGSEEADLLSSSVHGTEKTQAIPGNSLRCSPFQSTLFPMATNTKTCLTSSAPSGESTTATFHRTPLFGNTKKEPQSFPKTSTGLNMFLSNPSCVPSGCENPRERKAFNDSDTINMLSNPTLNKAPSKTEDSGQREDNSLPTFKTAKEQLWADQKKRSHQSQHTSKSFNGAIKKSLGAGRSRGIFGKFVPPVSNKQDGSEQNGNVKPKSSRAGSAEPAHLTDDRLKNVEPRMVELIMNEIMDHGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVVNLMSKEQCCLTDEETELVVQQSDGFSGADMTQLCREASLGPIRSLHTADIATISPDQVRPIAYIDFENAFRTVRPSVSPKDLELYENWNKTFGCGK 677 Q6DDU8 Fidgetin-like fignl1 8355 None SL-0198 Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BPY9}. UNIPROT Q6DDU8 Pfam PF00004 Pfam PF09336 PROSITE PS00674 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}. GO:0000228 GO:0048471 GO:0005524 GO:0016887 GO:0016787 GO:0000287 GO:0046034 Unknown UniProt Sequence Analysis MQIPETSSVHQNEWQRDVFVLSSGTCLPQQKAEVYRAHLAQIQYAWANSEISEASAVHLFKKYAEKYSAILDSDKLEIGLNNYADSILTMAKCQRNESDKWQSSLTTNNVLKLKSVQEMAEAGRRAQLSLLNSTDASVRVGNEIGTSGYSTVLAHNVLRNPSHAVPHAASSDCQIPEGSSNFLQNSKVSAFTKANTSSNTLINNSIPINTSLMQRNEVKAPTTFSTQSGPNVFSSTTSVYSGKRKACYALGDESTDIQPKPLVQRQLASKEATGDSDFKTAKEQLWVDQQKKHSNQPQRNPGPLYGGGKKSLGAARSRGLHGKFIPPLPRQEDVEDSNRKVYGQGNSEMNSTSDEHLKNIEPKMIELIMSEIMDHGPPLNWDDIAGLEFAKTTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFTVARCHQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVVSLMSKEHCSLTEQEVEAIVLQADGFSGADMTQLCREAALGPIRSIQLMDISTITAEQVRPIAYIDFQSAFLVVRPSVSQKDLELYENWNKTFGCGR 655 A4IHT0 Fidgetin-like fignl1 8364 None SL-0198 Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BPY9}. UNIPROT A4IHT0 Pfam PF00004 Pfam PF17862 Pfam PF09336 PROSITE PS00674 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}. GO:0000228 GO:0048471 GO:0005524 GO:0016887 GO:0016787 GO:0000287 GO:0008568 GO:0030674 GO:0046034 Unknown UniProt Sequence Analysis MQVPESSLAHLSEWQRDAFVLSSGTCLPQQKAEVYRAHLAQIQYAWANSEISEASAVHLFKKYAEKYSAIIDSDKLEIGLNNYADSILTLAKCQRNESDKWQSSLTTNNVLKLKSVQDMAVAGRRTQLSKSSADASVRVGNGINTSGYSAGLGNNVLRNSGYTVPHAALSDCQMPGGSANFLQKPKISAFTIANTTSVANTSSNTLINNSISMTSSLMQSNEDKDPASFSGHMFLPTTSVHSGKRKAYSALGNESSDIKPNPLVQRQLTNKEATCESGFKTAKEQLWVDQQKKYSNQPQRNPSPLYGGAKKSLGAARSRGLHGKFVPPVPRQEDVQDSNRKVYGQGNSEMNAPSDERLKNIEPKMIELIMSEIMDHGPPLNWDDIAGLEFAKTTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFTVARCHQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSDDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVVSLMAKEHCSLAEQEVEAIVLQADGFSGADMTQLCREAALGPIRSIQLMDISTITPEQVRPIAYIDFQSAFLVVRPSVSQKDLELYENWNKTFGCGR 656 Q9LH52 Leucine-rich FLR1 3702 None SL-0198 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}. UNIPROT Q9LH52 UNIPROT Q93ZC1 UNIPROT Q9C7D9 UNIPROT Q9M7E7 Pfam PF00560 Pfam PF08263 Promotes flowering transition in long days (LD). {ECO:0000269|PubMed:22319055}. GO:0005737 GO:0005634 GO:0048471 GO:0005886 GO:0048574 GO:0048510 GO:0010228 Unknown UniProt Sequence Analysis MKLFVHLSIFFSILFITLPSSYSCTENDKNALLQIKKALGNPPLLSSWNPRTDCCTGWTGVECTNRRVTGLSVTSGEVSGQISYQIGDLVDLRTLDFSYLPHLTGNIPRTITKLKNLNTLYLKHTSLSGPIPDYISELKSLTFLDLSFNQFTGPIPGSLSQMPKLEAIQINDNKLTGSIPNSFGSFVGNVPNLYLSNNKLSGKIPESLSKYDFNAVDLSGNGFEGDAFMFFGRNKTTVRVDLSRNMFNFDLVKVKFARSIVSLDLSQNHIYGKIPPALTKLHLEHFNVSDNHLCGKIPSGGLLQTFEPSAFAHNICLCGTPLKAC 325 Q9NZU1 Leucine-rich FLRT1 9606 None SL-0198 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}. UNIPROT Q9NZU1 UNIPROT Q8WVA2 Pfam PF13855 Pfam PF01462 PROSITE PS50853 PROSITE PS51450 OMIM 604806 DisGeNET 23769 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}. Q70AK3 EBI-8042356 0.40 O43155 EBI-8042606 0.27 Q9UN70 EBI-21556493 0.35 Q9NZU0 EBI-21556493 0.35 Q9HAR2 EBI-21556493 0.35 Q9H2G9 EBI-21556493 0.35 Q96JH8 EBI-21556493 0.35 Q92569 EBI-21556493 0.35 P42338 EBI-21556493 0.35 P42336 EBI-21556493 0.35 P27986 EBI-21556493 0.35 O95490 EBI-21556493 0.35 O94910 EBI-21556493 0.35 O60245 EBI-21556493 0.35 O14917 EBI-21556493 0.35 O00459 EBI-21556493 0.35 A6NFQ2 EBI-21556493 0.35 Q9HC97 EBI-20807418 0.37 P05067 EBI-20768351 0.40 GO:0005911 GO:0031410 GO:0030659 GO:0005789 GO:0031012 GO:0005615 GO:0005925 GO:0005887 GO:0044306 GO:0032809 GO:0048471 GO:0005886 GO:0030674 GO:0007155 GO:0016358 GO:0008543 GO:1990138 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDLRDWLFLCYGLIAFLTEVIDSTTCPSVCRCDNGFIYCNDRGLTSIPADIPDDATTLYLQNNQINNAGIPQDLKTKVNVQVIYLYENDLDEFPINLPRSLRELHLQDNNVRTIARDSLARIPLLEKLHLDDNSVSTVSIEEDAFADSKQLKLLFLSRNHLSSIPSGLPHTLEELRLDDNRISTIPLHAFKGLNSLRRLVLDGNLLANQRIADDTFSRLQNLTELSLVRNSLAAPPLNLPSAHLQKLYLQDNAISHIPYNTLAKMRELERLDLSNNNLTTLPRGLFDDLGNLAQLLLRNNPWFCGCNLMWLRDWVKARAAVVNVRGLMCQGPEKVRGMAIKDITSEMDECFETGPQGGVANAAAKTTASNHASATTPQGSLFTLKAKRPGLRLPDSNIDYPMATGDGAKTLAIHVKALTADSIRITWKATLPASSFRLSWLRLGHSPAVGSITETLVQGDKTEYLLTALEPKSTYIICMVTMETSNAYVADETPVCAKAETADSYGPTTTLNQEQNAGPMASLPLAGIIGGAVALVFLFLVLGAICWYVHQAGELLTRERAYNRGSRKKDDYMESGTKKDNSILEIRGPGLQMLPINPYRAKEEYVVHTIFPSNGSSLCKATHTIGYGTTRGYRDGGIPDIDYSYT 646 Q6RKD8 Leucine-rich Flrt1 10090 None SL-0198 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}. UNIPROT Q6RKD8 UNIPROT Q14DT7 UNIPROT Q6RKD9 Pfam PF13855 Pfam PF01462 PROSITE PS50853 PROSITE PS51450 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}. GO:0005911 GO:0031410 GO:0030659 GO:0005789 GO:0005615 GO:0005925 GO:0005887 GO:0044306 GO:0032809 GO:0048471 GO:0005104 GO:0007155 GO:0016358 GO:0008543 GO:1990138 GO:0051965 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDLRDWLFLCYGLIAFLTEVIDSTTCPSVCRCDNGFIYCNDRGLTSIPSDIPDDATTLYLQNNQINNAGIPQDLKTKVKVQVIYLYENDLDEFPINLPRSLRELHLQDNNVRTIARDSLARIPLLEKLHLDDNSVSTVSIEEDAFADSKQLKLLFLSRNHLSSIPSGLPHTLEELRLDDNRISTIPLHAFKGLNSLRRLVLDGNLLANQRIADDTFSRLQNLTELSLVRNSLAAPPLNLPSAHLQKLYLQDNAISHIPYNTLAKMRELERLDLSNNNLTTLPRGLFDDLGNLAQLLLRNNPWFCGCNLMWLRDWVRARAAVVNVRGLMCQGPEKVRGMAIKDITSEMDECFEAGSQGGAANAAAKTTVSNHASATTPQGSLFTLKAKRPGLRLPDSNIDYPMATGDGAKTLVIQVKPLTADSIRITWKAMLPASSFRLSWLRLGHSPAVGSITETLVQGDKTEYLLTALEPKSTYIICMVTMETGNTYVADETPVCAKAETADSYGPTTTLNQEQNAGPMAGLPLAGIIGGAVALVFLFLVLGAICWYVHRAGELLTRERVYNRGSRRKDDYMESGTKKDNSILEIRGPGLQMLPINPYRSKEEYVVHTIFPSNGSSLCKGAHTIGYGTTRGYREAGIPDVDYSYT 646 Q9NZ56 Formin-2 FMN2 9606 None SL-0198 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}. UNIPROT Q9NZ56 UNIPROT B0QZA7 UNIPROT B4DP05 UNIPROT Q59GF6 UNIPROT Q5VU37 UNIPROT Q9NZ55 PDB 2YLE PDB 3R7G Pfam PF02181 PROSITE PS51444 OMIM 606373 OMIM 616193 DisGeNET 56776 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}. 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. P43353 EBI-21500028 0.35 Q8WUD1 EBI-21500361 0.35 Q7KYR7 EBI-21541130 0.35 Q9Y664 EBI-21597637 0.35 Q8NB37 EBI-21611026 0.35 Q9BVQ7 EBI-21645803 0.35 Q92870 EBI-21653121 0.35 P37173 EBI-21668347 0.35 Q12974 EBI-21791071 0.35 Q96IK1 EBI-21835435 0.35 P29466 EBI-21873638 0.35 P55145 EBI-20907608 0.40 O15194 EBI-27115784 0.27 P07947 EBI-30849899 0.44 GO:0005938 GO:0005737 GO:0030659 GO:0005829 GO:0005783 GO:0005789 GO:0005902 GO:0005730 GO:0005634 GO:0048471 GO:0005886 GO:0005819 GO:0003779 GO:0006974 GO:0071456 GO:0051295 GO:0070649 GO:0051758 GO:0035556 GO:0046907 GO:0043066 GO:0042177 GO:0048477 GO:0040038 GO:2000781 GO:0015031 GO:0016192 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q9JL04} MGNQDGKLKRSAGDALHEGGGGAEDALGPRDVEATKKGSGGKKALGKHGKGGGGGGGGGESGKKKSKSDSRASVFSNLRIRKNLSKGKGAGGSREDVLDSQALQTGELDSAHSLLTKTPDLSLSADEAGLSDTECADPFEVTGPGGPGPAEARVGGRPIAEDVETAAGAQDGQRTSSGSDTDIYSFHSATEQEDLLSDIQQAIRLQQQQQQQLQLQLQQQQQQQQLQGAEEPAAPPTAVSPQPGAFLGLDRFLLGPSGGAGEAPGSPDTEQALSALSDLPESLAAEPREPQQPPSPGGLPVSEAPSLPAAQPAAKDSPSSTAFPFPEAGPGEEAAGAPVRGAGDTDEEGEEDAFEDAPRGSPGEEWAPEVGEDAPQRLGEEPEEEAQGPDAPAAASLPGSPAPSQRCFKPYPLITPCYIKTTTRQLSSPNHSPSQSPNQSPRIKRRPEPSLSRGSRTALASVAAPAKKHRADGGLAAGLSRSADWTEELGARTPRVGGSAHLLERGVASDSGGGVSPALAAKASGAPAAADGFQNVFTGRTLLEKLFSQQENGPPEEAEKFCSRIIAMGLLLPFSDCFREPCNQNAQTNAASFDQDQLYTWAAVSQPTHSLDYSEGQFPRRVPSMGPPSKPPDEEHRLEDAETESQSAVSETPQKRSDAVQKEVVDMKSEGQATVIQQLEQTIEDLRTKIAELERQYPALDTEVASGHQGLENGVTASGDVCLEALRLEEKEVRHHRILEAKSIQTSPTEEGGVLTLPPVDGLPGRPPCPPGAESGPQTKFCSEISLIVSPRRISVQLDSHQPTQSISQPPPPPSLLWSAGQGQPGSQPPHSISTEFQTSHEHSVSSAFKNSCNIPSPPPLPCTESSSSMPGLGMVPPPPPPLPGMTVPTLPSTAIPQPPPLQGTEMLPPPPPPLPGAGIPPPPPLPGAGILPLPPLPGAGIPPPPPLPGAAIPPPPPLPGAGIPLPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGVGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPRVGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGAGIPPPPPLPGMGIPPAPAPPLPPPGTGIPPPPLLPVSGPPLLPQVGSSTLPTPQVCGFLPPPLPSGLFGLGMNQDKGSRKQPIEPCRPMKPLYWTRIQLHSKRDSSTSLIWEKIEEPSIDCHEFEELFSKTAVKERKKPISDTISKTKAKQVVKLLSNKRSQAVGILMSSLHLDMKDIQHAVVNLDNSVVDLETLQALYENRAQSDELEKIEKHGRSSKDKENAKSLDKPEQFLYELSLIPNFSERVFCILFQSTFSESICSIRRKLELLQKLCETLKNGPGVMQVLGLVLAFGNYMNGGNKTRGQADGFGLDILPKLKDVKSSDNSRSLLSYIVSYYLRNFDEDAGKEQCLFPLPEPQDLFQASQMKFEDFQKDLRKLKKDLKACEVEAGKVYQVSSKEHMQPFKENMEQFIIQAKIDQEAEENSLTETHKCFLETTAYFFMKPKLGEKEVSPNAFFSIWHEFSSDFKDFWKKENKLLLQERVKEAEEVCRQKKGKSLYKIKPRHDSGIKAKISMKT 1722 Q9JL04 Formin-2 Fmn2 10090 None SL-0198 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}. UNIPROT Q9JL04 UNIPROT Q505D3 Pfam PF02181 PROSITE PS51444 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}. P68135 EBI-16095077 0.44 Q6NZM9 EBI-26473528 0.35 GO:0015629 GO:0005884 GO:0005938 GO:0005737 GO:0030659 GO:0005829 GO:0005783 GO:0005789 GO:0005902 GO:0005730 GO:0005634 GO:0048471 GO:0005886 GO:0005819 GO:0003779 GO:0008017 GO:0051017 GO:0045010 GO:0006974 GO:0071456 GO:0051295 GO:0070649 GO:0051758 GO:0046907 GO:0016344 GO:0043066 GO:0042177 GO:0048477 GO:0040038 GO:2000781 GO:0015031 GO:0016192 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:21983562} MGNQDGKLKRSAGDASHEGGGAEDAAGPRDAEITKKASGSKKALGKHGKGGGGSGETSKKKSKSDSRASVFSNLRIRKNLTKGKGACDSREDVLDSQALPIGELDSAHSIVTKTPDLSLSAEETGLSDTECADPFEVIHPGASRPAEAGVGIQATAEDLETAAGAQDGQRTSSGSDTDIYSFHSATEQEDLLSDIQQAIRLQQQQQQKLLLQDSEEPAAPPTAISPQPGAFLGLDQFLLGPRSEAEKDTVQALPVRPDLPETTKSLVPEHPPSSGSHLTSETPGYATAPSAVTDSLSSPAFTFPEAGPGEGAAGVPVAGTGDTDEECEEDAFEDAPRGSPGEEWVPEVEEASQRLEKEPEEGMRESITSAVVSLPGSPAPSPRCFKPYPLITPCYIKTTTRQLSSPNHSPSQSPNQSPRIKKRPDPSVSRSSRTALASAAAPAKKHRLEGGLTGGLSRSADWTEELGVRTPGAGGSVHLLGRGATADDSGGGSPVLAAKAPGAPATADGFQNVFTGRTLLEKLFSQQENGPPEEAEKFCSRIIAMGLLLPFSDCFREPCNQNAGSSSAPFDQDQLYTWAAVSQPTHSMDYSEGQFPRREPSMWPSSKLPEEEPSPKDVDTEPKSSILESPKKCSNGVQQEVFDVKSEGQATVIQQLEQTIEDLRTKIAELEKQYPALDLEGPRGLSGLENGLTASADVSLDALVLHGKVAQPPRTLEAKSIQTSPTEEGRILTLPPPKAPPEGLLGSPAAASGESALLTSPSGPQTKFCSEISLIVSPRRISVQLDAQQIQSASQLPPPPPLLGSDSQGQPSQPSLHTESETSHEHSVSSSFGNNCNVPPAPPLPCTESSSFMPGLGMAIPPPPCLSDITVPALPSPTAPALQFSNLQGPEMLPAPPQPPPLPGLGVPPPPPAPPLPGMGIPPPPPLPGMGIPPPPPLPGMGISPLPPLPGMGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGSGIPPPPALPGVAIPPPPPLPGMGVPPPAPPPPGAGIPPPPLLPGSGPPHSSQVGSSTLPAAPQGCGFLFPPLPTGLFGLGMNQDRVARKQLIEPCRPMKPLYWTRIQLHSKRDSSPSLIWEKIEEPSIDCHEFEELFSKTAVKERKKPISDTISKTKAKQVVKLLSNKRSQAVGILMSSLHLDMKDIQHAVVNLDNSVVDLETLQALYENRAQSDELEKIEKHSRSSKDKENAKSLDKPEQFLYELSLIPNFSERVFCILFQSTFSESICSIRRKLELLQKLCETLKNGPGVMQVLGLVLAFGNYMNAGNKTRGQADGFGLDILPKLKDVKSSDNSRSLLSYIVSYYLRNFDEDAGKEQCVFPLAEPQELFQASQMKFEDFQKDLRKLKKDLKACEAEAGKVYQVSSAEHMQPFKENMEQFISQAKIDQESQEAALTETHKCFLETTAYYFMKPKLGEKEVSPNVFFSVWHEFSSDFKDAWKKENKLILQERVKEAEEVCRQKKGKSLYKVKPRHDSGIKAKISMKT 1578 P51113 Fragile fmr1 8355 None SL-0198 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}. UNIPROT P51113 Pfam PF05641 Pfam PF16098 Pfam PF12235 Pfam PF00013 Pfam PF17904 Pfam PF18336 PROSITE PS51641 PROSITE PS50084 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}. GO:0070161 GO:0030424 GO:0043679 GO:0042995 GO:0010369 GO:0005694 GO:0000775 GO:0005737 GO:0036464 GO:0010494 GO:0030425 GO:1902737 GO:0043197 GO:0019897 GO:0032433 GO:0097386 GO:0030426 GO:1990812 GO:0043005 GO:0071598 GO:0005730 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005844 GO:0098794 GO:0014069 GO:0045211 GO:0098793 GO:0042734 GO:1990904 GO:0045202 GO:0003682 GO:0070840 GO:0002151 GO:0035064 GO:0008017 GO:0035198 GO:0003730 GO:0048027 GO:0003729 GO:0034046 GO:0008266 GO:0046982 GO:0042803 GO:0003723 GO:0035613 GO:0033592 GO:1990825 GO:0035197 GO:0030371 GO:0006281 GO:0007215 GO:0006397 GO:0051028 GO:2000766 GO:0010629 GO:1900453 GO:2000301 GO:0017148 GO:0045947 GO:1901386 GO:0007399 GO:0060999 GO:0051491 GO:2000637 GO:1902416 GO:1901800 GO:0002092 GO:0045727 GO:0000381 GO:0060998 GO:0051489 GO:0060964 GO:0043488 GO:0098908 GO:0046928 GO:0008380 GO:0060538 Unknown UniProt Sequence Analysis MEELAVEVRGSNGAFYKAFMKDVHEDSITVTFENNWQQERQIPFHDVRFPPPSGYNKDINERDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKSSFHKVKLDVPEDLRQMCAKDSAHKDFKKAVGAFSVSYDSENYQLVILSVNEVSIKRASMLSDMHFRSLRTKLSLMLRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQEAVKKARTYLEFAENVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENDKNISQEEGIVPFVFVGTKDSITNATVLLDYHLNYLKEVDQLRLERLQIDEQLRHIGASSRPPPNRPDKEKGYLSEDCSGTVRGSRPYSNRGRSRRGTGYASGTNSEASNASETESDHRDELSDWSLAPAEDDRDNYHRRGDGRRRGGTRGQGMRGRGGFKGNDDQPRPDNRQRNSRETKARTSDGSLQIRLDCNNERSVHTKTLQNASVDGSRLRTGKDRVQKKEKTDGVDGPQVVVNGVP 564 Q2KHP9 Fragile fmr1 8355 None SL-0198 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}. UNIPROT Q2KHP9 Pfam PF05641 Pfam PF16098 Pfam PF12235 Pfam PF00013 Pfam PF17904 Pfam PF18336 PROSITE PS51641 PROSITE PS50084 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}. GO:0070161 GO:0030424 GO:0043679 GO:0042995 GO:0010369 GO:0005694 GO:0000775 GO:0005737 GO:0036464 GO:0010494 GO:0030425 GO:1902737 GO:0043197 GO:0019897 GO:0032433 GO:0097386 GO:0030426 GO:1990812 GO:0043005 GO:0071598 GO:0005730 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005844 GO:0098794 GO:0014069 GO:0045211 GO:0098793 GO:0042734 GO:1990904 GO:0045202 GO:0003682 GO:0070840 GO:0002151 GO:0035064 GO:0008017 GO:0035198 GO:0003730 GO:0048027 GO:0003729 GO:0034046 GO:0008266 GO:0046982 GO:0042803 GO:0003723 GO:0035613 GO:0033592 GO:1990825 GO:0035197 GO:0030371 GO:0006281 GO:0007215 GO:0006397 GO:0051028 GO:2000766 GO:0010629 GO:1900453 GO:2000301 GO:0017148 GO:0045947 GO:1901386 GO:0007399 GO:0060999 GO:0051491 GO:2000637 GO:1902416 GO:1901800 GO:0002092 GO:0045727 GO:0000381 GO:0060998 GO:0051489 GO:0060964 GO:0043488 GO:0098908 GO:0046928 GO:0008380 GO:0060538 Unknown UniProt Sequence Analysis MEELAVEVRGSNGAFYKAFVKDVHEDSITVTFENNWQQEKQIPFHDVRFPPPSGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIDRLRSVNPNKSATKNSFHKVKLDVPEDLRQMCAKDSAHKDFKKAVGAFSVSYDSENYQLVILSVNEVTIKRANMLCDMHFRSLRTKLSLMLRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQEAVKKARTYLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENDKNISQEEGNVPFVFVGTKDSITNATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPSNRPDKEKGYLSEDCSGTVRGSRPYNNRGRSRRGTGYASGTNSEASNASETESDHRDELSDWSLAPAEDDRDNYHRRGDGRRRGGMRGQGMRGRGGFKGNDDQPRPDNRQRNSRETKARTSDGSLQIRIDCNNERSVHTKTLQNASVEGSRLRTGKDRIQKKEKTDGVDGPQVVVNGVP 564 Q06787 Fragile FMR1 9606 None SL-0198 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}. UNIPROT Q06787 UNIPROT A6NNH4 UNIPROT D3DWT0 UNIPROT D3DWT1 UNIPROT D3DWT2 UNIPROT G8JL90 UNIPROT Q16578 UNIPROT Q5PQZ6 UNIPROT Q99054 PDB 2BKD PDB 2FMR PDB 2LA5 PDB 2QND PDB 4OVA PDB 4QVZ PDB 4QW2 PDB 5DE5 PDB 5DE8 PDB 5DEA PDB 5UWJ PDB 5UWO Pfam PF05641 Pfam PF16098 Pfam PF12235 Pfam PF00013 Pfam PF17904 Pfam PF18336 PROSITE PS51641 PROSITE PS50084 OMIM 300623 OMIM 300624 OMIM 309550 OMIM 311360 OMIM 616034 DisGeNET 2332 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}. 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. A1L4K1 EBI-10224474 0.56 P0DTD1 EBI-25509375 0.35 P10909 EBI-21371844 0.00 P21980 EBI-25856705 0.56 P63165 EBI-21388180 0.00 P63279 EBI-11105225 0.35 O95793 EBI-366371 0.43 Q9UL18 EBI-7641969 0.35 P63073 EBI-2000674 0.35 A0A5P8YGX7 EBI-2869681 0.00 P03372 EBI-2878124 0.35 Q92731 EBI-2880211 0.46 Q13131 EBI-3213822 0.35 Q7TMB8 EBI-3649150 0.37 Q7L576 EBI-3649503 0.49 Q96F07 EBI-3649591 0.53 Q06787 EBI-8619896 0.69 Q5JVS0 EBI-7032254 0.40 Q6QDQ4 EBI-5276631 0.35 P48059 EBI-5660443 0.00 Q13137 EBI-6115370 0.55 A7MCY6 EBI-6116450 0.35 Q9UHD2 EBI-6116602 0.35 Q9JHG6 EBI-8013831 0.40 Q86VP6 EBI-21322532 0.35 Q13617 EBI-21327106 0.35 Q13618 EBI-21329068 0.35 P61326 EBI-6551517 0.35 P38919 EBI-6551387 0.35 Q8NC51 EBI-8844408 0.35 Q9NWT6 EBI-12502476 0.35 P51116 EBI-25478814 0.66 P05412 EBI-11324725 0.35 Q9JLI8 EBI-11023430 0.35 Q96FV9 EBI-11034504 0.35 P27635 EBI-11035646 0.35 D6RFU6 EBI-11044384 0.35 P54227 EBI-11048628 0.35 Q91YN9 EBI-11052510 0.35 Q9NYF8 EBI-11086629 0.35 Q61768 EBI-11094840 0.35 Q8R5C0 EBI-11096914 0.35 A0AVT1 EBI-11105405 0.35 Q08AG7 EBI-11108327 0.35 Q8BH65 EBI-11109889 0.35 P37840 EBI-11113842 0.35 P04062 EBI-11114072 0.35 P83887 EBI-11115300 0.35 Q9Y2D8 EBI-11379249 0.27 Q9UJV9 EBI-11473486 0.35 Q6IQ23 EBI-16398399 0.35 Q9JIN6 EBI-15097151 0.35 Q08460 EBI-15097151 0.35 Q6ICG8 EBI-21880135 0.35 Q9BQE9 EBI-21882089 0.35 Q8IY47 EBI-21882089 0.35 Q08380 EBI-21882089 0.35 Q7Z417 EBI-15562677 0.44 Q6ZNJ1 EBI-16749633 0.35 P09622 EBI-20304669 0.35 P36957 EBI-20305285 0.35 P08559 EBI-20306509 0.35 P46013 EBI-20562326 0.35 Q12824 EBI-20624550 0.27 Q9UPY3 EBI-20621391 0.35 Q3KP66 EBI-20715953 0.35 P10636 EBI-20799058 0.35 Q13428 EBI-20929176 0.40 A2A935 EBI-21022882 0.35 Q5S007 EBI-21360986 0.35 P35637 EBI-21221307 0.35 Q96S59 EBI-21369245 0.00 O95267 EBI-21369403 0.00 Q9NP66 EBI-21369822 0.00 Q7L5Y9 EBI-21369724 0.00 O60884 EBI-21369710 0.00 Q9Y6X2 EBI-21369904 0.00 Q9BSL1 EBI-21369945 0.00 P40123 EBI-21370139 0.00 Q99784 EBI-21369996 0.00 Q9UQB8 EBI-21370061 0.00 Q14919 EBI-21370370 0.00 O00471 EBI-21370498 0.00 Q14314 EBI-21370849 0.00 Q9UBU8 EBI-21370917 0.00 Q8N5Y2 EBI-21370931 0.00 Q13438 EBI-21370945 0.00 O14647 EBI-21371152 0.00 P61964 EBI-21371193 0.00 Q9UKN5 EBI-21371207 0.00 Q9UNN5 EBI-21371221 0.00 Q9Y496 EBI-21371235 0.00 Q96RF0 EBI-21371415 0.00 Q9C026 EBI-21371538 0.00 Q96CW1 EBI-21371769 0.00 Q96N64 EBI-21371660 0.00 Q96PV6 EBI-21371646 0.00 Q96PY5 EBI-21371620 0.00 Q00610 EBI-21371927 0.00 Q8N1A0 EBI-21371994 0.00 Q12860 EBI-21372035 0.00 Q14194 EBI-21372447 0.00 Q96L42 EBI-21372275 0.00 Q8N3I7 EBI-21372220 0.00 P29400 EBI-21372182 0.00 Q8WXF8 EBI-21372962 0.00 Q8TF20 EBI-21373160 0.00 Q6PEW1 EBI-21373134 0.00 Q1L5Z9 EBI-21373054 0.00 Q12882 EBI-21373320 0.00 Q14204 EBI-21373282 0.00 P29692 EBI-21373439 0.00 O43491 EBI-21373658 0.00 Q9H4G0 EBI-21373644 0.00 O60293 EBI-21373492 0.00 P33121 EBI-21373794 0.00 P42566 EBI-21373716 0.00 Q9Y483 EBI-21373970 0.00 Q70YC4 EBI-21374286 0.00 Q9UPW8 EBI-21374527 0.00 Q9UPY8 EBI-21374400 0.00 Q96RU3 EBI-21374719 0.00 Q9UBB6 EBI-21375011 0.00 P21333 EBI-21375025 0.00 Q9Y2J2 EBI-21374970 0.00 O60333 EBI-21374889 0.00 Q9BT88 EBI-21375171 0.00 Q9Y5W8 EBI-21375052 0.00 O95490 EBI-21375435 0.00 Q9UJ04 EBI-21375449 0.00 Q9C040 EBI-21375699 0.00 O94874 EBI-21376033 0.00 Q7Z460 EBI-21375713 0.00 Q96JC1 EBI-21375752 0.00 O75044 EBI-21376062 0.00 Q8N488 EBI-21376128 0.00 O75533 EBI-21376142 0.00 Q9UPN3 EBI-21376184 0.00 Q9ULA0 EBI-21376333 0.00 Q6PID6 EBI-21376319 0.00 Q8NAP3 EBI-21376630 0.00 Q8TF01 EBI-21376898 0.00 Q96DZ5 EBI-21376912 0.00 O43166 EBI-21377092 0.00 Q9Y4E5 EBI-21377023 0.00 Q9NUQ6 EBI-21376926 0.00 Q9ULX6 EBI-21377424 0.00 Q96NJ3 EBI-21377397 0.00 Q06210 EBI-21377371 0.00 Q9UHB7 EBI-21377556 0.00 Q9ULD5 EBI-21377623 0.00 Q9UMS4 EBI-21377802 0.00 P38159 EBI-21377775 0.00 Q86WH2 EBI-21378180 0.00 Q9HBT6 EBI-21378166 0.00 Q5JPE7 EBI-21378278 0.00 Q8N660 EBI-21378426 0.00 Q6NZI2 EBI-21378344 0.00 P07305 EBI-21378914 0.00 Q9BWC9 EBI-21378823 0.00 Q00341 EBI-21378943 0.00 P61978 EBI-21379125 0.00 P11021 EBI-21379273 0.00 Q5HYM0 EBI-21379476 0.00 P78318 EBI-21379562 0.00 Q13123 EBI-21379655 0.00 O14782 EBI-21379843 0.00 A6QL64 EBI-21379817 0.00 O60282 EBI-21379969 0.00 P33176 EBI-21379927 0.00 Q12840 EBI-21379882 0.00 A8MQT2 EBI-21380484 0.00 Q15784 EBI-21380833 0.00 Q14494 EBI-21380847 0.00 Q9UQ80 EBI-21381113 0.00 P67809 EBI-21380954 0.00 Q16656 EBI-21380927 0.00 Q6P4R8 EBI-21380889 0.00 P05165 EBI-21381471 0.00 Q15154 EBI-21381512 0.00 Q9UJX3 EBI-21381861 0.00 O95071 EBI-21381759 0.00 Q9UBS4 EBI-21382031 0.00 Q7LFL8 EBI-21381914 0.00 Q99719 EBI-21382462 0.00 Q9NZR2 EBI-21382344 0.00 Q9H0C5 EBI-21382290 0.00 Q00169 EBI-21382196 0.00 O43236 EBI-21382476 0.00 P46100 EBI-21382624 0.00 Q5T0N5 EBI-21382791 0.00 Q6ZN54 EBI-21382753 0.00 Q8WUP2 EBI-21382702 0.00 Q8NDB2 EBI-21382915 0.00 Q8TEP8 EBI-21383160 0.00 Q8TC92 EBI-21382981 0.00 Q8NEU8 EBI-21383268 0.00 Q15172 EBI-21383310 0.00 Q9P0M6 EBI-21383440 0.00 Q6VMQ6 EBI-21383754 0.00 Q3V6T2 EBI-21383663 0.00 Q96IV0 EBI-21383887 0.00 P10644 EBI-21383768 0.00 P05771 EBI-21383926 0.00 Q9Y5G2 EBI-21384294 0.00 Q9UHQ4 EBI-21384245 0.00 Q8NFW8 EBI-21384164 0.00 Q9NQZ6 EBI-21384137 0.00 Q5T6F2 EBI-21383995 0.00 Q2TAA8 EBI-21383952 0.00 P17980 EBI-21384575 0.00 Q9NR46 EBI-21384475 0.00 Q9NRA8 EBI-21384346 0.00 Q6PEZ3 EBI-21384756 0.00 O00231 EBI-21384666 0.00 Q8N2N9 EBI-21385221 0.00 Q9P246 EBI-21385083 0.00 Q9Y2V7 EBI-21384947 0.00 Q9NS37 EBI-21385397 0.00 P15622 EBI-21385411 0.00 Q9UNH7 EBI-21385440 0.00 Q53G59 EBI-21385611 0.00 Q15424 EBI-21385936 0.00 P62979 EBI-21385886 0.00 P62750 EBI-21385846 0.00 P35268 EBI-21385832 0.00 Q9C0C9 EBI-21386016 0.00 Q9H2G4 EBI-21386093 0.00 P23246 EBI-26509668 0.55 Q96BJ3 EBI-21386472 0.00 Q2KHR2 EBI-21386486 0.00 Q86XZ4 EBI-21386554 0.00 P28370 EBI-21386642 0.00 P51532 EBI-21386670 0.00 Q14527 EBI-21386656 0.00 P18583 EBI-21387034 0.00 Q13813 EBI-21387265 0.00 P21579 EBI-21387640 0.00 P21675 EBI-21387657 0.00 Q14241 EBI-21387697 0.00 Q15906 EBI-21387723 0.00 P10600 EBI-21387750 0.00 P10828 EBI-21387764 0.00 P05452 EBI-21387855 0.00 P09936 EBI-21388194 0.00 Q15361 EBI-21388064 0.00 O96028 EBI-21388313 0.00 P52746 EBI-21388613 0.00 Q99676 EBI-21388653 0.00 P21506 EBI-21388441 0.00 Q06732 EBI-21388507 0.00 Q06730 EBI-21388493 0.00 Q13029 EBI-21388784 0.00 Q86XK2 EBI-21389330 0.00 Q6ZS17 EBI-21388993 0.00 A6NKB5 EBI-21389170 0.00 P51114 EBI-25478796 0.75 P45974 EBI-21389685 0.00 Q8IZ26 EBI-21389671 0.00 Q9UQM7 EBI-21389808 0.00 Q6PIJ6 EBI-21389822 0.00 Q9H7E2 EBI-25485785 0.55 Q9BZR9 EBI-21389862 0.00 P51784 EBI-21389928 0.00 P04632 EBI-21389954 0.00 Q2LD37 EBI-21390138 0.00 Q9BSF8 EBI-21390192 0.00 Q86W92 EBI-21390487 0.00 Q5VT25 EBI-21390408 0.00 Q96JF6 EBI-21390326 0.00 Q5H9K5 EBI-21390257 0.00 Q9BR77 EBI-21390230 0.00 O75925 EBI-21390743 0.00 Q92538 EBI-21391002 0.00 P52179 EBI-21391016 0.00 P12814 EBI-21390951 0.00 O15379 EBI-21391129 0.00 O14617 EBI-21391403 0.00 O75928 EBI-21391700 0.00 O60229 EBI-21391481 0.00 Q8WV44 EBI-21391773 0.00 P54296 EBI-21391903 0.00 Q9NYA4 EBI-21391824 0.00 Q13023 EBI-21392373 0.00 Q9NRD5 EBI-26509641 0.55 Q9UII2 EBI-21392257 0.00 O15066 EBI-21392218 0.00 O75376 EBI-21392586 0.00 Q9Y4A8 EBI-21392529 0.00 Q5JY77 EBI-21392894 0.00 P50749 EBI-21392944 0.00 P43243 EBI-21392970 0.00 Q9UKI8 EBI-21393215 0.00 Q16181 EBI-21393295 0.00 O43295 EBI-21393383 0.00 Q8N5U6 EBI-21393422 0.00 Q8N7X4 EBI-25856749 0.56 Q86TI2 EBI-25856739 0.56 Q8TCT7 EBI-25856729 0.56 O43257 EBI-25856721 0.56 P45880 EBI-25856713 0.56 Q15583 EBI-25856697 0.56 P49768 EBI-25856689 0.56 P62714 EBI-25856681 0.56 P08473 EBI-25856673 0.56 P19419 EBI-25856665 0.56 Q14790 EBI-25856657 0.56 Q06481 EBI-25856649 0.56 P09972 EBI-26509515 0.37 Q9ULU4 EBI-26509702 0.37 Q8WW38 EBI-26509693 0.37 O95359 EBI-26509686 0.37 Q9H0F6 EBI-26509677 0.37 P61289 EBI-26509659 0.37 Q9BZL4 EBI-26509650 0.37 Q7Z6G3 EBI-26509632 0.37 Q14764 EBI-26509623 0.37 Q5TCQ9 EBI-26509614 0.37 Q8N163 EBI-26509605 0.37 Q9NSC5 EBI-26509596 0.37 Q9C0E4 EBI-26509587 0.37 Q16760 EBI-26509560 0.37 Q9H773 EBI-26509551 0.37 Q13554 EBI-26509542 0.37 Q9NWD9 EBI-26509524 0.37 P55265 EBI-26367348 0.35 Q7Z7C8 EBI-26367348 0.35 Q04637 EBI-26367348 0.35 Q8TAA9 EBI-26367348 0.35 Q05639 EBI-26367348 0.35 O43242 EBI-26367348 0.35 Q9H307 EBI-26367348 0.35 Q9Y5V3 EBI-26367348 0.35 Q15007 EBI-26367348 0.35 O43660 EBI-26367348 0.35 Q08211 EBI-26367348 0.35 Q9NZI8 EBI-26367348 0.35 Q9P013 EBI-26367348 0.35 P41221 EBI-26367348 0.35 Q9BUF5 EBI-26367348 0.35 O00154 EBI-26367348 0.50 Q6NT76 EBI-26367348 0.35 O00425 EBI-26367348 0.35 Q9ULK5 EBI-26367348 0.35 O60832 EBI-26367348 0.35 Q99700 EBI-26367348 0.35 P48634 EBI-26367348 0.35 Q14157 EBI-26367348 0.35 Q9Y520 EBI-26367348 0.35 P39880 EBI-26367348 0.35 Q8WWM7 EBI-26367348 0.35 Q14444 EBI-26367348 0.35 Q96I24 EBI-26367348 0.35 Q13948 EBI-26367348 0.35 Q9HBM6 EBI-26367348 0.35 Q53F19 EBI-26397711 0.35 P0DTC9 EBI-26877965 0.35 A0A0F6B063 EBI-27033283 0.35 D0ZRB2 EBI-27033344 0.35 P35226 EBI-27109494 0.35 P43405 EBI-28935283 0.35 Q9UN86 EBI-28955513 0.35 Q6ZMQ8 EBI-32723474 0.27 Q06124 EBI-32723738 0.27 Q86UE4 EBI-34580762 0.35 GO:0070161 GO:0030424 GO:0043679 GO:0015030 GO:0042995 GO:0010369 GO:0005694 GO:0000775 GO:0005737 GO:0036464 GO:0010494 GO:0005829 GO:0030425 GO:1902737 GO:0043197 GO:0044326 GO:0019897 GO:0032433 GO:0097386 GO:0030426 GO:1990812 GO:0043232 GO:0016020 GO:1990124 GO:0005845 GO:0043005 GO:0043025 GO:0071598 GO:0005730 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005844 GO:0098794 GO:0014069 GO:0045211 GO:0098793 GO:0042734 GO:1990904 GO:0045202 GO:0003682 GO:0003677 GO:0070840 GO:0002151 GO:0042802 GO:0035064 GO:0008017 GO:0035198 GO:0140693 GO:0003730 GO:0048027 GO:0003729 GO:0034046 GO:0008266 GO:0046982 GO:0042803 GO:0043022 GO:0003723 GO:0035613 GO:0033592 GO:1990825 GO:0035197 GO:0031369 GO:0045182 GO:0030371 GO:0044325 GO:0098586 GO:0006281 GO:0031047 GO:0007215 GO:0044830 GO:0006397 GO:0051028 GO:2000766 GO:1900453 GO:1902373 GO:2000301 GO:0017148 GO:0045947 GO:1901386 GO:0007399 GO:0060999 GO:0051491 GO:1901254 GO:2000637 GO:1902416 GO:1901800 GO:0001934 GO:0002092 GO:2001022 GO:0045727 GO:0000381 GO:0060998 GO:0051489 GO:0060964 GO:0043488 GO:0098908 GO:0046928 GO:0008380 Unknown UniProt Sequence Analysis MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP 632 P35922 Fragile Fmr1 10090 None SL-0198 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}. UNIPROT P35922 Pfam PF05641 Pfam PF16098 Pfam PF12235 Pfam PF00013 Pfam PF17904 Pfam PF18336 PROSITE PS51641 PROSITE PS50084 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}. P33175 EBI-16728828 0.35 Q61584 EBI-8598304 0.56 P26323 EBI-653886 0.37 Q7TMB8 EBI-2000004 0.58 P63073 EBI-2000515 0.43 P49452 EBI-8573213 0.35 Q9JHG6 EBI-8014106 0.47 P52927 EBI-9986179 0.35 Q5SQX6 EBI-16727864 0.35 Q7TPH6 EBI-16728828 0.35 Q9Z2D8 EBI-16728828 0.35 Q8CJG0 EBI-16728828 0.35 Q6PDG5 EBI-16728828 0.35 P62996 EBI-16728828 0.35 Q9EPQ8 EBI-16728828 0.35 Q80YR5 EBI-16728828 0.35 Q6RHR9 EBI-16728828 0.35 P97379 EBI-16728828 0.35 O35218 EBI-16728828 0.35 Q9JIY2 EBI-16728828 0.35 P53995 EBI-16728828 0.35 P83510 EBI-16728828 0.35 Q8R151 EBI-16728828 0.35 Q7TQJ8 EBI-16728828 0.35 Q8CGF6 EBI-16728828 0.35 P52479 EBI-16728828 0.35 Q91VX2 EBI-16728828 0.35 Q91W18 EBI-16728828 0.35 Q8CHG7 EBI-16728828 0.35 P80560 EBI-16728828 0.35 Q3V1L4 EBI-16728828 0.35 Q8R4U7 EBI-16728828 0.35 Q6Y7W8 EBI-16728828 0.35 Q9WVR4 EBI-16728828 0.35 Q6A0A9 EBI-16728828 0.35 Q61701 EBI-16728828 0.35 Q60900 EBI-16728828 0.35 Q60899 EBI-16728828 0.35 Q6NZJ6 EBI-16728828 0.35 Q8C008 EBI-16728828 0.35 O70305 EBI-16728828 0.35 Q61315 EBI-16728828 0.35 Q9Z1D7 EBI-16728828 0.35 Q6IQX8 EBI-16728828 0.35 Q91VL9 EBI-16728828 0.35 Q5I043 EBI-16728828 0.35 A2AN08 EBI-16728828 0.35 P70399 EBI-16728828 0.35 Q569Z6 EBI-16728828 0.35 Q8BHJ5 EBI-16728828 0.35 Q920B9 EBI-16728828 0.35 Q8C804 EBI-16728828 0.35 E1U8D0 EBI-16728828 0.35 P61406 EBI-16728828 0.35 Q3TKT4 EBI-16728828 0.35 Q62141 EBI-16728828 0.35 Q80U72 EBI-16728828 0.35 P46061 EBI-16728828 0.35 Q9ERU9 EBI-16728828 0.35 Q9JIF0 EBI-16728828 0.35 P62137 EBI-16728828 0.35 Q9R0L6 EBI-16728828 0.35 P60335 EBI-16728828 0.35 Q8BSQ9 EBI-16728828 0.35 Q99NH2 EBI-16728828 0.35 Q8C015 EBI-16728828 0.35 B2RRE7 EBI-16728828 0.35 E9Q7G0 EBI-16728828 0.35 Q5F2E7 EBI-16728828 0.35 Q9D6T0 EBI-16728828 0.35 Q80TM9 EBI-16728828 0.35 Q6KCD5 EBI-16728828 0.35 P46935 EBI-16728828 0.35 Q61026 EBI-16728828 0.35 P09405 EBI-16728828 0.35 Q9EPN1 EBI-16728828 0.35 Q69ZK1 EBI-16728828 0.35 P60762 EBI-16728828 0.35 P97820 EBI-16728828 0.35 Q9QYH6 EBI-16728828 0.35 Q9QXZ0 EBI-16728828 0.35 Q3UMG5 EBI-16728828 0.35 Q5XJV6 EBI-16728828 0.35 P70168 EBI-16728828 0.35 Q9QXL1 EBI-16728828 0.35 A2AIV2 EBI-16728828 0.35 Q6ZQ88 EBI-16728828 0.35 Q99JP6 EBI-16728828 0.35 Q4U2R1 EBI-16728828 0.35 P70288 EBI-16728828 0.35 Q9QZQ8 EBI-16728828 0.35 Q9WV60 EBI-16728828 0.35 Q61545 EBI-16728828 0.35 P84089 EBI-16728828 0.35 Q8BMB0 EBI-16728828 0.35 Q9Z148 EBI-16728828 0.35 Q3UJB9 EBI-16728828 0.35 Q60838 EBI-16728828 0.35 Q8R1A4 EBI-16728828 0.35 P13864 EBI-16728828 0.35 Q80Y83 EBI-16728828 0.35 Q62167 EBI-16728828 0.35 O54833 EBI-16728828 0.35 Q60737 EBI-16728828 0.35 Q80TV8 EBI-16728828 0.35 A2AJK6 EBI-16728828 0.35 Q6PDQ2 EBI-16728828 0.35 Q8K389 EBI-16728828 0.35 Q6A068 EBI-16728828 0.35 Q8VDP4 EBI-16728828 0.35 P23198 EBI-16728828 0.35 Q8K3W3 EBI-16728828 0.35 Q99PV8 EBI-16728828 0.35 Q9QYE3 EBI-16728828 0.35 Q9Z1K7 EBI-16728828 0.35 Q70FJ1 EBI-16728828 0.35 Q9DBR0 EBI-16728828 0.35 P61164 EBI-16728828 0.35 F6SEU4 EBI-16728828 0.35 Q4ACU6 EBI-16728828 0.35 Q5DU25 EBI-16728828 0.35 Q68FF6 EBI-16728828 0.35 Q6PFD5 EBI-16728828 0.35 Q62108 EBI-16728828 0.35 Q91XM9 EBI-16728828 0.35 Q811D0 EBI-16728828 0.35 A2AGT5 EBI-16728828 0.35 O88737 EBI-16728828 0.35 P61205 EBI-16728828 0.35 Q8BGS3 EBI-16728828 0.35 O88532 EBI-16728828 0.35 Q8BJH1 EBI-16728828 0.35 Q6VNB8 EBI-16728828 0.35 P70398 EBI-16728828 0.35 A2RSJ4 EBI-16728828 0.35 Q80X50 EBI-16728828 0.35 Q9R1R2 EBI-16728828 0.35 Q62318 EBI-16728828 0.35 Q9Z321 EBI-16728828 0.35 E9Q0S6 EBI-16728828 0.35 Q8BKI2 EBI-16728828 0.35 Q8BYI9 EBI-16728828 0.35 P39447 EBI-16728828 0.35 Q9QXE7 EBI-16728828 0.35 Q60864 EBI-16728828 0.35 P56873 EBI-16728828 0.35 O54781 EBI-16728828 0.35 Q62261 EBI-16728828 0.35 Q6NZL0 EBI-16728828 0.35 Q3UHU5 EBI-16728828 0.35 A2AQ25 EBI-16728828 0.35 Q6P4S6 EBI-16728828 0.35 P58801 EBI-16728828 0.35 P69566 EBI-16728828 0.35 P70388 EBI-16728828 0.35 O35295 EBI-16728828 0.35 P42669 EBI-16728828 0.35 Q3TLH4 EBI-16728828 0.35 Q7TPM1 EBI-16728828 0.35 Q7TSC1 EBI-16728828 0.35 Q62101 EBI-16728828 0.35 P63318 EBI-16728828 0.35 P68404 EBI-16728828 0.35 Q76MZ3 EBI-16728828 0.35 Q68FH0 EBI-16728828 0.35 Q922S4 EBI-16728828 0.35 P48725 EBI-16728828 0.35 O08919 EBI-16728828 0.35 P46460 EBI-16728828 0.35 P08551 EBI-16728828 0.35 Q9WU42 EBI-16728828 0.35 Q60974 EBI-16728828 0.35 O09000 EBI-16728828 0.35 P28660 EBI-16728828 0.35 Q8VE19 EBI-16728828 0.35 E9PWI3 EBI-16728828 0.35 Q8K310 EBI-16728828 0.35 P63085 EBI-16728828 0.35 Q91ZX7 EBI-16728828 0.35 Q7TME0 EBI-16728828 0.35 Q8BZL8 EBI-16728828 0.35 O55203 EBI-16728828 0.35 P70662 EBI-16728828 0.35 O88447 EBI-16728828 0.35 P28738 EBI-16728828 0.35 Q61768 EBI-16728828 0.35 P28740 EBI-16728828 0.35 Q3U0V1 EBI-16728828 0.35 Q3UXZ9 EBI-16728828 0.35 Q6ZPR4 EBI-16728828 0.35 Q08460 EBI-16728828 0.35 Q8C863 EBI-16728828 0.35 Q8R0S2 EBI-16728828 0.35 P46660 EBI-16728828 0.35 Q60625 EBI-16728828 0.35 O88895 EBI-16728828 0.35 Q91VW5 EBI-16728828 0.35 A2A699 EBI-16728828 0.35 A2ATK9 EBI-16728828 0.35 Q8C3F2 EBI-16728828 0.35 Q05BC3 EBI-16728828 0.35 P70372 EBI-16728828 0.35 Q9QXY6 EBI-16728828 0.35 P63168 EBI-16728828 0.35 Q9JHU4 EBI-16728828 0.35 O08553 EBI-16728828 0.35 P39053 EBI-16728828 0.35 Q3UH60 EBI-16728828 0.35 O70566 EBI-16728828 0.35 O54784 EBI-16728828 0.35 Q02248 EBI-16728828 0.35 Q0V8T9 EBI-16728828 0.35 P12960 EBI-16728828 0.35 Q6ZQ08 EBI-16728828 0.35 Q80U49 EBI-16728828 0.35 Q6A065 EBI-16728828 0.35 Q6P9K8 EBI-16728828 0.35 Q60865 EBI-16728828 0.35 Q8C1B1 EBI-16728828 0.35 Q923T9 EBI-16728828 0.35 Q6PHZ2 EBI-16728828 0.35 P28652 EBI-16728828 0.35 P11798 EBI-16728828 0.35 Q8R0S4 EBI-16728828 0.35 Q8CC27 EBI-16728828 0.35 Q8R3Z5 EBI-16728828 0.35 Q5RJI5 EBI-16728828 0.35 O08539 EBI-16728828 0.35 Q9D219 EBI-16728828 0.35 Q60875 EBI-16728828 0.35 Q6P9R4 EBI-16728828 0.35 Q8C4V1 EBI-16728828 0.35 Q6DFV3 EBI-16728828 0.35 Q99NH0 EBI-16728828 0.35 Q8CJG1 EBI-16728828 0.35 Q9ESC8 EBI-16728828 0.35 Q9EP53 EBI-16734894 0.35 Q9D415 EBI-16725590 0.35 Q3UHD9 EBI-16750831 0.35 Q6UWE0 EBI-22050272 0.35 Q6NZM9 EBI-26472902 0.35 D0ZPH9 EBI-27035192 0.35 GO:0070161 GO:0030424 GO:1904115 GO:0043679 GO:0015030 GO:0044297 GO:0042995 GO:0010369 GO:0005694 GO:0000775 GO:0005737 GO:0036464 GO:0010494 GO:0005829 GO:0030425 GO:1902737 GO:0043197 GO:0044327 GO:0044326 GO:0019897 GO:0032433 GO:0097386 GO:0098978 GO:0030426 GO:1990812 GO:0098686 GO:0016020 GO:1990124 GO:0015630 GO:0005845 GO:0043005 GO:0043025 GO:0071598 GO:0005730 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005844 GO:0098794 GO:0099524 GO:0014069 GO:0045211 GO:0098793 GO:0099523 GO:0042734 GO:1990635 GO:1990904 GO:0005791 GO:0098685 GO:0032797 GO:0005790 GO:0097444 GO:0045202 GO:0043195 GO:0003682 GO:0070840 GO:0002151 GO:0042802 GO:0035064 GO:0008017 GO:0035198 GO:0003730 GO:0048027 GO:0003729 GO:0034046 GO:0008266 GO:0019904 GO:0046982 GO:0042803 GO:0019901 GO:0019903 GO:0043022 GO:0000340 GO:0003723 GO:0035613 GO:0033592 GO:1990825 GO:0035197 GO:0031369 GO:0045182 GO:0030371 GO:0044325 GO:0008089 GO:0098586 GO:0007417 GO:0060996 GO:0006281 GO:0098976 GO:0031047 GO:0007215 GO:0098977 GO:0044830 GO:0006397 GO:0051028 GO:2000766 GO:0010629 GO:1900453 GO:1902373 GO:0043524 GO:0045665 GO:0010955 GO:0002091 GO:2000301 GO:0017148 GO:0045947 GO:1901386 GO:0060999 GO:0051491 GO:0010628 GO:1901254 GO:0048170 GO:1900454 GO:1900273 GO:2000637 GO:1902416 GO:1901800 GO:0001934 GO:0002092 GO:2001022 GO:0050806 GO:0045727 GO:0000381 GO:0060998 GO:0051489 GO:0060964 GO:1905244 GO:0043488 GO:0098908 GO:0046928 GO:0099578 GO:0099577 GO:0097396 GO:0008380 GO:0035176 GO:0019226 Unknown UniProt Sequence Analysis MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPERQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLEVPEDLRQMCAKESAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLILRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKSVPQEEEIMPPSSLPSNNSRVGPNSSEEKKHLDTKENTHFSQPNSTKVQRVLVVSSIVAGGPQKPEPKAWQGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKGYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRRGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTADGSLQSASSEGSRLRTGKDRNQKKEKPDSVDGLQPLVNGVP 614 Q5R9B4 Fragile FMR1 9601 None SL-0198 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}. UNIPROT Q5R9B4 Pfam PF05641 Pfam PF16098 Pfam PF12235 Pfam PF00013 Pfam PF17904 Pfam PF18336 PROSITE PS51641 PROSITE PS50084 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}. GO:0070161 GO:0030424 GO:0043679 GO:0042995 GO:0010369 GO:0005694 GO:0000775 GO:0005737 GO:0036464 GO:0010494 GO:0030425 GO:1902737 GO:0043197 GO:0019897 GO:0032433 GO:0097386 GO:0030426 GO:1990812 GO:0005845 GO:0043005 GO:0071598 GO:0005730 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005844 GO:0098794 GO:0014069 GO:0045211 GO:0098793 GO:0042734 GO:1990904 GO:0045202 GO:0003682 GO:0070840 GO:0002151 GO:0035064 GO:0008017 GO:0035198 GO:0003730 GO:0048027 GO:0003729 GO:0034046 GO:0008266 GO:0046982 GO:0042803 GO:0035613 GO:0033592 GO:1990825 GO:0035197 GO:0030371 GO:0006281 GO:0031047 GO:0007215 GO:0006397 GO:0051028 GO:2000766 GO:0010629 GO:1900453 GO:2000301 GO:0017148 GO:0045947 GO:1901386 GO:0007399 GO:0060999 GO:0051491 GO:2000637 GO:1902416 GO:1901800 GO:0002092 GO:0045727 GO:0000381 GO:0060998 GO:0051489 GO:0060964 GO:0043488 GO:0098908 GO:0046928 GO:0008380 GO:0060538 Unknown UniProt Sequence Analysis MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKESAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLEIKENSTHFSQPNSTKVQRGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFEGNDDHSRTDNRPRNPREAKGRTTDGSLQNTSSEGNRLRTGKDRNRKKEKPDSVDGQQPLVNGVP 594 Q80WE1 Fragile Fmr1 10116 None SL-0198 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}. UNIPROT Q80WE1 UNIPROT P70568 Pfam PF05641 Pfam PF16098 Pfam PF12235 Pfam PF00013 Pfam PF17904 Pfam PF18336 PROSITE PS51641 PROSITE PS50084 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}. Q9R0N3 EBI-9526900 0.35 F1M0Z1 EBI-26961439 0.35 GO:0070161 GO:0030424 GO:1904115 GO:0043679 GO:0015030 GO:0044297 GO:0042995 GO:0010369 GO:0005694 GO:0000775 GO:0005737 GO:0036464 GO:0010494 GO:0005829 GO:0030425 GO:1902737 GO:0043197 GO:0044327 GO:0044326 GO:0019897 GO:0032433 GO:0097386 GO:0098978 GO:0030426 GO:1990812 GO:0098686 GO:0016020 GO:1990124 GO:0015630 GO:0005845 GO:0043005 GO:0043025 GO:0071598 GO:0005730 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005844 GO:0098794 GO:0099524 GO:0014069 GO:0098793 GO:0099523 GO:0042734 GO:1990635 GO:1990904 GO:0005791 GO:0098685 GO:0032797 GO:0005790 GO:0097444 GO:0045202 GO:0043195 GO:0003682 GO:0070840 GO:0002151 GO:0042802 GO:0035064 GO:0008017 GO:0035198 GO:0003730 GO:0048027 GO:0003729 GO:0034046 GO:0008266 GO:0019904 GO:0046982 GO:0042803 GO:0019901 GO:0019903 GO:0043022 GO:0000340 GO:0003723 GO:0035613 GO:0033592 GO:1990825 GO:0035197 GO:0031369 GO:0045182 GO:0030371 GO:0044325 GO:0008089 GO:0006974 GO:0072711 GO:1904009 GO:0035865 GO:0034644 GO:0098586 GO:0007417 GO:0060996 GO:0050974 GO:0006281 GO:0098976 GO:0031047 GO:0007215 GO:0098977 GO:0044830 GO:0006397 GO:0051028 GO:2000766 GO:0010629 GO:1900453 GO:1902373 GO:0043524 GO:0045665 GO:0010955 GO:0002091 GO:2000301 GO:0017148 GO:0045947 GO:1901386 GO:0001541 GO:0060999 GO:0051491 GO:0010628 GO:1901254 GO:0048170 GO:1900454 GO:1900273 GO:2000637 GO:1902416 GO:1901800 GO:0001934 GO:0002092 GO:2001022 GO:0050806 GO:0045727 GO:0000381 GO:0060998 GO:0051489 GO:0060964 GO:1905244 GO:0043488 GO:0098908 GO:0046928 GO:0006417 GO:0099578 GO:0099577 GO:0014823 GO:0042220 GO:0051602 GO:0034698 GO:0070555 GO:0097396 GO:0009416 GO:0008380 GO:0060538 GO:0035176 GO:0019226 Unknown UniProt Sequence Analysis MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPERQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLEVPEDLRQMCAKESAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLILRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKSVPQEEENLPPSSLPSNNSRVGSNSSEEKKHLDTKENTHFSQPNSTKVQRGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKGYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPRETKGRTTDGSLQSTSSEGSRLRTGKDRNQKKEKPDSVDGLQPLVNGVP 593 Q6GLC9 Fragile fmr1 8364 None SL-0198 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}. UNIPROT Q6GLC9 Pfam PF05641 Pfam PF16098 Pfam PF12235 Pfam PF00013 Pfam PF17904 Pfam PF18336 PROSITE PS51641 PROSITE PS50084 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}. GO:0070161 GO:0030424 GO:0043679 GO:0042995 GO:0010369 GO:0005694 GO:0000775 GO:0005737 GO:0036464 GO:0010494 GO:0030425 GO:1902737 GO:0043197 GO:0044326 GO:0019897 GO:0032433 GO:0097386 GO:0030426 GO:1990812 GO:0016020 GO:0043005 GO:0043025 GO:0071598 GO:0005730 GO:0005654 GO:0005634 GO:0043204 GO:0048471 GO:0005844 GO:0098794 GO:0014069 GO:0045211 GO:0098793 GO:0042734 GO:1990904 GO:0045202 GO:0003682 GO:0070840 GO:0002151 GO:0035064 GO:0008017 GO:0035198 GO:0003730 GO:0048027 GO:0003729 GO:0034046 GO:0008266 GO:0046982 GO:0042803 GO:0003723 GO:0035613 GO:0033592 GO:1990825 GO:0035197 GO:0045182 GO:0030371 GO:0007420 GO:0048755 GO:0051216 GO:0050890 GO:0006281 GO:0021905 GO:0007215 GO:0006397 GO:0051028 GO:2000766 GO:0010629 GO:1900453 GO:2000301 GO:0017148 GO:0045947 GO:1901386 GO:0014036 GO:0048812 GO:0060999 GO:0051491 GO:2000637 GO:1902416 GO:1901800 GO:0001934 GO:0002092 GO:2001022 GO:0045727 GO:0000381 GO:0060998 GO:0051489 GO:0060964 GO:0090365 GO:0043488 GO:0098908 GO:0046928 GO:0008380 GO:0060538 Unknown UniProt Sequence Analysis MEELAVEVRGSNGAFYKAFVKDVHEDSITVTFENNWQQERQIPFHDVRFPPPSGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKNSFHKVKLDVPEDLRQMCAKDSAHKDFKKAVGAFSVSYDSENYQLVILSVNEVTIKRANMLSDMHFRSLRTKLSLMLRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQEAVKKARTYLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENDKNISPEEGMVPFVFVGTKDSITNATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRPDKEKGYQSEDLSGTGRGSRPYNNRGRSRRGTGYASDIRYGDPDYRKTTYPEYPRSQAFWIKGTNSEASNASETESDHRDELSDWSLAPAEDDRDNYHRRGDGRRRGGPRGQGMRGRGGFKGNDDQPRPDNRQRNSRETKARTSDGSLQIRIDCNNERSVHTKTLQNASVEGSRLRTGKDRVQKKEKSEVVDGPQVVVNGIP 590 Q6PIV2 Forkhead FOXR1 9606 None SL-0198 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}. UNIPROT Q6PIV2 UNIPROT B0YJ15 UNIPROT Q08AS8 UNIPROT Q86UT9 UNIPROT Q8IXX2 Pfam PF00250 PROSITE PS50039 OMIM 615755 DisGeNET 283150 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}. 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}. O14656 EBI-25847482 0.56 P50222 EBI-10253813 0.56 Q53SE7 EBI-10253831 0.56 Q8N9N5 EBI-10253841 0.56 Q96CD2 EBI-10253853 0.78 Q9UBU8 EBI-11319459 0.35 Q969R5 EBI-11319459 0.35 Q9BZS1 EBI-11319459 0.35 Q00532 EBI-11319459 0.35 Q9NSD9 EBI-11319459 0.35 P01040 EBI-11319459 0.35 Q9Y4A5 EBI-11319459 0.35 Q96L91 EBI-11319459 0.53 O95347 EBI-11319459 0.35 Q969U6 EBI-11319459 0.35 Q52LR7 EBI-11319459 0.53 Q9NPF5 EBI-11319459 0.53 P01106 EBI-11319459 0.35 P31276 EBI-11319459 0.35 Q6PIV2 EBI-11319459 0.35 Q9NXR8 EBI-11319459 0.53 O60264 EBI-11319459 0.35 O95619 EBI-11319459 0.53 Q9H2F5 EBI-11319459 0.35 P04198 EBI-11319459 0.35 O96019 EBI-11319459 0.35 Q05BQ5 EBI-11319459 0.53 Q9NV56 EBI-11319459 0.53 Q15014 EBI-11319459 0.35 P61244 EBI-11319459 0.35 Q9H0E9 EBI-11319459 0.35 Q92993 EBI-11319459 0.35 Q9UBN7 EBI-11321774 0.35 Q99523 EBI-11321774 0.35 Q96T76 EBI-11321774 0.35 Q16720 EBI-11321774 0.35 P53621 EBI-11321774 0.35 Q96IK5 EBI-25252587 0.56 Q96LK0 EBI-24531695 0.56 Q7L190 EBI-24582359 0.56 Q9HAF1 EBI-21816916 0.35 Q15906 EBI-21816916 0.35 P50225 EBI-21816916 0.35 P01023 EBI-25830325 0.56 Q92870 EBI-25831871 0.56 G5E9A7 EBI-25843815 0.56 P50570 EBI-25845425 0.56 P51608 EBI-25876038 0.56 D3DTS7 EBI-25883900 0.56 Q16637 EBI-25891888 0.56 Q86WV8 EBI-25893897 0.56 Q8TB36 EBI-25923540 0.56 Q7Z412 EBI-25925249 0.56 P37840 EBI-25941226 0.56 P42858 EBI-25944360 0.56 GO:0000785 GO:0005737 GO:0005634 GO:0048471 GO:0001228 GO:0000981 GO:0001227 GO:1990837 GO:0007420 GO:0045944 GO:0006357 Unknown UniProt Sequence Analysis MGNELFLAFTTSHLPLAEQKLARYKLRIVKPPKLPLEKKPNPDKDGPDYEPNLWMWVNPNIVYPPGKLEVSGRRKREDLTSTLPSSQPPQKEEDASCSEAAGVESLSQSSSKRSPPRKRFAFSPSTWELTEEEEAEDQEDSSSMALPSPHKRAPLQSRRLRQASSQAGRLWSRPPLNYFHLIALALRNSSPCGLNVQQIYSFTRKHFPFFRTAPEGWKNTVRHNLCFRDSFEKVPVSMQGGASTRPRSCLWKLTEEGHRRFAEEARALASTRLESIQQCMSQPDVMPFLFDL 292 Q3UTB7 Forkhead Foxr1 10090 None SL-0198 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}. UNIPROT Q3UTB7 Pfam PF00250 PROSITE PS50039 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}. GO:0005737 GO:0005634 GO:0048471 GO:0001228 GO:0001227 GO:1990837 GO:0007420 GO:0045944 GO:0006357 Unknown UniProt Sequence Analysis MGNECFLTFTTTHLSEAEQKLALYRLQLVEPPKLPLEKKTNPDKDGPDIKPNLWMWVNPNMVYPPGKLEVAVKEEDQSALSAFQPALKEEEDSCSEASEVQQPLPPCRQKRKQRRSTVPLPLAPGRRAPLENPWRLPQAISPEGRLWSRPPLHYFHLIALALRNSPPCGLSVQQIYSFTREHFPFFRTAPEAWKNTVRHNLSFRDSFEKVPASRQGGASTGPRSCLWKLTEEGHRRFSKEARTLASTQLQSIQQCMSQPGVKPFLFDL 268 H0UZ81 Fibronectin FSD2 10141 None SL-0198 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}. UNIPROT H0UZ81 Pfam PF00041 Pfam PF00622 PROSITE PS50188 PROSITE PS50853 GO:0005634 GO:0048471 GO:0016529 Unknown UniProt Sequence Analysis MEEEAGEEPRLDRPTAPKDFHFYNMDLYDSEDRLPLFPEENTRLRRQTIQAEMTYDPKEVGNSFVDEGRMGVPAYPPYGIKRREPGWEQRDWRLEGEVETEDQDQDFSQWSMAGQSQALWESYRYTHGRASEEYECYVIPEEEDEEEAADLFCVTCRTPIRAVEKDFGEHKEHEVTPLSKALESAKEEIHKNMYKLEQQIIEMENFASHLEEVFITVEENFGRQEQNFESHYNGILETLAQKYEEKIQALGEKKKEKLEALYGQLVSCGENLDTCKELMETIEEMCHEEKVDFLKVSNETLGKFLKTKTDVEIAAQPEFEDQTLDFSDVEQLMGSMNTILAPSAPVINPQAPNSATGSSVRVCWSLYADDTVESYQLSYRPVRDSLPGKEQAEFTVTVKESYCSVTNLEPNTQYEFWVIAQNRAGPSPSSEHAMYMTAPSPPIIKTEAIRSCEEAALICWESGNLNPVDSYTVELTQVEEPAASGVTESVVGIPICESLIQLQPGQSYTICVRALNVGGPSARSTPATVRTTGSYFPLNKATCHPWLTISEDGFTVIRSERKNLTQELQPQQTQFTRCVAIMGNLIPVRGRHYWEIEMDEHLDYTVGVAFEDVPKQEDLGANGFSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYENSKLSFFNVDIAQHLYTFSCQLQQFVHPCFSLEKPGCLKIHNGISMPMHATFY 719 A1L4K1 Fibronectin FSD2 9606 None SL-0198 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}. UNIPROT A1L4K1 UNIPROT B3KVG1 UNIPROT B7ZM02 Pfam PF00041 Pfam PF00622 PROSITE PS50188 PROSITE PS50853 DisGeNET 123722 Q14324 EBI-5661041 0.00 Q7Z3I7 EBI-10172604 0.60 Q7Z3B3 EBI-10178303 0.56 O95990 EBI-10192906 0.56 P10768 EBI-10197227 0.78 P17024 EBI-10199416 0.56 P28070 EBI-10204607 0.56 P29972 EBI-10204944 0.56 P31146 EBI-10205786 0.78 Q00994 EBI-10222282 0.72 Q06787 EBI-10224474 0.56 Q08117 EBI-10224779 0.67 Q14738 EBI-10233892 0.56 Q15973 EBI-10237322 0.56 Q16670 EBI-10238175 0.56 Q3B820 EBI-10240125 0.56 Q53FD0 EBI-10242267 0.56 Q5JS98 EBI-10244397 0.56 Q6NYC8 EBI-10251682 0.72 Q6P1J9 EBI-10252260 0.78 Q6PJG3 EBI-10253974 0.56 Q86VK4 EBI-10259792 0.56 Q86YD7 EBI-10260722 0.72 Q8IY31 EBI-10262646 0.56 Q8N381 EBI-10265171 0.56 Q8N8B7 EBI-10267719 0.56 Q8NEF3 EBI-10270620 0.56 Q8TAU3 EBI-10272085 0.72 Q8TD31 EBI-10274456 0.72 Q96BZ8 EBI-10282596 0.72 Q96NC0 EBI-10291592 0.56 Q96SQ5 EBI-10293466 0.72 Q9BXY8 EBI-10301478 0.56 Q9H0A9 EBI-10304145 0.60 Q9H0E9 EBI-10304359 0.72 Q9H6F0 EBI-10307479 0.56 Q9H788 EBI-10308323 0.72 Q9HC52 EBI-10310314 0.72 Q9P0T4 EBI-10317754 0.72 Q9UGP5 EBI-10320763 0.60 Q9UIE0 EBI-10321904 0.56 Q9Y3B7 EBI-10327384 0.72 Q8IXW7 EBI-21249370 0.37 Q99608 EBI-21251010 0.37 Q9H0I2 EBI-24276119 0.56 Q8TBB1 EBI-24292204 0.56 Q9P1Y5 EBI-24292226 0.56 Q9H9D4 EBI-24302090 0.56 Q5T619 EBI-24309981 0.56 Q96EG3 EBI-24311294 0.56 Q96AL5 EBI-24314166 0.56 Q8IVT4 EBI-24315626 0.56 Q6NX45 EBI-24321517 0.56 Q9BT49 EBI-24325694 0.56 Q9BWG6 EBI-24340348 0.56 Q96HB5 EBI-24349830 0.56 Q9UK33 EBI-24352123 0.56 P78358 EBI-24352383 0.56 Q96EZ8 EBI-24352759 0.56 Q8WWY3 EBI-24355284 0.56 O76064 EBI-24355797 0.56 Q9ULM2 EBI-24362843 0.56 Q96HP4 EBI-25253734 0.56 O43602 EBI-25254540 0.56 P0CB47 EBI-25255462 0.56 P56524 EBI-25255284 0.56 Q3SY00 EBI-25255985 0.56 O60645 EBI-25258050 0.56 Q9P2K3 EBI-24366860 0.56 P13682 EBI-24478087 0.56 Q07002 EBI-24478674 0.56 Q969G3 EBI-24492471 0.56 O95295 EBI-24500672 0.56 Q2TBE0 EBI-24508217 0.56 O14964 EBI-24370108 0.56 Q8TAB5 EBI-24382819 0.56 O43482 EBI-24385225 0.56 Q14119 EBI-24388342 0.56 Q2TBA0 EBI-24398616 0.56 Q99633 EBI-24401399 0.56 Q5W5X9 EBI-25260730 0.56 Q9ULD5 EBI-24422254 0.56 Q6ZNE5 EBI-24423012 0.56 Q9Y2P0 EBI-24424287 0.56 O60941 EBI-24426448 0.56 O95363 EBI-24427910 0.56 Q96PV4 EBI-24432894 0.56 Q9BQ89 EBI-24438032 0.56 P36508 EBI-24445889 0.56 P53365 EBI-24447892 0.56 Q8IYE0 EBI-24463350 0.56 Q9UJV3 EBI-24468925 0.56 Q9Y247 EBI-24470709 0.56 P46013 EBI-20562326 0.35 Q9Y394 EBI-20903160 0.40 P40426 EBI-22133174 0.37 GO:0005634 GO:0048471 GO:0016529 Unknown UniProt Sequence Analysis MEEESGEELGLDRSTPKDFHFYHMDLYDSEDRLHLFPEENTRMRKVVQAEMANESRGAGDGKAQRDLQEEVDELVHLYGLEDDHELGDEFVDENIPRTGVSEYPPYMMKRRDPAREQRDWRLSGEAAEAEDLGFGGWGSAGQCQDLREAYRYTHGRASEEYECYVIPEEEDEEEAADVFCVTCKTPIRAFQKVFDEHKEHEVIPLNEALESAKDEIHKNMYKLEKQIIEMENFANHLEEVFITVEENFGKQEQNFESHYNEILETLAQKYEEKIQALGEKKKEKLEALYGQLVSCGENLDTCKELMETIEEMCHEEKVDFIKDAVAMADRLGKFLKTKTDVEISAQPEFEDQTLDFSDVEQLMGSINTIPAPSAPVINPQVPNSATGSSVRVCWSLYSDDTVESYQLSYRPVQDSSPGTDQAEFTVTVKETYCSVTNLVPNTQYEFWVTAHNRAGPSPSSERAVYMTAPSPPIIKTKEIRSCEEAVLICWESGNLNPVDSYTVELTQAESPEASGVTESVVGIPTCESVVQLQPGRSYIIYVRALNMGGPSVRSEPATVHTIGSYFRLNKDTCHPWLTISEDGLTAVRSERRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQEDLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHEFVHPCFSLEKPGCLKVHNGISMPKHVTFY 749 Q8BZ52 Fibronectin Fsd2 10090 None SL-0198 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}. UNIPROT Q8BZ52 UNIPROT A0A140T8J1 UNIPROT E9QMV0 Pfam PF00041 Pfam PF13765 Pfam PF00622 PROSITE PS50188 PROSITE PS50853 GO:0005634 GO:0048471 GO:0016529 Unknown UniProt Sequence Analysis MEEEAEEESGLGRSAAPKDFHFYHMDLYDSEDRLQLFPGDSSRIRREVTQAEDDRELGDEFVDEHRLGTLGYPSYGMRRRDPGREPRDWGEAAEAEDLGYGGGQGPLDQCQDLREAYRYTHGRASEEYECYVIPEEEDEEEPADVFCITCKTPVRTVEKDFDTHKEHEVTPISKALEHAKDEVHKNMCKLEQQIIEMENFASHLEEVFITVEENFGRQEQNFECHYNGILETLAQKYEEKIQALGEKKREKLEALYGQLVSCGENLDACRELMETVEEMCHEEKVEFLKDAVAMTDRLGKFLKTKTDVELSAQPEFEDQTLDFSDVEQLMDAINTIPAPSAPVINPQAPNSATGSSVRVCWSLYSDDTVESYQLSYRPVQDSSSGKDRAEFTMMVKETYCSVTNLEPNTQYEFWVIAQNRTGPSPCSEHAVYMTAPSPPSIKTEAIRSCEEAVLICWESGNLNPVDSYTVELIQAETPEASGVTESVVGIPTCESLIQLQPRHSYTIYVRALNVGGTSARSEPATVHTTGSYFQLNKDTCHPWLTISEDGFTVVRSEKKSFRKELPPSKTQFTRCVAVMGNLIPVRGRHYWEVEVAEHLDYTVGVACEDVPKQEDLGANSLSWCMRHTFVSKRHRYEFLHNKMTPDIRITVAPRKIGVLLDYENAKLSFFNVDIAQHLYTFSCQLHQFVHPCFSLEKSGCLKICNGISMPKHVTFF 716 P25028 Mitosis fs 7227 None SL-0178 Nucleus envelope. Nucleus, nucleoplasm. Cytoplasm. Note=In the nuclear envelope during interphase to metaphase. And in the nucleoplasm and cytoplasm during anaphase and telophase. UNIPROT P25028 UNIPROT Q8T057 UNIPROT Q9W4W0 UNIPROT Q9W4W1 PROSITE PS00028 Cell cycle-dependent nuclear envelope component required for embryonic mitosis. P08928 EBI-872894 0.27 P19889 EBI-8296323 0.40 P02283 EBI-872898 0.27 O61307 EBI-9946542 0.35 GO:0005737 GO:0005635 GO:0005652 GO:0005654 GO:0051301 GO:0006325 GO:0030261 GO:0006260 GO:0000278 GO:0006997 GO:0007344 Unknown UniProt Sequence Analysis MSFSNVLIMRQPDEGKCHICKRVFCCGKCRQKHQFKAHAIAVREPLGLRSAGGGIIEHRHQMESGATTIYVFCPICERRPLLLREEMHGELLAHIETCHLPLRCRKCQRNYTRVDDLREFSKCVDQQQSCTDVTGATETSKATLKKAANSTAISTQTSPSVTPISLINMRWKAKSRVTHEEFISDSVSSIRNLSSFSNSSIRRSIGQLGVNPSETMEKGKVIRSTSTPLHVESVFAKPKEPITFNASTGGHVSSIYHEEPSPTPESNPVQQQQQQQQPLQQRAWKMGARNKMSAATPLRQVMSKSIQKAFVEHGGMMVHQPPSAVVQRRVRLDLSEHSSHEAAGSSALDLRLSPAMRRTQSESSASEVNSGSSSSYSTSRNADLCKRQFLLSAQKLTTESIIITRTNSSSQKTSSTVYNSCESVEIIRSTSESAEVCHVPAITPIRVTGAGINKKQIKFETPPKSSQQMRSNGEGDETKDQFFTPEPGTPEIPERRHRQAIVPRQLSGEFSPKKDKPKEKGLAVMALISPPLQQPRVRPPLRECRQQRVYSGVQDVGEPEVVDAEEEDEVFRPTNASTCNDKKLEAPNSGRLWSLMSSMMRLPASLRGEREKDRDRDRDSDKENAGSGSLIRRCASIAGSLVRPSARDSSMEDQQCLKRKRTQTLDSQYCSPLSPSSSSKRYRIRPREPIERMRRQ 696 P0C044 F F 11104 None SL-0382 Host cytoplasm {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. UNIPROT P0C044 Pfam PF01543 GO:0044220 GO:0019028 GO:0005198 Unknown UniProt Sequence Analysis MSTNPKPQKKKTNVTPTVAHRTSSSRVAVRSLVEFTCCRAGALDWVCARRERLPSGRNLEVDVSLSPRLVGPRAGPGLSPGTLGPSMAMRAAGGRDGSCLPVALGLAGAPQTPGVGRAIWVRSSIPLRAASPTSWGTYRSSAPLLEALPGPWRMASGFWKTA 162 P0C045 F F 63746 None SL-0382 Host cytoplasm {ECO:0000269|PubMed:12810869}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12810869}. UNIPROT P0C045 Pfam PF01543 Contributes to the DDX58/RIG-I-mediated inhibition of type I interferon production. {ECO:0000269|PubMed:27404108}. Q63HM2 EBI-10685725 0.51 P05156 EBI-9352054 0.37 O60844 EBI-9352018 0.37 P05155 EBI-9352014 0.37 P04004 EBI-9352010 0.37 P07858 EBI-9352006 0.37 P01019 EBI-9351994 0.37 P61106 EBI-9351990 0.37 P25311 EBI-9351982 0.37 O75352 EBI-9351986 0.37 P15907 EBI-9351998 0.37 P51522 EBI-9352002 0.37 Q9UHV9 EBI-10685314 0.54 GO:0042025 GO:0044220 GO:0019028 GO:0001848 GO:0019899 GO:0097655 GO:0031267 GO:0005198 GO:0035375 GO:0051494 GO:0039540 Unknown UniProt Sequence Analysis MSTNPKPQRKKPNVTPTVAHRTSSSRVAVRSLVEFTCCRAGALDWVCARRGRLPSGRNLEVDVSLSPRHVGPRAGPGLSPGTLGPSMAMRVAGGRDGSCLPVALGLAGAPQTPGVGRAIWVRSSIPLRAASPTSWGTYRSSAPLLEALPGPWRMASGFWKTA 162 P04406 Glyceraldehyde-3-phosphate GAPDH 9606 None SL-0198 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}. UNIPROT P04406 UNIPROT E7EUT4 UNIPROT P00354 UNIPROT Q53X65 PDB 1U8F PDB 1ZNQ PDB 3GPD PDB 4WNC PDB 4WNI PDB 6ADE PDB 6IQ6 PDB 6M61 PDB 6YND PDB 6YNE PDB 6YNF PDB 6YNH Pfam PF02800 Pfam PF00044 PROSITE PS00071 OMIM 138400 DisGeNET 2597 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}. P00533 EBI-1188138 0.79 Q04864 EBI-360834 0.00 Q99759 EBI-362433 0.00 Q99558 EBI-363130 0.00 O43353 EBI-363706 0.00 Q9UHD2 EBI-7476716 0.56 P20333 EBI-364783 0.00 Q13077 EBI-365002 0.00 P60709 EBI-353790 0.40 Q13268 EBI-354614 0.40 Q92993 EBI-25857246 0.56 P15927 EBI-707645 0.51 Q9NXU5 EBI-728720 0.00 Q9BX70 EBI-728775 0.00 Q16363 EBI-729012 0.00 Q15102 EBI-729096 0.00 Q9UN74 EBI-729117 0.00 O00231 EBI-729159 0.00 P50453 EBI-729279 0.00 P04183 EBI-7398156 0.55 O43504 EBI-730105 0.00 Q06830 EBI-730582 0.00 P08238 EBI-709762 0.35 O60861 EBI-7720940 0.40 O60739 EBI-1072279 0.00 O00141 EBI-1075257 0.00 Q9H0J4 EBI-1078469 0.00 P10599 EBI-25857222 0.68 P63104 EBI-7194241 0.40 Q27957 EBI-7025783 0.27 P01023 EBI-7183126 0.35 Q14653 EBI-7476716 0.35 P32121 EBI-1642567 0.35 P42771 EBI-1641665 0.35 P48637 EBI-7830840 0.40 P28482 EBI-2115126 0.00 O15264 EBI-2255044 0.35 Q07820 EBI-7173317 0.35 P00558 EBI-7907378 0.54 P04406 EBI-7907471 0.59 Q3KSU8 EBI-2622922 0.37 P03372 EBI-2877710 0.35 Q99459 EBI-7954144 0.35 P12004 EBI-8302829 0.57 Q9H492 EBI-3044058 0.35 Q9GZQ8 EBI-3045543 0.35 P60520 EBI-3046676 0.35 Q9H0R8 EBI-3048562 0.35 O95166 EBI-3050465 0.35 P49768 EBI-3385373 0.37 Q06187 EBI-3505275 0.35 P43351 EBI-3646827 0.35 Q96Q15 EBI-3903995 0.35 Q15051 EBI-4286917 0.35 P04083 EBI-7095327 0.37 P20073 EBI-7098273 0.37 P55957 EBI-7104540 0.37 P24522 EBI-7152962 0.37 P68032 EBI-7157149 0.37 P00505 EBI-7157215 0.37 Q14469 EBI-7157494 0.37 Q15046 EBI-7157574 0.37 Q13952 EBI-7157626 0.37 Q99650 EBI-7157758 0.37 Q92882 EBI-7157808 0.37 P52756 EBI-7157858 0.37 P62258 EBI-7157955 0.37 P49841 EBI-7165309 0.55 Q9Y6H6 EBI-7183576 0.37 Q16637 EBI-7389132 0.37 P37840 EBI-7391160 0.37 P18084 EBI-5659917 0.00 P15336 EBI-5529812 0.35 P04487 EBI-6157560 0.35 P0C1C6 EBI-6158469 0.35 P03496 EBI-6158649 0.35 P19320 EBI-6189915 0.35 Q00537 EBI-6380868 0.35 Q13164 EBI-6380894 0.35 Q86VP6 EBI-21322532 0.35 Q13616 EBI-21323857 0.35 Q92905 EBI-21325777 0.35 Q13617 EBI-21327106 0.35 Q13620 EBI-21327757 0.53 Q15843 EBI-21328206 0.35 Q7L5N1 EBI-21328549 0.35 Q13618 EBI-21329068 0.35 Q9WMX2 EBI-9078245 0.37 P42858 EBI-9053301 0.67 P48147 EBI-9550467 0.64 Q15303 EBI-9687710 0.37 P04626 EBI-9687897 0.55 Q60823 EBI-9702520 0.42 Q13043 EBI-10049589 0.35 P51451 EBI-10102766 0.35 P05109 EBI-10098112 0.65 P35228 EBI-10091932 0.50 P06702 EBI-10091932 0.35 Q00325 EBI-10091892 0.35 P62805 EBI-10091892 0.35 Q96FW1 EBI-10770198 0.35 P19838 EBI-11322719 0.35 P05412 EBI-11323169 0.35 Q13098 EBI-10766278 0.35 O35071 EBI-10996866 0.35 P36895 EBI-11008521 0.35 Q8N2N9 EBI-11053871 0.35 Q96G25 EBI-11053871 0.35 Q8NG31 EBI-11053871 0.35 P48039 EBI-11575898 0.37 P54274 EBI-11310274 0.37 Q9BSI4 EBI-11310284 0.51 Q96AP0 EBI-11310294 0.37 Q9NUX5 EBI-11310304 0.37 Q9UBX2 EBI-11614356 0.35 P06929 EBI-26506766 0.37 P06427 EBI-26507442 0.37 P24835 EBI-26507526 0.37 P56945 EBI-15099384 0.35 Q6IQ23 EBI-16398399 0.35 Q16082 EBI-15487660 0.37 Q9BZE9 EBI-21690090 0.35 O14556 EBI-21690090 0.35 Q15915 EBI-21696712 0.35 Q92696 EBI-21736347 0.35 Q920M9 EBI-15571980 0.44 Q7MWG4 EBI-15591000 0.40 P16749 EBI-15833083 0.41 P04075 EBI-16426431 0.35 P00441 EBI-20303881 0.50 P25705 EBI-21929063 0.35 Q96HJ9 EBI-21929593 0.35 Q9Y2Z9 EBI-21930056 0.35 O00483 EBI-21930681 0.35 O75489 EBI-21931040 0.35 Q96FC7 EBI-21931532 0.35 Q9H6K4 EBI-21931410 0.35 Q3MIX3 EBI-21935154 0.35 P0C7P0 EBI-21935930 0.35 Q99807 EBI-21936186 0.35 Q8TB22 EBI-21937705 0.35 Q9NQH7 EBI-21937834 0.35 Q9C002 EBI-21938261 0.35 Q9HAC7 EBI-21938493 0.35 O00746 EBI-21940120 0.35 Q8N3Z0 EBI-21940471 0.35 Q86U44 EBI-20594935 0.35 Q9HCE5 EBI-20595531 0.35 Q8TDU9 EBI-20807086 0.37 P02730 EBI-20795573 0.40 P04920 EBI-20795563 0.40 P10636 EBI-20799352 0.35 Q8NFJ5 EBI-20902056 0.40 Q6A163 EBI-20904168 0.40 O76041 EBI-20904328 0.40 Q03936 EBI-20906200 0.40 P04908 EBI-20906576 0.40 Q5TZA2 EBI-20909272 0.40 P57740 EBI-20910640 0.40 Q99442 EBI-20911552 0.40 O75602 EBI-20914552 0.40 O95425 EBI-20916064 0.40 Q5VST9 EBI-20920604 0.40 Q502W7 EBI-20925058 0.40 P48751 EBI-20926210 0.40 Q00535 EBI-20926978 0.40 A1A4G5 EBI-20927136 0.40 Q69YH5 EBI-20928976 0.40 Q13283 EBI-20929856 0.40 Q63HK5 EBI-20929960 0.40 Q5T6S3 EBI-20931832 0.40 Q6P1J9 EBI-20932880 0.40 O95139 EBI-20934708 0.40 O15015 EBI-20935244 0.40 A8MT65 EBI-20937020 0.40 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 O96013 EBI-26962273 0.35 Q5T7N2 EBI-20993270 0.46 P52292 EBI-20993846 0.35 Q9H9Z2 EBI-20993846 0.35 P13693 EBI-20992046 0.35 Q5S007 EBI-21360986 0.35 O60260 EBI-21135687 0.35 P13569 EBI-25416349 0.35 Q16526 EBI-21981854 0.35 O95292 EBI-21993601 0.35 P0DOF2 EBI-25603126 0.35 P69479 EBI-25568044 0.35 Q9BY14 EBI-25504841 0.35 P0DTD1 EBI-25509444 0.35 P0DTC3 EBI-25510118 0.35 P0DTD3 EBI-25510342 0.35 P17612 EBI-25857214 0.56 Q9UIJ7 EBI-25857278 0.56 Q8WUY3 EBI-25857270 0.56 Q9UHX1 EBI-25857262 0.56 O00471 EBI-25857254 0.56 Q9BPW9 EBI-25857238 0.56 O75344 EBI-25857230 0.56 P06241 EBI-25857206 0.56 P35222 EBI-25857198 0.56 Q14194 EBI-25857190 0.56 Q9UQM7 EBI-25857182 0.56 Q6UY14 EBI-25857286 0.56 Q96GZ6 EBI-25857296 0.56 Q8NEA9 EBI-25857304 0.56 P05067 EBI-25936448 0.56 Q7Z417 EBI-26513452 0.37 Q9BYB0 EBI-26514195 0.37 P51531 EBI-26515253 0.37 P49815 EBI-26516083 0.37 P52298 EBI-26397282 0.35 Q09161 EBI-26399030 0.35 Q8TB24 EBI-26518569 0.35 Q5U458 EBI-26450034 0.35 P14240 EBI-26968430 0.35 P60880 EBI-26578093 0.35 Q99608 EBI-26955247 0.27 P06401 EBI-26871590 0.35 P35226 EBI-27109494 0.35 Q92630 EBI-28952196 0.27 P42695 EBI-28951349 0.50 P0DTC9 EBI-28955760 0.35 Q13619 EBI-30863570 0.35 Q8WV16 EBI-30863977 0.35 Q05DH4 EBI-34574576 0.27 GO:0005737 GO:0005829 GO:0070062 GO:0097452 GO:0043231 GO:0005811 GO:0016020 GO:0015630 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:1990904 GO:0031982 GO:0019828 GO:0097718 GO:0004365 GO:0042802 GO:0008017 GO:0051287 GO:0050661 GO:0035605 GO:0061844 GO:0071346 GO:0050832 GO:0006006 GO:0006096 GO:0051873 GO:0031640 GO:0000226 GO:0010951 GO:0017148 GO:0051402 GO:0035606 GO:0001819 GO:0043123 GO:0032481 GO:0050821 GO:0016241 Unknown UniProt Sequence Analysis MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE 335 Q9C5H9 Gamma-tubulin GCP2 3702 None SL-0178 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. UNIPROT Q9C5H9 UNIPROT F4KGZ8 UNIPROT Q9LF43 Pfam PF04130 Pfam PF17681 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}. Q9LT56 EBI-4521088 0.37 GO:0005938 GO:0055028 GO:0005737 GO:0000923 GO:0000930 GO:0008275 GO:0005635 GO:0000922 GO:0043015 GO:0031122 GO:0048229 GO:0033566 GO:0051321 GO:0007020 GO:0000278 GO:0090063 GO:0051225 Unknown UniProt Sequence Analysis MESMTPISCPTTPRWNQDRPFLTGRFHQETRASSKFADSKRFTLDSSSSGVEQAIGCYDTPVQELIVIDDLLSALVGIEGRYISIKRFHGKEDSIAFQVDPSMDLALQELAKRIFPLCEYYLLIDQFVESSSQFKNGLVNHAFAAALRALLLDYQAMVAQLEHQFRLGRLSIQGLWFYCQPMMGSMRALAAVIQQASTKQFVGSGVLNLLQSQAKAMAGDNSVRSLLEKMTECASNAYLSILERWVYEGIIDDPYGEFFIAENRSLKKESLSQDSTAKYWSQRYSLKDTIPGFLANIAATILTTGKYLNVMRECGHNVQVPISERSKLTIFGSNHHYLECIKAAHEFASIELVNLIKDKYDLVGRLRSIKHYLLLDQGDFLVHFMDIAREELNKKVHEISVEKLQSLLDLALRTTAAAADPRHEDLTCCVDRASLLTTLGMHKDTDSNSIEDPMSITGLETFSLSYKVQWPLSIVISKKALSKYQLIFRFLFHCKHVERQLCGAWQIHQGIRSMNSKGTAILRSSLLCRSMLKFISSLLHYLTFEVLEPNWHVMHDRLQSTRSVDEVIQHHDFFLDKCLRGCLLLLPDVLKKMEKLKSVCLQYAAATQWLISSSIDINSQSHPQKTMIRDTTVTESIFNFEREFNSELQSLGPVLSKGSQAEPYLTHLSQWILGVSKE 678 Q9FG37 Gamma-tubulin GCP3 3702 None SL-0178 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. UNIPROT Q9FG37 Pfam PF04130 Pfam PF17681 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. Q39069 EBI-2651346 0.00 GO:0005938 GO:0055028 GO:0005737 GO:0009898 GO:0000923 GO:0000930 GO:0008275 GO:0005874 GO:0005635 GO:0005819 GO:0000922 GO:0043015 GO:0015631 GO:0031122 GO:0051321 GO:0007020 GO:0000278 GO:0090063 GO:0009624 GO:0051225 Unknown UniProt Sequence Analysis MEDDDQQKAADLVQELVLRLVSQNPQTPNLDPNSPAFLKTLRYAFRILSSRLTPSVLPDATAIAESLKRRLATQGKSSDALAFADLYTKFASKTGPGSVNNKWALVYLLKIVSDDRKSAINGLDSSVLLPNLGIGDTGNGVLSRGEAKKKDWSNGVLLVSKDPENLRDIAFREYAILVKEENEVTEEVLVRDVLYASQGIDGKYVKFNSEIDGYAVQESVKVPRATRIMVRMLSELGWLFRKVKTFITESMDRFPAEDVGTVGQAFCAALQDELSDYYKLLAVLEAQAMNPIPLVSESASSNNYLSLRRLSVWFAEPMVKMRLMAVLVDKCKVLRGGAMAGAIHLHAQHGDPLVHDFMMSLLRCVCSPLFEMVRSWVLEGELEDTFGEFFVVGQPVKVDLLWREGYKLHPAMLPSFISPSLAQRILRTGKSINFLRVCCDDHGWADAASEAAAASGTTTRRGGLGYGETDALEHLVTEAAKRIDKHLLDVLYKRYKFKEHCLAIKRYLLLGQGDFVQYLMDIVGPKLSEPANNISSFELAGFLEAAIRASNAQYDDRDMLDRLRVKMMPHGSGDRGWDVFSLEYEARVPLDTVFTESVLSKYLRVFNFLWKLKRVEHALIGIWKTMKPNCITSNSFVKLQSSVKLQLLSALRRCQVLWNEMNHFVTNFQYYIMFEVLEVSWSNFSKEMEAAKDLDDLLAAHEKYLNAIVGKSLLGEQSQTIRESLFVLFELILRFRSHADRLYEGIHELQIRSKESGREKNKSQEPGSWISEGRKGLTQRAGEFLQSMSQDMDSIAKEYTSSLDGFLSLLPLQQSVDLKFLFFRLDFTEFYSRLHSKG 838 O56860 p3 gag 53182 None SL-0382 [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}. UNIPROT O56860 Pfam PF03276 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}. GO:0042025 GO:0044220 GO:0044163 GO:0019013 GO:0003677 GO:0003723 GO:0075521 GO:0046718 GO:0019076 Unknown UniProt Sequence Analysis MARELNPLQLQQLYINNGLQPNPGHGDIIAVRFTGGPWGPGDRWARVTIRLQDNTGQPLQVPGYDLEPGIINLREDILIAGPYNLIRTAFLDLEPARGPERHGPFGDGRLQPGDGLSEGFQPITDEEIQAEVGTIGAARNEIRLLREALQRLQAGGVGRPIPGAVLQPQPVIGPVIPINHLRSVIGNTPPNPRDVALWLGRSTAAIEGVFPIVDQVTRMRVVNALVASHPGLTLTENEAGSWNAAISALWRKAHGAAAQHELAGVLSDINKKEGIQTAFNLGMQFTDGNWSLVWGIIRTLLPGQALVTNAQSQFDLMGDDIQRAENFPRVINNLYTMLGLNIHGQSIRPRVQTQPLQTRPRNPGRSQQGQLNQPRPQNRANQSYRPPRQQQQHSDVPEQRDQRGPSQPPRGSGGGYNFRRNPQQPQRYGQGPPGPNPYRRFGDGGNPQQQGPPPNRGPDQGPRPGGNPRGGGRGQGPRNGGGSAAAVHTVKASENETKNGSAEAVDGGKKGGKD 514 O14976 Cyclin-G-associated GAK 9606 None SL-0198 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. UNIPROT O14976 UNIPROT Q5U4P5 UNIPROT Q9BVY6 PDB 4C57 PDB 4C58 PDB 4C59 PDB 4O38 PDB 4Y8D PDB 5Y7Z PDB 5Y80 Pfam PF00069 Pfam PF10409 PROSITE PS51182 PROSITE PS50076 PROSITE PS51181 PROSITE PS50011 PROSITE PS00108 OMIM 602052 DisGeNET 2580 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}. O14966 EBI-9247728 0.35 O15169 EBI-731365 0.00 O60763 EBI-759358 0.37 P10275 EBI-1632203 0.37 Q9Q2G4 EBI-6174875 0.35 Q9NQ11 EBI-6377262 0.51 Q5S007 EBI-9247177 0.79 P11142 EBI-9655962 0.69 Q9UL15 EBI-9655962 0.35 Q38SD2 EBI-9659083 0.44 Q76MZ3 EBI-10991736 0.35 A2AUM9 EBI-10994361 0.35 P63005 EBI-11041417 0.35 P10126 EBI-11048962 0.35 G3X972 EBI-11079358 0.35 P09497 EBI-11081190 0.35 Q9NYZ3 EBI-11081743 0.35 Q13492 EBI-11082344 0.35 Q00610 EBI-11082478 0.35 O15027 EBI-11083608 0.35 Q9Z1Z0 EBI-11112182 0.35 P15735 EBI-11135895 0.35 P51805 EBI-11150908 0.35 Q07912 EBI-11150908 0.35 Q96CW1 EBI-11150908 0.35 Q9H2Y7 EBI-11150908 0.35 Q5TB80 EBI-11150908 0.35 Q8TEH3 EBI-11150908 0.35 Q8N684 EBI-11150908 0.35 Q9Y496 EBI-11150908 0.35 Q14789 EBI-11150908 0.35 Q2M2I8 EBI-11150908 0.35 Q8N556 EBI-11150908 0.35 O43175 EBI-11150908 0.35 O75146 EBI-11150908 0.53 P47756 EBI-11150908 0.35 P27482 EBI-11150908 0.35 P53992 EBI-11150908 0.35 Q14677 EBI-11150908 0.35 Q9UHB6 EBI-11150908 0.35 P49757 EBI-11150908 0.35 Q9ULH0 EBI-11150908 0.35 P42566 EBI-11150908 0.35 P55735 EBI-11150908 0.35 Q13813 EBI-11150908 0.35 Q96PK6 EBI-11150908 0.35 E9PK67 EBI-11150908 0.35 Q96FJ0 EBI-11150908 0.53 Q8IVT2 EBI-11150908 0.35 P53675 EBI-11150908 0.35 P09496 EBI-11150908 0.35 P08047 EBI-11150908 0.35 Q9H0K6 EBI-11150908 0.35 Q8WXE9 EBI-11150908 0.35 Q27J81 EBI-11150908 0.35 P14384 EBI-11150908 0.35 P28066 EBI-11150908 0.35 Q3B7T1 EBI-11150908 0.35 Q6ZRV2 EBI-11150908 0.35 Q9UBH6 EBI-11150908 0.35 O00159 EBI-11150908 0.35 Q16643 EBI-11150908 0.35 Q5T0W9 EBI-11150908 0.35 O00443 EBI-11150908 0.35 H0YEF7 EBI-11150908 0.35 Q9NSY1 EBI-11150908 0.35 F5GWT4 EBI-11150908 0.35 Q9UM54 EBI-11150908 0.35 Q8N3V7 EBI-11150908 0.35 P62158 EBI-11150908 0.35 Q9UK73 EBI-11150908 0.35 P63010 EBI-11150908 0.35 O94973 EBI-11150908 0.35 Q13470 EBI-11150908 0.35 Q8TDG2 EBI-11150908 0.35 O00291 EBI-11150908 0.35 O95782 EBI-11150908 0.35 Q9BY43 EBI-11150908 0.35 P98082 EBI-11150908 0.35 P29703 EBI-11525188 0.56 P56945 EBI-15099463 0.35 Q8IWL3 EBI-13943458 0.35 Q6IQ23 EBI-16398399 0.35 Q8TBP5 EBI-21502646 0.35 Q9P296 EBI-21519943 0.35 Q8N3R9 EBI-21627185 0.35 Q9UJ41 EBI-21644136 0.35 O95630 EBI-21667922 0.35 Q9NZL4 EBI-21711136 0.35 Q09019 EBI-21714883 0.35 Q9ULV8 EBI-21715242 0.35 Q8N2M8 EBI-21714908 0.35 Q96SL4 EBI-21714987 0.35 Q9NSE4 EBI-21715157 0.35 Q01968 EBI-16412116 0.35 Q9Y6W8 EBI-16721689 0.35 O43493 EBI-16800265 0.27 Q9Y4C4 EBI-20590176 0.44 Q9Y586 EBI-21261050 0.35 P49023 EBI-25376663 0.35 Q9C0B5 EBI-25637382 0.35 P51617 EBI-28935882 0.35 Q9BYP7 EBI-28946054 0.35 P31947 EBI-30814567 0.44 P04637 EBI-34581131 0.35 GO:0005737 GO:0005829 GO:0005925 GO:0005794 GO:0043231 GO:0016020 GO:0048471 GO:0098793 GO:0031982 GO:0005524 GO:0051087 GO:0030276 GO:0030332 GO:0106310 GO:0004674 GO:0007049 GO:0051085 GO:0072318 GO:1905224 GO:0072583 GO:0007029 GO:0007030 GO:0090160 GO:0010977 GO:0034067 GO:0072659 GO:0006468 GO:0006898 GO:0016191 Unknown UniProt Sequence Analysis MSLLQSALDFLAGPGSLGGASGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDVGSGREYALKRLLSNEEEKNRAIIQEVCFMKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEITRNTTPMYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAARNVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYMCDMVAEEPITPHSKPILVRAVVMTPVPLFSKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSREAPPWENSSMRGLNPKILFSSREEQQDILSKFGKPELPRQPGSTAQYDAGAGSPEAEPTDSDSPPSSSADASRFLHTLDWQEEKEAETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQEDGVDLLGLHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAWTETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPDPFADLGDLSSGLQGSPAGFPPGGFIPKTATTPKGSSSWQTSRPPAQGASWPPQAKPPPKACTQPRPNYASNFSVIGAREERGVRAPSFAQKPKVSENDFEDLLSNQGFSSRSDKKGPKTIAEMRKQDLAKDTDPLKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVGMADLVAPEQVKKHYRRAVLAVHPDKAAGQPYEQHAKMIFMELNDAWSEFENQGSRPLF 1311 Q99KY4 Cyclin-G-associated Gak 10090 None SL-0198 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}. UNIPROT Q99KY4 UNIPROT Q6P1I8 UNIPROT Q6P9S5 UNIPROT Q8BM74 UNIPROT Q8K0Q4 Pfam PF00226 Pfam PF00069 Pfam PF10409 PROSITE PS51182 PROSITE PS50076 PROSITE PS51181 PROSITE PS50011 PROSITE PS00108 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}. P97378 EBI-7652953 0.51 Q8CI32 EBI-9248889 0.40 GO:0005737 GO:0005829 GO:0005925 GO:0005794 GO:0043231 GO:0048471 GO:0031982 GO:0005524 GO:0030276 GO:0030332 GO:0106310 GO:0004674 GO:0007049 GO:0072318 GO:1905224 GO:0072583 GO:0007029 GO:0009913 GO:0002064 GO:0061436 GO:0048853 GO:0007030 GO:0090160 GO:0035622 GO:0030216 GO:0010977 GO:0061351 GO:0060563 GO:2000179 GO:2000648 GO:0034067 GO:0072659 GO:0006468 GO:0006898 GO:0048863 GO:0072089 Unknown UniProt Sequence Analysis MSLLQSALDFLAGPGSLGGAAGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDLGSGREYALKRLLSNEEEKNRAIIQEVCFLKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLKRVECKGPLSCDSILKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPVERLSIAEVVRQLQEIAAARNVNPKAPITELLEQNGGYGNSGPSRAQPPCGGTVNSSGVLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRAPHLHSLYTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYVCDMVAEEPITPHSKPMLVKSVVMTPVPLFSKQRNGCRPFCEVYVGEERVTTTSQEYDRMKEFKIEDGKAVIPLGVTVQGDVLIIIYHARATLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSREAPPWENTSLRGLNPKILFSNREEQQDILSKFGKPELPRQPGSTAQYDAEAGSPEAEITESDSPQSSSTDTNHFLHTLDWQEEKEPETGLDNTSPKESQSVLIADGDGSEVSDEEEASFPSEERKPGAGEDTPRLAAGTKQQDLIFDVGMLAAPQEPVQPEEGVDLLGLHSEGDLRPAAPLQACGVPSSNTDLLSCLLEPSDAAQVGPPGDLLGGEAPLLLASPVSPLGLQNNLQGKVPDTVDPFDQFLLSSNSDTQPCSKPDLFGEFLNSDSVASSTAFPSTHSAPPPSCSTAFLHLGDLPAEPSKVIASSSHPDLLGGWDTWADTATPGPASIPVPEGTLFSSAGHPAPPGPNPSQTKSQNLDPFADLSDLSSSLQGLPAGLPAGGFVGAPAPTQKSNSPWQANRPTAPGTSWTPQAKPAPRASEQLRSHFSVIGAREERGVRVPSFAQKPKVSENDFEDLLPNQGFSKSDKKGPKTMAEMRKQELARDTDPLKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVSMADLVTPEQVKKQYRRAVLVVHPDKATGQPYEQYAKMIFMELNDAWSEFENQGSRPLF 1305 P97874 Cyclin-G-associated Gak 10116 None SL-0198 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}. UNIPROT P97874 Pfam PF00226 Pfam PF00069 Pfam PF10409 PROSITE PS51182 PROSITE PS50076 PROSITE PS51181 PROSITE PS50011 PROSITE PS00108 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}. P39052 EBI-6947872 0.38 Q5XIE8 EBI-26440627 0.35 GO:0005737 GO:0005829 GO:0005925 GO:0005794 GO:0043231 GO:0048471 GO:0031982 GO:0005524 GO:0030276 GO:0030332 GO:0106310 GO:0004674 GO:0007049 GO:0048468 GO:0072318 GO:1905224 GO:0072583 GO:0007029 GO:0009913 GO:0002064 GO:0061436 GO:0048853 GO:0007030 GO:0090160 GO:0035622 GO:0030216 GO:0010977 GO:0061351 GO:0060563 GO:2000179 GO:2000648 GO:0034067 GO:0072659 GO:0006468 GO:0006898 GO:0048863 GO:0072089 Unknown UniProt Sequence Analysis MSLLQSALDFLAGPGSLGGAAGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDLGSGREYALKRLLSNEEEKNRAIIQEVCFLKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLRRVECKGPLSCDSILKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRGMLKVNPEERLSIAEVVRQLQEIAAARNVNPKAPITELLEQNGGYGNSGPSRAQPPSGGPVNSSGVLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRAPHLHSLYTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYVCDMVAEEPITPHSKPMLVKSVVMTPVPLFSKQRNGCRPFCEVYVGEERVTTTSQEYDRMKEFKIEDGKAVIPLGITVQGDVLTIIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSRDVPPWENTSLRGLNPKILFSNREEQQDILSKFGKPELPRQPGSTAQYDAEAGSPEAEITESDSPQSSSTDTNHFLHTLDWQEEKDPETGVDNTSPKESQSNLIADGDGSEVSDEEEASCPSEERKPGAGEDTPRLAAGTRQQDLIFDVGMLAAPQEPVQPEEGVDLLGLHSEGDLRPAAPLQASGVQSSNTDLLSSLLEPSDASQVGPPGDLLGGETPLLLASPVSLLGVQSNLQGKVPDTVDPFDQFLLPSSSDTQPCSKPDLFGEFLNSDSVASSTAFPSTHSAPPPSCSTAFLHLGDLPAEPNKVIASSSHPDLLGGWDTWAETALPGPASMPVPEGTLFSSAGHPAPPGPNPSQTKSQNPDPFADLSDLSSSLQGLPAGLPAGSFVGTSATTHKSNSSWQTTRPTAPGTSWPPQAKPAPRASEQLRSHFSVIGAREERGVRAPSFAQKPKVSENDFEDLLPNQGFSKSDKKGPKTMAEMRKQELARDTDPFKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVSMADLVTPEQVKKQYRRAVLVVHPDKATGQPYEQSAKMIFMELNDAWSEFENQGSRPLF 1305 O60318 Germinal-center MCM3AP 9606 None SL-0178 SL-0185 [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}. UNIPROT O60318 UNIPROT C9JL56 UNIPROT Q2M3C1 UNIPROT Q6PJP6 UNIPROT Q9BSY5 UNIPROT Q9UMT4 PDB 4DHX Pfam PF16766 Pfam PF16769 Pfam PF16768 Pfam PF03399 PROSITE PS50250 OMIM 603294 OMIM 618124 DisGeNET 8888 [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}. 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. O94985 EBI-311611 0.37 Q9NYQ7 EBI-308834 0.37 P84022 EBI-7232431 0.37 O15198 EBI-7261838 0.37 Q9NPA8 EBI-734236 0.00 Q9P0N5 EBI-735082 0.00 Q9UKK9 EBI-735262 0.00 Q14194 EBI-737126 0.00 Q5NGE6 EBI-2796304 0.00 Q5NIJ3 EBI-2804997 0.00 A0A0F7REH3 EBI-2816349 0.00 Q81KK8 EBI-2829932 0.00 A0A2U2GVV1 EBI-2846769 0.00 Q7CIS2 EBI-2864681 0.00 Q0WC40 EBI-2864674 0.00 P25054 EBI-3437195 0.00 P60953 EBI-3438542 0.00 P63000 EBI-3449487 0.00 P30304 EBI-3906561 0.37 P62487 EBI-3912322 0.37 Q09472 EBI-3929206 0.37 Q6P1J9 EBI-7116410 0.37 Q9BPY3 EBI-7148250 0.37 Q9H5I1 EBI-7393874 0.37 Q9H5J8 EBI-7394492 0.37 Q15714 EBI-7408152 0.37 Q8BUH2 EBI-10991696 0.35 Q9CYN2 EBI-11000176 0.35 Q9BVG8 EBI-11004364 0.35 Q9NSK0 EBI-11004456 0.35 P13533 EBI-11004546 0.35 P54132 EBI-11057507 0.35 Q9R1K9 EBI-11111151 0.35 Q6P5F9 EBI-11603310 0.35 C5E524 EBI-12584088 0.35 Q194T2 EBI-12587357 0.35 Q9H0B3 EBI-21526575 0.35 Q12798 EBI-21576600 0.35 Q9BTL4 EBI-21675209 0.35 P60896 EBI-15970583 0.35 Q5JVF3 EBI-15970583 0.35 Q15149 EBI-20929080 0.40 P12004 EBI-21256683 0.37 Q9NRI5 EBI-21391268 0.00 P0DOF2 EBI-25603126 0.35 P0DTC5 EBI-25685699 0.35 P07947 EBI-30849071 0.44 GO:0005694 GO:0005737 GO:0005829 GO:0031965 GO:0044615 GO:0005654 GO:0005634 GO:0070390 GO:0003682 GO:0010484 GO:0004402 GO:0042393 GO:0003676 GO:0006406 GO:0034728 GO:0016973 GO:0015031 GO:0016446 Unknown UniProt Sequence Analysis MNPTNPFSGQQPSAFSASSSNVGTLPSKPPFRFGQPSLFGQNSTLSGKSSGFSQVSSFPASSGVSHSSSVQTLGFTQTSSVGPFSGLEHTSTFVATSGPSSSSVLGNTGFSFKSPTSVGAFPSTSAFGQEAGEIVNSGFGKTEFSFKPLENAVFKPILGAESEPEKTQSQIASGFFTFSHPISSAPGGLAPFSFPQVTSSSATTSNFTFSKPVSSNNSLSAFTPALSNQNVEEEKRGPKSIFGSSNNSFSSFPVSSAVLGEPFQASKAGVRQGCEEAVSQVEPLPSLMKGLKRKEDQDRSPRRHGHEPAEDSDPLSRGDHPPDKRPVRLNRPRGGTLFGRTIQDVFKSNKEVGRLGNKEAKKETGFVESAESDHMAIPGGNQSVLAPSRIPGVNKEEETESREKKEDSLRGTPARQSNRSESTDSLGGLSPSEVTAIQCKNIPDYLNDRTILENHFGKIAKVQRIFTRRSKKLAVVHFFDHASAALARKKGKSLHKDMAIFWHRKKISPNKKPFSLKEKKPGDGEVSPSTEDAPFQHSPLGKAAGRTGASSLLNKSSPVKKPSLLKAHQFEGDSFDSASEGSEGLGPCVLSLSTLIGTVAETSKEKYRLLDQRDRIMRQARVKRTDLDKARTFVGTCLDMCPEKERYMRETRSQLSVFEVVPGTDQVDHAAAVKEYSRSSADQEEPLPHELRPLPVLSRTMDYLVTQIMDQKEGSLRDWYDFVWNRTRGIRKDITQQHLCDPLTVSLIEKCTRFHIHCAHFMCEEPMSSFDAKINNENMTKCLQSLKEMYQDLRNKGVFCASEAEFQGYNVLLSLNKGDILREVQQFHPAVRNSSEVKFAVQAFAALNSNNFVRFFKLVQSASYLNACLLHCYFSQIRKDALRALNFAYTVSTQRSTIFPLDGVVRMLLFRDCEEATDFLTCHGLTVSDGCVELNRSAFLEPEGLSKTRKSVFITRKLTVSVGEIVNGGPLPPVPRHTPVCSFNSQNKYIGESLAAELPVSTQRPGSDTVGGGRGEECGVEPDAPLSSLPQSLPAPAPSPVPLPPVLALTPSVAPSLFQLSVQPEPPPPEPVPMYSDEDLAQVVDELIQEALQRDCEEVGSAGAAYAAAALGVSNAAMEDLLTAATTGILRHIAAEEVSKERERREQERQRAEEERLKQERELVLSELSQGLAVELMERVMMEFVRETCSQELKNAVETDQRVRVARCCEDVCAHLVDLFLVEEIFQTAKETLQELQCFCKYLQRWREAVTARKKLRRQMRAFPAAPCCVDVSDRLRALAPSAECPIAEENLARGLLDLGHAGRLGISCTRLRRLRNKTAHQMKVQHFYQQLLSDVAWASLDLPSLVAEHLPGRQEHVFWKLVLVLPDVEEQSPESCGRILANWLKVKFMGDEGSVDDTSSDAGGIQTLSLFNSLSSKGDQMISVNVCIKVAHGALSDGAIDAVETQKDLLGASGLMLLLPPKMKSEDMAEEDVYWLSALLQLKQLLQAKPFQPALPLVVLVPSPGGDAVEKEVEDGLMLQDLVSAKLISDYTVTEIPDTINDLQGSTKVLQAVQWLVSHCPHSLDLCCQTLIQYVEDGIGHEFSGRFFHDRRERRLGGLASQEPGAIIELFNSVLQFLASVVSSEQLCDLSWPVTEFAEAGGSRLLPHLHWNAPEHLAWLKQAVLGFQLPQMDLPPLGAPWLPVCSMVVQYASQIPSSRQTQPVLQSQVENLLHRTYCRWKSKSPSPVHGAGPSVMEIPWDDLIALCINHKLRDWTPPRLPVTSEALSEDGQICVYFFKNDLKKYDVPLSWEQARLQTQKELQLREGRLAIKPFHPSANNFPIPLLHMHRNWKRSTECAQEGRIPSTEDLMRGASAEELLAQCLSSSLLLEKEENKRFEDQLQQWLSEDSGAFTDLTSLPLYLPQTLVSLSHTIEPVMKTSVTTSPQSDMMREQLQLSEATGTCLGERLKHLERLIRSSREEEVASELHLSALLDMVDI 1980 Q9WUU9 Germinal-center Mcm3ap 10090 None SL-0178 SL-0185 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}. UNIPROT Q9WUU9 UNIPROT Q7TS87 Pfam PF16766 Pfam PF16769 Pfam PF16768 Pfam PF03399 PROSITE PS50250 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}. Q9Z0S9 EBI-20974677 0.37 GO:0005694 GO:0005737 GO:0005829 GO:0031965 GO:0044615 GO:0005654 GO:0005634 GO:0070390 GO:0003682 GO:0010484 GO:0004402 GO:0042393 GO:0003676 GO:0006406 GO:0034728 GO:0016973 GO:0015031 GO:0016446 Unknown UniProt Sequence Analysis MHPVNPFGGQQPSAFAVSSSTTGTYQTKSPFRFGQPSLFGQNSTPSKSLAFSQVPSFATPSGGSHSSSLPAFGLTQTSSVGLFSSLESTPSFAATSSSSVPGNTAFSFKSTSSVGVFPSGATFGPETGEVAGSGFRKTEFKFKPLENAVFKPIPGPESEPEKTQSQISSGFFTFSHPVGSGSGGLTPFSFPQVTNSSVTSSSFIFSKPVTSNTPAFASPLSNQNVEEEKRVSTSAFGSSNSSFSTFPTASPGSLGEPFPANKPSLRQGCEEAISQVEPLPTLMKGLKRKEDQDRSPRRHCHEAAEDPDPLSRGDHPPDKRPVRLNRPRGGTLFGRTIQEVFKSNKEAGRLGSKESKESGFAEPGESDHAAVPGGSQSTMVPSRLPAVTKEEEESRDEKEDSLRGKSVRQSKRREEWIYSLGGVSSLELTAIQCKNIPDYLNDRAILEKHFSKIAKVQRVFTRRSKKLAVIHFFDHASAALARKKGKGLHKDVVIFWHKKKISPSKKLFPLKEKLGESEASQGIEDSPFQHSPLSKPIVRPAAGSLLSKSSPVKKPSLLKMHQFEADPFDSGSEGSEGLGSCVSSLSTLIGTVADTSEEKYRLLDQRDRIMRQARVKRTDLDKARAFVGTCPDMCPEKERYLRETRSQLSVFEVVPGTDQVDHAAAVKEYSRSSADQEEPLPHELRPSAVLSRTMDYLVTQIMDQKEGSLRDWYDFVWNRTRGIRKDITQQHLCDPLTVSLIEKCTRFHIHCAHFMCEEPMSSFDAKINNENMTKCLQSLKEMYQDLRNKGVFCASEAEFQGYNVLLNLNKGDILREVQQFHPDVRNSPEVNFAVQAFAALNSNNFVRFFKLVQSASYLNACLLHCYFNQIRKDALRALNVAYTVSTQRSTVFPLDGVVRMLLFRDSEEATNFLNYHGLTVADGCVELNRSAFLEPEGLCKARKSVFIGRKLTVSVGEVVNGGPLPPVPRHTPVCSFNSQNKYVGESLATELPISTQRAGGDPAGGGRGEDCEAEVDVPTLAVLPQPPPASSATPALHVQPLAPAAAPSLLQASTQPEVLLPKPAPVYSDSDLVQVVDELIQEALQVDCEEVSSAGAAYVAAALGVSNAAVEDLITAATTGILRHVAAEEVSMERQRLEEEKQRAEEERLKQERELMLTQLSEGLAAELTELTVTECVWETCSQELQSAVEIDQKVRVARCCEAVCAHLVDLFLAEEIFQTAKETLQELQCFCKYLQRWREAVAARKKFRRQMRAFPAAPCCVDVNDRLQALVPSAECPITEENLAKGLLDLGHAGKVGVSCTRLRRLRNKTAHQIKVQHFHQQLLRNAAWAPLDLPSIVSEHLPMKQKRRFWKLVLVLPDVEEQTPESPGRILENWLKVKFTGDDSMVGDIGDNAGDIQTLSVFNTLSSKGDQTVSVNVCIKVAHGTLSDSALDAVETQKDLLGTSGLMLLLPPKVKSEEVAEEELSWLSALLQLKQLLQAKPFQPALPLVVLVPSSRGDSAGRAVEDGLMLQDLVSAKLISDYIVVEIPDSVNDLQGTVKVSGAVQWLISRCPQALDLCCQTLVQYVEDGISREFSRRFFHDRRERRLASLPSQEPSTIIELFNSVLQFLASVVSSEQLCDISWPVMEFAEVGGSQLLPHLHWNSPEHLAWLKQAVLGFQLPQMDLPPPGAPWLPVCSMVIQYTSQIPSSSQTQPVLQSQVENLLCRTYQKWKNKSLSPGQELGPSVAEIPWDDIITLCINHKLRDWTPPRLPVTLEALSEDGQICVYFFKNLLRKYHVPLSWEQARMQTQRELQLSHGRSGMRSIHPPTSTFPTPLLHVHQKGKKKEESGREGSLSTEDLLRGASAEELLAQSLSSSLLEEKEENKRFEDQLQQWLSQDSQAFTESTRLPLYLPQTLVSFPDSIKTQTMVKTSTSPQNSGTGKQLRFSEASGSSLTEKLKLLERLIQSSRAEEAASELHLSALLEMVDM 1971 P11017 Guanine GNB2 9913 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62879}. Cell membrane {ECO:0000250|UniProtKB:P62879}. UNIPROT P11017 UNIPROT A5D7A9 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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. GO:0005737 GO:0005834 GO:0048471 GO:0003924 GO:0051020 GO:0044877 GO:0030159 GO:0007186 GO:1901379 Unknown UniProt Sequence Analysis MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYAFTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN 340 P62879 Guanine GNB2 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:16498633}. Cell membrane {ECO:0000269|PubMed:28219978}. UNIPROT P62879 UNIPROT B3KPU1 UNIPROT P11016 UNIPROT P54312 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 OMIM 139390 OMIM 619464 OMIM 619503 DisGeNET 2783 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. 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. P04626 EBI-8770853 0.35 P0C6X7 EBI-25507431 0.37 P10909 EBI-21693789 0.35 Q99759 EBI-362076 0.00 Q9Y572 EBI-363730 0.00 P04632 EBI-732037 0.00 Q14164 EBI-1074963 0.00 Q9Y4K3 EBI-1079942 0.00 P49286 EBI-1188355 0.53 Q70EL3 EBI-2512984 0.40 P83917 EBI-2556579 0.40 P11440 EBI-2556914 0.40 Q8BFT2 EBI-2558223 0.40 Q9D2X5 EBI-2561173 0.40 Q80X56 EBI-2561540 0.40 Q8BHX1 EBI-2562723 0.40 Q0VEJ0 EBI-2563897 0.40 P03372 EBI-2878124 0.35 P48729 EBI-3907887 0.37 P11177 EBI-3909631 0.37 P20073 EBI-7098405 0.37 P38936 EBI-7123717 0.37 Q9BPY3 EBI-7147527 0.37 P24522 EBI-7153265 0.37 Q14451 EBI-7160608 0.37 P49841 EBI-7165519 0.55 P18754 EBI-7349763 0.37 P42229 EBI-7392908 0.37 Q15714 EBI-7407723 0.37 P15336 EBI-5529812 0.35 P03496 EBI-6156949 0.35 Q9WMX2 EBI-9079674 0.37 P42858 EBI-9071699 0.67 P05549 EBI-9679115 0.37 P35579 EBI-11004631 0.35 P36895 EBI-11008521 0.35 Q8VC57 EBI-11009211 0.35 P80315 EBI-11016531 0.35 P80314 EBI-11019324 0.35 P80318 EBI-11029579 0.35 Q96H55 EBI-11031416 0.35 P21333 EBI-11038784 0.35 Q61879 EBI-11041929 0.35 P51149 EBI-11050319 0.35 Q9JHJ0 EBI-11063313 0.35 P58771 EBI-11063826 0.35 Q16643 EBI-11080402 0.35 Q8N3V7 EBI-11086992 0.35 Q8CCJ3 EBI-11104920 0.35 Q9Z1Z0 EBI-11110688 0.35 Q6P5F9 EBI-11603310 0.35 P60033 EBI-20568535 0.60 Q6IQ23 EBI-16398399 0.35 Q05322 EBI-15481401 0.35 P48960 EBI-21506471 0.35 P18075 EBI-21530438 0.35 P28335 EBI-21534882 0.35 Q01415 EBI-21540352 0.35 P26842 EBI-21555258 0.35 O14530 EBI-21558244 0.35 Q2Y0W8 EBI-21566582 0.35 Q9NRX5 EBI-21567084 0.35 Q16288 EBI-21583226 0.35 Q9H813 EBI-21593240 0.35 Q9Y262 EBI-21610950 0.35 Q9Y345 EBI-21615000 0.35 Q2MV58 EBI-21625612 0.35 Q5VTA0 EBI-21649184 0.35 Q07954 EBI-21684279 0.35 Q9NRE1 EBI-21684885 0.35 Q9GZM7 EBI-21699118 0.35 O15496 EBI-21699277 0.35 P14091 EBI-21699601 0.35 Q6UWB1 EBI-21703330 0.35 Q9NVU0 EBI-21705041 0.35 P08754 EBI-21709056 0.35 Q9UKJ8 EBI-21717781 0.35 Q13371 EBI-21726063 0.35 Q9NQP4 EBI-21726063 0.35 Q99471 EBI-21726063 0.35 Q92526 EBI-21726063 0.35 Q13148 EBI-21726063 0.67 P78371 EBI-21726063 0.35 P63218 EBI-21726063 0.35 P63092 EBI-21726063 0.35 P61758 EBI-21726063 0.35 P50991 EBI-21726063 0.35 P49368 EBI-21726063 0.35 P40227 EBI-21726063 0.35 P17987 EBI-21726063 0.35 P04083 EBI-21726063 0.35 O60925 EBI-21726063 0.35 O15212 EBI-21726063 0.35 Q9NWX5 EBI-21736726 0.35 P48544 EBI-21754197 0.35 O95154 EBI-21755189 0.35 P08833 EBI-21768638 0.35 Q86WS5 EBI-21771386 0.35 P30519 EBI-21779750 0.35 Q9NTU7 EBI-21783449 0.35 Q8WVH0 EBI-21802744 0.35 Q6ZMY9 EBI-21818150 0.35 Q8N1E6 EBI-21820146 0.35 Q8WTQ1 EBI-21825173 0.35 Q96GD3 EBI-21834539 0.35 Q9UNU6 EBI-21839336 0.35 Q99808 EBI-21849345 0.35 O43827 EBI-21853419 0.35 Q9BZP6 EBI-21862020 0.35 P32455 EBI-21864916 0.35 O60383 EBI-21866276 0.35 Q8N8M0 EBI-21867232 0.35 P28799 EBI-21877218 0.35 P04278 EBI-21877199 0.35 Q96CM8 EBI-21877340 0.40 Q3SY56 EBI-21877291 0.35 Q99518 EBI-21877353 0.40 P27824 EBI-16788621 0.27 Q96I36 EBI-16791250 0.27 P23258 EBI-16800113 0.27 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 Q5T7N2 EBI-20993270 0.35 Q5S007 EBI-21360986 0.35 Q9H0J9 EBI-21263845 0.35 O43924 EBI-21019227 0.35 Q8N6Q3 EBI-21402192 0.35 P13569 EBI-25416349 0.53 Q13115 EBI-25372724 0.35 Q15139 EBI-25395029 0.35 P0DOF2 EBI-25603126 0.35 O76071 EBI-25477658 0.35 Q9BY14 EBI-25504841 0.35 Q9C0B5 EBI-25637382 0.35 Q5VVX9 EBI-25859638 0.56 Q969M7 EBI-25859630 0.56 Q8N2K1 EBI-25859622 0.56 Q8WVN8 EBI-25859614 0.56 Q9H0Y0 EBI-25859606 0.56 Q9NT62 EBI-25859598 0.56 Q9C0C9 EBI-25859588 0.56 Q7Z7E8 EBI-25859570 0.56 Q9Y2X8 EBI-25859562 0.56 Q9NPD8 EBI-25859554 0.56 Q16763 EBI-25859546 0.56 Q6NXQ4 EBI-25859538 0.56 O00762 EBI-25859524 0.56 O14933 EBI-25859516 0.56 P61081 EBI-25859508 0.56 P61077 EBI-25859476 0.56 P62837 EBI-25859468 0.56 P51668 EBI-25859460 0.56 P61086 EBI-25859442 0.56 Q7KZS0 EBI-25859500 0.56 P62256 EBI-25859492 0.56 P62253 EBI-25859484 0.56 O60260 EBI-25879531 0.56 P40337 EBI-25895413 0.56 Q9Y3C5 EBI-25918235 0.56 Q7Z699 EBI-25930439 0.56 P00441 EBI-25934837 0.56 P37840 EBI-25940648 0.56 Q13363 EBI-27047305 0.35 P35226 EBI-27108918 0.35 Q05513 EBI-28938998 0.35 Q12792 EBI-28939213 0.35 Q13188 EBI-28939324 0.35 Q86V86 EBI-28942203 0.35 Q8IVW4 EBI-28942376 0.35 Q8TEA7 EBI-28943849 0.35 Q8TF76 EBI-28943924 0.35 Q92772 EBI-28944167 0.35 Q9HCP0 EBI-28946348 0.35 GO:0005737 GO:0005829 GO:0070062 GO:0005615 GO:0005925 GO:0005834 GO:0005765 GO:0016020 GO:0048471 GO:0005886 GO:0031982 GO:0003924 GO:0051020 GO:0044877 GO:0030159 GO:0007186 GO:1901379 Unknown UniProt Sequence Analysis MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYAFTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN 340 P62880 Guanine Gnb2 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62879}. Cell membrane {ECO:0000250|UniProtKB:P62879}. UNIPROT P62880 UNIPROT P11016 UNIPROT P54312 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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. P37840 EBI-2933536 0.35 Q92556 EBI-8764414 0.40 P42858 EBI-9072041 0.35 Q3U1F9 EBI-12603102 0.35 P22682 EBI-12600757 0.35 Q9D415 EBI-16725590 0.35 Q3UHD9 EBI-16736255 0.35 Q9NRI5 EBI-26612017 0.35 Q4ACU6 EBI-26960892 0.35 GO:0044297 GO:0005737 GO:0005834 GO:0043209 GO:0048471 GO:0005886 GO:0032991 GO:0005246 GO:0003924 GO:0051020 GO:0044877 GO:0030159 GO:0007186 GO:1901379 Unknown UniProt Sequence Analysis MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYAFTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN 340 P54313 Guanine Gnb2 10116 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62879}. Cell membrane {ECO:0000250|UniProtKB:P62879}. UNIPROT P54313 UNIPROT Q71SU9 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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. P80386 EBI-16400563 0.35 Q2Q0I9 EBI-15563359 0.40 O75886 EBI-22259612 0.35 P98077 EBI-22260014 0.35 Q92835 EBI-22260917 0.35 Q7M4L6 EBI-22260664 0.35 Q13239 EBI-22261339 0.35 O15357 EBI-22261281 0.35 Q9UGK3 EBI-22262317 0.35 P43403 EBI-22266118 0.35 GO:0044297 GO:0005737 GO:0005834 GO:0048471 GO:0005886 GO:0032991 GO:0005246 GO:0051020 GO:0044877 GO:0030159 GO:0007186 GO:1901379 Unknown UniProt Sequence Analysis MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYAFTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN 340 P79147 Guanine GNB3 9615 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT P79147 UNIPROT Q0PY31 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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. GO:0048471 GO:0007165 Unknown UniProt Sequence Analysis MGEMEQLRQEAEQLKKQIADARKACADTTLAELVSGLEVVGRVQMRTRRTLRGHLAKIYAMHWATDSKLLVSASQDGKLIVWDTYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNMCSIYSLKSREGNVKVSRELSAHTGYLSCCRFLDDNNIVTSSGDTTCALWDIETGQQKTVFVGHTGDCMSLAVSPDFKLFISGACDASAKLWDVREGTCRQTFTGHESDINAICFFPNGEAICTGSDDASCRLFDLRADQELTAYSDESIICGITSVAFSLSGRLLFAGYDDFNCNIWDSMKGERVGILSGHDNRVSCLGVTADGMAVATGSWDSFLKVWN 340 Q4R7Y4 Guanine GNB2L1 9541 None SL-0198 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}. UNIPROT Q4R7Y4 Pfam PF00400 PROSITE PS00678 PROSITE PS50082 PROSITE PS50294 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}. GO:0005737 GO:0030425 GO:0030496 GO:0043025 GO:0005634 GO:0043204 GO:0048471 GO:0001891 GO:0015935 GO:0005080 GO:0030292 GO:0030971 GO:0043022 GO:0042169 GO:0006915 GO:0007049 GO:0071363 GO:0007369 GO:0030308 GO:0050765 GO:0030178 GO:0043065 GO:0030335 GO:2000543 GO:0042998 GO:0043547 GO:0032436 GO:0001934 GO:0031334 GO:0051726 GO:0051302 GO:2000114 GO:0032880 GO:0006417 GO:0048511 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P63244} MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR 317 P32456 Guanylate-binding GBP2 9606 None SL-0198 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}. UNIPROT P32456 UNIPROT Q6GPH0 UNIPROT Q6IAU2 UNIPROT Q86TB0 PDB 6VKJ PDB 7E58 Pfam PF02263 Pfam PF02841 PROSITE PS51715 OMIM 600412 DisGeNET 2634 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}. O60238 EBI-7104878 0.37 Q9Y2M5 EBI-731149 0.00 Q9BX70 EBI-731425 0.00 P51114 EBI-731995 0.00 P61604 EBI-732205 0.00 Q15102 EBI-732725 0.00 Q12972 EBI-732929 0.00 P21673 EBI-733247 0.00 P50453 EBI-733295 0.00 Q92734 EBI-733535 0.00 Q9Y333 EBI-735007 0.00 P49903 EBI-735757 0.00 A0A348ACF3 EBI-2833431 0.00 Q8ZE38 EBI-2869144 0.00 A0A3N4B6Z3 EBI-2869151 0.00 P20073 EBI-7098307 0.37 P55957 EBI-7104587 0.37 P67870 EBI-7133432 0.37 P24522 EBI-7153188 0.37 P49841 EBI-7165379 0.37 Q13387 EBI-7238167 0.37 Q15418 EBI-7369975 0.37 Q13188 EBI-7393045 0.37 Q9WMX2 EBI-9081889 0.51 Q58FG0 EBI-21835834 0.35 Q9UEY8 EBI-21835834 0.35 Q9H0R5 EBI-21835834 0.63 Q8N8V2 EBI-21835834 0.35 Q58FF7 EBI-21835834 0.35 P69905 EBI-21835834 0.35 P57721 EBI-21835834 0.35 P35611 EBI-21835834 0.35 P08238 EBI-21835834 0.35 P07900 EBI-21835834 0.35 P32455 EBI-21864916 0.63 P32456 EBI-26453963 0.57 Q96PP8 EBI-26454129 0.51 Q96PP9 EBI-26472562 0.51 GO:0005737 GO:0031410 GO:0005829 GO:0005794 GO:0000139 GO:0005654 GO:0005634 GO:0048471 GO:0005525 GO:0003924 GO:0042802 GO:0042803 GO:0071346 GO:0071347 GO:0071356 GO:0050830 GO:0042832 GO:0006955 GO:0034504 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:21151871} MAPEINLPGPMSLIDNTKGQLVVNPEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKKNGFSLGSTVKSHTKGIWMWCVPHPKKPEHTLVLLDTEGLGDIEKGDNENDSWIFALAILLSSTFVYNSMGTINQQAMDQLHYVTELTDRIKANSSPGNNSVDDSADFVSFFPAFVWTLRDFTLELEVDGEPITADDYLELSLKLRKGTDKKSKSFNDPRLCIRKFFPKRKCFVFDWPAPKKYLAHLEQLKEEELNPDFIEQVAEFCSYILSHSNVKTLSGGIPVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVEKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFMKNSFKDVDQMFQRKLGAQLEARRDDFCKQNSKASSDCCMALLQDIFGPLEEDVKQGTFSKPGGYRLFTQKLQELKNKYYQVPRKGIQAKEVLKKYLESKEDVADALLQTDQSLSEKEKAIEVERIKAESAEAAKKMLEEIQKKNEEMMEQKEKSYQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFENESKRLQKDIWDIQMRSKSLEPICNIL 591 Q9Z0E6 Guanylate-binding Gbp2 10090 None SL-0198 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}. UNIPROT Q9Z0E6 UNIPROT Q4FK03 UNIPROT Q8CIC6 UNIPROT Q921N2 UNIPROT Q9R1I0 Pfam PF02263 Pfam PF02841 PROSITE PS51715 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}. Q6P542 EBI-6909752 0.35 Q3U1F9 EBI-12603102 0.35 GO:0015629 GO:0005737 GO:0031410 GO:0005829 GO:0005794 GO:0000139 GO:0005654 GO:0005634 GO:0048471 GO:0020005 GO:0012506 GO:0003779 GO:0019955 GO:0019899 GO:0019003 GO:0005525 GO:0003924 GO:0051879 GO:0042802 GO:0042803 GO:0030507 GO:0044406 GO:0035458 GO:0071346 GO:0071222 GO:0050830 GO:0042832 GO:0009617 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:9858320} MASEIHMSEPMCLIENTEAQLVINQEALRILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKRTGFSLGSTVQSHTKGIWMWCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAVLLSSTFIYNSIGTINQQAMDQLHYVTELTDLIKSKSSPDQSGVDDSANFVGFFPTFVWTLRDFSLELEVNGKPVTSDEYLEHSLTLKKGADKKTKSFNEPRLCIRKFFPKRKCFIFDRPAQRKQLSKLETLREEELCGEFVEQVAEFTSYILSYSSVKTLCGGIIVNGPRLKSLVQTYVGAISNGSLPCMESAVLTLAQIENSAAVQKAITHYEEQMNQKIQMPTETLQELLDLHRPIESEAIEVFLKNSFKDVDQKFQTELGNLLVAKRDAFIKKNMDVSSARCSDLLEDIFGPLEEEVKLGTFSKPGGYYLFLQMRQELEKKYNQAPGKGLQAEAMLKNYFDSKADVVETLLQTDQSLTEAAKEVEEERTKAEAAEAANRELEKKQKEFELMMQQKEKSYQEHVKKLTEKMKDEQKQLLAEQENIIAAKLREQEKFLKEGFENESKKLIREIDTLKQNKSSGKCTIL 589 Q63663 Guanylate-binding Gbp2 10116 None SL-0198 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}. UNIPROT Q63663 Pfam PF02263 Pfam PF02841 PROSITE PS51715 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}. GO:0005737 GO:0031410 GO:0005794 GO:0000139 GO:0005634 GO:0048471 GO:0005525 GO:0003924 GO:0042802 GO:0042803 GO:0044406 GO:0035458 GO:0071346 GO:0071347 GO:0071222 GO:0071356 GO:0050830 GO:0042832 GO:0034504 GO:0009617 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:8148370} MASEIHMLQPMCLIENTEAHLVINQEALRILSAINQPVVVVAIVGLYRTGKSYLMNKLAGKRTGFSLGSTVQSHTKGIWMWCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAVLLSSTFVYNSMGTINQQAMDQLHYVTELTDLIKSKSSPDQSGIDDSANFVGFFPTFVWALRDFSLELEVNGKLVTPDEYLEHSLTLKKGADKKTKSFNEPRLCIRKFFPKRKCFIFDRPALRKQLCKLETLGEEELCSEFVEQVAEFTSYIFSYSAVKTLSGGIIVNGPRLKSLVQTYVGAISSGSLPCMESAVLTLAQIENSAAVQKAITHYEEQMNQKIQMPTETLQELLDLHRLIEREAIEIFLKNSFKDVDQKFQTELGNLLISKRDAFIKKNSDVSSAHCSDLIEDIFGPLEEEVKQGTFSKPGGYFLFLQMRQELEKKYNQAPGKGLEAEAVLKKYFESKEDIVETLLKTDQSLTEAAKEIEVERIKAETAEAANRELAEKQEKFELMMQQKEESYQEHVRQLTEKMKEEQKKLIEEQDNIIALKLREQEKFLREGYENESKKLLREIENMKRRQSPGKCTIL 589 Q9H0R5 Guanylate-binding GBP3 9606 None SL-0198 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}. UNIPROT Q9H0R5 UNIPROT A2A317 UNIPROT A6NF86 UNIPROT B2RTW0 UNIPROT F8UW81 UNIPROT Q05D54 UNIPROT Q5T8L8 UNIPROT Q5T8L9 UNIPROT Q6P3V3 UNIPROT Q9NV33 Pfam PF02263 Pfam PF02841 PROSITE PS51715 OMIM 600413 DisGeNET 2635 Exhibits antiviral activity against influenza virus. {ECO:0000269|PubMed:22106366}. P32456 EBI-21835834 0.63 O95819 EBI-8547663 0.59 Q5NF74 EBI-2798928 0.00 P32455 EBI-21864916 0.63 P60903 EBI-20909232 0.40 P16403 EBI-20912036 0.40 Q9H0R5 EBI-26472578 0.51 Q96PP8 EBI-26472594 0.51 GO:0005737 GO:0031410 GO:0005829 GO:0000139 GO:0048471 GO:0005525 GO:0003924 GO:0042802 GO:0042803 GO:0071346 GO:0071347 GO:0071356 GO:0051607 Unknown UniProt Sequence Analysis MAPEIHMTGPMCLIENTNGELVANPEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKNKGFSLGSTVKSHTKGIWMWCVPHPKKPEHTLVLLDTEGLGDVKKGDNQNDSWIFTLAVLLSSTLVYNSMGTINQQAMDQLYYVTELTHRIRSKSSPDENENEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLEYSLKLTQGTSQKDKNFNLPRLCIRKFFPKKKCFVFDLPIHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIKVNGPRLESLVLTYINAISRGDLPCMENAVLALAQIENSAAVQKAIAHYDQQMGQKVQLPAETLQELLDLHRVSEREATEVYMKNSFKDVDHLFQKKLAAQLDKKRDDFCKQNQEASSDRCSALLQVIFSPLEEEVKAGIYSKPGGYCLFIQKLQDLEKKYYEEPRKGIQAEEILQTYLKSKESVTDAILQTDQILTEKEKEIEVECVKAESAQASAKMVEEMQIKYQQMMEEKEKSYQEHVKQLTEKMERERAQLLEEQEKTLTSKLQEQARVLKERCQGESTQLQNEIQKLQKTLKKKTKRYMSHKLKI 595 Q96PP9 Guanylate-binding GBP4 9606 None SL-0198 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}. UNIPROT Q96PP9 UNIPROT B2R630 UNIPROT Q05D63 UNIPROT Q6NSL0 UNIPROT Q86T99 Pfam PF02263 Pfam PF02841 PROSITE PS51715 OMIM 612466 DisGeNET 115361 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}. P32456 EBI-26472562 0.51 Q8TCS8 EBI-20907752 0.40 P32455 EBI-26472554 0.51 Q96PP9 EBI-26472586 0.51 Q96PP8 EBI-26472602 0.51 GO:0031410 GO:0005829 GO:0005794 GO:0000139 GO:0005634 GO:0048471 GO:0005886 GO:0005525 GO:0003924 GO:0042802 GO:0042803 GO:0071346 GO:0050830 GO:0042832 Unknown UniProt Sequence Analysis MGERTLHAAVPTPGYPESESIMMAPICLVENQEEQLTVNSKALEILDKISQPVVVVAIVGLYRTGKSYLMNRLAGKRNGFPLGSTVQSETKGIWMWCVPHLSKPNHTLVLLDTEGLGDVEKSNPKNDSWIFALAVLLSSSFVYNSVSTINHQALEQLHYVTELAELIRAKSCPRPDEAEDSSEFASFFPDFIWTVRDFTLELKLDGNPITEDEYLENALKLIPGKNPKIQNSNMPRECIRHFFRKRKCFVFDRPTNDKQYLNHMDEVPEENLERHFLMQSDNFCSYIFTHAKTKTLREGIIVTGKRLGTLVVTYVDAINSGAVPCLENAVTALAQLENPAAVQRAADHYSQQMAQQLRLPTDTLQELLDVHAACEREAIAVFMEHSFKDENHEFQKKLVDTIEKKKGDFVLQNEEASAKYCQAELKRLSEHLTESILRGIFSVPGGHNLYLEEKKQVEWDYKLVPRKGVKANEVLQNFLQSQVVVEESILQSDKALTAGEKAIAAERAMKEAAEKEQELLREKQKEQQQMMEAQERSFQEYMAQMEKKLEEERENLLREHERLLKHKLKVQEEMLKEEFQKKSEQLNKEINQLKEKIESTKNEQLRLLKILDMASNIMIVTLPGASKLLGVGTKYLGSRI 640 Q61107 Guanylate-binding Gbp4 10090 None SL-0198 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}. UNIPROT Q61107 UNIPROT Q8VEC5 Pfam PF02263 Pfam PF02841 PROSITE PS51715 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}. GO:0031410 GO:0005829 GO:0005794 GO:0000139 GO:0005634 GO:0048471 GO:0005886 GO:0020005 GO:0005525 GO:0003924 GO:0042802 GO:0042803 GO:0044406 GO:0035458 GO:0071346 GO:0071356 GO:0050830 GO:0042832 GO:0051607 GO:0001818 GO:0046426 GO:0032480 GO:0034345 GO:0045070 GO:0043122 Unknown UniProt Sequence Analysis MEAPICLVENWKNQLTVNLEAIRILEQIAQPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLDTEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINQQALEQLHFVTELTQLIRAKSSPREDKVKDSSEFVGFFPDFIWAVRDFALELKLNGRPITEDEYLENALKLIQGDNLKVQQSNMTRECIRYFFPVRKCFVFDRPTSDKRLLLQIENVPENQLERNFQVESEKFCSYIFTNGKTKTLRGGVIVTGNRLGTLVQTYVNAINSGTVPCLENAVTTLAQRENSIAVQKAADHYSEQMAQRMRLPTDTLQELLTVHAACEKEAIAVFMEHSFKDDEQEFQKKLVVTIEERKEEFIRQNEAASIRHCQAELERLSESLRKSISCGAFSVPGGHSLYLEARKKIELGYQQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERSFRENIAKLQEKMESEKEMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEISHLREEMERTRRKPSLFGQILDTIGNAFIMILPGAGKLFGVGLKFLGSLSS 620 P35197 ADP-ribosylation GCS1 559292 None SL-0198 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. UNIPROT P35197 UNIPROT D6VRC9 PDB 5FJX Pfam PF01412 PROSITE PS50115 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}. P84077 EBI-620364 0.37 P16140 EBI-785523 0.35 P10592 EBI-785523 0.53 P53919 EBI-858904 0.00 P10591 EBI-3670433 0.35 P11484 EBI-3688456 0.35 P32589 EBI-3725254 0.35 Q12136 EBI-16255956 0.00 P38169 EBI-16257096 0.00 P39981 EBI-16257116 0.00 P40073 EBI-16257136 0.00 P53108 EBI-16257156 0.00 P53093 EBI-16257176 0.00 P53039 EBI-16257196 0.00 P14359 EBI-16257216 0.00 P12688 EBI-16257236 0.00 P36164 EBI-16257256 0.00 Q12016 EBI-16257276 0.00 P33328 EBI-16257296 0.00 P06197 EBI-16257316 0.00 P14020 EBI-16257336 0.00 GO:0005856 GO:0005829 GO:0005768 GO:0005739 GO:0048471 GO:0005802 GO:0003779 GO:0005096 GO:0046872 GO:0030037 GO:0006888 GO:0043001 GO:0006890 Unknown UniProt Sequence Analysis MSDWKVDPDTRRRLLQLQKIGANKKCMDCGAPNPQWATPKFGAFICLECAGIHRGLGVHISFVRSITMDQFKPEELLRMEKGGNEPLTEWFKSHNIDLSLPQKVKYDNPVAEDYKEKLTCLCEDRVFEEREHLDFDASKLSATSQTAASATPGVAQSREGTPLENRRSATPANSSNGANFQKEKNEAYFAELGKKNQSRPDHLPPSQGGKYQGFGSTPAKPPQERSAGSSNTLSLENFQADPLGTLSRGWGLFSSAVTKSFEDVNETVIKPHVQQWQSGELSEETKRAAAQFGQKFQETSSYGFQAFSNFTKNFNGNAEDSSTAGNTTHTEYQKIDNNDKKNEQDEDKWDDF 352 Q8N9F7 Lysophospholipase GDPD1 9606 None SL-0198 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}. UNIPROT Q8N9F7 UNIPROT A8W735 UNIPROT Q56VR1 UNIPROT Q8N4E3 Pfam PF03009 PROSITE PS51704 OMIM 616317 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}. K9N7C7 EBI-26374966 0.35 P0DOE9 EBI-6138583 0.35 P62079 EBI-21619035 0.35 P69905 EBI-21822769 0.35 P68871 EBI-21822769 0.35 P19823 EBI-21822769 0.35 P19652 EBI-21822769 0.35 P0C0L4 EBI-21822769 0.35 P06727 EBI-21822769 0.35 P04217 EBI-21822769 0.35 P02790 EBI-21822769 0.35 P02787 EBI-21822769 0.35 P02768 EBI-21822769 0.35 P02765 EBI-21822769 0.35 P02763 EBI-21822769 0.35 P02652 EBI-21822769 0.35 P02647 EBI-21822769 0.35 P02042 EBI-21822769 0.35 P01876 EBI-21822769 0.35 P01859 EBI-21822769 0.35 P01857 EBI-21822769 0.35 P01042 EBI-21822769 0.35 P01024 EBI-21822769 0.35 P01023 EBI-21822769 0.35 P01011 EBI-21822769 0.35 P01009 EBI-21822769 0.35 P00751 EBI-21822769 0.35 P00738 EBI-21822769 0.35 P00450 EBI-21822769 0.35 GO:0005783 GO:0005789 GO:0016021 GO:0016020 GO:0048471 GO:0004622 GO:0046872 GO:0008081 GO:0046475 GO:0070291 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSSTAAFYLLSTLGGYLVTSFLLLKYPTLLHQRKKQRFLSKHISHRGGAGENLENTMAAFQHAVKIGTDMLELDCHITKDEQVVVSHDENLKRATGVNVNISDLKYCELPPYLGKLDVSFQRACQCEGKDNRIPLLKEVFEAFPNTPINIDIKVNNNVLIKKVSELVKRYNREHLTVWGNANYEIVEKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHTMSRSQKFLIWLSDLLLMRKALFDHLTARGIQVYIWVLNEEQEYKRAFDLGATGVMTDYPTKLRDFLHNFSA 314 Q9CRY7 Lysophospholipase Gdpd1 10090 None SL-0198 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}. UNIPROT Q9CRY7 UNIPROT Q9CT14 UNIPROT Q9D4X7 Pfam PF03009 PROSITE PS51704 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}. GO:0005783 GO:0005789 GO:0016021 GO:0016020 GO:0048471 GO:0004622 GO:0046872 GO:0008081 GO:0046475 GO:0070291 GO:0006644 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSSTAAFCLLSTLGGYLVTSFLLLKYPALLHQRKKQRFLSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKCEGKDTRIPLLKEVFEAFPETPINIDIKVNNNVLIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHTISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPTKLKDFLNNFSA 314 Q0VGK4 Lysophospholipase Gdpd1 10116 None SL-0198 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}. UNIPROT Q0VGK4 Pfam PF03009 PROSITE PS51704 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}. GO:0005783 GO:0005789 GO:0016021 GO:0016020 GO:0048471 GO:0004622 GO:0046872 GO:0008081 GO:0046475 GO:0070291 GO:0006644 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSSTAAFCLLSTLGGYLVTSFLLLKYPALLHQRKKQRFLSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKCEGTDTRIPLLKEVFEAFPETPINIDIKVNNNVLIQKVSELVKQYKREHLTVWGNASSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHIISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFLNNMSA 314 Q7L5L3 Lysophospholipase GDPD3 9606 None SL-0198 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}. UNIPROT Q7L5L3 UNIPROT Q9H652 Pfam PF03009 PROSITE PS51704 OMIM 616318 DisGeNET 79153 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}. Q13617 EBI-21327106 0.35 P01160 EBI-21572983 0.35 Q5VU43 EBI-21573806 0.35 Q15915 EBI-21696712 0.35 Q8IW40 EBI-21747275 0.35 O43918 EBI-21790262 0.35 O43781 EBI-28931148 0.35 O95382 EBI-28931448 0.35 P54619 EBI-28938518 0.35 Q14296 EBI-28941126 0.35 Q8IVW4 EBI-28942376 0.35 GO:0005783 GO:0005789 GO:0070062 GO:0016021 GO:0048471 GO:0004622 GO:0046872 GO:0008081 GO:0046475 GO:0070291 GO:0034638 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSLLLYYALPALGSYAMLSIFFLRRPHLLHTPRAPTFRIRLGAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVYFSPGHFAHGSDRRMVRLEDLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYLGLLPFIPIPEKFFFCFLPNIINRTYFPFSCSCLNQLLAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGVITDYPTALRHYLDNHGPAARTS 318 Q99LY2 Lysophospholipase Gdpd3 10090 None SL-0198 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}. UNIPROT Q99LY2 UNIPROT Q9D1C0 Pfam PF03009 PROSITE PS51704 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}. GO:0005783 GO:0005789 GO:0016021 GO:0048471 GO:0004622 GO:0046872 GO:0008081 GO:0046475 GO:0070291 GO:0034638 GO:0006644 Transmembrane UniProt Sequence Analysis {ECO:0000255} MIPLLYFVLPTLGSYVMLSIFFLRRPHLLHTPRAPVFPIRLAAHRGGSGERLENTMEAVENSMAQRADLLEFDCQLTRDGVVVVSHDKNLSRQSGLNKDVNTLDFEELPLYKEELEIYFSPGHFAHGSDRHMISLEDVFQKFPRTPMCLEVKERNEELIHKVANLTRRFDRNEITIWAAEKSSVMKRCRAANPEMPMAFTIWRSFWILLLYYLGLLPFVSIPEKFFFCFLPTIINRTYFPFRCGWMNQLSATITKWIIMRKSLIRHLQDRGVQVLFWCLNEESDFEVAFSLGANGVMTDYPTALRHYLDKQEEETQPPQPEALSCLSLKK 330 Q3KTM2 Glycerophosphodiester GDPD5 9031 None SL-0198 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}. UNIPROT Q3KTM2 Pfam PF03009 PROSITE PS51704 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}. P0CB50 EBI-2464235 0.59 Q06830 EBI-2464259 0.40 P35700 EBI-2464725 0.40 GO:0012505 GO:0030426 GO:0016021 GO:0016020 GO:0048471 GO:0005886 GO:0047389 GO:0008889 GO:0004435 GO:0006629 GO:0007399 GO:0045666 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVKHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTKWERLWFLILTSSFFLTLVWFYFWWEVHNDYNEINWFLYNRMGYWSDWSIPILVTTAAGFTYITVLLILALCHIAVGQQMNLHWLHKIGLMTTLITTVVTMSSIAQLWDDEWEMVFISLQATAPFLHIGALAAVTALSWLIAGQFARMEKATSQMLMVTAYLAVVVALYLVPLTISSPCIMEKKALGPKPAIIGHRGAPMLAPENTLMSFQKAVEQKIYGVQADVILSYDGVPFLMHDKTLRRTTNVEEVFPGRAYEHSSMFNWTDLEMLNAGEWFLRNDPFWTAGSLSRSDYLEAANQSVCKLADMLEVIKDNTSLILNFQDLPPDHPYYTSYINITLKTILASGIQQQAVMWLPDTERQLVRQIAPAFQQTSGLKLDAERLREKGIVKLNLRYTKVTNEDVRDYMAANLSVNLYTVNEPWLYSILWCTGVPSVTSDSSHVLRKVPFPIWLMPPDEYRLIWITSDLISFIIIVGVFIFQNYHNDQWRLGSIRTYNPEQIMLSAAVRRSSRDVKIMKEKLIFSEINNGVETTDELSLCSENGYANEMVTPTDHRDTRLRMN 599 Q8WTR4 Glycerophosphodiester GDPD5 9606 None SL-0198 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}. UNIPROT Q8WTR4 UNIPROT Q49AQ5 UNIPROT Q6UX76 UNIPROT Q7Z4S0 UNIPROT Q8N781 UNIPROT Q8NCB7 UNIPROT Q8TB77 Pfam PF03009 PROSITE PS51704 OMIM 609632 DisGeNET 81544 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}. O75844 EBI-21566764 0.35 Q14677 EBI-16430940 0.56 Q8NC56 EBI-21566764 0.35 Q81WF2 EBI-2833213 0.00 P50542 EBI-10276098 0.56 Q8IUQ4 EBI-10276108 0.56 Q70JA7 EBI-21566764 0.35 Q9Y6N7 EBI-21566764 0.35 Q9Y6I9 EBI-21566764 0.35 Q9Y397 EBI-21566764 0.35 Q9UNK0 EBI-21566764 0.35 Q9UI09 EBI-21566764 0.35 Q9UEU0 EBI-21566764 0.35 Q9NV66 EBI-21566764 0.35 Q9NUE0 EBI-21566764 0.35 Q9NQ84 EBI-21566764 0.35 Q9BX95 EBI-21566764 0.35 Q9BWL3 EBI-21566764 0.35 Q9BTX1 EBI-21566764 0.35 Q9BRX8 EBI-21566764 0.35 Q9BRB3 EBI-21566764 0.35 Q969P0 EBI-21566764 0.35 Q969E2 EBI-21566764 0.35 Q92838 EBI-21566764 0.35 Q8WUY1 EBI-21566764 0.35 Q8N4L2 EBI-21566764 0.35 Q6UW68 EBI-21566764 0.35 Q6NUM9 EBI-21566764 0.35 Q5VT66 EBI-21566764 0.35 Q14654 EBI-21566764 0.35 P62341 EBI-21566764 0.35 P43304 EBI-21566764 0.35 O75380 EBI-21566764 0.35 O43306 EBI-21566764 0.35 O43181 EBI-21566764 0.35 O15400 EBI-21566764 0.35 O00461 EBI-21566764 0.35 P0CG08 EBI-21566764 0.35 Q6PEX3 EBI-22134456 0.37 GO:0012505 GO:0030426 GO:0016021 GO:0016020 GO:0048471 GO:0005886 GO:0047389 GO:0008889 GO:0004435 GO:0006629 GO:0007399 GO:0045666 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVRHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTPWERLWFLLLTFTFGLTLTWLYFWWEVHNDYDEFNWYLYNRMGYWSDWPVPILVTTAAAFAYIAGLLVLALCHIAVGQQMNLHWLHKIGLVVILASTVVAMSAVAQLWEDEWEVLLISLQGTAPFLHVGAVAAVTMLSWIVAGQFARAERTSSQVTILCTFFTVVFALYLAPLTISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADITISLDGVPFLMHDTTLRRTTNVEEEFPELARRPASMLNWTTLQRLNAGQWFLKTDPFWTASSLSPSDHREAQNQSICSLAELLELAKGNATLLLNLRDPPREHPYRSSFINVTLEAVLHSGFPQHQVMWLPSRQRPLVRKVAPGFQQTSGSKEAVASLRRGHIQRLNLRYTQVSRQELRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHALSQVPSPLWIMPPDEYCLMWVTADLVSFTLIVGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRDVSIMKEKLIFSEISDGVEVSDVLSVCSDNSYDTYANSTATPVGPRGGGSHTKTLIERSGR 605 Q640M6 Glycerophosphodiester Gdpd5 10090 None SL-0198 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}. UNIPROT Q640M6 UNIPROT Q8R0T5 UNIPROT Q8R3N5 Pfam PF03009 PROSITE PS51704 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}. GO:0030424 GO:0005789 GO:0030426 GO:0016021 GO:0016020 GO:0043025 GO:0097038 GO:0005886 GO:0047389 GO:0008889 GO:0004435 GO:0021895 GO:0006629 GO:0045746 GO:0030182 GO:0031175 GO:0007219 GO:0045787 GO:0045666 GO:0048505 GO:0021522 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVRHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTPWERLWFLLLVCTFSLTLTWLYFWWGVHNDYDEFNWYLYNRMGYWSDWSVPILVTSAAAFTYIAGLLVLALCHIAVGQQLNLHWIHKMGLVVILASTVVAMSAVAQLWEDEWEVLLISLQGTAPFLHIGALVAITALSWIVAGQFARAERSSSQLTILCTFFAVVFTFYLIPLTISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARRPAAMLNWTVLQRLNAGQWFLKTDPFWTASSLSPSDHREVQNQSICSLAELLELAKGNASLLLNLRDPPRDHPYRGSFLNVTLEAVLRSGFPQHQVMWLFNRQRPLVRKMAPGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHTLSRVPSPLWIMPPDEYCLMWVTADLISFSLIIGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRDVSIMKEKLIFSEISDGVEVSDELSVCSDSSYDTYANANSTATPVGPRNAGSRAKTVTEQSGH 607 Q04839 mRNA GFD1 559292 None SL-0178 SL-0182 SL-0185 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}. UNIPROT Q04839 UNIPROT D6W081 PDB 3LCN Pfam PF17331 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}. P20449 EBI-7998113 0.66 P30822 EBI-11611503 0.35 P38147 EBI-390120 0.37 P32505 EBI-390345 0.80 P53040 EBI-391560 0.37 P32793 EBI-392742 0.37 P15442 EBI-8014718 0.40 P39936 EBI-6331305 0.00 P50111 EBI-2132826 0.51 Q04839 EBI-2132792 0.37 P10591 EBI-3670521 0.35 P11484 EBI-3688520 0.35 Q12315 EBI-6473225 0.44 GO:0005737 GO:0031965 GO:0005643 GO:0044877 GO:0006406 GO:0015031 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:10523319} MPLESIWADAPDEEPIKKQKPSHKRSNNNKKNNNSRWSNESSSNNKKKDSVNKVKNNKGNHESKTKNKIKETLPREKKPPHSQGKISPVSESLAINPFSQKATEISPPPVSPSKMKTTKTQSKQDTASKMKLLKKKIEEQREILQKTHHKNQQQQVLMDFLNDEGSSNWVDDDEEELILQRLKTSLKI 188 Q32L41 GTP GCHFR 9913 None SL-0178 SL-0182 Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. UNIPROT Q32L41 Pfam PF06399 Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine (By similarity). {ECO:0000250}. GO:0005737 GO:0005829 GO:0030425 GO:0042470 GO:0031965 GO:0005654 GO:0005634 GO:0044549 GO:0009890 GO:0043105 Unknown UniProt Sequence Analysis MPYLLISTQIRMEVGPTVVGDEHSDPELMQHLGASKRSVLGNNFSEYYVNDPPRIVLDKLERRGFRVLSMTGVGQTLVWCLHKE 84 Q6PBT6 GTP gchfr 7955 None SL-0178 SL-0182 Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. UNIPROT Q6PBT6 Pfam PF06399 Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. {ECO:0000250}. GO:0005737 GO:0005829 GO:0031965 GO:0005634 GO:0044549 GO:0009890 GO:0043105 Unknown UniProt Sequence Analysis MPYILISTQIRLETGPTMVGDEYSDPSIMNYLGARKITVLGNNFSEYHVDEPPRLVLDKLDKIGYRVVSMTGVGQTLVWCLHKESSNTL 89 P30047 GTP GCHFR 9606 None SL-0178 SL-0182 Nucleus {ECO:0000269|PubMed:16778797}. Nucleus membrane {ECO:0000269|PubMed:16778797}. Cytoplasm, cytosol {ECO:0000269|PubMed:16778797}. UNIPROT P30047 UNIPROT B2R4L6 UNIPROT B7ZLM8 UNIPROT Q2M1Q2 UNIPROT Q99749 PDB 6Z80 PDB 6Z85 PDB 7ACC PDB 7AL9 PDB 7ALA PDB 7ALB PDB 7ALC PDB 7ALQ Pfam PF06399 OMIM 602437 DisGeNET 2644 Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine. {ECO:0000269|PubMed:16778797}. O75147 EBI-21786208 0.35 P30793 EBI-958378 0.37 P20155 EBI-21762493 0.35 Q8N0Z8 EBI-21786208 0.35 Q9Y450 EBI-21786208 0.35 Q96RR4 EBI-21786208 0.35 Q7Z5L9 EBI-21786208 0.35 Q5JSL3 EBI-21786208 0.35 Q13951 EBI-21786208 0.35 Q04637 EBI-21786208 0.35 O76041 EBI-21786208 0.35 O00168 EBI-21862664 0.35 GO:0005737 GO:0005829 GO:0030425 GO:0042470 GO:0031965 GO:0005654 GO:0005634 GO:0032991 GO:0016597 GO:0004857 GO:0044549 GO:0030742 GO:0044877 GO:0009890 GO:0043105 GO:0042133 GO:0006809 GO:0065003 Unknown UniProt Sequence Analysis MPYLLISTQIRMEVGPTMVGDEQSDPELMQHLGASKRRALGNNFYEYYVDDPPRIVLDKLERRGFRVLSMTGVGQTLVWCLHKE 84 P99025 GTP Gchfr 10090 None SL-0178 SL-0182 Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. UNIPROT P99025 UNIPROT Q8BH29 Pfam PF06399 Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine (By similarity). {ECO:0000250}. GO:0005737 GO:0005829 GO:0030425 GO:0042470 GO:0031965 GO:0005654 GO:0005634 GO:0032991 GO:0016597 GO:0019899 GO:0004857 GO:0044549 GO:0030742 GO:0044877 GO:0009890 GO:0043105 GO:0065003 Unknown UniProt Sequence Analysis MPYLLISTQIRMEVGPTMVGDEHSDPELMQHLGASKRSVLGNNFYEYYVNDPPRIVLDKLECKGFRVLSMTGVGQTLVWCLHKE 84 P70552 GTP Gchfr 10116 None SL-0178 SL-0182 Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. UNIPROT P70552 PDB 1IS7 PDB 1IS8 PDB 1JG5 PDB 1WPL Pfam PF06399 Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine. P22288 EBI-1032731 0.62 GO:0005737 GO:0005829 GO:0030425 GO:0042470 GO:0031965 GO:0005654 GO:0005634 GO:0032991 GO:0016597 GO:0019899 GO:0004857 GO:0044549 GO:0030742 GO:0044877 GO:0009890 GO:0043105 GO:0065003 GO:0045428 Unknown UniProt Sequence Analysis MPYLLISTQIRMEVGPTMVGDEHSDPELMQQLGASKRRVLGNNFYEYYVNDPPRIVLDKLECRGFRVLSMTGVGQTLVWCLHKE 84 Q6GM84 GTP gchfr 8355 None SL-0178 SL-0182 Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. UNIPROT Q6GM84 Pfam PF06399 Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. {ECO:0000250}. GO:0005829 GO:0031965 GO:0009890 Unknown UniProt Sequence Analysis MPYVLISTQIRMETGPTIVGDEFSDLVLMAQLEADKRTVLGNNFSEYYVNEPPRVTLNKLERLGYRVVSMTGVGQTLVWCLHKE 84 Q6NVA8 GTP gchfr 8364 None SL-0178 SL-0182 Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. UNIPROT Q6NVA8 UNIPROT Q28DT4 Pfam PF06399 Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. {ECO:0000250}. GO:0005737 GO:0005829 GO:0031965 GO:0005634 GO:0044549 GO:0009890 GO:0043105 Unknown UniProt Sequence Analysis MPYVLISTQIRMETGPTIVGDEFSDTQLMAQLEADKRTVLGNNFSEYCVNEPPRVTLNKLEKLGYRVVSMTGVGQTLVWCLHKE 84 Q80WJ1 Gametogenetin Ggn 10090 None SL-0198 [Isoform 1]: Cytoplasm, perinuclear region. Note=Localizes along the nuclear membrane. [Isoform 2]: Cytoplasmic vesicle. [Isoform 3]: Nucleus, nucleolus. UNIPROT Q80WJ1 UNIPROT Q5EBP4 UNIPROT Q80WI9 UNIPROT Q80WJ0 Pfam PF15685 May be involved in spermatogenesis. {ECO:0000269|PubMed:12574169}. Q5SV77 EBI-4370065 0.54 Q9R109 EBI-4370118 0.54 Q6K1E7 EBI-3890501 0.44 GO:0031410 GO:0016021 GO:0005635 GO:0005730 GO:0048471 GO:0042802 GO:0031625 GO:0030154 GO:0006302 GO:0007566 GO:0007276 GO:0008104 GO:0065003 GO:0007283 Unknown UniProt Sequence Analysis MGNVQSEPSAGGGSRKEQASDRASDSRRTPLVEPEVTPSSPAMRLARGLGVWFPGSSGPPGLLIPPEPQASSSPLPLTLELPSPVTPPPEEAAAVSTPPPPPVGTLLPAPSKWRKPTGTSVPRIRGLLEASHRGQGDPPSLRPLPPLPRQLTEKDPVLRAPAPPPTPLEPRKQLPPAPSTCDPQPLSRRITLASSATSPTESQVRHSSEGQAAGGAHGGVPPQAGEGEMARSATSESGLSLLCKVTFKSGPHLSPTSASGPLAAKASPGAGGGGLFASSGAISYAEVLKQGPQPPGATRPLGEVPPGATRPLGEVPRAAQETEGGDGDGEGCSGPPSVPAPLARALPPPPYTTFPGSKPKFDWVSPPDGTERHFRFNGAVGGIGAPRRRTTTLSGPWGSPPPRSGQTHPSSGPRRPTPALLAPPMFIFPAPNNGEPVRPVPPSPQQIPPLPPPPPTPPATPPPAPPPTPQPPALPRTPILVARPPTPGPGHLESALAPTPPSTLSPTAAADQVPAATPATVTSQVPATATAELSPPMPQPKTRTRRNKGPRAARGVIREEGTSGDGPREPNTAPVTDSSSGGGGGGSNGTSTAGASNKGTARHWPPFEVLNSCPCKCYCRHQRRHRRLPRNVSAWLSTPTNHLSEPPWVATVKLAGSLVAGLEHYDLQATHST 673 P56966 Geranylgeranyl GGPS1 9913 None SL-0198 Cytoplasm {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95749}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O95749}. UNIPROT P56966 UNIPROT Q0VC78 Pfam PF00348 PROSITE PS00723 PROSITE PS00444 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}. GO:0005737 GO:0005829 GO:0005654 GO:0048471 GO:0030018 GO:0004161 GO:0004311 GO:0004337 GO:0042802 GO:0046872 GO:0004659 GO:0045337 GO:0033384 GO:0033386 GO:0008299 GO:0006720 Unknown UniProt Sequence Analysis MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLNHPDAVKLFTRQLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLDTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTENIDIKKYCVHYLENVGSFEYTRNTLKELESKAYKQIDARGGNPELVALIKHLSKMFKEENE 300 O95749 Geranylgeranyl GGPS1 9606 None SL-0198 Cytoplasm {ECO:0000269|PubMed:32403198}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32403198}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:32403198}. UNIPROT O95749 UNIPROT A8MVQ8 UNIPROT Q5T2C8 UNIPROT Q6NW19 PDB 2Q80 PDB 6C56 PDB 6C57 PDB 6G31 PDB 6G32 PDB 6R4V Pfam PF00348 PROSITE PS00723 PROSITE PS00444 OMIM 606982 OMIM 619518 DisGeNET 9453 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}. 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. O00244 EBI-10179290 0.56 O95749 EBI-10483772 0.74 O00560 EBI-24510551 0.56 Q7Z5A8 EBI-21529283 0.35 Q17RF5 EBI-21556823 0.35 Q9NZB2 EBI-21564038 0.35 Q9NWH9 EBI-21564038 0.35 Q9H7X3 EBI-21564038 0.35 Q2TAM9 EBI-21564038 0.35 P46940 EBI-21564038 0.35 A6NKD9 EBI-21564038 0.35 Q12950 EBI-21599483 0.35 Q9H9P5 EBI-21622067 0.35 Q8WV44 EBI-21636495 0.35 Q9Y228 EBI-21696444 0.35 O75386 EBI-21712804 0.35 Q3SYB3 EBI-21720692 0.35 P18509 EBI-21725612 0.35 B2RXF5 EBI-21730871 0.35 P62701 EBI-21738776 0.35 Q96BR6 EBI-21784034 0.35 Q9H5V7 EBI-21792317 0.35 Q9H8E5 EBI-21793591 0.35 Q86TJ2 EBI-21794778 0.35 Q6ZMY9 EBI-21818150 0.35 P12724 EBI-21818048 0.35 Q86W54 EBI-21818307 0.35 GO:0005737 GO:0005829 GO:0005654 GO:0048471 GO:0030018 GO:0004161 GO:0004311 GO:0004337 GO:0042802 GO:0046872 GO:0004659 GO:0045337 GO:0033384 GO:0033386 GO:0008299 GO:0006720 Unknown UniProt Sequence Analysis MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTENIDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE 300 Q9WTN0 Geranylgeranyl Ggps1 10090 None SL-0198 Cytoplasm {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95749}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O95749}. UNIPROT Q9WTN0 Pfam PF00348 PROSITE PS00723 PROSITE PS00444 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}. GO:0005737 GO:0005829 GO:0005654 GO:0048471 GO:0030018 GO:0004161 GO:0004311 GO:0004337 GO:0042802 GO:0046872 GO:0004659 GO:0045337 GO:0033384 GO:0033386 GO:0008299 GO:0006720 Unknown UniProt Sequence Analysis MEKTKEKAERILLEPYRYLLQLPGKQVRSKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDSSKLRRGFPVAHSIYGVPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDTYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLDTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTENIDIKKYCVQYLEDVGSFAYTRHTLRELEAKAYKQIEACGGNPSLVALVKHLSKMFTEENK 300 Q6F596 Geranylgeranyl Ggps1 10116 None SL-0198 Cytoplasm {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95749}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O95749}. UNIPROT Q6F596 Pfam PF00348 PROSITE PS00723 PROSITE PS00444 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}. GO:0005737 GO:0005829 GO:0005654 GO:0048471 GO:0030018 GO:0004161 GO:0004311 GO:0004337 GO:0042802 GO:0046872 GO:0004659 GO:0045337 GO:0033384 GO:0033386 GO:0008299 GO:0006720 Unknown UniProt Sequence Analysis MEKTKEKAERILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDSSKLRRGFPVAHSIYGVPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDTYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLDTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTENIDIKKYCVQYLEDVGSFEYTRYTLRELEAKAYKQIEACGGNPSLVALVKHLSKMFTEENE 300 P36268 Inactive GGT2P 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:23682772}. Endoplasmic reticulum {ECO:0000269|PubMed:23682772}. Note=Co-localizes with calnexin in the endoplasmic reticulum. UNIPROT P36268 PROSITE PS00462 OMIM 137181 [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}. GO:0005783 GO:0070062 GO:0048471 GO:0005886 GO:0006751 GO:1901750 GO:0031179 GO:0002682 GO:0050727 Unknown UniProt Sequence Analysis MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAMAADAKQCLEIGRDTLRDGGSAVDAAIAALLCVGLMNAHSMGIGVGLFLTIYNSTTGKAEVINAREVAPRLAFASMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAVLENKRTVIEQQPVLWYVFCRDRKVLREGERLTLPRLADTYEMLAIEGAQAFYNGSLMAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDAVLYMPSARLSGPVLALILNILKGYNFSRESVETPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRSQISDHTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVCSPVSGILFNNEWTTSALPAFTNEFGAPPSPANFIQPGKQPLLSMCLTIMVGQDGQVRMVVGAAGGTQITTDTALAIIYNLWFGYDVKRAVEEPRLHNKLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAALDSRKGGEPAGY 569 Q8N2G8 GH3 GHDC 9606 None SL-0178 Endoplasmic reticulum {ECO:0000250|UniProtKB:Q99J23}. Nucleus envelope {ECO:0000250|UniProtKB:Q99J23}. UNIPROT Q8N2G8 UNIPROT B4DQS4 UNIPROT E9PDB5 UNIPROT Q9BXM6 Pfam PF03321 OMIM 608587 Q9R1X4 EBI-11011611 0.35 Q14114 EBI-11117560 0.35 P22460 EBI-21505491 0.35 P32297 EBI-21506200 0.35 Q9Y5I4 EBI-21510892 0.35 Q9UGM1 EBI-21517134 0.35 Q2Y0W8 EBI-21566582 0.35 Q9UN71 EBI-21584146 0.35 Q96FV3 EBI-21591007 0.35 Q9H813 EBI-21593240 0.35 Q01814 EBI-21599092 0.35 P62079 EBI-21619035 0.35 Q15884 EBI-21620222 0.35 Q9Y312 EBI-21626257 0.35 Q9Y5M8 EBI-21633655 0.35 Q7Z3C6 EBI-21657035 0.35 Q16281 EBI-21687526 0.35 Q9Y5H8 EBI-21695064 0.35 Q96T55 EBI-21753509 0.35 Q9BY50 EBI-21815157 0.35 P48201 EBI-21833166 0.35 P07766 EBI-21842586 0.35 P49682 EBI-21274037 0.35 P32302 EBI-21274058 0.40 Q7TLC7 EBI-26377368 0.35 Q2TAZ0 EBI-26443127 0.35 GO:0005737 GO:0005783 GO:0005576 GO:0016020 GO:0005635 GO:0034774 GO:0035580 GO:0016881 Unknown UniProt Sequence Analysis MLLWPLLLLLLLLPTLALLRQQRSQDARLSWLAGLQHRVAWGALVWAATWQRRRLEQSTLHVHQSQQQALRWCLQGAQRPHCSLRRSTDISTFRNHLPLTKASQTQQEDSGEQPLPPTSNQDLGEASLQATLLGLAALNKAYPEVLAQGRTARVTLTSPWPRPLPWPGNTLGQVGTPGTKDPRALLLDALRSPGLRALEAGTAVELLDVFLGLETDGEELAGAIAAGNPGAPLRERAAELREALEQGPRGLALRLWPKLQVVVTLDAGGQAEAVAALGALWCQGLAFFSPAYAASGGVLGLNLQPEQPHGLYLLPPGAPFIELLPVKEGTQEEAASTLLLAEAQQGKEYELVLTDRASLTRCRLGDVVRVVGAYNQCPVVRFICRLDQTLSVRGEDIGEDLFSEALGRAVGQWAGAKLLDHGCVESSILDSSAGSAPHYEVFVALRGLRNLSEENRDKLDHCLQEASPRYKSLRFWGSVGPARVHLVGQGAFRALRAALAACPSSPFPPAMPRVLRHRHLAQCLQERVVS 530 Q99J23 GH3 Ghdc 10090 None SL-0178 Endoplasmic reticulum {ECO:0000269|PubMed:11735219}. Nucleus envelope {ECO:0000269|PubMed:11735219}. UNIPROT Q99J23 UNIPROT A2A5D7 UNIPROT Q99J92 Pfam PF03321 GO:0005737 GO:0005783 GO:0005635 GO:0016881 Unknown UniProt Sequence Analysis MLLLWLLLLLLLLVPLLAILWQQRSRGARPCWLISLQHRVAWGMLGWAAAWQQWRLDRSTLNVGQSQQQALMWCLKKAQGSCCLPREDTDMRTFRNHLPLTQTSHTQEQESEETLPSPASPQYHGDASLQATLLGLITLNKAYPEALAPGSTACVTPTSPWPCSVPWLGHALGRVSPDGAKDPRTLLLEALISPGLRVLEARTAVELLDVFVGLEADGEELAEAIAAGILGTLLPKRAAELKEALEQGPRGLARRLWPKLQVVVTLDSGGQAEAVAALRVLWCQGLAFFSPAYAASGGVVALNLWPERPQGSYLLPPGVPFIELLPIKEGTQEEAASTLLLTDAQREKEYELVLTNHTSLTRCRLGDVVQVVGTYNQCPVVRFTCRLGQTLNVRGEVTDETVFSVALAQAVGQWPGAKLLDHVCVESRVLDSCEGSAPHYEVFVELRGLRNLSEENRDKLDNCLQEASAQYKSLRFRGSVGPAKVHLVRPGSFRVLREALAAFSSSSCRPPEMPRVIRLRHLAQLLQKRVIS 532 Q22663 Globin-like glb 6239 None SL-0178 SL-0180 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}. UNIPROT Q22663 Pfam PF00042 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}. GO:0005737 GO:0016020 GO:0005652 GO:0005886 GO:0020037 GO:0046872 GO:0019825 GO:0005344 GO:0015671 GO:0001666 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:23251335} MGSSTSTPAPPPKKNKPEGRKADNQILNSYQKSIVRNAWRHMSQKGPSNCGSTITRRMMARKSTIGDILDRSTLDYHNLQIVEFLQKVMQSLDEPDKISKLCQEIGQKHAKYRRSKGMKIDYWDKLGEAITETIREYQGWKIHRESLRAATVLVSYVVDQLRFGYSRGLHVQGSRETKEDDEE 183 Q95ZK7 Defective gld 6239 None SL-0198 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}. UNIPROT Q95ZK7 UNIPROT Q95ZK6 PDB 3N89 PDB 4ZRL Pfam PF17905 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}. O17670 EBI-334985 0.00 G5EDS1 EBI-336095 0.00 G5EFL5 EBI-341465 0.00 Q95QA6 EBI-341819 0.00 O17087 EBI-3891184 0.51 O76572 EBI-6535647 0.37 Q10666 EBI-11467458 0.37 Q10953 EBI-11467642 0.37 Q8I4M5 EBI-14989511 0.63 Q09312 EBI-14989599 0.37 Q9N5M6 EBI-14989696 0.54 GO:0005737 GO:0043186 GO:0048471 GO:0030880 GO:0031379 GO:1990749 GO:0019904 GO:0003723 GO:0009792 GO:0018992 GO:0042078 GO:0042006 GO:0051321 GO:0000281 GO:0006378 GO:0006397 GO:0051100 GO:0002119 GO:0000280 GO:0010628 GO:0060903 GO:0045836 GO:0045840 GO:0040018 GO:0006417 GO:0043631 GO:0007283 GO:0040025 Unknown UniProt Sequence Analysis MGEQSHEKDHDEAHSYNPFVRSAVEYDADTRLQMAENAASARKLFVSSALKDIIVNPENFYHDFQQSAQMAEDANQRRQVSYNTKREAHIHQLKAQGLPLPSNIPMIEINPTRVTLNMEFESQYYSLMTSDNGDHENVASIMAETNTLIQLPDRSVGGTTPDPFAQQVTITGYFGDVDRARMLMRRNCHFTVFMALSKMKMPLHELQAHVRQNPIQNVEMSFVDAPEKNGIVTTYLRITAREKNQHELIEAAKRLNEILFRESPAPENNFTLHFTLSTYYVDQVLGSSSTAQLMPVIERETTTIISYPCYNNRNETRGNIYEIKVVGNIDNVLKARRYIMDLLPISMCFNIKNTDMAEPSRVSDRNIHMIIDESGIILKMTPSVYEPADLLSGEVPLNCASLRSKEFNIKKLYTAYQKVLSKKFDFIAPQPNDYDNSIWHHSLPANFLKNFNMPCRGELSDGSNGRRHRSSSIASSRSKHSYMSKGKQFSESSGGPSRSHTRVSSFSENSSTVPIMQFPTPHFAPPMLTPHHHMLKYVYLQQHQQAQTFLKGAAGLHPGTHIMFPPPIIVDGSFVSALPFADPVVFDGFPYVHGLFPVNEAEQHRNHRESSPSLRSTQEIRKPSRNMGNRPSSSTGSYYPSTTPRQRVYEQVREDDLRSHIGSRRTSVNGDDQNVESMHDQGYERQYPRQHQRLQKDDQQRWKTGSRGDIHSSRTINVHRDVRNSNEYDFHVGNSGPAKRSPSLEQVQLQMTHHLKLKSNDVDLDHEKLYMHESPHNDSDTTVSASGFGNDLMDGDFVQRFLSNANINESGRRPRTVSCFTEKDGQSARYIDSDGAYSVVDHASTHQSRSYDSFRKVGDNGVTKTILEPRARVEKDYGKISLEHKTKYSNEYGDEEKSAENDTSSLGSRQYRIDPMKLIASVRESSEQLPRIHERQFSDVLNEKEKEIADKSIESTVTQDLSLDETSTY 969 G5EFL0 Poly(A) gld 6239 None SL-0198 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}. UNIPROT G5EFL0 Pfam PF01909 Pfam PF03828 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}. O02101 EBI-25616084 0.35 GO:0005737 GO:0005730 GO:0043186 GO:0048471 GO:0005844 GO:0031499 GO:0005524 GO:0046872 GO:0004652 GO:0051321 GO:0006378 GO:0031123 Unknown UniProt Sequence Analysis MNEDSRLSSSQQPSTSTPRSSIPSTMNSDEPNTCRRLSQSQEQPSTSRTCKSETPEFGYSDSLPFAPWRRKRYGLNIQGLHEEIVDMYHWIKPNEIESRLRTKVFEKVRDSVLRRWKQKTIKISMFGSLRTNLFLPTSDIDVLVECDDWVGTPGDWLAETARGLEADNIAESVMVYGGAFVPIVKMVDRDTRLSIDISFNTVQGVRAASYIAKVKEEFPLIEPLVLLLKQFLHYRNLNQTFTGGLSSYGLVLLLVNFFQLYALNMRSRTIYDRGVNLGHLLLRFLELYSLEFNFEEMGISPGQCCYIPKSASGARYGHKQAQPGNLALEDPLLTANDVGRSTYNFSSIANAFGQAFQILLVAVTLRERKGKNHVAMRAYKGSLLHLIMPFTSKELTYRNWLMSGVLSMPGQEAPASYDLNQLHNTLVSPMVDLSRYAWLRKAPAKAEKRDSRPLTIVNPADDRQTLAQQLKKQILEQTEAKKSLEKMPACDDNKKEEELVATRETDVELEAEDTESEGHHNGENDLILTGPPLPTSTQSVNTSATVSTAASISEREDTDSPGLSSSMGNQSSEEDEDNGINNRNNSAVPVQFKKPFNEVVAQPARESKRTQTTSEDKMQDQFHFNGYSYPPPSRYAAGTAAPSHKHRNAHPQRQRPSIRNLSQGSDGSDEYNVESWNNNIRQGRRASSNSPSPSRQQTNTRNCGPTNNIPYDSFRSQNKNSTLDGSNNSSEEPITMYADVVKKKSSITTSTNTSTADVNVTNGNPIPANGIIPQSMAVVNVGRGSYRNALTTSPMTPPSAHTSMQKQHHLRKDNECGFDNNSATSSTDLSHHQPQLVPPVNRLQR 845 Q0WPZ7 mRNA GLE1 3702 None SL-0178 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT Q0WPZ7 UNIPROT Q9SAE5 Pfam PF07817 Required for seed viability. {ECO:0000269|PubMed:22898497}. GO:0005737 GO:0005635 GO:0044614 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0016973 GO:0015031 GO:0006446 GO:0006449 GO:0048316 Unknown UniProt Sequence Analysis MGIVLEPPCPKSVDGISIDPEPNWNFESLVAEIASVEKKLNGFSMYPQPITNTTLRMGRRGGGFVMHVSEDEMESDEGEESDDEEEEEDHSQICTAGKRFACDELYLSDESDEEFDHEPEYMMNKLGLAESALYEVINDHQTEIKDDIRNQVSVVETEIMNEIETSLSAIARVEKYSETRKEVERKLDLQYQRKVAEALDTHLTAVQREHKIKSQIEERKIRSEEAQEEARRKERAHQEEKIRQEKARAEAQMLAKIRAEEEKKEVERKAAREVAEKEVADRKAAEQKLAEQKAVIESVTGSSATSNAQAGGNSIRAAESALILENHRLKKLEELETTNQSLKSRSNENFSSFEKHIGRVIRQISGTKDSVSGKINDIVKIFKDPRCPVSISIAAFAKKMVTTKEKPNPFACSYVIVYINSQFPQVMDILLAEFHKACIYTVPKHIVNSQSAWDSDAYERLDSIMRLYGALVQTDIRVGNATNVHGIEHGWAWLARFLNKIPANRATATALNSFLQTAGFGLHQRYKSQFLKVVNVVREHFLQKLRAKKDTSDLLVIIAEITAYLDDRMYLKEPEGRAMKTTSTLSSELTAELNQPNYNQNYQRNDYRNYY 611 Q3ZBK7 mRNA GLE1 9913 None SL-0178 SL-0185 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}. UNIPROT Q3ZBK7 Pfam PF07817 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}. GO:0005814 GO:0005813 GO:0036064 GO:0005737 GO:0005829 GO:0031965 GO:0044614 GO:0005730 GO:0042802 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0016973 GO:0015031 GO:0006446 GO:0006449 Unknown UniProt Sequence Analysis MPSEGRCWETLQALRSCDKGRLCYDRDWLLRGEDVLQECMSLPKLSSYSGWVVDHVLPHIQKNAPPSETSASSVSTSALDQPSSVPRSPLRNPAYSPVSSATSNGTKDKYESPHTEPVVLQSPRGMKVEGCIRMYELVHRMKGAEGLRQWQEEQEKKVRALSEMASEQLKRFDERKELKHHKEFQDLREVMEKSSREALGQQEKLKAEHRHRAKILNLKLREAEQQRLKQEEQERLRKEEGQARLRGLYALQEEVLHLSQQLDASDQHRDLLQVDLSAFRTRGNQLCSLVSGIIRATSENGFPTVEDQAAAEGALQEMRDLLSNLHQEIRRACEEKRRRDEEEARIKQQESQMQQRPEAHKELPVPNQGPGAKPNEDLQMKVQDSTMQWYQQLQEASSRCVLAFEGLSNSKDSQAKKIKMDLQKAATIPVSQISTIAGSKLKEIFDKIHSLLSGKPVQSGGRSVSVTLNPQGLDFVQYKLAEKFVKQGEEEVASHHEAAFPIAVVASGIWELHPRVGALILAHLHKKCPYSVPFYPAFKEGMALEDYQRMLGYQVKDSKVEQQDNFLKRMSGMIRLYAAIIQLRWPYGNRQETHPHGLNHGWRWLAQILNMEPLSDVTATLLFDFLEVCGNALMKQYQVQFWKMILLIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQHREVPVPKGFLTASFWRS 698 G0S7F3 mRNA GLE1 759272 None SL-0178 SL-0182 SL-0185 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}. UNIPROT G0S7F3 UNIPROT G0ZGT9 PDB 6B4G PDB 6B4H Pfam PF07817 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}. GO:0031965 GO:0005643 GO:0016973 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q12315} MAGSSPLNHHLWSSPSRTVEEILAEDRNSEARHRYLLELARKEHERVREEAARIYREQLAREERERLLAERRKEEERIRLEQQIAAENARLNALKATRIEIPPLLPDPVPAPSTVNGKPTLPAAVATEAKRCPSEPSLVNGIASNGVVEAPAAASIKTLEPAKPAASAFKAAGSATTAAPVAPIASVQPSTNGVVSAVASTPKTAPPAPTETPPDRYVEIHRNLKGLRKYMAEQAKTNLKLKQRMGDMRREIRKSVGQLTTGGMAANKDKQQKIKSILTEALSNQVESALVDPNNFVVEPRKPVEGATNNDPLLPSIFVYLINIFAKAAISQFINEAGARPETADPVGICVAAILSEPDFLWRGASLIDILIAKFRIVCPVLFGYRGSEKTEQGRQRLGWWKESGQWISEQQHMDRMTGLGAGFAAISLRKFALSKKQNPYPPRFYWMAMAKIVNTPPAEISNTQCVVLKAMVQNYEAKFIEFYGSAAIAALRTALIDFPARAPHKSAAVNSLEVLAQMLKRDTGLDLG 529 Q6DRB1 mRNA gle1 7955 None SL-0178 SL-0185 Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q53GS7}. UNIPROT Q6DRB1 UNIPROT Q502U5 Pfam PF07817 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}. GO:0005737 GO:0005576 GO:0044614 GO:0000822 GO:0005543 GO:0031369 GO:0060287 GO:0006406 GO:0048666 GO:0016973 GO:0015031 GO:0060296 GO:0006446 GO:0006449 GO:0014044 GO:0014037 GO:0014010 Unknown UniProt Sequence Analysis MPSENLRWETLEALKNSPKGKLKYSPDWVEKGEDVLAGCVEVPSLSPLSGQILKRMSPRMLLKNCSRSSSVRDTSPGLSEEAAVCRSAPISPRLKRSSCSLPAVSIQTEEEEEKEEEEKAEVVVEAPAVSPEASVSTPPAVSVLSPRATQISGCIRMCEQKHKAKAKMELSLRQEQQERLVATVANHESEQLKRFEEFMELKQRQEHQSIRDTNEKEAQESLGRQEKLREEHRHRMKILNLRLREMEQQRLREVELERQRQVEGRERHRAINAIQEEVLQLNRLLQPQQSTHAEVEHAPYITRGNQLCSQLSEVVPAAADDQFPSVEDLSVAERALQEMRSLVRSLQEAVSQAAERKKKKEQEEEEEKRRQEQLKAQQEEQKKSAALSAKEKAKKEGLQTGADDSTLKWYNSLQDLANQCAQAFDDLNKAKDTQTKKLKMELQKAATTPVSQIANSSGAPLKEAFEKIDKLLSRRPVTSAGKTVSTSQHPQGLEFASYRLAEKFVKQGEEEVASNHSAAFPIGAVASGIWELHPKIGDLILAHLHKKCPYAVPHYPPMESGTSVEDYQKILGYRVDEGKVEGQDSFLKRMSGMIRLYAAIIQMRWPYSSKQGLHLHGMNHGWRWMAQILNMEPLADITATILFDFLEVCGNALMKQYRVQFWKLILIINEEYFPRYLCFASILHFTCIHWLQNIE 695 Q55FW7 mRNA gle1 44689 None SL-0178 SL-0185 Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. UNIPROT Q55FW7 Pfam PF07817 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}. GO:0005737 GO:0031012 GO:0044614 GO:0000922 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0016973 GO:0015031 GO:0006446 GO:0006449 Unknown UniProt Sequence Analysis MNKTSSNNISNTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNRILSPFKRNNSKENGNGSVTITLEPLVSPFKLIKSNFKDDVHTNNINNNNNKIKRFLDEDNEFEITIPIRRSGNSINFNIGIVPSSNKKQQQQQQQQQKQKQKKKKTLSPLKKAPGIYSLKDLTIDSDSDSDSYSDNDDNEEYNIKLKSPIKNKIVNNNNNQQQQQKQKEKEEKEEKEKVEKDKKEKDKKKLILNSFQSELIINRVEREREIKINRIVEEKNKEIDDKWVEIKEYNQNQMIKERKEFHSQQIRLNNLIKKQHKKDIKEFSIKLKQAKQKHQSELSESLSLLNQLNKLEQQEIDRHNEELLKYELAIKEEKRKQQQLIERYEQKKREEKQRQLQQEQKEKQEKLEKEEKEKEQQEQQKQLLIKLAKEKEEKEKFEKEQQQQKEKELQKEKELLQQKEKEKEKEKLQQQQQQQQQQQQQQQQQLQQQQQQQNQQNNNLGYIKKDGIIFSLNENSKNFNDFKERSKEFDMIIKFINEKKSMLSREMVEFERQNSKLINIAINQISASQEQVNEKTNKLIKSIQDSQQSDYLKKSTILSIVKKSLSQVESQITFHNASSFPLALVLVRVGEKYPELIDCLLASLNEKCCYTVPYYVSPKENESQSSISKRMGYAFSNDIVGDNDKPIETEDEFHKRICGYLSLYCALILKSEQPHKSSSSSSSSSSSTMMFGFGTQIGNNNNNKLINKNLNIESSLRWLKDLVSLRPRRITSYLFVTFFTHLGNLLSKNQKSSLEFKIIVGKIVEENFFNQMNKPGTEGSFSRLKNLIEEYYKTGTFQQHEGVDF 837 Q9V4W1 mRNA Gle1 7227 None SL-0178 SL-0185 Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. UNIPROT Q9V4W1 Pfam PF07817 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}. Q9VT04 EBI-9943330 0.35 P18824 EBI-9949245 0.35 P49415 EBI-9965823 0.35 GO:0005737 GO:0005643 GO:0044614 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0016973 GO:0015031 GO:0006446 GO:0006449 Unknown UniProt Sequence Analysis MDDMMRAMDCLNMAATLRNAALASATCTGRTLGEDREPIWVEGSRKTPEPPLPEESPAPEPNNEIPLLPKIDFEPNISCFPDLQAINASIVRRELEEEGKRCVRQQLKAIRDKQDAMRLSRETQQRKEERQRDQLQQKALRERNESLLIQKADQMTAAQLEAQQREQLALRQQIDQKLHKLALEGVSRCQRRFNQKYEGIAKILLSLNPETVKVCAAQNTQLKELGQKFEQLVSSVKMGNCEMQSQFLCSIIKAEEFCKSLDALELDIIKQLAEFSEQIQQQLKMEAAKKLEDERQRQQQQEEERQKLEEQQKLEEQEKLRKEKEESAAKEKQQEAETAKADAANVPAPLEPKSQDVPPAATATSTSVHPDRLKFYNDILALYQSKVDAVKPLQTEESLKQYRTGCQRAINLPLNAISAVSPQHLAQNFDKLYSFFAGQPTKVMNGTITINDHPLARDYCMLLMAKKFVSQTETAICSNPQAAFPFASVIITFWKLLPDFGKVFLAYMYKESPFLVPYVIPQQQGQTPEQYLKTIGYRLTDKNELEKPDIYLKRQTGLARLYAAVIISQGRKAAGPDECFELNEGWLWLAHMVHVKPLPDISATLIMEILQTLGFELWRTYGKQFVKLLVYIQNIYMPQLAAYDEGGPKTRLEMLLAKFLRERQIAQAVGVLPPGFW 677 Q53GS7 mRNA GLE1 9606 None SL-0178 SL-0185 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}. UNIPROT Q53GS7 UNIPROT O75458 UNIPROT Q53GT9 UNIPROT Q5VVU1 UNIPROT Q8NCP6 UNIPROT Q9UFL6 PDB 6B4F PDB 6B4I PDB 6B4J Pfam PF07817 OMIM 253310 OMIM 603371 OMIM 611890 DisGeNET 2733 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}. 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. O75694 EBI-8873568 0.37 P49790 EBI-11076796 0.35 P57740 EBI-11160436 0.35 Q14974 EBI-11115566 0.35 P06103 EBI-1955784 0.40 O00303 EBI-1955532 0.57 Q53GS7 EBI-8873329 0.58 Q86UP2 EBI-8873563 0.37 Q6PFD9 EBI-10994876 0.35 Q8BH74 EBI-10997196 0.35 Q9ERU9 EBI-10999306 0.35 P63280 EBI-11044140 0.35 Q96EE3 EBI-11086798 0.35 P03427 EBI-14404759 0.35 Q9GZY0 EBI-21528397 0.35 P10412 EBI-21665473 0.35 Q9BTL4 EBI-21675209 0.35 Q15050 EBI-21678544 0.35 Q9UBU9 EBI-21728803 0.35 Q8N4J0 EBI-21736494 0.35 Q02539 EBI-21742951 0.35 P58499 EBI-25859236 0.56 Q9UBF1 EBI-25859228 0.56 Q9Y575 EBI-25859218 0.56 Q9Y2M5 EBI-25859210 0.56 Q00994 EBI-25859202 0.56 Q9UGC6 EBI-25859194 0.56 O75409 EBI-25859186 0.56 Q9Y2L8 EBI-25859178 0.56 Q29RF7 EBI-25859170 0.56 Q9Y483 EBI-25859162 0.56 Q9NS23 EBI-25859154 0.56 Q16520 EBI-25859146 0.56 O76041 EBI-25859138 0.56 Q9Y239 EBI-25859130 0.56 Q9UNE7 EBI-25859122 0.56 O60641 EBI-25859114 0.56 Q86V28 EBI-25859106 0.56 O75558 EBI-25859098 0.56 O75379 EBI-25859090 0.56 O75925 EBI-25859082 0.56 Q9UNS2 EBI-25859074 0.56 Q99598 EBI-25859066 0.56 P54274 EBI-25859058 0.56 Q12824 EBI-25859050 0.56 Q9BR81 EBI-25859042 0.56 Q16621 EBI-25859034 0.56 P27338 EBI-25859026 0.56 P26439 EBI-25859018 0.56 P06241 EBI-25859010 0.56 O15287 EBI-25859002 0.56 O60220 EBI-25858994 0.56 Q9UER7 EBI-25858986 0.56 P51798 EBI-25858978 0.56 P24863 EBI-25858970 0.56 Q96D59 EBI-25859358 0.56 Q68EA5 EBI-25859350 0.56 A5D8V7 EBI-25859340 0.56 Q9UII2 EBI-25859332 0.56 Q8IY31 EBI-25859324 0.56 Q8WYH8 EBI-25859316 0.56 Q5T0J7 EBI-25859308 0.56 Q9GZS3 EBI-25859300 0.56 Q8NHQ1 EBI-25859292 0.56 Q969K3 EBI-25859284 0.56 Q9NS71 EBI-25859268 0.56 Q96FW1 EBI-25859260 0.56 Q96EN9 EBI-25859252 0.56 Q8TAG9 EBI-25859244 0.56 Q8N895 EBI-25859382 0.56 Q8IYD9 EBI-25859374 0.56 Q86WT6 EBI-25859366 0.56 Q68G74 EBI-25859424 0.56 Q96M61 EBI-25859416 0.56 Q7Z698 EBI-25859398 0.56 Q8IZU1 EBI-25859390 0.56 Q04912 EBI-32725158 0.27 GO:0005814 GO:0005813 GO:0036064 GO:0005737 GO:0005829 GO:0005615 GO:0016020 GO:0005635 GO:0031965 GO:0005643 GO:0044614 GO:0005730 GO:0042802 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0006913 GO:0016973 GO:0015031 GO:0006446 GO:0006449 Unknown UniProt Sequence Analysis MPSEGRCWETLKALRSSDKGRLCYYRDWLLRREDVLEECMSLPKLSSYSGWVVEHVLPHMQENQPLSETSPSSTSASALDQPSFVPKSPDASSAFSPASPATPNGTKGKDESQHTESMVLQSSRGIKVEGCVRMYELVHRMKGTEGLRLWQEEQERKVQALSEMASEQLKRFDEWKELKQHKEFQDLREVMEKSSREALGHQEKLKAEHRHRAKILNLKLREAEQQRVKQAEQERLRKEEGQIRLRALYALQEEMLQLSQQLDASEQHKALLKVDLAAFQTRGNQLCSLISGIIRASSESSYPTAESQAEAERALREMRDLLMNLGQEITRACEDKRRQDEEEAQVKLQEAQMQQGPEAHKEPPAPSQGPGGKQNEDLQVKVQDITMQWYQQLQDASMQCVLTFEGLTNSKDSQAKKIKMDLQKAATIPVSQISTIAGSKLKEIFDKIHSLLSGKPVQSGGRSVSVTLNPQGLDFVQYKLAEKFVKQGEEEVASHHEAAFPIAVVASGIWELHPRVGDLILAHLHKKCPYSVPFYPTFKEGMALEDYQRMLGYQVKDSKVEQQDNFLKRMSGMIRLYAAIIQLRWPYGNRQEIHPHGLNHGWRWLAQILNMEPLSDVTATLLFDFLEVCGNALMKQYQVQFWKMLILIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQHKDIPVPKGFLTSSFWRS 698 Q8R322 mRNA Gle1 10090 None SL-0178 SL-0185 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}. UNIPROT Q8R322 UNIPROT A3KGV8 UNIPROT Q3TT10 UNIPROT Q3TU23 UNIPROT Q3UD65 UNIPROT Q8BT16 UNIPROT Q9D4A6 Pfam PF07817 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}. Q4KLN8 EBI-26596375 0.35 GO:0005814 GO:0005813 GO:0036064 GO:0005737 GO:0005829 GO:0005635 GO:0031965 GO:0005643 GO:0044614 GO:0005730 GO:0042802 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0006913 GO:0016973 GO:0015031 GO:0006446 GO:0006449 Unknown UniProt Sequence Analysis MPSDGRCWETLRALRNTSKGRLRYDREWLLRYEDVLEECMSLPKLSSYSGWVVDHILPNTSGHTQESAPSSDNSPSSGSASGLYQSSLLKSPVRSSPQSPSPSSPNGTQSTHESPFTEPIAPQSSRAIKVEGCIRMYELAHRMRGTEGLRQWQEEQERKVRALSEMASEQLKRFDELKELKLHKEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKILNLKLREAEQQRVKQAEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLCGLISSIIRTTLESGYPTAENQAEAERALQEMRDLLSDLEQEITRASQVKKKHEEEAKVKRQESQVQQGPAPPTQTSAPSPSPVGAQNEDLQVKVQDSTMQWYQQLQDASAKCVLAFEDLTSSKDSQTKKIKMDLQKAATIPVSQISTIAGSKLKEIFDKIHSLLSGKPVQSGGRSVSVTLNPQGLDFVQYKLAEKFVKQGEEEVASHHEAAFPIAVVASGIWMLHPKVGDLILAHLHKKCPYSVPFYPAFKEGMALEDYQRMLGYQVTDSKVEQQDNFLKRMSGMIRLYAAIIQLQWPYGNRQEAHPHGLNHGWRWLAQVLNMEPLSDVTATLLFDFLEVCGNALMKQYQVQFWKMILLIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQRREIPVPRGFLTTSFWRS 699 Q5RAS2 mRNA GLE1 9601 None SL-0178 SL-0185 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}. UNIPROT Q5RAS2 Pfam PF07817 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}. GO:0005737 GO:0005643 GO:0016973 GO:0015031 Unknown UniProt Sequence Analysis MPSEGRCWETLQALRSSDKGRLCYYRDWLLRGEDVLEECMCLPKLSSYSGWVVEHVLPHMQENQPLSETSPSSTSASALDQPSFVPKSPDTSSAFSPASPATPNGTKGKDESQHTESMVLQSSRGIKVEGCIRMYELVHRMKGTEGLRQWQEEQERKVRALSEMASEQLKRFDEWKELKQHKEFQDLREVMEKSSREALGHQEKLKAEHRHRAKILNLKLREAEQQRVKQAEQERLRKEEGQVRLRALYALREEMLQLSQQLDASEQHKGLLKVDLAAFQTRGNQLCSLISGIIRASSESGYPTTESQAEAERALQEMRDLLMNLGQEITRACEDKRRQDEEEAQVKLQEAQMQQRPEAHKEPPAPSQGPGGKQNEDLQVKVQDITMQWYQQLQDASMQCVLTFEGLTNSKDSQAKKIKMDLQKAATIPVSQISTIAGSKLKEIFDKIHSLLSGKPVQSGGRSVSVTLNPQGLDFVQYKLAEKFVKQGEEEVASHHEAAFPIAVVASGIWELHPRVGDLILAHLHKKCPYSVPFYPTFKEGMALEDYQRMLGYQVKDSKVEQQDNFLKRMSGMIRLYAAIIQLRWPYGNRQEIHPHGLNHGWRWLAQILNMEPLSDVTATLLFDFLEVCGNALMKQYQVQFWKMLILIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQHKDIPVPKGFLTSSFWRS 698 Q4KLN4 mRNA Gle1 10116 None SL-0178 SL-0185 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}. UNIPROT Q4KLN4 Pfam PF07817 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}. GO:0005814 GO:0005813 GO:0036064 GO:0005737 GO:0005635 GO:0044614 GO:0042802 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0016973 GO:0015031 GO:0006446 GO:0006449 Unknown UniProt Sequence Analysis MPSDGRCWETLRALRNSSKGRLRYDREWLLRYEDVLEECMSLPKLSSYSGWVVDHILPNTSHHTQENAPSSDNSPSSGSASGLYQSTLKSPVRSSPQSPSPSTPSGTQSAHESPFTEPIALQSSRAIKVEGCIRMYELAHRMRGTEGLRQWQEEQERKVQALSEMASEQLKRFDELKELKLHKEFRDLQEVMEKSTREALGHQEKLKAEHRHRAKILNLKLREAEQQRVKQAEQEQLRKEEGQIRLRSLYTLQEEVLQLNQQLDASSQHKDLLNVDLAAFQTRGNQLCGLISGIIRTTLESGYPTAENQAEAERVLQEMRDLLSNLEQEITRASEMKKKDEEEARVKLQESQVQQGPGAPTKTSAPSPSLVGTQSEDLQVKVQDSTMQWYQQLQDASAKCVLAFEDLTSSKDSQIKKIKMDLQKAATIPVSQISTIAGSKLKEVFDKIHSLLSGKPVQSGGRSVCVTLNPQGLDFVQYKLAEKFVKQGEEEVASHHEAAFPIAVVASGIWMLHPKVGDLILAHLHKKCPYSVPFYPAFKEGMPLEDYQRMLGYQVTDSKVEQQDNFLKRMSGMIRLYAAIIQLQWPYGSRQEAHPHGLNHGWRWLAQILNMEPLSDVTATLLFDFLEVCGNALMKQYQVQFWKMILLIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQRREIPVPKGFLTPSFWRS 698 O94652 mRNA gle1 284812 None SL-0178 SL-0182 SL-0185 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}. UNIPROT O94652 Pfam PF07817 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}. Q09847 EBI-21243865 0.37 GO:0005737 GO:0005829 GO:0005635 GO:0031965 GO:0034399 GO:0005643 GO:0044614 GO:0005634 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0016973 GO:0015031 GO:0006446 GO:0006449 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:16823372} MDTKTTPLIHAKLDEKIISSYNDANGLDIDDLWDIYNEKTRRMIHIISQRYKPKKQSPFPVIADENVRIFPPLHKTIDWAKKRNVEEQNLIEQSITESQRIFSEKQRLEQERFNRELLEKKRIEAERQRLKDEEERRKKELMEKEKKEKERIRLIEEQKHKENEQRRLKQEQIDAKRKEEEAREKRMKETFKDDPEEDSNMAWSIIHKIKTEVVAPISEKKELKNYCFTQKRKITPRLGQITKSNSQIMKITQLLQQTFQEARNTDPLVYKWVLNFFCKSVVKQAEAEVAVNPISAYPLAKVCLLLQTQNADLKDLLFARLQKNCPWVIPFWYDHGTENGKKKMGFKKLSDGHWEQNTTYNERQCGIFAVYAAILSLDDSLAPESWRTFSRLLNLPSPSQLMKSDLELGQTLCSIVSTYLDIAGQSLLRIYGRQAKKLIVCSFSEAYLGANGGGSQYGRLRIVGEDWMKGQGGLKFSFEP 480 Q12315 mRNA GLE1 559292 None SL-0178 SL-0182 SL-0185 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. UNIPROT Q12315 UNIPROT D6VRE7 PDB 3PEU PDB 3PEV PDB 3RRM PDB 3RRN PDB 6B4E Pfam PF07817 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}. P14907 EBI-849734 0.32 P20449 EBI-15806702 0.76 P20676 EBI-849734 0.32 P32500 EBI-11888204 0.37 P34077 EBI-849734 0.32 P35729 EBI-849734 0.32 P36161 EBI-849734 0.32 P38181 EBI-849734 0.32 P39705 EBI-849734 0.32 P40064 EBI-849734 0.32 P40066 EBI-849734 0.32 P40368 EBI-849734 0.32 P40477 EBI-849734 0.32 P46673 EBI-849734 0.32 P47054 EBI-849734 0.32 P48837 EBI-849734 0.32 P49686 EBI-849734 0.74 P49687 EBI-849734 0.32 P52593 EBI-849734 0.32 P52891 EBI-849734 0.32 P53011 EBI-849734 0.32 Q02199 EBI-849734 0.32 Q02629 EBI-849734 0.53 Q02630 EBI-849734 0.32 Q03790 EBI-849734 0.32 Q04839 EBI-6473225 0.44 Q05166 EBI-849734 0.32 P38305 EBI-761900 0.40 Q12445 EBI-849734 0.32 Q02159 EBI-860728 0.00 P32505 EBI-1566458 0.35 Q12315 EBI-8873470 0.53 P12385 EBI-1928244 0.40 P05453 EBI-1954427 0.52 P06103 EBI-1955816 0.40 Q04067 EBI-1955824 0.40 P38074 EBI-8764779 0.37 P33302 EBI-20815093 0.37 GO:0005737 GO:0005739 GO:0005635 GO:0031965 GO:0005643 GO:0044614 GO:0008047 GO:0000822 GO:0005543 GO:0031369 GO:0006406 GO:0006397 GO:0006913 GO:0016973 GO:0015031 GO:0006446 GO:0006449 GO:0006409 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:10523319} MRFVFDEVFNSDTDSPEFEETCSTTSSTSSQCPTPEPSPAIKLPSFTKVGTKKLVNESVVILDPALENALRDLNLQSKLIPINEPIVAASSIIVPHSTNMPLPRASHSSLLDNAKNSNATAPLLEAIEESFQRKMQNLVLANQKEIQSIRENKRRVEEQRKRKEEEERKRKEAEEKAKREQELLRQKKDEEERKRKEAEAKLAQQKQEEERKKIEEQNEKERQLKKEHEAKLLQQKDKLGKAVTNFDKISKMFWHYKDKIAQIKQDIVLPIKKADVNVRNLLSRHKRKINPKFGQLTNSNQQLFKIQNELTQLINDTKGDSLAYHWILNFIAKAVVHQAETEVRVKPESALPLGKLTLYLLVQFPELQELFMARLVKKCPFVIGFTCEIDTEKGRQNMGWKRNNENKWEDNTSYDERMGGILSLFAIITRLQLPQEFITTTSHPFPIALSWHILARICNTPLNLITNTHFVILGSWWDAAAVQFLQAYGNQASKLLILIGEELTSRMAEKKYVGAARLRILLEAWQNNNMESFPEMSP 538 G0SEA3 mRNA GLE2 759272 None SL-0178 SL-0182 SL-0185 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}. UNIPROT G0SEA3 UNIPROT G0ZGV3 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. GO:0005829 GO:0031965 GO:0034399 GO:0005643 GO:0016973 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:P40066} MAGLFGTTTSTTTSTLGDLKNDVELGSPPEDSITDLSFNPNPNDPKDFLAVSSWDKKVRVYEIAANGQNQGKVQMEHEGPVFAVDFFKDGTKVISAGADKQAKVLDLASGQAMQVAAHDAPIRCVKYFEAGGTPMAVTGSWDKTIKYWDFRSATPAGTVQCQERVYTMDVKENLLVIGTADRYIDVINLKEPVKFYKTLQSPLKWQTRVVSCFTDSQGFAIGSIEGRCAIQYVEDKDQSMNFSFKCHRDTPQNNVTNVHAVNAISFHPQHGTFSTAGSDGTFHFWDKDAKHRLKGYPNVGGSITATKFNRNGTIFAYAISYDWSKGYQGNTANYPTKVMLHPVLGDECKPRPSVKKR 357 P40066 mRNA GLE2 559292 None SL-0178 SL-0182 SL-0185 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. UNIPROT P40066 UNIPROT D3DM14 Pfam PF00400 PROSITE PS50082 PROSITE PS50294 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}. P14907 EBI-797307 0.44 P34077 EBI-813993 0.27 P38305 EBI-761900 0.40 Q12315 EBI-849734 0.32 Q02630 EBI-795280 0.61 P11484 EBI-797307 0.35 P10591 EBI-797307 0.35 P40368 EBI-797307 0.44 P40477 EBI-797307 0.44 P10592 EBI-813993 0.27 P47054 EBI-813993 0.27 P48837 EBI-813993 0.27 Q04599 EBI-813993 0.27 P36516 EBI-813993 0.27 P22353 EBI-813993 0.27 P36523 EBI-813993 0.27 P36525 EBI-813993 0.27 Q06678 EBI-813993 0.27 P32337 EBI-7490608 0.40 P47019 EBI-8229717 0.22 P24870 EBI-2611503 0.35 P24869 EBI-2617071 0.35 P22696 EBI-2883245 0.00 P38915 EBI-4375569 0.35 P38129 EBI-4380674 0.35 P35177 EBI-4383599 0.35 Q03330 EBI-4385804 0.35 P53040 EBI-4390624 0.35 GO:0005737 GO:0005635 GO:0031965 GO:0005643 GO:0003723 GO:0043130 GO:0051664 GO:0006913 GO:0016973 GO:0000973 GO:0015031 GO:2000728 GO:0006405 GO:0000972 Peripheral UniProt Sequence Analysis MSFFNRSNTTSALGTSTAMANEKDLANDIVINSPAEDSISDIAFSPQQDFMFSASSWDGKVRIWDVQNGVPQGRAQHESSSPVLCTRWSNDGTKVASGGCDNALKLYDIASGQTQQIGMHSAPIKVLRFVQCGPSNTECIVTGSWDKTIKYWDMRQPQPVSTVMMPERVYSMDNKQSLLVVATAERHIAIINLANPTTIFKATTSPLKWQTRCVACYNEADGYAIGSVEGRCSIRYIDDGMQKKSGFSFKCHRQTNPNRAPGSNGQSLVYPVNSIAFHPLYGTFVTAGGDGTFNFWDKNQRHRLKGYPTLQASIPVCSFNRNGSVFAYALSYDWHQGHMGNRPDYPNVIRLHATTDEEVKEKKKR 365 P34689 ATP-dependent glh 6239 None SL-0198 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}. UNIPROT P34689 UNIPROT Q22873 UNIPROT Q7KQH5 UNIPROT Q9TXH4 Pfam PF00270 Pfam PF00271 Pfam PF00098 PROSITE PS00039 PROSITE PS51192 PROSITE PS51194 PROSITE PS51195 PROSITE PS50158 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}. P91001 EBI-1571788 0.51 O44408 EBI-1571866 0.40 Q9U3F4 EBI-1571938 0.40 P34689 EBI-1571975 0.40 O01836 EBI-1571991 0.40 GO:0005737 GO:0005634 GO:0043186 GO:0048471 GO:0005524 GO:0016887 GO:0017151 GO:0008432 GO:0043621 GO:0003723 GO:0003724 GO:0008270 GO:0030154 GO:0007276 GO:0007281 GO:0009791 GO:0016070 Unknown UniProt Sequence Analysis MSDGWSDSESAAKAKTGFGSGGGFGGGNNGGSGFGGGKNGGTGFGGGNTGGSGFGGGNTGGSGFGGGKTGGSGFGGGNTCGSGFGGGSTGGSPYGGASSGFGGSTATSGFGSGEKSSAFGGSGGFGGSATGFGSGGGSFGGGNSGFGEGGHGGGERNNNCFNCQQPGHRSSDCPEPRKEREPRVCYNCQQPGHTSRECTEERKPREGRTGGFGGGAGFGNNGGNDGFGGDGGFGGGEERGPMKCFNCKGEGHRSAECPEPPRGCFNCGEQGHRSNECPNPAKPREGVEGEGPKATYVPVEDNMEDVFNMQKISEGLMFNKFFDAEVKLTSSEKTVGIKPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGGCYPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDAMGFGTDIETIVNYDSMPRKENRQTLMFSATFPDSVQEAARAFLRENYVMIAIDKIGAANKCVLQEFERCERSEKKDKLLELLGIDIDSYTTEKSAEVYTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISEDCSLLSELVGVLADAQQIVPDWMQGAAGGNYGASGFGSSVPTQVPQDEEGW 763 Q27994 Solute SLC2A4 9913 None SL-0198 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}. UNIPROT Q27994 UNIPROT P79104 UNIPROT Q29RP5 UNIPROT Q6SI69 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 PROSITE PS00217 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}. GO:0030659 GO:0005829 GO:0012505 GO:0005768 GO:0009897 GO:0070062 GO:0032593 GO:0005887 GO:0016020 GO:0045121 GO:0048471 GO:0005886 GO:0042383 GO:0005802 GO:0030140 GO:0005355 GO:0015304 GO:0015149 GO:0010021 GO:0050873 GO:0032869 GO:0071470 GO:0071356 GO:0042593 GO:0044381 GO:1904659 GO:0015749 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPSGFQQIGSEDGEPPRQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPEGPGSIPPGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLFNNALAVLGGTLMGLAKAAASYEMLILGRFFIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVTGILIAQVLGLESMLGTATLWPLLLGITVLPALLQMVLLPLCPESPRYLYIIRNLEGPARKSLKRLTGWADVSEVLAELKEEKRKLERERPLSLLQLLGSHTHRQPLVIAIVLQLSQQLSGINAVFYYSTSIFESAGVEKPAYATIGAGVVNTVFTLVSVFLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFSNWTCNFIIGMGFQYVADAMGPYVFLLFAVLLLGFFIFTFLKVPETRGRTFDQISAVFHRTPSLLEQEVKPSTELEYLGPDEHD 509 Q9XST2 Solute SLC2A4 9615 None SL-0198 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}. UNIPROT Q9XST2 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 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}. GO:0030659 GO:0012505 GO:0032593 GO:0005887 GO:0016020 GO:0048471 GO:0005886 GO:0005355 GO:0015304 GO:0015149 GO:0032869 GO:0044381 GO:1904659 GO:0015749 Transmembrane UniProt Sequence Analysis {ECO:0000255} TSIFETAGVGQPAYATIGAGVVNTVFTLVSVFLVERAGRRTLHLLGLAGMCGCAILMTIALLLLERLPAMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFCNWTSNFIIGMGFQYIAXAMGPYVFLLFAVLLLAFFIFTFLKVPETR 162 P14672 Solute SLC2A4 9606 None SL-0198 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}. UNIPROT P14672 UNIPROT Q05BQ3 UNIPROT Q14CX2 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 PROSITE PS00217 OMIM 125853 OMIM 138190 DisGeNET 6517 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}. 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. Q9UER7 EBI-367160 0.63 P03410 EBI-9676334 0.49 O43889 EBI-12701388 0.56 Q9UKB3 EBI-21896803 0.35 Q8WU79 EBI-21896803 0.35 GO:0005905 GO:0030136 GO:0030659 GO:0005829 GO:0012505 GO:0009897 GO:0070062 GO:0032593 GO:0005887 GO:0016020 GO:0045121 GO:0005771 GO:0048471 GO:0005886 GO:0098793 GO:0042383 GO:0016529 GO:0030315 GO:0005802 GO:0030140 GO:0012506 GO:0055056 GO:0005355 GO:0015304 GO:0015149 GO:0010021 GO:0050873 GO:0005975 GO:0071456 GO:0032869 GO:0071470 GO:0071356 GO:0042593 GO:0046323 GO:0044381 GO:1904659 GO:0007611 GO:0007616 GO:0015749 GO:0031550 GO:0098694 GO:0045471 GO:0007614 GO:0150104 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPSGFQQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPEGPSSIPPGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLVNNVLAVLGGSLMGLANAAASYEMLILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILIAQVLGLESLLGTASLWPLLLGLTVLPALLQLVLLPFCPESPRYLYIIQNLEGPARKSLKRLTGWADVSGVLAELKDEKRKLERERPLSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFETAGVGQPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFSNWTSNFIIGMGFQYVAEAMGPYVFLLFAVLLLGFFIFTFLRVPETRGRTFDQISAAFHRTPSLLEQEVKPSTELEYLGPDEND 509 P14142 Solute Slc2a4 10090 None SL-0198 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}. UNIPROT P14142 UNIPROT Q3TPK6 UNIPROT Q9JJN9 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 PROSITE PS00217 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}. Note=Defects in Slc2a4 may be the cause of certain post- receptor defects in non-insulin-dependent diabetes mellitus (NIDDM). Q6P5E6 EBI-7540254 0.46 Q3U7R1 EBI-15762008 0.50 GO:0009986 GO:0005905 GO:0030136 GO:0005737 GO:0030659 GO:0005829 GO:0012505 GO:0005768 GO:0009897 GO:0070062 GO:0032593 GO:0016021 GO:0005887 GO:0043231 GO:0016020 GO:0045121 GO:0005771 GO:0048471 GO:0005886 GO:0098793 GO:0042383 GO:0016529 GO:0030315 GO:0005802 GO:0030140 GO:0031982 GO:0012506 GO:0055056 GO:0005355 GO:0015304 GO:0015149 GO:0005360 GO:0010021 GO:0050873 GO:0071456 GO:0032869 GO:0071470 GO:0071356 GO:0042593 GO:0046323 GO:0044381 GO:1904659 GO:0007611 GO:0007616 GO:0015749 GO:0031550 GO:0098694 GO:0045471 GO:0007614 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPSGFQQIGSDDGEPPRQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNATWLGRQGPGGPDSIPQGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLANNVLAVLGGALMGLANAAASYEILILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILVAQVLGLESMLGTATLWPLLLALTVLPALLQLILLPFCPESPRYLYIIRNLEGPARKSLKRLTGWADVSDALAELKDEKRKLERERPMSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFESAGVGQPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFSNWTCNFIVGMGFQYVADAMGPYVFLLFAVLLLGFFIFTFLKVPETRGRTFDQISAAFRRTPSLLEQEVKPSTELEYLGPDEND 509 Q9XT10 Solute SLC2A4 9823 None SL-0198 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}. UNIPROT Q9XT10 Pfam PF00083 PROSITE PS50850 PROSITE PS00217 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}. GO:0030659 GO:0012505 GO:0032593 GO:0005887 GO:0016020 GO:0048471 GO:0005886 GO:0005355 GO:0015304 GO:0015149 GO:0032869 GO:0044381 GO:1904659 GO:0015749 Transmembrane UniProt Sequence Analysis {ECO:0000255} QQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPNGPGSIPPGTLTTLWALSVAIFSVGGMFSSFLLGIISQWLGRKKAMLFNNTLAVLAGALMGLAKAAASYEMLILGRFLIGAYSGLASGLVPMYVGEIAPTHLRGALGTLNQLA 174 P19357 Solute Slc2a4 10116 None SL-0198 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}. UNIPROT P19357 UNIPROT P97900 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 PROSITE PS00217 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}. Note=It is a candidate for certain post-receptor defects in non-insulin-dependent diabetes mellitus. O54861 EBI-921030 0.35 P10536 EBI-921030 0.35 Q3L7M0 EBI-921030 0.35 P34067 EBI-921030 0.35 Q794F9 EBI-921030 0.35 O70351 EBI-921030 0.35 P62246 EBI-921030 0.35 Q9Z1A6 EBI-921030 0.35 O55012 EBI-921030 0.35 Q5I0E7 EBI-921030 0.35 Q64428 EBI-921030 0.35 Q63524 EBI-921030 0.35 Q2PS20 EBI-921030 0.35 O70257 EBI-921030 0.35 Q5XIA1 EBI-921030 0.35 P97700 EBI-921030 0.35 Q6NX65 EBI-921030 0.35 Q8R490 EBI-921030 0.35 P13264 EBI-921030 0.35 Q8R3Z7 EBI-921030 0.35 Q9JJM9 EBI-921030 0.35 Q4QRB4 EBI-921030 0.35 Q8K3W5 EBI-921030 0.35 P12368 EBI-921030 0.35 Q4QQW8 EBI-921030 0.35 P21263 EBI-921030 0.35 Q8CGU6 EBI-921030 0.35 Q8VI04 EBI-921030 0.35 Q812C4 EBI-921030 0.35 Q5U367 EBI-921030 0.35 Q7TSP3 EBI-921030 0.35 Q7TPK5 EBI-921030 0.35 Q7TPJ0 EBI-921030 0.35 Q7TPB1 EBI-921030 0.35 Q7TP77 EBI-921030 0.35 Q7TP72 EBI-921030 0.35 Q7TP59 EBI-921030 0.35 Q7TP54 EBI-921030 0.35 Q7TP34 EBI-921030 0.35 Q7TP13 EBI-921030 0.35 Q7TP11 EBI-921030 0.35 Q7TP08 EBI-921030 0.35 P26453 EBI-921030 0.35 Q7M0E3 EBI-921030 0.35 Q794E4 EBI-921030 0.35 Q792I0 EBI-921030 0.35 Q75NI5 EBI-921030 0.35 P05982 EBI-921030 0.35 P05765 EBI-921030 0.35 P05712 EBI-921030 0.35 P69897 EBI-921030 0.35 P68182 EBI-921030 0.35 P68101 EBI-921030 0.35 P05197 EBI-921030 0.35 P05065 EBI-921030 0.35 P04906 EBI-921030 0.35 P04897 EBI-921030 0.35 P63095 EBI-921030 0.35 P04797 EBI-921030 0.50 P04785 EBI-921030 0.35 P04764 EBI-921030 0.35 P04762 EBI-921030 0.35 Q3KRE8 EBI-921030 0.35 P62890 EBI-921030 0.35 P04644 EBI-921030 0.35 P04642 EBI-921030 0.35 P04636 EBI-921030 0.35 P04466 EBI-921030 0.35 P04462 EBI-921030 0.35 P04218 EBI-921030 0.35 P04182 EBI-921030 0.35 P62738 EBI-921030 0.35 P02600 EBI-921030 0.35 P63259 EBI-921030 0.35 P68136 EBI-921030 0.35 P02466 EBI-921030 0.35 P01346 EBI-921030 0.35 P00507 EBI-921030 0.35 O88960 EBI-921030 0.35 O88941 EBI-921030 0.35 O88767 EBI-921030 0.35 O88761 EBI-921030 0.35 O88656 EBI-921030 0.35 O88638 EBI-921030 0.35 O88989 EBI-921030 0.35 M0RC99 EBI-921030 0.35 G3V7P1 EBI-921030 0.35 Q5U1Z2 EBI-921030 0.35 Q52KJ9 EBI-921030 0.35 Q5BK63 EBI-921030 0.35 Q499V7 EBI-921030 0.35 Q5EBA9 EBI-921030 0.35 O70282 EBI-921030 0.35 P29266 EBI-921030 0.35 P28480 EBI-921030 0.35 P28075 EBI-921030 0.35 P28042 EBI-921030 0.35 P27952 EBI-921030 0.35 P27881 EBI-921030 0.35 P62961 EBI-921030 0.35 P27791 EBI-921030 0.35 P63086 EBI-921030 0.35 P27653 EBI-921030 0.35 P27615 EBI-921030 0.35 P27605 EBI-921030 0.35 P26772 EBI-921030 0.35 P84083 EBI-921030 0.35 P26051 EBI-921030 0.35 P63245 EBI-921030 0.35 P25235 EBI-921030 0.35 P62919 EBI-921030 0.35 P62859 EBI-921030 0.35 P62853 EBI-921030 0.35 P24368 EBI-921030 0.35 P24268 EBI-921030 0.35 P67779 EBI-921030 0.35 P24050 EBI-921030 0.35 P23965 EBI-921030 0.35 P23928 EBI-921030 0.35 P23514 EBI-921030 0.35 P23358 EBI-921030 0.35 P62832 EBI-921030 0.35 P21708 EBI-921030 0.35 P21670 EBI-921030 0.35 P21533 EBI-921030 0.35 P21213 EBI-921030 0.35 P20417 EBI-921030 0.35 P63074 EBI-921030 0.35 P84092 EBI-921030 0.35 P20069 EBI-921030 0.35 P19945 EBI-921030 0.35 P19804 EBI-921030 0.35 P97536 EBI-921030 0.35 P42667 EBI-921030 0.35 P97519 EBI-921030 0.35 P83888 EBI-921030 0.35 P83732 EBI-921030 0.35 P81155 EBI-921030 0.35 P80385 EBI-921030 0.35 P70645 EBI-921030 0.35 Q5XIH7 EBI-921030 0.35 P70550 EBI-921030 0.35 P70500 EBI-921030 0.35 P70490 EBI-921030 0.35 P70470 EBI-921030 0.35 P62718 EBI-921030 0.35 P62716 EBI-921030 0.35 P62703 EBI-921030 0.35 P62630 EBI-921030 0.35 P62628 EBI-921030 0.35 P62425 EBI-921030 0.35 P62332 EBI-921030 0.35 P62282 EBI-921030 0.35 P62278 EBI-921030 0.35 P62271 EBI-921030 0.35 P62268 EBI-921030 0.35 P62260 EBI-921030 0.35 P62250 EBI-921030 0.35 P62243 EBI-921030 0.35 P62198 EBI-921030 0.35 P62193 EBI-921030 0.35 P62142 EBI-921030 0.35 P62138 EBI-921030 0.35 P62083 EBI-921030 0.35 P61983 EBI-921030 0.35 P61980 EBI-921030 0.35 P61805 EBI-921030 0.35 P61751 EBI-921030 0.35 P61621 EBI-921030 0.35 P61589 EBI-921030 0.35 O54980 EBI-921030 0.35 O54715 EBI-921030 0.35 O35854 EBI-921030 0.35 Q6IFV1 EBI-921030 0.35 O35796 EBI-921030 0.35 O35763 EBI-921030 0.35 O35511 EBI-921030 0.35 O35509 EBI-921030 0.35 Q5EGY4 EBI-921030 0.35 P16884 EBI-921030 0.35 O35264 EBI-921030 0.35 O35244 EBI-921030 0.35 O35142 EBI-921030 0.35 O35094 EBI-921030 0.35 O08839 EBI-921030 0.35 O08772 EBI-921030 0.35 O08651 EBI-921030 0.35 O08618 EBI-921030 0.35 P19234 EBI-921030 0.35 P06685 EBI-921030 0.35 P63039 EBI-921030 0.35 P18484 EBI-921030 0.35 P18421 EBI-921030 0.35 P18420 EBI-921030 0.35 P18418 EBI-921030 0.35 P18163 EBI-921030 0.35 P17764 EBI-921030 0.35 P17220 EBI-921030 0.35 P17209 EBI-921030 0.35 P17164 EBI-921030 0.35 P62828 EBI-921030 0.35 P17077 EBI-921030 0.35 P17074 EBI-921030 0.35 P61354 EBI-921030 0.35 P62909 EBI-921030 0.35 P17046 EBI-921030 0.35 P16975 EBI-921030 0.35 P16638 EBI-921030 0.35 P62850 EBI-921030 0.35 P16036 EBI-921030 0.35 P15999 EBI-921030 0.35 P15791 EBI-921030 0.35 P15651 EBI-921030 0.35 P15178 EBI-921030 0.35 P14604 EBI-921030 0.35 P14562 EBI-921030 0.35 P14408 EBI-921030 0.35 P84100 EBI-921030 0.35 P13803 EBI-921030 0.35 P13596 EBI-921030 0.35 P13471 EBI-921030 0.35 P13437 EBI-921030 0.35 P13383 EBI-921030 0.35 P13086 EBI-921030 0.35 P62902 EBI-921030 0.35 P12749 EBI-921030 0.35 P12001 EBI-921030 0.35 P11980 EBI-921030 0.35 P11960 EBI-921030 0.35 P11884 EBI-921030 0.35 P11883 EBI-921030 0.35 P11762 EBI-921030 0.35 P11730 EBI-921030 0.35 Q9QZK5 EBI-921030 0.35 Q9QUR2 EBI-921030 0.35 Q9JMJ4 EBI-921030 0.35 Q9JMB5 EBI-921030 0.35 Q9JLZ1 EBI-921030 0.35 Q9JLH7 EBI-921030 0.35 Q9JLA3 EBI-921030 0.35 Q9JK11 EBI-921030 0.35 Q9JIJ7 EBI-921030 0.35 Q9JI85 EBI-921030 0.35 Q9JHY2 EBI-921030 0.35 Q9JHW5 EBI-921030 0.35 Q9JHW0 EBI-921030 0.35 Q9JHU5 EBI-921030 0.35 Q9JHB5 EBI-921030 0.35 Q9HB97 EBI-921030 0.35 Q9ES40 EBI-921030 0.35 Q9ERR2 EBI-921030 0.35 Q9ERM8 EBI-921030 0.35 Q9ERF9 EBI-921030 0.35 Q9ER30 EBI-921030 0.35 Q9EQX9 EBI-921030 0.35 Q9EQV6 EBI-921030 0.35 Q6P7S1 EBI-921030 0.35 Q9EPV3 EBI-921030 0.35 Q9EPJ3 EBI-921030 0.35 Q9EPH8 EBI-921030 0.35 Q9EPC6 EBI-921030 0.35 Q9EPB1 EBI-921030 0.35 Q99PW3 EBI-921030 0.35 Q99PD4 EBI-921030 0.35 Q99NA6 EBI-921030 0.35 Q99NA5 EBI-921030 0.35 Q71TY3 EBI-921030 0.35 Q71SY3 EBI-921030 0.35 Q71DI1 EBI-921030 0.35 Q5M9G3 EBI-921030 0.35 Q6W3E9 EBI-921030 0.35 Q6TUG0 EBI-921030 0.35 Q6RUV5 EBI-921030 0.35 Q6RJR6 EBI-921030 0.35 Q2TA68 EBI-921030 0.35 Q6QI88 EBI-921030 0.35 Q6QI86 EBI-921030 0.35 Q6QI16 EBI-921030 0.35 Q6Q7Y5 EBI-921030 0.35 Q6Q0N3 EBI-921030 0.35 Q6PEC5 EBI-921030 0.35 Q6PEC4 EBI-921030 0.35 Q6PDV8 EBI-921030 0.35 Q6PDV7 EBI-921030 0.35 Q6PDV1 EBI-921030 0.35 Q6PCU2 EBI-921030 0.35 Q6PCT9 EBI-921030 0.35 Q68FQ0 EBI-921030 0.35 Q6P9V9 EBI-921030 0.35 Q6P9U9 EBI-921030 0.35 Q6P9U3 EBI-921030 0.35 Q6P9U0 EBI-921030 0.35 Q6P9T8 EBI-921030 0.35 Q6P7A9 EBI-921030 0.35 Q6P799 EBI-921030 0.35 Q6P792 EBI-921030 0.35 Q6P791 EBI-921030 0.35 Q9QXQ0 EBI-921030 0.54 Q6P777 EBI-921030 0.35 Q6P762 EBI-921030 0.35 Q6P6W6 EBI-921030 0.35 Q6P6V8 EBI-921030 0.35 Q9ES53 EBI-921030 0.35 Q9ER34 EBI-921030 0.35 Q6P6V0 EBI-921030 0.35 Q6P6R2 EBI-921030 0.35 P68370 EBI-921030 0.35 Q6P685 EBI-921030 0.35 Q6P503 EBI-921030 0.35 Q6P502 EBI-921030 0.35 Q6P4Z9 EBI-921030 0.35 Q6P2A5 EBI-921030 0.35 Q6P0K8 EBI-921030 0.35 Q6NYB7 EBI-921030 0.35 Q68FV6 EBI-921030 0.35 Q8R4A1 EBI-921030 0.35 Q6AY48 EBI-921030 0.35 P56571 EBI-921030 0.35 Q5XIH3 EBI-921030 0.35 Q3MHT4 EBI-921030 0.35 Q9Z336 EBI-921030 0.35 Q9Z2X5 EBI-921030 0.35 Q9Z2Q1 EBI-921030 0.35 Q9Z2L0 EBI-921030 0.35 Q6IRK9 EBI-921030 0.35 Q9Z1X1 EBI-921030 0.35 Q9Z1W6 EBI-921030 0.35 Q9Z1P2 EBI-921030 0.35 Q9Z1E1 EBI-921030 0.35 Q9Z0V6 EBI-921030 0.35 Q9Z0V5 EBI-921030 0.35 Q9Z0U8 EBI-921030 0.35 Q9WVK7 EBI-921030 0.35 Q9WVK3 EBI-921030 0.35 Q9WVC0 EBI-921030 0.35 Q9WVB1 EBI-921030 0.35 Q2PQA9 EBI-921030 0.35 Q9WU82 EBI-921030 0.35 Q9WVR3 EBI-921030 0.35 Q9R1J8 EBI-921030 0.35 Q9R063 EBI-921030 0.35 Q9QZV8 EBI-921030 0.35 Q9QZR6 EBI-921030 0.35 Q99N27 EBI-921030 0.35 Q99J82 EBI-921030 0.35 Q99068 EBI-921030 0.35 Q924W3 EBI-921030 0.35 Q924S5 EBI-921030 0.35 Q924M6 EBI-921030 0.35 Q923V8 EBI-921030 0.35 Q920L2 EBI-921030 0.35 Q920J4 EBI-921030 0.35 Q920A6 EBI-921030 0.35 Q91ZW6 EBI-921030 0.35 Q91Y81 EBI-921030 0.35 P82995 EBI-921030 0.35 Q91XL4 EBI-921030 0.35 Q8VHV7 EBI-921030 0.35 Q8VHJ0 EBI-921030 0.35 Q8VHI8 EBI-921030 0.35 Q8VHF5 EBI-921030 0.35 Q5XIP0 EBI-921030 0.35 Q5XIP9 EBI-921030 0.35 Q5M7W1 EBI-921030 0.35 Q5XIU9 EBI-921030 0.35 Q5XIT9 EBI-921030 0.35 P56574 EBI-921030 0.35 Q3T1L0 EBI-921030 0.35 Q5FVH2 EBI-921030 0.35 Q4V8B7 EBI-921030 0.35 Q68FS9 EBI-921030 0.35 D3ZJR1 EBI-921030 0.35 Q5EBA4 EBI-921030 0.35 Q68FW4 EBI-921030 0.35 Q5XI73 EBI-921030 0.35 Q6AY55 EBI-921030 0.35 Q5U1Y1 EBI-921030 0.35 Q3KR97 EBI-921030 0.35 Q4V8B5 EBI-921030 0.35 Q66H98 EBI-921030 0.35 Q5BJX1 EBI-921030 0.35 Q5FVH0 EBI-921030 0.35 Q8R491 EBI-921030 0.35 Q3KR80 EBI-921030 0.35 Q32KK2 EBI-921030 0.35 Q66H12 EBI-921030 0.35 P11598 EBI-921030 0.35 P61212 EBI-921030 0.35 P61206 EBI-921030 0.35 P61107 EBI-921030 0.35 P61023 EBI-921030 0.35 P60901 EBI-921030 0.35 P60892 EBI-921030 0.35 P60711 EBI-921030 0.35 P60192 EBI-921030 0.35 P60123 EBI-921030 0.35 P58405 EBI-921030 0.35 P55161 EBI-921030 0.35 P54921 EBI-921030 0.35 P54311 EBI-921030 0.35 P54001 EBI-921030 0.35 P62907 EBI-921030 0.35 P52944 EBI-921030 0.35 P52555 EBI-921030 0.35 P52296 EBI-921030 0.35 P51868 EBI-921030 0.35 P51583 EBI-921030 0.35 P50878 EBI-921030 0.35 P62815 EBI-921030 0.35 P50503 EBI-921030 0.35 P50430 EBI-921030 0.35 P50408 EBI-921030 0.35 P50137 EBI-921030 0.35 P49432 EBI-921030 0.35 P49242 EBI-921030 0.35 P49134 EBI-921030 0.35 P48721 EBI-921030 0.35 P48679 EBI-921030 0.35 P48675 EBI-921030 0.35 P48500 EBI-921030 0.35 P48037 EBI-921030 0.35 P48004 EBI-921030 0.35 P47942 EBI-921030 0.35 P47853 EBI-921030 0.35 P46462 EBI-921030 0.35 P45592 EBI-921030 0.35 P45479 EBI-921030 0.35 P63004 EBI-921030 0.35 P42930 EBI-921030 0.35 Q6MGB8 EBI-921030 0.35 P97629 EBI-921030 0.35 Q6MGB5 EBI-921030 0.35 Q6MG76 EBI-921030 0.35 P55063 EBI-921030 0.35 Q6MG60 EBI-921030 0.35 Q6MG30 EBI-921030 0.35 Q6LED0 EBI-921030 0.35 Q6J4T4 EBI-921030 0.35 Q62636 EBI-921030 0.35 Q6IRE4 EBI-921030 0.35 Q66X93 EBI-921030 0.35 Q6IN22 EBI-921030 0.35 Q6IMX8 EBI-921030 0.35 P28073 EBI-921030 0.35 Q6IE67 EBI-921030 0.35 Q6GQP4 EBI-921030 0.35 Q9JLJ3 EBI-921030 0.35 Q64591 EBI-921030 0.35 Q64560 EBI-921030 0.35 Q64537 EBI-921030 0.35 Q64536 EBI-921030 0.35 Q64375 EBI-921030 0.35 Q64232 EBI-921030 0.35 Q63965 EBI-921030 0.35 Q63750 EBI-921030 0.35 Q63716 EBI-921030 0.35 Q63699 EBI-921030 0.35 Q63635 EBI-921030 0.35 Q63615 EBI-921030 0.35 Q63598 EBI-921030 0.35 Q63584 EBI-921030 0.35 Q63570 EBI-921030 0.35 Q63569 EBI-921030 0.35 P62870 EBI-921030 0.35 Q9QZM5 EBI-921030 0.35 G3V6H1 EBI-921030 0.35 Q5FWT1 EBI-921030 0.35 Q5XI43 EBI-921030 0.35 Q5U2V8 EBI-921030 0.35 Q4KM74 EBI-921030 0.35 Q5BJK8 EBI-921030 0.35 Q5U302 EBI-921030 0.35 Q4QQV0 EBI-921030 0.35 Q5EB77 EBI-921030 0.35 Q5XII0 EBI-921030 0.35 Q5XID6 EBI-921030 0.35 Q3B7V5 EBI-921030 0.35 Q5BJT7 EBI-921030 0.35 Q5FVQ4 EBI-921030 0.35 Q4G061 EBI-921030 0.35 Q5M843 EBI-921030 0.35 Q5XIQ4 EBI-921030 0.35 D4A414 EBI-921030 0.35 Q5PQM3 EBI-921030 0.35 Q32PX6 EBI-921030 0.35 Q5U2X8 EBI-921030 0.35 Q68FT7 EBI-921030 0.35 Q4G067 EBI-921030 0.35 Q4V8H5 EBI-921030 0.35 Q5XIM0 EBI-921030 0.35 Q5PQL2 EBI-921030 0.35 Q7TP47 EBI-921030 0.35 Q68FY0 EBI-921030 0.35 Q7TP24 EBI-921030 0.35 Q7TMC7 EBI-921030 0.35 P05426 EBI-921030 0.35 Q641X3 EBI-921030 0.35 Q68FR9 EBI-921030 0.35 Q5U3Z7 EBI-921030 0.35 Q32KJ5 EBI-921030 0.35 Q6AYH5 EBI-921030 0.35 Q5M918 EBI-921030 0.35 Q5XIM9 EBI-921030 0.35 Q5XIU4 EBI-921030 0.35 Q3KRE0 EBI-921030 0.35 Q498E0 EBI-921030 0.35 Q4FZT0 EBI-921030 0.35 Q5XIG8 EBI-921030 0.35 Q4AEF8 EBI-921030 0.35 P81799 EBI-921030 0.35 Q66H94 EBI-921030 0.35 Q5XI04 EBI-921030 0.35 Q6AYS3 EBI-921030 0.35 Q3MIE7 EBI-921030 0.35 Q68FT4 EBI-921030 0.35 P68511 EBI-921030 0.35 P11507 EBI-921030 0.35 P11442 EBI-921030 0.35 P11240 EBI-921030 0.35 P11232 EBI-921030 0.35 P62845 EBI-921030 0.35 P62963 EBI-921030 0.35 P10888 EBI-921030 0.35 P10860 EBI-921030 0.35 P10760 EBI-921030 0.35 P10719 EBI-921030 0.35 P62755 EBI-921030 0.35 P63326 EBI-921030 0.35 P09895 EBI-921030 0.35 P09527 EBI-921030 0.35 P09456 EBI-921030 0.35 P63324 EBI-921030 0.35 P09330 EBI-921030 0.35 P08503 EBI-921030 0.35 P08461 EBI-921030 0.35 P08413 EBI-921030 0.35 P63018 EBI-921030 0.35 P08081 EBI-921030 0.35 P08010 EBI-921030 0.35 P07895 EBI-921030 0.35 P07872 EBI-921030 0.35 P07871 EBI-921030 0.35 P07824 EBI-921030 0.35 P07633 EBI-921030 0.35 P07154 EBI-921030 0.35 P07153 EBI-921030 0.35 P07150 EBI-921030 0.35 P06761 EBI-921030 0.35 P06760 EBI-921030 0.35 P63100 EBI-921030 0.35 P41123 EBI-921030 0.35 P40307 EBI-921030 0.35 P40112 EBI-921030 0.35 P39052 EBI-921030 0.35 P62914 EBI-921030 0.35 P38983 EBI-921030 0.35 P38659 EBI-921030 0.35 P38650 EBI-921030 0.35 P37397 EBI-921030 0.35 P37285 EBI-921030 0.35 P63088 EBI-921030 0.35 P36972 EBI-921030 0.35 P36202 EBI-921030 0.35 P35704 EBI-921030 0.35 P35565 EBI-921030 0.35 P35435 EBI-921030 0.35 P35434 EBI-921030 0.35 P35427 EBI-921030 0.35 P35286 EBI-921030 0.35 P35284 EBI-921030 0.35 P35281 EBI-921030 0.35 P68255 EBI-921030 0.35 P63102 EBI-921030 0.35 P35213 EBI-921030 0.35 P35053 EBI-921030 0.35 P34926 EBI-921030 0.35 P34064 EBI-921030 0.35 P34058 EBI-921030 0.35 P32551 EBI-921030 0.35 P32089 EBI-921030 0.35 P31977 EBI-921030 0.35 P31399 EBI-921030 0.35 P31232 EBI-921030 0.35 P31000 EBI-921030 0.35 P30904 EBI-921030 0.35 P30839 EBI-921030 0.35 P30427 EBI-921030 0.35 P29457 EBI-921030 0.35 P29419 EBI-921030 0.35 P29315 EBI-921030 0.35 P29314 EBI-921030 0.35 Q63507 EBI-921030 0.35 Q63448 EBI-921030 0.35 P62982 EBI-921030 0.35 Q63377 EBI-921030 0.35 Q63347 EBI-921030 0.35 Q63321 EBI-921030 0.35 Q63312 EBI-921030 0.35 Q63258 EBI-921030 0.35 Q63151 EBI-921030 0.35 Q63083 EBI-921030 0.35 Q63081 EBI-921030 0.35 P02454 EBI-921030 0.35 Q63016 EBI-921030 0.35 Q63002 EBI-921030 0.35 Q62952 EBI-921030 0.35 Q62920 EBI-921030 0.35 Q62908 EBI-921030 0.35 Q62902 EBI-921030 0.35 Q62871 EBI-921030 0.35 Q62991 EBI-921030 0.35 Q62786 EBI-921030 0.35 Q62764 EBI-921030 0.35 Q62698 EBI-921030 0.35 Q62667 EBI-921030 0.35 Q62638 EBI-921030 0.35 Q60587 EBI-921030 0.35 P62997 EBI-921030 0.35 P63170 EBI-921030 0.35 Q10758 EBI-921030 0.35 Q10728 EBI-921030 0.35 Q09073 EBI-921030 0.35 Q08850 EBI-921030 0.35 Q08163 EBI-921030 0.35 Q07984 EBI-921030 0.35 Q07936 EBI-921030 0.35 Q07266 EBI-921030 0.35 Q06647 EBI-921030 0.35 Q05962 EBI-921030 0.35 Q04462 EBI-921030 0.35 Q02253 EBI-921030 0.35 Q01205 EBI-921030 0.35 Q00972 EBI-921030 0.35 P97852 EBI-921030 0.35 GO:0009986 GO:0005905 GO:0030136 GO:0005737 GO:0030659 GO:0005829 GO:0012505 GO:0005768 GO:0009897 GO:0070062 GO:0032593 GO:0016021 GO:0005887 GO:0043231 GO:0016020 GO:0045121 GO:0005771 GO:0048471 GO:0005886 GO:0098793 GO:0042383 GO:0016529 GO:0030315 GO:0005802 GO:0030140 GO:0012506 GO:0055056 GO:0005355 GO:0015304 GO:0015149 GO:0010021 GO:0050873 GO:0071456 GO:0032869 GO:0071470 GO:0071356 GO:0042593 GO:0046323 GO:0044381 GO:1904659 GO:0007611 GO:0007616 GO:0015749 GO:0031550 GO:0098694 GO:0045471 GO:0007614 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPSGFQQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNATWLGRQGPGGPDSIPQGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLANNVLAVLGGALMGLANAAASYEILILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILVAQVLGLESMLGTATLWPLLLAITVLPALLQLLLLPFCPESPRYLYIIRNLEGPARKSLKRLTGWADVSDALAELKDEKRKLERERPLSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFELAGVEQPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPSMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFSNWTCNFIVGMGFQYVADAMGPYVFLLFAVLLLGFFIFTFLRVPETRGRTFDQISATFRRTPSLLEQEVKPSTELEYLGPDEND 509 Q9VJL6 Glia GMF 7227 None SL-0198 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}. UNIPROT Q9VJL6 UNIPROT Q8MSR7 UNIPROT Q9NK59 Pfam PF00241 PROSITE PS51263 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}. Q95RB1 EBI-238317 0.00 Q9VJA1 EBI-242035 0.00 GO:0071944 GO:0030027 GO:0005634 GO:0048471 GO:0003779 GO:0071933 GO:0071846 GO:0007298 GO:0034316 GO:0030833 GO:0031344 Unknown UniProt Sequence Analysis MSDNQICDISNEVLEELKKFRFSKSKNNAALILKVDREKQTVVLDEFIDDISVDELQDTLPGHQPRYVIYTYKMVHDDQRISYPMCFIFYTPRDSQIELQMMYACTKSALQREVDLTRVYEIRELDELTEEWLKAKLK 138 O36388 Envelope gM 654901 None SL-0415 SL-0418 SL-0419 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}. UNIPROT O36388 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MKSSKKDIFILHIWLKLMGCYVFMFITSVVLPIAAMFPNLGFPCYYNTLVDYSKLNLREKNQAQHLTPTLFLEAPEMFFYVTYSFIVDCCSLVYYALAAVAVVKAKKHAPGLMALSQWIMAVGSPTLLYMAVLKLWTIQLYIHTLSYKHIYLAAFVYCLHWLLSMVYTECYITNVSSQWTSSELKKTIPENILLYRVVHVLKPIMMNVHLSVVALETLIFCLSFMMAIGNSFYVMVSDIVFGAINLYLILPIIWYFVTEFWLSKYLPRQFGFYFGVLVASIILILPVVRYDKIFVAAQIHRAVSINIAMIPLCALVALLVRACRVYTDRKKIAYTALPSKPQTIKYTKPIEPSTKQAPDSSIFLEEESDTDFEQ 374 P52370 Envelope gM 10323 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P52370 UNIPROT O39493 Pfam PF01528 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}. GO:0044175 GO:0044177 GO:0044178 GO:0033644 GO:0044201 GO:0016021 GO:0019031 GO:0044423 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MAGSAQPAAVHWRLWLAQVGVFAGLALLLLITLIGAASPGAGLPCFYAAIVNYNARNLSADGGAWAQRELGARHPALFLETPTTAAFSAYTAVVLLAVAAFDVAAAIIIRRENSGGFAAAYHMNALATLATPPGALLLGALAAWTLQAAVLLLSHKIMVLAAATYLAHLAPPAAFVGLFCTAGLPGAEYAQAVHALRERSPRAHRLLGPGRAVMINLAGGLLALIIGTAPLMLGQLLGAGLGLSLAQTVVAGVTVFCLAAVLFLVLTELVLSRYTQVLPGPAFGTLVAASCIAVASHDYFHQLRGVVRTQAPRAAARVKLALAGVALLAVAMLVLRLVRACLHHRRKGSAFYGHVSAARQQAARYIARARSSRGMAPLEGDAAALLDRGVASDDEEAVYEAHAPPRPPTIPLRRPEVPHSRASHPRPPPRSPPPAHVK 438 Q1HVE9 Envelope gM 82830 None SL-0415 SL-0418 SL-0419 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}. UNIPROT Q1HVE9 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MKSSKNDTFVYRTWFKTLVVYFVMFVMSAVVPITAMFPNLGYPCYFNALVDYGALNLTNYNLAHHLTPTLYLEPPEMFVYITLVFIADCVAFIYYACGEVALIKARKKVSGLTDLSAWVSAVGSPTVLFLAILKLWSIQVFIQVLSYKHVFLSAFVYFLHFLASVLHACACVTRFSPVWVVKAQDNSIPQDTFLWWVVFYLKPIVTNLYLGCLALETLVFSLSVFLALGNSFYFMVGDMVLGAVNLFLVLPIFWYILTEVWLASFLRHNFGFYCGMFIASIILILPLVRYEAVFVSAKLHTTVAINVAIIPILCSVAMLIRICRIFKSMRQGTDYVPVSETVELELESEPRPRPSRTPSPGRNRRRSSTSSSSSRSTRRQRPVSTQALISSVLPMTTDSEEEIFP 405 P03215 Envelope gM 10377 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P03215 UNIPROT Q777D4 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MKSSKNDTFVYRTWVKTLVVYFVMFVMSAVVPITAMFPNLGYPCYFNALVDYGALNLTNYNLAHHLTPTLYLEPPEMFVYITLVFIADCVAFIYYACGEVALIKARKKVSGLTDLSAWVSAVGSPTVLFLAILKLWSIQVFIQVLSYKHVFLSAFVYFLHFLASVLHACACVTRFSPVWVVKAQDNSIPQDTFLWWVVFYLKPVVTNLYLGCLALETLVFSLSVFLALGNSFYFMVGDMVLGAVNLFLILPIFWYILTEVWLASFLRHNFGFYCGMFIASIILILPLVRYEAVFVSAKLHTTVAINVAIIPILCSVAMLIRICRIFKSMRQGTDYVPVSETVELELESEPRPRPSRTPSPGRNRRRSSTSSSSSRSTRRQRPVSTQALVSSVLPMTTDSEEEIFP 405 Q3KSR7 Envelope gM 10376 None SL-0415 SL-0418 SL-0419 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}. UNIPROT Q3KSR7 Pfam PF01528 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}. Q9NSC5 EBI-2622194 0.37 Q02818 EBI-2622177 0.37 P0C763 EBI-9644923 0.37 Q3KSQ7 EBI-9645160 0.37 A6SZC0 EBI-9645170 0.37 P0C738 EBI-9645175 0.37 P03219 EBI-9645248 0.37 K9UT36 EBI-9645587 0.37 GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MKSSKNDTFVYRTWVKTLVVYFVMFVMSAVVPITAMFPNLGYPCYFNALVDYGALNLTNYNLAHHLTPTLYLEPPEMFVYITLVFIADCVAFIYYACGEVALIKARKKVSGLTDLSAWVSAVGSPTVLFLAILKLWSIQVFIQVLSYKHVFLSAFVYFLHFLASVLHACACVTRFSPVWVVKAQDNSIPQDTFLWWVVFYLKPVVTNLYLGCLALETLVFSLSVFLALGNSFYFMVGDMVLGAVNLFLILPIFWYILTEVWLASFMRHNFGFYCGMFIASIILILPLVRYEAVFVSAKLHTTVAINVAIIPILCSVAMLIRICRIFKSMRQGTDYVPVSETVELELESEPRPRPSRTPSPGRNRRRSSTSSSSSRSTRRQRPVSTQALVSSVLPMTTDSEEEIFP 405 P28948 Envelope gM 31520 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P28948 UNIPROT Q6DLF9 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MARRGAAVAEEPLLPSSGIVGIGPIEGINWRTWLVQVFCFALTTSVLFITLVTASLPQTGYPCFYGSLVDYTQKNHSVVDGVWMRQIAGGVAPTLFLETTSLVAFLYYTTLVLVAISFYLIISAVLVRRYARGKECTAVAGCTRPTTTLIASHVTLVLGTLATWLLQVVILLLSHKQAVLGAAVYVVHFVSLVFFCMSFSGLGTASAQYSSNLRILKTNLPALHKMAGPGRAVMTNLGMGMLGISLPILSLMLGIILANSFHITLWQTVTVAVGVFVALGLMFLIIVELIVSHYVHVLVGPALAVLVASSTLAVATHSYFVHFHAMVSVQAPNLATASKAIVGIMAVISIIMLVVRLVRAIMFHKKRNTEFYGRVKTVSSKARRYANKVRGPRRNPQPLNVAESRGMLLAEDSETDAEEPIYDVVSEEFETEYYDDPQRVPERSHRREYR 450 P52371 Envelope gM 82831 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P52371 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MKSSKSDLFIYKTWFKLLVLYFVMFVLSATVPIAASFPGLGFPCYYNALVNYSAINLTERNVAKHLTPTLYLEEPEMFAYMTFTFLVDCFAAVYYFLGALAIMLAKRHFVVSLTTLSQWIAMVGTPTLILIGMWRMWTIQLFIQTLSYKHIYLSAFVYLIHFLLSFLHTQCYISRNSQLWSLKVLEQGIPPNTLLDTVVFTIKPLLANCQLFCLGLEMLVFSLSFMMAIGNSFYVLVSDIVFGAINLYLALVLFWVLLTELYLVKYMTFVMGFYLGGLIGCIFLLVPLWRYEQIFVAANLRSPILINILVIFFLCTLSALVRLLRMTWFSPTKPSYEPIQLKNIKHRRVKLQSPSGPSILEEGSSDEGSEDSEEEEEL 378 Q9E6Q6 Envelope gM 10389 None SL-0415 SL-0418 SL-0419 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}. UNIPROT Q9E6Q6 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MASRARMERNYRGLSHIDYVHKKMWVVQAVCFGIAVLVFFGTLVAASINLTEGFPCFFAAVVDYRTVNTTLVHTGLTYPRLGGVVPVLFFQTKAVVFFFYATSIVFVFLVCYITVGAIISSKKHVGAAYMGSGAFVFSLMASPLTILLGTVSIWLLQAVVIVLAHKLIVLAAAVYLVHFSTITFFYGYFCGRGVDSKVYAEDISSAKDIDGSLHKLIGNVRAMMVNLLSIVYSIILIMSSLMFGMLLANSFTLKFWHVIVTVLITTSVLTLIYLLVIEFLIARYVHIILGAYIGLLIGYGMLWTTTCDYVNRFYYAMGANASNLRIACHSVLAVFTVLILLAMVVRLIRASLYHRRRSTRAYAKAMKLQQNVKHRLRQLRRSYKQRGSQSEDERALTQSRSAEASDEDTIYDRVYSGSESEWDD 424 P16733 Envelope gM 10360 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P16733 UNIPROT Q7M6T7 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MAPSHVDKVNTRTWSASIVFMVLTFVNVSVHLVLSNFPHLGYPCVYYHVVDFERLNMSAYNVMHLHTPMLFLDSVQLVCYAVFMQLVFLAVTIYYLVCWIKISMRKDKGMSLNQSTRDISYMGDSLTAFLFILSMDTFQLFTLTMSFRLPSMIAFMAAVHFFCLTIFNVSMVTQYRSYKRSLFFFSRLHPKLKGTVQFRTLIVNLVEVALGFNTTVVAMALCYGFGNNFFVRTGHMVLAVFVVYAIISIIYFLLIEAVFFQYVKVQFGYHLGAFFGLCGLIYPIVQYDTFLSNEYRTGISWSFGMLFFIWAMFTTCRAVRYFRGRGSGSVKYQALATASGEEVAVLSHHDSLESRRLREEEDDDDDEDFEDA 372 Q6SW43 Envelope gM 295027 None SL-0415 SL-0418 SL-0419 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}. UNIPROT Q6SW43 UNIPROT D2K3Q7 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0005886 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MAPSHVDKVNTRTWSASIVFMVLTFVNVSVHLVLSNFPHLGYPCVYYHVVDFERLNMSAYNVMHLHTPMLFLDSVQLVCYAVFMQLVFLAVTIYYLVCWIKISMRKDKGMSLNQSTRDISYMGDSLTAFLFILSMDTFQLFTLTMSFRLPSMIAFMAAVHFFCLTIFNVSMVTQYRSYKRSLFFFSRLHPKLKGTVQFRTLIVNLVEVALGFNTTVVAMALCYGFGNNFFVRTGHMVLAVFVVYAIISIIYFLLIEAVFFQYVKVQFGYHLGAFFGLCGLIYPIVQYDTFLSNEYRTGISWSFGMLFFIWAMFTTCRAVRYFRGRGSGSVKYQALATASGEEVAALSHHDSLESRRLREEEDDDDEDFEDA 371 P04288 Envelope gM 10299 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P04288 UNIPROT B9VQD7 UNIPROT Q09IC3 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0044220 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MGRPAPRGSPDSAPPTKGMTGARTAWWVWCVQVATFVVSAVCVTGLLVLASVFRARFPCFYATASSYAGVNSTAEVRGGVAVPLRLDTQSLVGTYVITAVLLLAVAVYAVVGAVTSRYDRALDAGRRLAAARMAMPHATLIAGNVCSWLLQITVLLLAHRISQLAHLVYVLHFACLVYFAAHFCTRGVLSGTYLRQVHGLMELAPTHHRVVGPARAVLTNALLLGVFLCTADAAVSLNTIAAFNFNFSAPGMLICLTVLFAILVVSLLLVVEGVLCHYVRVLVGPHLGAVAATGIVGLACEHYYTNGYYVVETQWPGAQTGVRVALALVAAFALGMAVLRCTRAYLYHRRHHTKFFMRMRDTRHRAHSALKRVRSSMRGSRDGRHRPAPGSPPGIPEYAEDPYAISYGGQLDRYGDSDGEPIYDEVADDQTDVLYAKIQHPRHLPDDDPIYDTVGGYDPEPAEDPVYSTVRRW 473 P89433 Envelope gM 10315 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P89433 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MGRRAPRGSPEAAPGADVAPGARAAWWVWCVQVATFIVSAICVVGLLVLASVFRDRFPCLYAPATSYAKANATVEVRGGVAVPLRLDTQSLLATYAITSTLLLAAAVYAAVGAVTSRYERALDAARRLAAARMAMPHATLIAGNVCAWLLQITVLLLAHRISQLAHLIYVLHFACLVYLAAHFCTRGVLSGTYLRQVHGLIDPAPTHHRIVGPVRAVMTNALLLGTLLCTAAAAVSLNTIAALNFNFSAPSMLICLTTLFALLVVSLLLVVEGVLCHYVRVLVGPHLGAIAATGIVGLACEHYHTGGYYVVEQQWPGAQTGVRVALALVAAFALAMAVLRCTRAYLYHRRHHTKFFVRMRDTRHRAHSALRRVRSSMRGSRRGGPPGDPGYAETPYASVSHHAEIDRYGDSDGDPIYDEVAPDHEAELYARVQRPGPVPDAEPIYDTVEGYAPRSAGEPVYSTVRRW 467 Q04630 Envelope gM 10370 None SL-0415 SL-0418 SL-0419 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}. UNIPROT Q04630 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MASSRVDTINLRIWLVSIICAALSFINVTVYLIAINFPNLGFPCAYFEINDLKAVNLSANNQIYQMTHQLYINPVQIICYVLIMAMLFLLIIIYYIVCCAKVFSSNKTSNVNQTTRDITWMGDTSSCFQFILIMDTFQLFVTALSFRLVALGAFAYCIFFVCFTTFNVTLITQFQSADKSFFAFQKIHPNLKGTVQFKTVVINLTELMLGYSTMFLGITTCLGVGNSIYIRSITVAYSSINTFLVMACIYSIVIEAVLVRYVKPLFGYYVGMFCGAVGLSFPILQYETFFESEWSTGLIINLAVIAIISIGFIICRLVRYLVKKKRRYKQLVNTESSSLMDENE 344 P52449 Envelope gM 36351 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P52449 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MASSRVDTINLRIWLVSIICAALSFINVTVHLIAINFPNLGFPCAYFEINDLKAVNLSANNEIYQMTHQLYINPVQIICYVLIMAILFLLIIIYYIVCCAKVFSSNKTSNVNQTTRDITWMGDTSSCFQFILIMDTFQLFVTALSFRLVALGAFAYSIFFVCFTTFNVTLITQFQSADKSFFAFQKIHPNLKGTVQFKTVVINLSELMLGYSTMFLGITTCLGVGNSIYIRSITVAFSSINTFLVMACIYSIVIEAVLVRYVKPLFGYYVGMFCGAVGLSFPILQYETFFESEWSTGLIINLSVVAIISIGFIICRLVRYLVKKKRRYKQLLNAESSSLMDENE 344 P52372 Envelope gM 57278 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P52372 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MALSRVDVINMRIWVLSIICACLTYVNVTVHLVAVHFPNLGFPCAYYEINDMKAINLSIRNDIRSLTPQLYLNPIQLICYVVFMDICFFFILVYYIVCCVKVFSSEKTPNINQSTRDITWMGDSLSCFQFVLTMDTYQFFVTCLSFRLVTLAAFTYCLFFICFTAFTLTMITQYQSSERSFFVLKRIHPKLKGTIKYKTIIINMIELMLGFSSMVFAITICLGLGNNFYIKSSTVAFASINTFFVMSFVYSLVIELILHQYVKVQFGLHFGILFGILGLTYPILKYDSLFKTEWTVKFIVNLAVITIVCLSFIICRLIRFFMRKHHNYKKLPTTVEDLDVLEEANE 346 F5HDD0 Envelope gM 868565 None SL-0415 SL-0418 SL-0419 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}. UNIPROT F5HDD0 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MRASKSDRFLMSSWVKLLFVAVIMYICSAVVPMAATYEGLGFPCYFNNLVNYSALNLTVRNSAKHLTPTLFLEKPEMLVYIFWTFIVDGIAIVYYCLAAVAVYRAKHVHATTMMSMQSWIALLGSHSVLYVAILRMWSMQLFIHVLSYKHVLMAAFVYCIHFCISFAHIQSLITCNSAQWEIPLLEQHVPDNTMMESLLTRWKPVCVNLYLSTTALEMLLFSLSTMMAVGNSFYVLVSDAIFGAVNMFLALTVVWYINTEFFLVKFMRRQVGFYVGVFVGYLILLLPVIRYENAFVQANLHYIVAINISCIPILCILAIVIRVIRSDWGLCTPSAAYMPLATSAPTVDRTPTVHQKPPPLPAKTRARAKVKDISTPAPRTQYQSDHESDSEIDETQMIFI 400 P52373 Envelope gM 69156 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P52373 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MAKAGVMTLSHVDRMNLRTWTMAIACCLLSFVNIVVFSVAAHFPGIGFPCYYPRIIDFDNMNLTMYNAIHHLTPQLFLDPVQLIVYVIFTELIFFCVLSYYIVCWVQIYFRSEHGTQVNQSTRDINFMGDSATCFTFVLTMDTFQIFLLSLSFRLPSMVAFSKCMYFMCLTAFVVTLVTHYESRERSAFALSKIHPKLQGTIRYRTAVVNLTQLILGFATMVLAMSLALGFGNSFFVKTAHVVFGAMVAFAIVACVYFSIIESVLSRYMKVQFGYHIGTILGVCGAMYPIIRYEALNASSYARDINIGITVLLLLCVAFSVIRTVRFLLRRNKRYRALALDNEEIRALRSDAE 353 Q6UDH4 Envelope gM 670426 None SL-0415 SL-0418 SL-0419 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}. UNIPROT Q6UDH4 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MGNYYYGGQESRLERISWRMWMVEAACYIVLVLLTLVSSFASLSSTTGFPCFVGTVGESSFGGDLMGHGMTPARRDGVKIFFMSSPSTLFVVFSAVFVWLVVAVYLLLGGVRVKMCNFDSSYGASELSSAVATMTSLVTLSITAWAWQVFVLMLSYRQLTLAAVAFVGIFIAGLVFMLSFASGGKSPENYATFNSQLKTVCKDVHAVITAFKAVVLNLFCVVFGVWHLMLVMLGAVIMVLNFGVSIPKATTGALVVFIVLGLVYLMMIELVVSRYVHVLLGPHLGMIIALGIAGTSALSYAETLDEIMYASWKPVAAGILGAFSVIVLALAVLRAVRSYKFHKAAQSKFLQQVASVAQTVKNRARRERNGPRVHKRYYDAVPVDAYEDDPYRQSPRRSRHGEAEDVIYENMKY 413 Q01017 Envelope gM 10383 None SL-0415 SL-0418 SL-0419 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}. UNIPROT Q01017 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MMKASRSDTFMLRTWIQLLVLFVIMFIMSAILPIAASVEGLGFPCYFPNLVDYSLLNLTLRNAAKHLTPTLFLEAPELFVYITWSVLVDLASAIYYVVGALAILQARKTHLTSMITLQTWINLVGSHTMLFIGIARMWTLQLFIHVLSYKHVMLAAFIYFLHFCLSYMHTLSLVSRNSPKWSVLLMEQHIPKQSLLSTILDYGKPLCVNMYLSLLALEMLVFSLGFMMAIGNSFYILVSDTVLASINLYFVLTTFWYMMTEMFLQDYLKLQFGFYLGVFSGSLILLLPVLRYEAVFVSANLHKTVAVNIAMIPAMCVIAMMFRLFRYSQQVRKPENSYTPLPKRFKKRRQKQDQQLIMVETSDEEL 366 Q85041 Envelope gM 33703 None SL-0415 SL-0418 SL-0419 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}. UNIPROT Q85041 UNIPROT Q5PP86 UNIPROT Q85042 Pfam PF01528 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}. A0A142I9X8 EBI-11701393 0.35 Q8QXN7 EBI-11689133 0.37 GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 GO:0019068 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MCGPRNAEAVSWRSWLIEVCGFALAALTLVLTLIFASLPEMGFPCFYATVADYDTLNDTSGGVWTRQPLVAPALFLETPTVTSFFGFTATVLLAHALYAVAGAVVLRREAGRLAFQPSVVLYAASTVAAPGTLMLGALCAWTLQAVVLLMAHKQAGLAAAAYITHFVFLALFGACHACKGTGDVRAALAASPPLRRVAVHARAVVTNVVLGAVGLGAAVVGLMLGVLLANSFHISLWKTAEAALAVFTLLALALMVFVEVVVSGYVQVLPTPAFCVLVASAAFGVSAHRYFAKFSEALGETHGVVIGTRAVLAVLSLIALAMIVVRLVRACIAHRARGSRFYANVDKARTTARRYLQKRLHGRGNDEYLLAPGSGDDEFDDGDEVVYENLGFE 393 P09298 Envelope gM 10338 None SL-0415 SL-0418 SL-0419 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}. UNIPROT P09298 Pfam PF01528 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}. GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MGTQKKGPRSEKVSPYDTTTPEVEALDHQMDTLNWRIWIIQVMMFTLGAVMLLATLIAASSEYTGIPCFYAAVVDYELFNATLDGGVWSGNRGGYSAPVLFLEPHSVVAFTYYTALTAMAMAVYTLITAAIIHRETKNQRVRQSSGVAWLVVDPTTLFWGLLSLWLLNAVVLLLAYKQIGVAATLYLGHFATSVIFTTYFCGRGKLDETNIKAVANLRQQSVFLYRLAGPTRAVFVNLMAALMAICILFVSLMLELVVANHLHTGLWSSVSVAMSTFSTLSVVYLIVSELILAHYIHVLIGPSLGTLVACATLGTAAHSYMDRLYDPISVQSPRLIPTTRGTLACLAVFSVVMLLLRLMRAYVYHRQKRSRFYGAVRRVPERVRGYIRKVKPAHRNSRRTNYPSQGYGYVYENDSTYETDREDELLYERSNSGWE 435 Q77NP2 Envelope gM 341980 None SL-0415 SL-0418 SL-0419 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}. UNIPROT Q77NP2 Pfam PF01528 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}. Q6QCN0 EBI-7927240 0.37 Q6QCM8 EBI-7927258 0.37 Q77NP2 EBI-7927293 0.55 Q71S71 EBI-7927311 0.37 Q8AZM1 EBI-7927329 0.55 Q4JQV0 EBI-2533294 0.00 Q4JQU8 EBI-2533670 0.00 Q0Q8R5 EBI-2533782 0.00 Q4JQT6 EBI-2534359 0.00 Q77NN8 EBI-2534791 0.00 Q77NN5 EBI-2534975 0.00 P0C764 EBI-2535168 0.00 GO:0044175 GO:0044178 GO:0044201 GO:0016021 GO:0019031 GO:0055036 Transmembrane UniProt Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035} MGTQKKGPRSEKVSPYDTTTPEVEALDHQMDTLNWRIWIIQVMMFTLGAVMLLATLIAASSEYTGIPCFYAAVVDYELFNATLDGGVWSGNRGGYSAPVLFLEPHSVVAFTYYTALTAMAMAVYTLITAAIIHRETKNQRVRQSSGVAWLVVDPTTLFWGLLSLWLLNAVVLLLAYKQIGVAATLYLGHFATSVIFTTYFCGRGKLDETNIKAVANLRQQSVFLYRLAGPTRAVFVNLMAALMAICILFVSLMLELVVANHLHTGLWSSVSVAMSTFSTLSVVYLIVSELILAHYIHVLIGPSLGTLVACATLGTAAHSYMDRLYDPISVQSPRLIPTTRGTLACLAVFSVVMLLLRLMRAYVYHRQKRSRFYGAVRRVPERVRGYIRKVKPAHRNSRRTNYPSQGYGYVYENDSTYETDREDELLYERSNSGWE 435 Q28294 Guanine GNAQ 9615 None SL-0178 SL-0182 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}. UNIPROT Q28294 Pfam PF00503 PROSITE PS51882 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}. GO:0005794 GO:0005834 GO:0016020 GO:0031965 GO:0001750 GO:0045202 GO:0001664 GO:0031683 GO:0005525 GO:0005096 GO:0003924 GO:0046872 GO:0001508 GO:0007189 GO:0007188 GO:0009649 GO:0007213 GO:0007215 GO:0007603 GO:0010543 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:P21279} MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV 359 P50148 Guanine GNAQ 9606 None SL-0178 SL-0182 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}. UNIPROT P50148 UNIPROT O15108 UNIPROT Q13462 UNIPROT Q6NT27 UNIPROT Q92471 UNIPROT Q9BZB9 PDB 6VU5 PDB 7EZM PDB 7F6H PDB 7F6I PDB 7F8W Pfam PF00503 PROSITE PS51882 OMIM 163000 OMIM 185300 OMIM 600998 DisGeNET 2776 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}. 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. P32302 EBI-7276612 0.40 P30556 EBI-7409738 0.40 P51884 EBI-3909602 0.37 P50897 EBI-3909621 0.37 Q9H0P0 EBI-3918371 0.37 Q8IWW8 EBI-3923179 0.37 Q9UGN5 EBI-7055495 0.44 P10276 EBI-6249283 0.56 Q14254 EBI-6249310 0.35 P49407 EBI-8309016 0.52 P16284 EBI-9984652 0.40 Q61879 EBI-11041929 0.35 Q6DN90 EBI-11896524 0.40 Q6IQ23 EBI-16398399 0.35 Q96QD9 EBI-21501187 0.35 Q13503 EBI-21501670 0.35 Q53EQ6 EBI-21523123 0.35 P21453 EBI-21539478 0.35 Q9NRW4 EBI-21542541 0.35 P09067 EBI-21543288 0.35 Q9NT62 EBI-21549217 0.35 Q9UHK0 EBI-21549449 0.35 O95136 EBI-21551126 0.35 Q6PEY0 EBI-21551307 0.35 Q8N5S1 EBI-21587332 0.35 Q16854 EBI-21603108 0.35 Q9NVR5 EBI-21603625 0.35 P02675 EBI-21646531 0.35 Q8TAG9 EBI-21673041 0.35 Q92845 EBI-21702814 0.35 Q96S94 EBI-21750627 0.35 Q8NFB2 EBI-21757603 0.35 Q6ZNA4 EBI-21806464 0.35 Q86VZ1 EBI-21809853 0.35 Q86Z23 EBI-21814288 0.35 Q9UN70 EBI-21824946 0.35 P63215 EBI-21830507 0.35 P50150 EBI-21830434 0.35 Q96AZ6 EBI-21849278 0.35 Q9NYW3 EBI-21852327 0.35 Q7Z698 EBI-21860016 0.35 Q8TCI5 EBI-21862131 0.35 Q8N446 EBI-21872004 0.35 Q7RTX9 EBI-21871985 0.35 Q8R455 EBI-15993574 0.59 Q969F8 EBI-21282286 0.40 P60033 EBI-25645944 0.35 P0DTC3 EBI-25686340 0.35 GO:0005737 GO:0070062 GO:0005794 GO:0005834 GO:0005765 GO:0031965 GO:0001750 GO:0005886 GO:0045202 GO:0001664 GO:0031683 GO:0005525 GO:0005096 GO:0003924 GO:0046872 GO:0001508 GO:0007202 GO:0007189 GO:0007188 GO:0007596 GO:0009649 GO:0007213 GO:0007215 GO:0006469 GO:0007603 GO:0050821 GO:0060828 GO:0010543 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:P21279} MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV 359 P21279 Guanine Gnaq 10090 None SL-0178 SL-0182 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}. UNIPROT P21279 UNIPROT Q6PFF5 PDB 2BCJ PDB 2RGN PDB 3AH8 PDB 4EKC PDB 4EKD PDB 4GNK PDB 4QJ3 PDB 4QJ4 PDB 4QJ5 PDB 5DO9 PDB 7SQ2 Pfam PF00503 PROSITE PS51882 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}. O08915 EBI-6979702 0.52 P11416 EBI-6259164 0.27 P08587 EBI-8071193 0.44 O54912 EBI-15571558 0.40 Q9ES08 EBI-15571606 0.40 Q01970 EBI-15939025 0.75 Q8R4D5 EBI-15993510 0.40 P41220 EBI-16037484 0.62 Q3UHD9 EBI-16736255 0.35 P62871 EBI-21282654 0.27 P63278 EBI-22091990 0.35 Q4ACU6 EBI-26960892 0.35 P16056 EBI-27112678 0.35 GO:0005901 GO:0044297 GO:0005829 GO:0030425 GO:0005794 GO:0005834 GO:0016020 GO:0031965 GO:0005886 GO:0045202 GO:0047391 GO:0001664 GO:0031683 GO:0005525 GO:0005096 GO:0003924 GO:0046872 GO:0044877 GO:0001508 GO:0007202 GO:0007189 GO:0007188 GO:1904888 GO:0048066 GO:0042733 GO:0086100 GO:0021884 GO:0007186 GO:0007215 GO:0007507 GO:0042711 GO:0010259 GO:0043066 GO:0043267 GO:0006469 GO:0016322 GO:0060158 GO:0007200 GO:0048661 GO:0009791 GO:0050821 GO:0008217 GO:0060828 GO:0045634 GO:0010543 GO:0001501 Lipid-Anchored UniProt Experimental Evidence {ECO:0000269|PubMed:8227063} MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV 359 Q2PKF4 Guanine GNAQ 9823 None SL-0178 SL-0182 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}. UNIPROT Q2PKF4 Pfam PF00503 PROSITE PS51882 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}. GO:0005794 GO:0005834 GO:0016020 GO:0031965 GO:0001750 GO:0045202 GO:0001664 GO:0031683 GO:0005525 GO:0005096 GO:0003924 GO:0046872 GO:0001508 GO:0007189 GO:0007188 GO:0009649 GO:0007213 GO:0007215 GO:0006469 GO:0007603 GO:0050821 GO:0060828 GO:0010543 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:P21279} MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV 359 P82471 Guanine Gnaq 10116 None SL-0178 SL-0182 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}. UNIPROT P82471 Pfam PF00503 PROSITE PS51882 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}. Q5XIE8 EBI-26438079 0.35 GO:0005901 GO:0044297 GO:0005829 GO:0030425 GO:0005794 GO:0005834 GO:0016020 GO:0031965 GO:0005886 GO:0045202 GO:0047391 GO:0001664 GO:0031683 GO:0005525 GO:0005096 GO:0003924 GO:0046872 GO:0044877 GO:0001508 GO:0007202 GO:0007189 GO:0007188 GO:1904888 GO:0048066 GO:0042733 GO:0086100 GO:0021884 GO:0007186 GO:0007215 GO:0007507 GO:0042711 GO:0010259 GO:0043066 GO:0043267 GO:0006469 GO:0016322 GO:0060158 GO:0007200 GO:0048661 GO:0009791 GO:0050821 GO:0008217 GO:0060828 GO:0045634 GO:0010543 GO:0001501 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:P21279} MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMVRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV 359 P38410 Guanine gnaq 8355 None SL-0178 SL-0182 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}. UNIPROT P38410 Pfam PF00503 PROSITE PS51882 Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. {ECO:0000250|UniProtKB:P50148}. GO:0005794 GO:0016020 GO:0031965 GO:0001750 GO:0005886 GO:0045202 GO:0001664 GO:0031683 GO:0005525 GO:0003924 GO:0046872 GO:0009649 GO:0007213 GO:0007603 Lipid-Anchored UniProt By Similarity {ECO:0000250|UniProtKB:P21279} MTLESIMACCLSEEAEEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFSAMQAMIRAMETLKIPYKYEHNKGHALLVREVDVEKVASFENPYVDAIKYLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRIATHGYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV 359 F4KHD8 Nuclear GB210 3702 None SL-0178 SL-0182 SL-0185 Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. UNIPROT F4KHD8 UNIPROT Q9FI62 GO:0005783 GO:0016021 GO:0005635 GO:0031965 GO:0005643 GO:0051028 GO:0015031 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVPVSFCFFFLLLLLSAGESSSQLVSGPHITDVNILLPPKMKNPVEYRLQGSDGCFKWSWDHHDILSVTPEFNSSSHCSTSARLRSISPYSGRKETAVYATDIQTGMVIRCKVFIDNFSRIQIFHNSIKLDLDGLSMLRVRAFDNEDNEFSSLVGLQFIWKLMPESGGSTHHLAHVPLKESPLTDCGGLCGYLDIQKKLEDSGVFADLFVVKGTKIGHEKVSVHLLEAPLTHIADEIVLTVAEAMSLEPRSPVYVLMGASFGYTLKVMRGNVPQAVDLPSPHHRWSVLNSSVAQVDSLIGLTKALSLGVTTVVVEDTRVAGHIQGSSINVVTPDTLILYISPWSMSGDLITESKPFPSSMHWYVVSGRQYLIQMKIFSGRPDAHEIYITETDDIKLYGKDSDYWKIVSLPDELSSEYGQRNSRILNAISPGLGELTSTLTYFSGHQESKEVLKVVQEIRVCEKVQFTLNSEDDTPKVLLPWTPAVYQEMELIVTGGCAKASSDYKWFTSDISILSVSAYGIIQAKRPGIATVKVVSTFDSQNFDEVIVEVSIPSSMVMLQNFPVETVVGSHLKAAVTMKALNGATFSRCDAFNSLIKWKTGSESFVIVNATSEMMMLDELRSMDSSPPCSRASIYTASTGRTVLQATLAKEFHYFDKSLSESIDLKATLTIGAYLPLSVRQDSDGNHHGGYWFDKAQEETDFGVSKLYLVPGTYVDVMLLGGPERWDDNVEFTETVKTLYEDEEDLTSRVNVHHEVDRRANMYRISCQKLGSYKLVFLRGNLLGIDHPVPAVAEALLSVHCSLPSSVVLIVDEPVNKLDVIRAASQADRAPGRLRVTPVTVANGQIIRVAAVGISEFGEAFSNSSTLSLRWELTSCNNLAYWDDDYNSKMTKSGWERFLALRNESGLCTVRATVSGIDYSFKSQYSTLLPQGSESTLTDAVRLQLVSTLRVTPEFNLVFFNPNAKVNLSMTGGSCLWEAVVNNSRVAEVIRPPSGLQCSQMMLSPKGLGTTIVTVYDIGVSPPLSALALIKVADVDWIKIASGDEISIMEGSTHSIDLLTGIDDGMTFDSSQYSLMDIMVHIEDDLVEHVTVDEDSLSVGEHVATSSFKIAARRLGITTLYVSARQQSGGKVLSQTIKVEVYSPPRLHPQGIFLVPGASYVLTIEGGPTMNVSVDYTTVDNEVAKIEKSGRLYATSPGNTTIYATIYGSEGAVICQAIGNAEVGLPATAMLVAQSDTVAVGHEMPVSPSFPEGDLLSFYELCSAYKWTIEDEKVLIFIASSINVEENAGFVNVVQGRSAGKTRVTIAFSCDFVSPGLYSESRTYEASMILSVVPDLPLSLGAPMTWVLPPFYTSSGLLPSSSEPQKHRDGQSHRGNIVYSILKDCSSRADFERDTISINGGSVKTTDSNNVACIQAKDRTSGRIEIAACVRVAEVAQIRMKSEGIPFHVIDLAVGGELELPINYYDTLGIPFLEAHGVTTYNVETNHRDVVFIKTVNDQPSAYIKGIKHGKALIRVSIGDNLRKSDYVLVSVGAHIFPQNPVIHTGNLLNFSITGADNEVTGQWFTSNRSVISVNVASGQAKAISQGSTHVTFKGHGLKLQTKVTVLFGNTIYVDSPGETLTNVHVPAEGYKFPVKFRENKFAVTEHGNKATFNCQVDPPFIGYTKPWMDLDTGNTYCLFFPYSPEHLVHSMSITKDMKPHVSFSVDASLKEARRVSGSASALLIGGFSVTGPDKLNINPDSNTTIISLVGNTDVQIHCRNKGRLSISLIKRDDFGIAGHAQYKVNVLRSEQFTDRIIITLPATGQIVEIDVCYDTGESLVASSKDGYSVLLKILWGVLVLVVSVIILMKVIDRQVPTGATGTATYSGNAAQGTPERRSGTVIYHEESPRTPSPFMEYVKRTVDETPYYRREGRRRFNPQNTM 1923 Q86D96 Guanine GA1 5722 None SL-0198 Cytoplasm. Cytoplasm, perinuclear region. Endomembrane system; Lipid-anchor. Note=Predominantly perinuclear. UNIPROT Q86D96 Pfam PF00503 PROSITE PS51882 Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. {ECO:0000250}. GO:0012505 GO:0016020 GO:0048471 GO:0031683 GO:0005525 GO:0003924 GO:0007186 Lipid-Anchored UniProt Sequence Analysis {ECO:0000255} MGCSASKPSEPSNAKLPSAPVPKKVEQVPEPKPEPQPQPEPQPQPEPPKPAEPAPAPAPAPEPQKPAEPAPKVVAVEDDTNEAYGLLLCGAGESGKTTFTRQLKLRYLNGFNEKDCRDFLRTIRGNLVETMQLLLVWLEHNNIEIEDSELSSMAQDIIDVDPQDCEFNEELVEKLKALWENEQIKKAFEHKDETAVPDHMPYFFAKIDELAGEDYIPSNEDVLRARIRSIGIEAITFDLQGARIRIFDVGGQKSERSKWANVMNQVEGVIFCVSFAEFDKPMFEDQNVLRINDSLEIFGNITHQEKFSNSPIFLVCNKFDVFTEKIKNTDAFVKIFPEFSGDSHNPEACADYLIQRFLDKAAPLSEDRPIIQYKIVALNGDQVVETADAICKFISDKYYQDA 402 B3G515 G-protein gper1 7955 None SL-0198 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}. UNIPROT B3G515 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0070161 GO:0030424 GO:0016323 GO:0030659 GO:0005856 GO:0032591 GO:0005769 GO:0005789 GO:0000139 GO:0016021 GO:0031966 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0045211 GO:0055037 GO:0004930 GO:0030284 GO:0005496 GO:1990239 GO:0006915 GO:0007420 GO:0007049 GO:0030154 GO:0071392 GO:0060047 GO:0051447 GO:0043524 GO:1900194 GO:0040019 GO:2000179 GO:0001934 GO:0045944 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEEQTTNVIQIYVNGTEQFNASFDFNITDVKESTDTYEFYIIGLFLSCLYTIFLFPIGFIGNILILVVNLNHRERMTIPDLYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYVALTSSMSSSPLRTMQHAKLSCSLIWMASILATLLPFTIVQTQHTGEVHFCFANVFEIQWLEVTIGFLIPFSIIGLCYSLIVRTLMRAQKHKGLWPRRQKALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSKRTDTTLWHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKLRLFIKRKASWSVVYRFCNHTLDLQIPVRSESEV 353 Q99527 G-protein GPER1 9606 None SL-0198 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}. UNIPROT Q99527 UNIPROT A8K6C5 UNIPROT B5BUJ1 UNIPROT O00143 UNIPROT O43494 UNIPROT Q13631 UNIPROT Q6FHL1 UNIPROT Q96F42 UNIPROT Q99981 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 OMIM 601805 DisGeNET 2852 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}. A0A6L7HHX2 EBI-2833018 0.00 GO:0070161 GO:0030424 GO:0043679 GO:0005737 GO:0030659 GO:0005829 GO:0030425 GO:0043198 GO:0044327 GO:0032591 GO:0005769 GO:0005783 GO:0005789 GO:0005794 GO:0000139 GO:0098686 GO:0005887 GO:0043231 GO:0045095 GO:0031966 GO:0005635 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0048786 GO:0042734 GO:0055037 GO:0005802 GO:0003682 GO:0038054 GO:0004930 GO:0030284 GO:0005496 GO:1990239 GO:0007189 GO:0030263 GO:0007049 GO:0030154 GO:0071392 GO:0071333 GO:0071389 GO:0071375 GO:0071356 GO:0007186 GO:0006954 GO:0045087 GO:0030518 GO:0010948 GO:0008285 GO:0070373 GO:0045599 GO:0010629 GO:0050728 GO:0002695 GO:0051055 GO:0051898 GO:1904706 GO:0007399 GO:0019228 GO:0030264 GO:0043065 GO:2000724 GO:0030335 GO:0008284 GO:0043280 GO:0007204 GO:2000353 GO:0045742 GO:0070374 GO:2001238 GO:0045745 GO:0010628 GO:0032962 GO:0032024 GO:0043410 GO:0050769 GO:0001956 GO:0014068 GO:1903078 GO:0001934 GO:0090200 GO:0051281 GO:0045944 GO:0070474 GO:0051726 GO:0051480 GO:0043401 GO:0042311 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDVTSQARGVGLEMYPGTAQPAAPNTTSPELNLSHPLLGTALANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHERYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALARAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRVLVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLNPLIYSFLGETFRDKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV 375 F7EQ49 G-protein GPER1 9544 None SL-0198 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}. UNIPROT F7EQ49 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0070161 GO:0030424 GO:0043679 GO:0016323 GO:0005737 GO:0030659 GO:0005829 GO:0030425 GO:0043198 GO:0044327 GO:0032591 GO:0005769 GO:0005783 GO:0005789 GO:0098978 GO:0005794 GO:0000139 GO:0098686 GO:0099055 GO:0099056 GO:0045095 GO:0031966 GO:0005635 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0048786 GO:0042734 GO:0055037 GO:0005802 GO:0003682 GO:0038054 GO:0030284 GO:0005496 GO:1990239 GO:0007189 GO:0030263 GO:0007049 GO:0030154 GO:0071392 GO:0071333 GO:0071389 GO:0071375 GO:0071356 GO:0006954 GO:0045087 GO:0030518 GO:0010948 GO:0008285 GO:0070373 GO:0045599 GO:0010629 GO:0050728 GO:0002695 GO:0051055 GO:0051898 GO:1904706 GO:0007399 GO:0019228 GO:0030264 GO:0043065 GO:2000724 GO:0030335 GO:0008284 GO:0043280 GO:0007204 GO:2000353 GO:0045742 GO:0070374 GO:2001238 GO:0045745 GO:0010628 GO:0032962 GO:0032024 GO:0043410 GO:0050769 GO:0001956 GO:0014068 GO:1903078 GO:0001934 GO:0090200 GO:0051281 GO:0045944 GO:0070474 GO:0051726 GO:0051480 GO:0043401 GO:0042311 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEVTSQARGMGLEMYPGTMQPAAPNTTSPELNLSHPLLGASLANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHEQYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALARAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRVLVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLNPLIYSFLGETFREKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV 375 B0F9W3 G-protein gper1 29154 None SL-0198 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. UNIPROT B0F9W3 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0070161 GO:0030424 GO:0016323 GO:0030659 GO:0005856 GO:0032591 GO:0005769 GO:0005789 GO:0000139 GO:0016021 GO:0031966 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0045211 GO:0055037 GO:0004930 GO:0005496 GO:1990239 GO:0007189 GO:0006915 GO:0007049 GO:0030154 GO:0071392 GO:0071371 GO:0051447 GO:1900194 GO:0007399 GO:0043401 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEEQTTSLVWIYVNSTEQLNTSYEYNTTYLIEDSDKYQSYVIGLFLSCLYTILLFPIGFIGNILILVVNLNHRGKMAIPDLYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYIALANSMSSSPLRTMQHAKLSCGLIWMASILATLLPFTIVQTQHRGEVHFCFANVFEIQWLEVTIGFLVPFSIIGLCYSLIGRILMRSQKHRGLWPRRQKALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSQRTATTLRHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKLRLFIKQKASWSVVNRFCHHGLDLHLPVRSEVSEV 354 Q8BMP4 G-protein Gper1 10090 None SL-0198 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}. UNIPROT Q8BMP4 UNIPROT B2RRW0 UNIPROT Q9D392 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0070161 GO:0030424 GO:0043679 GO:0005737 GO:0030659 GO:0005829 GO:0030425 GO:0043198 GO:0044327 GO:0032591 GO:0005769 GO:0005783 GO:0005789 GO:0005794 GO:0000139 GO:0098686 GO:0016021 GO:0043231 GO:0045095 GO:0031966 GO:0043025 GO:0005635 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0045211 GO:0048786 GO:0042734 GO:0055037 GO:0005802 GO:0003682 GO:1903924 GO:0038054 GO:0030284 GO:0005496 GO:1990239 GO:0007189 GO:0030263 GO:0007049 GO:0030154 GO:0071392 GO:0071333 GO:0071389 GO:0071375 GO:0071356 GO:0007186 GO:0006954 GO:0045087 GO:0030520 GO:0030518 GO:0050804 GO:0010948 GO:0008285 GO:0070373 GO:0045599 GO:0010629 GO:0050728 GO:0002695 GO:0051055 GO:0051898 GO:1900121 GO:1904706 GO:0007399 GO:0019228 GO:0030264 GO:0043065 GO:2000724 GO:0030335 GO:0008284 GO:0043280 GO:0007204 GO:2000353 GO:0045742 GO:0070374 GO:2001238 GO:0045745 GO:0010628 GO:0032962 GO:0032024 GO:0043410 GO:0050769 GO:0001956 GO:0014068 GO:0042307 GO:0051897 GO:1903078 GO:0001934 GO:0090200 GO:0051281 GO:0045944 GO:0070474 GO:1905152 GO:0051726 GO:0051480 GO:0007210 GO:0043401 GO:0042311 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDATTPAQTVGVEIYLGPVWPAPSNSTPLALNLSLALREDAPGNLTGDLSEHQQYVIALFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAAADLILVADSLIEVFNLDEQYYDIAVLCTFMSLFLQINMYSSVFFLTWMSFDRYLALAKAMRCGLFRTKHHARLSCGLIWMASVSATLVPFTAVHLRHTEEACFCFADVREVQWLEVTLGFIMPFAIIGLCYSLIVRALIRAHRHRGLRPRRQKALRMIFAVVLVFFICWLPENVFISVHLLQWTQPGDTPCKQSFRHAYPLTGHIVNLAAFSNSCLNPLIYSFLGETFRDKLRLYVEQKTSLPALNRFCHATLKAVIPDSTEQSEVRFSSAV 375 O08878 G-protein Gper1 10116 None SL-0198 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}. UNIPROT O08878 Pfam PF00001 PROSITE PS00237 PROSITE PS50262 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}. GO:0070161 GO:0030424 GO:0043679 GO:0005737 GO:0030659 GO:0030425 GO:0043198 GO:0044327 GO:0032591 GO:0005769 GO:0005783 GO:0005789 GO:0005794 GO:0000139 GO:0098686 GO:0016021 GO:0045095 GO:0031966 GO:0043025 GO:0005635 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0048786 GO:0042734 GO:0055037 GO:0005802 GO:0003682 GO:1903924 GO:0038054 GO:0030284 GO:0005496 GO:1990239 GO:0007189 GO:0030263 GO:0007049 GO:0030154 GO:0071392 GO:0071333 GO:0071389 GO:0071375 GO:0071356 GO:0007186 GO:0006954 GO:0045087 GO:0030520 GO:0030518 GO:0050804 GO:0010948 GO:0008285 GO:0070373 GO:0045599 GO:0010629 GO:0050728 GO:0002695 GO:0051055 GO:0051898 GO:1900121 GO:1904706 GO:0007399 GO:0019228 GO:0030264 GO:0043065 GO:2000724 GO:0030335 GO:0008284 GO:0043280 GO:0007204 GO:2000353 GO:0045742 GO:0070374 GO:2001238 GO:0045745 GO:0010628 GO:0032962 GO:0032024 GO:0043410 GO:0050769 GO:0001956 GO:0014068 GO:0042307 GO:0051897 GO:1903078 GO:0001934 GO:0090200 GO:0051281 GO:0045944 GO:0070474 GO:1905152 GO:0051726 GO:0051480 GO:0007210 GO:0043401 GO:0042311 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAATTPAQDVGVEIYLGPVWPAPSNSTPLALNLSLALREDAPGNLTGDLSEHQQYVIALFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAAADLILVADSLIEVFNLDEQYYDIAVLCTFMSLFLQINMYSSVFFLTWMSFDRYLALAKAMRCGLFRTKHHARLSCGLIWMASVSATLVPFTAVHLRHTEEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRALIRAHRHRGLRPRRQKALRMIFAVVLVFFICWLPENVFISVHLLQWAQPGDTPCKQSFRHAYPLTGHIVNLAAFSNSCLSPLIYSFLGETFRDKLRLYVAQKTSLPALNRFCHATLKAVIPDSTEQSDVKFSSAV 375 Q7Z6J2 Protein TAMALIN 9606 None SL-0198 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}. UNIPROT Q7Z6J2 UNIPROT Q6PIF8 UNIPROT Q7Z741 PDB 2PNT Pfam PF00595 PROSITE PS50106 OMIM 612027 DisGeNET 160622 Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses. {ECO:0000250}. Q5NHN0 EBI-2806502 0.00 Q9BYF1 EBI-28949723 0.40 GO:0070161 GO:0098978 GO:0048471 GO:0005886 GO:0014069 GO:0045211 GO:0098685 GO:0042802 GO:0030165 GO:0031267 GO:0008104 GO:0099152 GO:0007165 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q8R4T5} MTLRRLRKLQQKEEAAATPDPAARTPDSEVAPAAPVPTPGPPAAAATPGPPADELYAALEDYHPAELYRALAVSGGTLPRRKGSGFRWKNLSQSPEQQRKVLTLEKEDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNGLNVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTLESVRSCLYGAGLLPGSLPFGPLLAVPGRPRGGARRARGDADDAVYHTCFFGDSEPPALPPPPPPARAFGPGPAETPAVGPGPGPRAALSRSASVRCAGPGGGGGGGAPGALWTEAREQALCGPGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL 395 Q9JJA9 General Tamalin 10090 None SL-0198 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}. UNIPROT Q9JJA9 UNIPROT Q9JKL0 Pfam PF00595 PROSITE PS50106 Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses. {ECO:0000250}. Q9QWI6 EBI-27100778 0.35 GO:0070161 GO:0005737 GO:0098978 GO:0005641 GO:0048471 GO:0005886 GO:0014069 GO:0045211 GO:0098685 GO:0042802 GO:0030165 GO:0031267 GO:0006886 GO:0008104 GO:0099152 GO:0007165 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:Q8R4T5} MTLRRLRKLQQKEEATAAPDPAGRAPDSEAARAAPLPSGPPAAAAPPGAPGEELYAALEDYHPAELYRALAVSGGTLPRRKGSGFRWKNFTQSPEQQRKVLTLEKGDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNGLNVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTLESVRSCLYGAGLLPGSLPFGPLLAAPGSARGGARRAKGDTDDAVYHTCFFGGAEPQALPPPPPPARALGPSSAETPASVLFPAPRSTLSRSASVRCAGPGGGGGAPGALWTEAREQALCGAGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL 392 Q8R4T5 General Tamalin 10116 None SL-0198 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}. UNIPROT Q8R4T5 PDB 2EGK PDB 2EGN PDB 2EGO Pfam PF00595 PROSITE PS50106 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}. P63035 EBI-8600171 0.37 Q91Y79 EBI-8600241 0.37 P14314 EBI-8600313 0.37 O94868 EBI-8600330 0.37 O15062 EBI-8600386 0.37 Q8R515 EBI-8600369 0.37 P97838 EBI-8600437 0.51 Q9Y592 EBI-8600403 0.37 P11274 EBI-8600478 0.37 O88573 EBI-8600550 0.37 O35431 EBI-8600652 0.52 O88382 EBI-8600638 0.70 P31016 EBI-8600666 0.52 P97836 EBI-8600894 0.40 Q62915 EBI-8600971 0.40 Q8R4T5 EBI-8600781 0.67 P31424 EBI-7361910 0.63 GO:0070161 GO:0098978 GO:0048471 GO:0005886 GO:0014069 GO:0045211 GO:0098685 GO:0042802 GO:0030165 GO:0031267 GO:0008104 GO:0099152 GO:0007165 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:11850456} MTLRRLRKLQQKEEATAAPDLAGRAPDSEAARAAPTPSGPPAAAAPPGAPGDELYAALEDYHPAELYRALAVSGGTLPRRKGSGFRWKNFTQSPEQQRKVLTLEKGDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNGLNVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTLESVRSCLYGAGLLPGSLPFGPLLAAPGGARGGSRRAKGDTDDAVYHTCFFGGAEPQALPPPPPPARAPGPGSAETPASVLCPAPRATLSRSASVRCAGPGGGGGGGAPGALWTEAREQALCGAGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL 394 Q55AP1 Metabotropic grlA 44689 None SL-0198 Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cell cortex {ECO:0000269|PubMed:17950724}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17950724}. UNIPROT Q55AP1 Pfam PF00003 Pfam PF02608 PROSITE PS50259 May play an important role in the terminal differentiation. {ECO:0000269|PubMed:17950724}. GO:0005938 GO:0005789 GO:0016021 GO:0005635 GO:0048471 GO:0005886 GO:0004930 GO:0030587 GO:0030435 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNKLKFLIILFITFLFNLKYINSLKQCKISVLLSGDWSDMGYNYQMNNARIKAESALNLEMSLCYKNLEVSIDLAKQAIEDSIKKGANFIVISSSVHTSIGYEYARLHRDKDIYWLIRGRGRPVPDDLPKVAVINFNTHLLHYTLGLVSGYLTTSGTVGFISPGPQILALANSNSFYLGALASRKNVTFLNAYTGSWYNPEVAYKASQMLISNGADFIGMSQDDMSVQKALMDSGKMALGITGFSNRLIWGSDIALSYITDWSDVFIKYAGHILNDTWPEYTDYYTTLAEGGSLLFDTFSYRVPSEVQKLVSLEIEKLKNSSYQPFRCNPMYSQINLNFDSNGCANDMEFKNTKLLLKGTDISKTINLGLYTIPIEFVDYSNSMKLGLTIVSGFCILFCIISMVLVIMFRHAKIIKSASPIFCLLILFGCIIIFSGCIIFSLSPTDGICGARVWLLSIGYTIFLGSLLVKNWRIWLLFDNPKLKKRSITNWKLYPFVAGILAADVLILALWQGLGDIRSESRIGIDSLTKYQYANVCSSNDQGSVALYILLVFHGIKLLAACFISFKIKAVDIEEFNESKPIASSIYIITFCLFIVIPLMVSPQSVASQVITIVVCAIVTTLISISLLFGSKFYMMATQGLALNQTFATNTKSSSFSLSLEKQKSKSNGLEFEDSDESEEKLPQIKNYSNSEIPNLQHNHSRLAHFSSDSCTSAEQDSKLDLENQNDENEIENNQNNQNNIVEDCQKVEKLEKDENLEKDENLEKDENLEKDNENQSIIQKKRLSKNFNQSEIDPDDV 798 Q75JT4 Metabotropic grlJ 44689 None SL-0178 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. UNIPROT Q75JT4 UNIPROT Q559S6 Pfam PF00003 Pfam PF02608 PROSITE PS50259 May act during the development and be a negative regulator. {ECO:0000269|PubMed:17501984}. GO:0005789 GO:0000139 GO:0016021 GO:0005635 GO:0031090 GO:0005886 GO:0004930 GO:1902610 GO:0031153 GO:0030587 GO:0030435 Transmembrane UniProt Sequence Analysis {ECO:0000255} MKILLYIAIILSFFSLITISSECKIAVLLSGSPNDLGYNYLMNEARVKAESELKLDFSIYYENLEESMEEAEKAFQDALHKGANLIVVGSFVHVGLGLKYAALTKDQDIYWIIRGNKRPNPDLPHVVILNFNSFELHYLLGYFSGLMTKTGIVGFVAPGPDVNTISTDNSFYLGAKYARPNITFLNVYVQSWYNPNVSYSAAKMLIKNGADLIGMSQDDMSCQKAMMDSGLIGIGATGYPTHLLFGGNVGVSYITNWTNLYVKYAQHVLNDDWPDYSSYFTNLSREDSIFIDDYSYKVPIDIQNLVNDEIQRLKNTSYIPYRSDPYLAQLGIPFDSKGLLVEDQFRANKKLLKGDSISKVIDFGQYSIPIEFIDYPNSLKYGVTIVSGVCIFICLVCMTLVVVFKKARVIKSSSPAFLLLILLGCCIIFAACILFAQSPTNQTCSARIWLLSLGYTLFLGNLLVKNWRIWLLFDNPKLKKRAITNWKLYPWVFAILAIDVMILAIWQGLGNINAESRIGYDSLTQYQYKNVCSSDDQGSIALYLLLVFHGLVLLVACFISFKIKVVDIEEFNESKPITTSVYIITFCLFIVIPLMVSPQSLTSQTTIICVCAIVTTLISMLLLFGSKFYKMATQGLAINETFATSTKSSSKSSKSSYGKDNPNPNAINFGEDDTSDETSEEKHKSPKQKSVNFSNKSNSHLAVFTSDEETSKTSKLSIDFENSSKDISIDQLQQQKQQPINTNGDLENKSNDKIDDDNDNSSVLSKRISNQQNGETEIDSNNV 783 Q32M21 Gasdermin-A2, Gsdma2 10090 None SL-0198 [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}. UNIPROT Q32M21 UNIPROT Q8CF01 UNIPROT Q9D810 Pfam PF04598 Pfam PF17708 [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}. GO:0005829 GO:0016021 GO:0048471 GO:0005886 GO:0005546 GO:0070273 GO:0001786 GO:0006915 GO:0042742 GO:0070269 Transmembrane UniProt By Similarity {ECO:0000250|UniProtKB:Q5Y4Y6} MSMFEDVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVRTDYTLLDVLEPGSSPSDPTLLGNFSFKNMLDVRVEGDVEVPTMMKVKGTVGLSQSSTLEVQMLSVAPTALENLHMERKLSADHPFLKEMREYKQNLYVVMEVVKAKQEVTLKRASNAISKFSLNLPSLGLQGSVNHKEAVTIPKGCVLAYRVRQLIIYGKDEWGIPYICTDNMPTFNPLCVLQRQGSTVQMISGEMHEDFKTLKKEVQQETQEVEKLSPVGRSSLLTSLSHLLGKKKELQDLEQMLEGALDKGHEVTLEALPKDVLLLKDAMDAILYFLGALTELSEEQLKILVKSLENKVLPVQLKLVESILEQNFLQDKEDVFPLRPDLLSSLGEEDQILTEALVGLSGLEVQRSGPQYTWNPDTCHNLCALYAGLSLLHLLSRDS 443 Q96QA5 Gasdermin-A, GSDMA 9606 None SL-0198 [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}. UNIPROT Q96QA5 UNIPROT Q32MC5 UNIPROT Q86VE7 UNIPROT Q8N1M6 Pfam PF04598 Pfam PF17708 OMIM 611218 DisGeNET 284110 [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}. O75593 EBI-11320921 0.35 P02654 EBI-23875424 0.56 P55056 EBI-25158560 0.56 O43309 EBI-21572679 0.35 Q9NU19 EBI-21575852 0.35 Q9UMR2 EBI-21616596 0.35 Q15915 EBI-21696712 0.35 Q5S007 EBI-21360986 0.35 Q9P2S5 EBI-25486895 0.35 P69479 EBI-25568044 0.35 O43781 EBI-28931148 0.35 Q14296 EBI-28941126 0.35 GO:0005829 GO:0016021 GO:0048471 GO:0005886 GO:0005546 GO:0070273 GO:0001786 GO:0006915 GO:0042742 GO:0070269 Transmembrane UniProt By Similarity {ECO:0000250|UniProtKB:Q5Y4Y6} MTMFENVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVRTDYTLLDVLEPGSSPSDPTDTGNFGFKNMLDTRVEGDVDVPKTVKVKGTAGLSQNSTLEVQTLSVAPKALETVQERKLAADHPFLKEMQDQGENLYVVMEVVETVQEVTLERAGKAEACFSLPFFAPLGLQGSINHKEAVTIPKGCVLAFRVRQLMVKGKDEWDIPHICNDNMQTFPPGEKSGEEKVILIQASDVGDVHEGFRTLKEEVQRETQQVEKLSRVGQSSLLSSLSKLLGKKKELQDLELALEGALDKGHEVTLEALPKDVLLSKEAVGAILYFVGALTELSEAQQKLLVKSMEKKILPVQLKLVESTMEQNFLLDKEGVFPLQPELLSSLGDEELTLTEALVGLSGLEVQRSGPQYMWDPDTLPRLCALYAGLSLLQQLTKAS 445 Q9EST1 Gasdermin-A, Gsdma 10090 None SL-0198 [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}. UNIPROT Q9EST1 UNIPROT A3KFN3 Pfam PF04598 Pfam PF17708 [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}. Q6AXH7 EBI-6876709 0.35 GO:0005737 GO:0005829 GO:0016021 GO:0048471 GO:0005886 GO:0005546 GO:0070273 GO:0001786 GO:0006915 GO:0042742 GO:0070269 Transmembrane UniProt By Similarity {ECO:0000250|UniProtKB:Q5Y4Y6} MTMFENVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVHTDYTLLDVLEPGSSPSDPTDSGNFSFKNMLDARVEGDVDVPKTVKVKGTAGLSRSSTLEVQTLSVAPTALENLHKERKLSADHPFLKEMRERGENLYVVMEVVETLQEVTLERAGKAEGCFSLPFFAPLGLQGSVNHKEAVTIPKGCVLAYRVRQLMVNGKDEWGIPHICNDSMQTFPPGEKPGEGKFILIQASDVGEMHEDFKTLKEEVQRETQEVEKLSPVGRSSLLTSLSHLLGKKKELQDLEQTLEGALDKGHEVTLEALPKDVLLSKDAMDAILYFLGALTVLSEAQQKLLVKSLEKKILPVQLKLVESTMEKNFLQDKEGVFPLQPDLLSSLGEEELILTEALVGLSGLEVQRSGPQYTWDPDTLPHLCALYAGLSLLQLLSKNS 446 F1R0H0 Solute slc2a10 7955 None SL-0198 Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}. UNIPROT F1R0H0 UNIPROT A8KB28 UNIPROT I1SV80 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000269|PubMed:22116938}. GO:0012505 GO:0016021 GO:0016020 GO:0048471 GO:0005355 GO:0015293 GO:0072359 GO:1904659 GO:0030903 GO:0055085 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGCSVLLLTITVSTLGGLVFGYELGIISGALPQLQTHFSLGCVQQEAVVSALLIGSLFASIIGGWLIDRHGRRTSILLSNLLILAGSVILTTGTSFFALVIGRAVIGFAMTVSSMSCCIFVSEMVTPERRGLMVTLYEVGITVGILIAYAVNYIFNNVPLTGWRYMFGFAIIPSLIQLASIVLLPKQAEVFVIHDDDSRQADRLTEETETSNQHQQSEKYGVSDLFKSKDNMRRRTVIGVGLVLSQQFTGQPNVLFYASTILFSVGFQSNASAILASVGFGIVKVIATLLAMLCSDRAGRRSLLIGGCSMLAVGLILTGFLCRQSVIDTTKRCTSVGPHSNLTLSAEHDEGVGFSSQTLDVHEHLRSFSQSEDIYKWIIFTCLMAVVSAFSVSFGPMTWVVLSEIFPKDIRGRAFSFINCFNVGANLIVSFSFLSIIDVIGLSGVFLMYGVVGIAGVVFIYLVLPETKGKSLQDIDRELSQTRMIHRQELCSIFQRRRFSPGYQRVQLTSTAT 513 O95528 Solute SLC2A10 9606 None SL-0198 Endomembrane system {ECO:0000269|PubMed:16550171}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16550171}. UNIPROT O95528 UNIPROT A8K4J6 UNIPROT Q3MIX5 UNIPROT Q9H4I6 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 OMIM 208050 OMIM 606145 DisGeNET 81031 Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000269|PubMed:11592815, ECO:0000269|PubMed:16550171}. 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. GO:0005829 GO:0012505 GO:0016021 GO:0016020 GO:0048471 GO:0005886 GO:0005351 GO:0055056 GO:0033300 GO:0005355 GO:0015293 GO:0060840 GO:0045454 GO:0072359 GO:0070837 GO:0072498 GO:0015757 GO:0098708 GO:1904659 GO:0008645 GO:0032683 GO:0010629 GO:2001045 GO:1902729 GO:0060392 GO:0030512 GO:0010628 GO:1902730 GO:0030511 GO:1903053 GO:0043588 GO:0055085 GO:0150104 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGHSPPVLPLCASVSLLGGLTFGYELAVISGALLPLQLDFGLSCLEQEFLVGSLLLGALLASLVGGFLIDCYGRKQAILGSNLVLLAGSLTLGLAGSLAWLVLGRAVVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEAGITVGILLSYALNYALAGTPWGWRHMFGWATAPAVLQSLSLLFLPAGTDETATHKDLIPLQGGEAPKLGPGRPRYSFLDLFRARDNMRGRTTVGLGLVLFQQLTGQPNVLCYASTIFSSVGFHGGSSAVLASVGLGAVKVAATLTAMGLVDRAGRRALLLAGCALMALSVSGIGLVSFAVPMDSGPSCLAVPNATGQTGLPGDSGLLQDSSLPPIPRTNEDQREPILSTAKKTKPHPRSGDPSAPPRLALSSALPGPPLPARGHALLRWTALLCLMVFVSAFSFGFGPVTWLVLSEIYPVEIRGRAFAFCNSFNWAANLFISLSFLDLIGTIGLSWTFLLYGLTAVLGLGFIYLFVPETKGQSLAEIDQQFQKRRFTLSFGHRQNSTGIPYSRIEISAAS 541 Q8VHD6 Solute Slc2a10 10090 None SL-0198 Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}. UNIPROT Q8VHD6 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000250|UniProtKB:O95528}. GO:0005829 GO:0012505 GO:0005887 GO:0016020 GO:0048471 GO:0005886 GO:0055056 GO:0033300 GO:0005355 GO:0015293 GO:0060840 GO:0045454 GO:0072359 GO:0070837 GO:0072498 GO:0098708 GO:1904659 GO:0032683 GO:0010629 GO:2001045 GO:1902729 GO:0060392 GO:0030512 GO:0010628 GO:1902730 GO:0030511 GO:1903053 GO:0043588 GO:0055085 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGLRPAVLLLCASVSLLGGLTFGYELAVISGALLPLQLNFGLSCLEQELLVGSLLLGALLASLVGGFLIDCYGRRRAILGSNAVLLAGSLILGLASSLPWLLLGRLSVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEVGITVGILFSYGLNYVLAGSPWGWRHMFGWAAAPALLQSLSLFLLPAGAEGTAAPKDLIPLQGRETSKPGLVKPQYSFLDLFRAQDGMWSRTVVGLGLVLFQQLTGQPNVLYYASTIFRSVGFHGGSSAVLASVGLGTVKVAATLVATGLVDRAGRRVLLLFGCALMALSVSGIGLVSFAVSLDSGPSCLATSNASQQVDLPGSSGLLVRSSLPPVLHTNGDQGQLVLSVTERPIHPVITASLGPVLNTASPVPTSPILEHTLLCWSALVCMMVYVSAFSVGFGPVTWLVLSEIYPAEIRGRAFAFCSSFNWAANLFISLSFLDLIGAIGLAWTFLLYGLTAVLGLAFIYLLVPETKGQSLAEIEQQFQTSRFPLNFGHRQRIGIQYHRLDVSSAS 536 Q6GN01 Solute slc2a10 8355 None SL-0198 Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}. UNIPROT Q6GN01 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000250|UniProtKB:O95528}. GO:0012505 GO:0016021 GO:0048471 GO:0022857 GO:0008643 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGLRSTTLVLAATSSLLGGLIFGYELGIISGALLMLKTVFQLTCFEQEALVSAVLFGALLASLIGGFIIDRSGRRTSIMGSNLVVLAGSIILIATSSFWWLVVGRVTVGFAISISSMACCIYVSEIVRPHQRGTLVSLYETGITVGILISYAMNYFLSAVNDGWKYMFGLAIIPAAFQFIVILFLPSKPHTLNFWEQDSDNGFIELEEAGESGEFKPDTYDKQYTFLDLFRSKDNMRTRTLLGLGLVLFQQFTGQPNVLYYASTIFRSVGFQSNSSAVLASVGLGVVKVASTLIAICFADKAGRRILLLAGCIVMTIAISGIGIVSFMVELDSHRDCGSIRSKNTSYGDSNASQLLGIIHAGTPTINTKDNLAHQLAMVIQSPSLSNSAGSKHTASMFPNSTVPPAGPDSNYAILNWITLLSMMAFVSAFSIGFGPMTWLVLSEIYPADIRGRAFAFCNSFNWAANLLITLTFLEVIGSIGLGWTFLLYGGVGLLAIAFIYFFIPETKGQSLEEIDQQLSSKRISKRRETSKGVRKRPSTGPPYQRVGKSNWT 553 Q0P4G6 Solute slc2a10 8364 None SL-0198 Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}. UNIPROT Q0P4G6 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000250|UniProtKB:O95528}. GO:0012505 GO:0016021 GO:0016020 GO:0048471 GO:0005355 GO:0015293 GO:0072359 GO:1904659 GO:0055085 Transmembrane UniProt Sequence Analysis {ECO:0000255} MGLSSPTLILAATVSLLGGIVFGYELGIISGALLVLKTVYQLTCFEQEALVSAVLFGALLASLIGGIIIDRWGRRTAILASNLVVLAGSIILIATSTFWWLIVGRVTIGFAISISSMACCIYVSEIVRPHQRGMLVSLYETGITVGILISYAMNYFLSGVNESWKYMFGLAIVPAAFQFISILFLPSKPHKLNFWEQDTDDGFIELEETGEAGEFKPDTYDRQYTFLDLFRSKDNMRTRTLLGLGLVLFQQFTGQPNVLYYASTIFQSVGFQSNSSAVLASVGLGVVKVASTLIAICFADKAGRRILLLAGCIVMTIAITGIGIVSFTVKMDSHRDCGSVTGRNMSSGESNVSQLLGIVHAETSTINTLDNSVHQLAMAIRSPSLANSASSNHKDLISQNSTVLPASPELPSNYTILNWITLLSMMAFVSAFSIGFGPMTWIVLSEIYPADIRGRAFAFCNSFNWAANLLITLTFLDVIASIGLSWTFLLYGVVGLLAIAFIYFFIPETKGQSLEEIDKQFSTKRILQKRETSKGVGKRPSSGPPYQRIGKASPS 555 Q5J316 Solute SLC2A12 9913 None SL-0198 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}. UNIPROT Q5J316 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Insulin-independent facilitative glucose transporter. {ECO:0000250|UniProtKB:Q8BFW9}. GO:0012505 GO:0016021 GO:0048471 GO:0005886 GO:0022857 GO:0008643 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVPVENAEGPSLLKPKGRAAETDGSDRASGGPHPPWARGCGMYTLLSSVTAAVSGFLVGYELGIISGALLQIRTLLVLTCHEQEMVVSSLLIGALLASLIGGVLIDRYGRRAAIILSSCLLGLGSLVLIISLSYTTLIGGRIAIGVFISLSSTATCVYIAEIAPQHRRGLLVSLNELMIVIGILFAYISNYAFANISHGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGHEEAASKVLGKLRAVLDTTEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAASLASTGVGVVKVISTIPATLLVDQVGSKTFLCIGSSVMAASLVTMGIVNLNIHMNFTSICRNHSPINQSLDESVFYGPGNLSASNDTLRESFKGMTFHSRSSLRPTRNDINGRGETTLASLPNAGLSQTEYQIVTDSADVPTFLKWLSLASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTDLIGLPWVCFIYTVMSLASLVFVIVFIPETKGCSLEQISVELAKENYVKNNICFMSHHREELVPKQLQKRKPQEQFLESKKLRGKGQPRQLSSEV 621 Q6NWF1 Solute slc2a12 7955 None SL-0198 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}. UNIPROT Q6NWF1 UNIPROT Q6PHV4 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Insulin-regulated facilitative glucose transporter. {ECO:0000269|PubMed:25326603}. GO:0012505 GO:0016021 GO:0016020 GO:0048471 GO:0005886 GO:0005355 GO:0015293 GO:0072359 GO:0044381 GO:1904659 GO:0060047 GO:0007507 GO:0003179 GO:0055085 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDAPEESIRMTSDPQSKIYVQNPDTHIHLEQGPSAKSGNGRALVLCSVSVACLSGLLMGYEMSLISGALLQLRDVLTLSCPEQEQVVGSLLLGAFLLSLGGGTILDHYGRRFTIILTALLCVLGTLLSVCVVSFWALVVGRMLVGMSVALSGTASCLYAAEVAPAAWRGRCVCVYELMVVLGMLLGFGLSWAFAGVPDGWRFTFGGALLPALLQAGVMPLLPDSPRFLLAQQREKEAHATLLRLRAGIKEVEPVEDELRAIRLAMGAERLHGFLDLFQSRDNMLQRLLVGAALVFLQQATGQPNILAYASTVLSSVGFHGNEAATLASTGFGVVKVGGTIPAIFLVDKVGPKALLCVGVVVMMLSTATLGAITMQSRTHVSSLCRGPGNTANFTLFETGDETDIQTNTPLGLYQPQNKLKTNTFLTSINDTREHWILNHTYNHRTALMETAELSKKDSAKIALQSLHEVSPSLKWISLVSLLVYVAGFSISLGPMVHVVLSAIFPTGIRGKAVSVISAFNWATNLLISMTFLTLTERIGLPTVIFSYSAMSFLLVVFVIVFVPETKGRSLEQISKELAMKNHLRGTLLCHRRKHKATAQPSQEEKALATV 610 Q8TD20 Solute SLC2A12 9606 None SL-0198 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}. UNIPROT Q8TD20 UNIPROT B3KV17 UNIPROT Q7Z6U3 UNIPROT Q96MR8 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 OMIM 610372 DisGeNET 154091 Insulin-independent facilitative glucose transporter. {ECO:0000250|UniProtKB:Q8BFW9}. Q15125 EBI-21562097 0.35 Q8IZQ1 EBI-21562097 0.35 Q9UPQ8 EBI-21562097 0.35 Q9H1U9 EBI-21562097 0.35 Q6DD88 EBI-21562097 0.35 P35453 EBI-21562097 0.35 Q9Y5Y5 EBI-21562097 0.35 Q9Y276 EBI-21562097 0.35 Q9UQ90 EBI-21562097 0.35 Q9UQ16 EBI-21562097 0.35 Q9NWH2 EBI-21562097 0.35 Q9NUT2 EBI-21562097 0.35 Q9NRX5 EBI-21562097 0.35 Q9NPF2 EBI-21562097 0.35 Q9H649 EBI-21562097 0.35 Q9H3K2 EBI-21562097 0.35 Q9BVK2 EBI-21562097 0.35 Q9BV35 EBI-21562097 0.35 Q9BRN9 EBI-21562097 0.35 Q96J84 EBI-21562097 0.35 Q96DA6 EBI-21562097 0.35 Q96D53 EBI-21562097 0.35 Q96A46 EBI-21562097 0.35 Q8WUK0 EBI-21562097 0.35 Q8WU79 EBI-21562097 0.35 Q8TD22 EBI-21562097 0.35 Q8TCT6 EBI-21562097 0.35 Q8NHH9 EBI-21562097 0.35 Q8N6M3 EBI-21562097 0.35 Q8N138 EBI-21562097 0.35 Q7Z7B1 EBI-21562097 0.35 Q6Y1H2 EBI-21562097 0.35 Q6P996 EBI-21562097 0.35 Q6P444 EBI-21562097 0.35 Q6NUK1 EBI-21562097 0.35 Q6JQN1 EBI-21562097 0.35 Q5VST6 EBI-21562097 0.35 Q53FV1 EBI-21562097 0.35 Q14156 EBI-21562097 0.35 Q13505 EBI-21562097 0.35 Q13395 EBI-21562097 0.35 Q0P651 EBI-21562097 0.35 P62341 EBI-21562097 0.35 P36915 EBI-21562097 0.35 P33981 EBI-21562097 0.35 P32189 EBI-21562097 0.35 P30536 EBI-21562097 0.35 P24468 EBI-21562097 0.35 P17152 EBI-21562097 0.35 P13498 EBI-21562097 0.35 O95671 EBI-21562097 0.35 O60779 EBI-21562097 0.35 O15258 EBI-21562097 0.35 Q96BW9 EBI-21562097 0.35 A6NJ78 EBI-21562097 0.35 GO:0012505 GO:0016021 GO:0016020 GO:0048471 GO:0005886 GO:0055056 GO:0005355 GO:0015293 GO:0072359 GO:1904659 GO:0008645 GO:0055085 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVPVENTEGPSLLNQKGTAVETEGSGSRHPPWARGCGMFTFLSSVTAAVSGLLVGYELGIISGALLQIKTLLALSCHEQEMVVSSLVIGALLASLTGGVLIDRYGRRTAIILSSCLLGLGSLVLILSLSYTVLIVGRIAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVIGILSAYISNYAFANVFHGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEGAASKVLGRLRALSDTTEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAASLASTGVGVVKVISTIPATLLVDHVGSKTFLCIGSSVMAASLVTMGIVNLNIHMNFTHICRSHNSINQSLDESVIYGPGNLSTNNNTLRDHFKGISSHSRSSLMPLRNDVDKRGETTSASLLNAGLSHTEYQIVTDPGDVPAFLKWLSLASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTDLIGLPWVCFIYTIMSLASLLFVVMFIPETKGCSLEQISMELAKVNYVKNNICFMSHHQEELVPKQPQKRKPQEQLLECNKLCGRGQSRQLSPET 617 Q9BE72 Solute SLC2A12 9541 None SL-0198 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}. UNIPROT Q9BE72 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Insulin-independent facilitative glucose transporter. {ECO:0000250|UniProtKB:Q8BFW9}. GO:0012505 GO:0016021 GO:0048471 GO:0005886 GO:0022857 GO:0008643 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVPVENTEGPNLLNQKGTAVETEGSYRASGSRHPPWARGCGMFTFLSSVTAAVSGLLVGYELGIISGALLQIKTLLTLSCHEQEMVVSSLLIGALLASLTGGVLIDRYGRRTAIILSSCLLGLGSLVLILSLSYTVLIVGRIAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVIGILSAYISNYAFANVFHGWKYMFGLVIPLGILQAIAMYFLPPSPRFLVMKGQEGAASKVLGRLRALSDATEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAASLASTGVGVVKVISTIPATLLVDHVGSKTFLCIGSSVMAASLVTMGIVNLNIHMNFTNICRSHNSINQSLDESVIYGPGNLSASNNTLRDHFKGIASHSRSSLMPLRNDVDKRGETTSASLLNAVLSHTEYQIVTDPGDVPAFLKWLSLASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTDLIGLPWVCFIYTIMSLASLLFVVMFIPETKGCSLEQISMELAKVNYVKNNICFMSHHQEELVPRQPQKRKPQEQLLECNKLCGRGQSRQLSPEN 621 Q8BFW9 Solute Slc2a12 10090 None SL-0198 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}. UNIPROT Q8BFW9 UNIPROT Q14B60 UNIPROT Q3UPR6 UNIPROT Q8BZB7 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Insulin-independent facilitative glucose transporter. {ECO:0000269|PubMed:23041416}. GO:0012505 GO:0016021 GO:0016020 GO:0048471 GO:0005886 GO:0005355 GO:0015293 GO:0072359 GO:1904659 GO:0055085 Transmembrane UniProt Sequence Analysis {ECO:0000255} MVPVENTEGPNLLNQKGREAETEGSCGASGGGHPACAGGPSMFTFLTSVTAAISGLLVGYELGLISGALLQIRTLLALTCHEQEMVVSSLLIGAFLASLTGGVLIDRYGRRLAIILSSCLLGLGSLVLIMSLSYTLLIMGRVAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVTGILFAYISNYAFANISNGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEESAGKVLRKLRVISDTTEELTLIKSSLKDEYQYSFWDLFRSKDNMRTRILIGLTLVFFVQTTGQPNILFYASTVLKSVGFQSNEAASLASTGVGVVKVVSTIPATLLVDHIGSKTFLCIGSSVMSASLLTMGIVNLNINMNFTNICRSHSLLNQSLEEFVFYATGNLSISNSSLREHFKRITPYSKGSFMPMGNGMEPKGEMTFTSSLPNAGLSRTEHQGVTDTAVVPAAYKWLSLASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGVNLLISLTFLTVTDLIGLSWVCFIYTIMSLASLAFVVLFIPETKGCSLEQISVELAKANYVKNNICFMSHHQEELVPTQLQKRKPQEQLPECNHLCGRGQSQRPSPDT 622 Q32NG5 Solute slc2a12 8355 None SL-0198 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}. UNIPROT Q32NG5 Pfam PF00083 PROSITE PS50850 PROSITE PS00216 Insulin-regulated facilitative glucose transporter. {ECO:0000250|UniProtKB:Q6NWF1}. GO:0012505 GO:0016021 GO:0048471 GO:0005886 GO:0022857 GO:0008643 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLAHSTAQDLILQQRSSDDHPQTNPRQTGCGAFIILSSVIAAISGLLVGYELGIISGALLQLQSLLELTCQQQEIVVSALLIGALVASLVGGCLIDLYGRRTTIIFTSILLVFANLLPVVVVSYGSLIAGRIFIGVSISLSAIATCVYIAELSPQDKRGMLVSLNELMIVAGILLAYICNYLFASVNNGWKYMFGLITPLAALQAVAMFFLPRSPRFLIMKGYDDAAGKVLQKLRATTDINEELTAIKSSIKAEYQYKFLDLFCSRDNMRARLLIGLTLSFFVQITGQPNILFYASTVLKSVGFQSTEAASLASTGIGVVKVVSTIPAIFLVDKIGSKTFLCIGSAVMAVSLVSVGLVSLQLDVNYNNICKVHTVQNHSLQDSFVYGPVALAKHNESLFEETGTWLESTKASYHSTSQNGTKLLHVSAPEDSSFGFTVKEPKVKSQSDEIPEYMKWLCLSSLLAFVAAFSIGLGPMAWLVQSEIFPAGIKGRAFAITSSMNWGMNLLISLTFLTLTEMIGLPWMLFGYALMSIASLVFVIMFVPNTKGRPLEEISKELANRSYMCNAVCHRRRSKKKLTPVALIQSPA 588 P39996 Glutathione GTT3 559292 None SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. UNIPROT P39996 UNIPROT D3DLN3 P15565 EBI-16294709 0.00 P00359 EBI-807469 0.35 P32324 EBI-807469 0.35 P00330 EBI-807469 0.35 P47088 EBI-856729 0.00 Q02159 EBI-860107 0.00 P48566 EBI-8443637 0.44 P39996 EBI-6331316 0.00 P40150 EBI-3798470 0.35 P02829 EBI-3811791 0.35 P48363 EBI-3817222 0.35 Q8N6L0 EBI-11530258 0.56 Q8N6G5 EBI-11530249 0.56 P52290 EBI-16254416 0.00 P40582 EBI-16298792 0.00 P32621 EBI-16298972 0.00 GO:0016021 GO:0016020 GO:0031965 GO:0034399 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPTKSTFSRWKKADLIDLANKLEIDGFPNYAKKSDMIDYLESHLNHLEKPVDFKDDYPELRSFYESMTVDQSKDERNEYGSGSGNGSGSGSCDTATNDSDLEKAYIKEDDDEKPQSGDETSATKPLSSRNANSNAKTNFNLLDFSTDNDSSTSAFTKFKFNFQEYLSDIRYQTQKLNENVQDYLSTISAVDTIFSLLEFSFLVRNILAAGQPTSSSSLASSLEAAVAAHNKYQYTLDFCLPILTWLLFFRGIPTLVSYYINFIRYDLNIELDPMTFNLTKFLISLAIFKTCNNKNIDFHSFRCVNQLWTQLCTVNRSLGMVPLVFSMVSCLLTLYVL 337 Q7Z2G1 Histone H2BW1 9606 None SL-0178 SL-0182 Nucleus membrane {ECO:0000269|PubMed:15475252}. Chromosome {ECO:0000269|PubMed:15475252}. UNIPROT Q7Z2G1 UNIPROT B1AK72 UNIPROT Q147W3 Pfam PF00125 OMIM 300507 DisGeNET 158983 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}. Q6NXS1 EBI-24677095 0.56 GO:0031965 GO:0005654 GO:0000786 GO:0003677 GO:0046982 GO:0030527 GO:0006334 Unknown UniProt Sequence Analysis MLRTEVPRLPRSTTAIVWSCHLMATASAMAGPSSETTSEEQLITQEPKEANSTTSQKQSKQRKRGRHGPRRCHSNCRGDSFATYFRRVLKQVHQGLSLSREAVSVMDSLVHDILDRIATEAGRLARSTKRQTITAWETRMAVRLLLPGQMGKLAESEGTKAVLRTSLYAIQQQRK 175 Q90474 Heat hsp90a 7955 None SL-0198 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. UNIPROT Q90474 UNIPROT Q5RG13 UNIPROT Q6DI33 Pfam PF02518 Pfam PF00183 PROSITE PS00298 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}. GO:0031672 GO:0005829 GO:0042470 GO:0043209 GO:0043025 GO:0005634 GO:0048471 GO:0005886 GO:0032991 GO:0030018 GO:0005524 GO:0016887 GO:0140662 GO:0097718 GO:0030235 GO:0051082 GO:0034605 GO:0050900 GO:0007517 GO:0030239 GO:0045429 GO:0006457 GO:0050821 GO:0010038 GO:0048769 GO:0030241 GO:0030240 GO:0014866 GO:0071688 Unknown UniProt Sequence Analysis MPEKSAQPVMEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSCKDLKIELIPDQKERTLTIIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYIWESAAGGSFTVKPDFGESIGRGTKVILHLKEDQSEYVEEKRIKEVVKKHSQFIGYPITLYIEKQREKEVDLEEGEKQEEEEVAAGEDKDKPKIEDLGADEDEDSKDGKNKRKKKVKEKYIDAQELNKTKPIWTRNPDDITNEEYGEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPRRAAFDLFENKKKRNNIKLYVRRVFIMDNCEELIPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLDLFTELAEDKDNYKKYYEQFSKNIKLGIHEDSQNRKKLSDLLRYYTSASGDEMVSLKDYVSRMKDTQKHIYYITGETKDQVANSAFVERLRKAGLEVIYMIEPIDEYCVQQLKEYDGKNLVSVTKEGLELPEDEEEKKKQDELKAKYENLCKIMKDILDKKIEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKSQALRDNSTMGYMTAKKHLEINPAHPIVETLREKAEADKNDKAVKDLVILLFETALLSSGFTLDDPQTHANRIYRMIKLGLGIDDDDSVVEEISQPAEEDMPVLEGDDDTSRMEEVD 725 M9PBE2 E3 Hakai 7227 None SL-0198 Nucleus {ECO:0000305}. Cell membrane {ECO:0000305|PubMed:19682089}. Cytoplasmic vesicle {ECO:0000305|PubMed:19682089}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:19682089}. UNIPROT M9PBE2 UNIPROT Q86NQ9 UNIPROT Q8INV9 UNIPROT Q8INW0 UNIPROT Q95RE3 UNIPROT Q9VIT1 Pfam PF18408 PROSITE PS00518 PROSITE PS50089 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}. Q9VU72 EBI-198772 0.00 A1Z9X0 EBI-200042 0.00 Q9VI24 EBI-200115 0.00 Q9VI16 EBI-200123 0.00 Q24558 EBI-200119 0.00 P25171 EBI-200127 0.00 Q7KTX7 EBI-200132 0.00 Q9W2M4 EBI-200136 0.00 Q9VU89 EBI-200140 0.00 Q9VU18 EBI-200144 0.00 Q9VI55 EBI-200148 0.00 Q8T0I9 EBI-200152 0.00 Q9V472 EBI-200156 0.00 Q4Z8K6 EBI-200160 0.00 Q9VGB9 EBI-200164 0.00 Q9V9R6 EBI-200172 0.00 Q9VN36 EBI-200176 0.00 Q9VRC3 EBI-200180 0.00 Q9XZU1 EBI-200184 0.00 Q9VSQ3 EBI-200188 0.00 Q9VC48 EBI-200192 0.00 Q9VMS5 EBI-200196 0.00 Q8MYW5 EBI-200200 0.00 Q9VGU7 EBI-200204 0.00 Q9W550 EBI-200208 0.00 Q9VZT6 EBI-200212 0.00 P54356 EBI-200216 0.00 Q9VJE3 EBI-200220 0.00 Q9VJ53 EBI-200224 0.00 Q9VXD4 EBI-200228 0.00 Q9VMD4 EBI-200232 0.00 Q9VFU6 EBI-200236 0.00 Q9VCM3 EBI-200240 0.00 Q8T3Y1 EBI-200244 0.00 B7YZT2 EBI-200248 0.00 Q9V9V8 EBI-200252 0.00 Q9VVV6 EBI-200256 0.00 Q9VF73 EBI-200260 0.00 P42282 EBI-200264 0.00 Q9W3J9 EBI-200268 0.00 Q9V9V0 EBI-200272 0.00 O46070 EBI-200276 0.00 Q9W5B6 EBI-200280 0.00 Q9VEA5 EBI-200284 0.00 M9MRI4 EBI-200288 0.00 Q9VKQ0 EBI-200292 0.00 Q9V4B8 EBI-200296 0.00 Q9VZM9 EBI-200300 0.00 Q9VSB2 EBI-200304 0.00 Q9VPE1 EBI-200308 0.00 Q9VQF9 EBI-200313 0.00 A1ZAC8 EBI-200317 0.00 Q9VDC1 EBI-200321 0.00 Q9W1R5 EBI-200325 0.00 Q9VSY2 EBI-200329 0.00 P11455 EBI-200333 0.00 Q9Y156 EBI-200337 0.00 Q9VAZ1 EBI-200345 0.00 Q8IQB8 EBI-200341 0.00 Q9VD25 EBI-200349 0.00 Q7K4Z4 EBI-200353 0.00 Q94981 EBI-200357 0.00 O76924 EBI-200361 0.00 O97365 EBI-200365 0.00 Q7JXC4 EBI-200369 0.00 P23696 EBI-200373 0.00 Q9V460 EBI-200377 0.00 A1Z8L7 EBI-200382 0.00 Q9VLP3 EBI-200386 0.00 Q9VHR4 EBI-200390 0.00 Q7K127 EBI-200394 0.00 Q9VHG0 EBI-200398 0.00 Q8T3X9 EBI-200402 0.00 Q9VHA9 EBI-200406 0.00 Q9V428 EBI-200410 0.00 Q9W379 EBI-200414 0.00 Q9W5X1 EBI-200418 0.00 Q9VXE7 EBI-200422 0.00 P22810 EBI-26730114 0.49 GO:0031410 GO:0005829 GO:0005634 GO:0048471 GO:0005886 GO:0036396 GO:0045296 GO:0061630 GO:0004842 GO:0008270 GO:0007015 GO:0040003 GO:0007391 GO:0007427 GO:0060429 GO:0030237 GO:0008258 GO:0007494 GO:0080009 GO:0016567 GO:0000381 GO:0030155 GO:0035282 Unknown UniProt Sequence Analysis MDTEEVKRGRGRGRGTRARGRGRGRGRGRGKKIDDSSIADAAALAASSCAALEDSPGRLDASEDSVMQELDKDGELETPGALEEPLPHGALGAVAASGNMTPATQQPQVLQQVPPPVMSQTTISLSLARAVDMEADISQLEAPTFTTLSRGPPEPMLRLKWNHKVSLIGEKVLNPMIHCCDQCDKPILVYGRMIPCKHVFCLKCARAEPIKSCPRCTDKVLRVEQSGLGTVFMCTHGGSRYGSSGCRRTYLSQRDLQAHINHRHVAPQPPPLQPQPQLSAMAEQPKMTDLGGVGLGLELHKQRKLSESSVPISVSASIASRPVLSRLPLTGGVGNIGSIGSIPPPGSAAAAQNAIHGGHSTLTLANLTRINNANAQECHQGKASLHHTLKKGTPHQSESVADASYYSSVLASFGSAAGNPGSGPPGGGATAAAQPANPSGSHSAVGPGALIGGSTDAPTGGSSGNWQQSQYYR 473 O80528 Serine/threonine-protein HASPIN 3702 None SL-0198 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}. UNIPROT O80528 UNIPROT Q84WE0 PROSITE PS50011 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}. GO:0005694 GO:0005737 GO:0005856 GO:0005634 GO:0048471 GO:0009524 GO:0005524 GO:0035402 GO:0072354 GO:0106310 GO:0035556 GO:0000278 GO:0006468 Unknown UniProt Sequence Analysis MGQRVDLWSEVIKSEEEDGDIPKIEAVFQRRKKPDKSSEAVNFGWLVKGARTSSVNGPKRDSWARSLSTRGRESIAVRAYVNNQPQKKAAGRKKPPIPKGKVVKAPDFQKEKEYFRDIDAFELLEESPSPNKSSTWTMGEQVVPEMPHLSTRLEKWLISKKLNHTCGPSSTLSKILENSAIHQESVCDNDAFDSLSLKTPDKSSAGNTSVFRLIPSCDENLAAEDVPVRKIKMESIDLEDELKRLSLTSDLIPTHQDFDQPILDLLSACGQMRPSNFIEAFSKFCEPESIVKIGEGTYGEAFRAGSSVCKIVPIDGDFRVNGEVQKRADELLEEVILSWTLNQLRECETTAQNLCPTYIKTQDIKLCQGPYDPILIKAWEEWDAKHGSENDHPDFPEKQCYVMFVLEHGGKDLESFVLLNFDEARSLLVQATAGLAVAEAAFEFEHRDLHWGNILLSRNNSDTLPFILEGKQVCIKTFGVQISIIDFTLSRINTGEKILFLDLTSDPYLFKGPKGDKQSETYRKMKAVTEDYWEGSFARTNVLWLIYLVDILLTKKSFERSSKHERELRSLKKRMEKYESAKEAVSDPFFSDMLMDQIS 599 P83103 Serine/threonine-protein Haspin 7227 None SL-0178 SL-0180 Nucleus lamina {ECO:0000269|PubMed:32750047}. Chromosome {ECO:0000269|PubMed:32750047}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8TF76}. UNIPROT P83103 UNIPROT Q7PLN2 PROSITE PS00107 PROSITE PS50011 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}. GO:0000785 GO:0005737 GO:0005652 GO:0005634 GO:0005819 GO:0005524 GO:0072354 GO:0106310 GO:0035556 GO:0000278 GO:2000720 GO:0034093 GO:0120187 GO:0043687 GO:0006468 Unknown UniProt Sequence Analysis MLSISKTKMDFLEEGRWKDPFDELLDSRTKLSKMNIVKQNVRVTYNIDSSVENSSYIEIKEPNHKNEPLTLEDCSIKVYCPSDSISTPCDKRLGGTTGLFETDLSPITRLKLEGVEDSRDKCADTNEADLYVNVEILFQNINSSPKKCSNFGKKRLSNLNKMVTAVHPSISLNPGKWRKSLNNFIRSKITETNFTKKVERRSSICQDRKSLVLKGEHKFENKYEEDVLKYCHQCTPLPFNTAYEQHKLLNTKKIGEGAYGEVFRCSRNQEVLKDHISDIVLKIIPLEGSTVINGEKQKTFSQILPEIIITKKMCSLRTSKTNSTNGFVSIQKVSLVKGRYPPHFIKLWEKYDNEKGSENDHPELFGDNQLFAVLELKFAGSDMANFKFLNSEQSYYALQQIILALAVGEEEYQFEHRDLHLGNILIEYTNKKHIVCTFKSSNLTLLSKGVNVTIIDYTLSRVTINDCCYFNDLSRDEELFQATGDYQYDVYRMMRNELKNNWSSFSPKTNIIWLSYVIVKVLDSVKYKSINTKVHRMYIDKIKELKNIIMTFESASHCANYLFNLN 566 Q2KIE2 HCLS1-associated HAX1 9913 None SL-0178 SL-0182 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}. UNIPROT Q2KIE2 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}. GO:0005938 GO:0031410 GO:0005739 GO:0031965 GO:0000932 GO:0005886 GO:0016529 GO:0043066 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:O00165} MSLFDLFRGFFGFSGPRSHRDPFFGGMTRDEDEDDEEEEEEGVTWGRGNSRFEGPQSPEEFSFGFSFSPGGGMRFHDNFGFDDLVRDFNNIFSEMGAWTLPSRPPELPGPESETPGERRQEGQTLRDSMLKYPDSHQPKIFGGGLESDARSESSKPAPDWGPQRPFHRFDDTWPVTPHSRAREDNDLDTQVSQEGLGPVLQPQPKSYFKSVSVTKITKPDGTVEERRTVVDSEGRKETTVTHQEAGSSPRDGPESPTPPSLDDSSSILDLFLGRWFRSR 279 O00165 HCLS1-associated HAX1 9606 None SL-0178 SL-0182 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}. UNIPROT O00165 UNIPROT A8W4W9 UNIPROT A8W4X0 UNIPROT B4DUJ7 UNIPROT Q5VYD5 UNIPROT Q5VYD7 UNIPROT Q96AU4 UNIPROT Q9BS80 OMIM 605998 OMIM 610738 DisGeNET 10456 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}. 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}. A0A142I5B9 EBI-20626314 0.35 Q99759 EBI-362136 0.00 Q04206 EBI-363244 0.00 P19438 EBI-364357 0.00 P20333 EBI-364585 0.00 Q16760 EBI-734287 0.00 O12160 EBI-7845312 0.64 O00303 EBI-758371 0.37 O70127 EBI-930216 0.40 Q6PSM0 EBI-930234 0.40 Q15714 EBI-1085974 0.00 P13569 EBI-1171360 0.35 Q8AZK7 EBI-9632715 0.53 O46385 EBI-7874199 0.27 Q5NE99 EBI-2806387 0.00 Q5NFJ2 EBI-2806394 0.00 A0A0F7R9R7 EBI-2811156 0.00 Q81VT8 EBI-2811888 0.00 A0A6L7HRI8 EBI-2813096 0.00 Q81M67 EBI-2816763 0.00 A0A2P0H993 EBI-2816781 0.00 A0A6H3ACS9 EBI-2832676 0.00 Q81SR4 EBI-2832662 0.00 A0A4Y1WB04 EBI-2832641 0.00 A0A6L8PU14 EBI-2832669 0.00 Q81KV7 EBI-2832655 0.00 Q81WU4 EBI-2832648 0.00 A0A6L7HHZ0 EBI-2832709 0.00 A0A6L7H2Q9 EBI-2832690 0.00 A0A6L7H5N1 EBI-2832683 0.00 A0A6L7HH25 EBI-2832697 0.00 A0A0J1KLZ7 EBI-2832716 0.00 A0A6H3AND8 EBI-2832723 0.00 A0A380PD11 EBI-2840043 0.00 A0A3N4AYP8 EBI-2843166 0.00 A0A3G5LD16 EBI-2843155 0.00 A0A380PL54 EBI-2847491 0.00 A0A380PNP6 EBI-2847479 0.00 Q8CLE0 EBI-2868346 0.00 Q8CZR2 EBI-2868335 0.00 Q8D014 EBI-2868325 0.00 A0A5P8YFI0 EBI-2868386 0.00 A0A380PFG3 EBI-2868379 0.00 Q8CKN6 EBI-2868353 0.00 A0A5P8YJT1 EBI-2868365 0.00 A0A5P8YBY1 EBI-2868372 0.00 Q7CG77 EBI-2868393 0.00 Q8ZBU3 EBI-2868430 0.00 Q7ARD3 EBI-2868400 0.00 Q8ZHF4 EBI-2868407 0.00 Q8ZCH3 EBI-2868418 0.00 P69961 EBI-2868442 0.00 Q8ZIY3 EBI-2868449 0.00 Q8ZDX4 EBI-2868456 0.00 P03372 EBI-3895734 0.53 P48454 EBI-3935613 0.37 P51692 EBI-3935643 0.37 P53779 EBI-3935623 0.55 P27694 EBI-3935633 0.37 P62877 EBI-3935653 0.37 Q9P1U0 EBI-3941813 0.37 P0DPB6 EBI-3941823 0.37 Q8TAQ5 EBI-3943650 0.37 Q14451 EBI-4288461 0.51 P0DOE9 EBI-6138583 0.35 Q8JPQ9 EBI-6159460 0.35 Q77M19 EBI-6268389 0.35 Q86Z02 EBI-6381086 0.35 O14980 EBI-8162190 0.40 Q9NPI6 EBI-8162243 0.27 Q13619 EBI-21324822 0.35 Q13618 EBI-21329068 0.35 Q8NHX9 EBI-8817387 0.59 Q9ULQ1 EBI-8817427 0.53 Q8TE30 EBI-8874742 0.35 P42858 EBI-9054212 0.67 P58340 EBI-9358437 0.40 Q8K2C9 EBI-9358459 0.40 Q13200 EBI-9358502 0.40 Q15773 EBI-9358480 0.40 Q16659 EBI-12502733 0.35 P57078 EBI-12503575 0.35 Q13563 EBI-9837080 0.37 P30411 EBI-9843662 0.37 P01583 EBI-10488769 0.62 Q13418 EBI-10103376 0.53 P06460 EBI-11723082 0.35 P69901 EBI-11733364 0.35 P36895 EBI-11008521 0.35 Q9NVH1 EBI-11107761 0.35 O43542 EBI-11129266 0.35 O00400 EBI-11135399 0.35 Q9BQE3 EBI-11139064 0.35 O94905 EBI-11425731 0.35 Q6P5F9 EBI-11603310 0.35 Q9BW83 EBI-12453281 0.35 Q71U36 EBI-11897791 0.53 Q68871 EBI-12518818 0.51 P03452 EBI-12577240 0.35 P06821 EBI-12577493 0.35 P03431 EBI-12579142 0.35 P03428 EBI-12579909 0.35 I6T1Z2 EBI-12581764 0.35 Q5EP37 EBI-12582596 0.35 Q1K9H5 EBI-12588098 0.35 B4URF7 EBI-12588729 0.35 Q7RTP6 EBI-13945615 0.35 O14829 EBI-14024386 0.35 Q9BY84 EBI-14027455 0.35 P13591 EBI-21602719 0.35 P10636 EBI-21602719 0.35 Q9UQM7 EBI-21602719 0.35 Q9UPY8 EBI-21602719 0.35 Q9ULP0 EBI-21602719 0.35 Q9P121 EBI-21602719 0.35 Q9NRW1 EBI-21602719 0.35 Q9H4G0 EBI-21602719 0.35 Q9H115 EBI-21602719 0.35 Q9BPU6 EBI-21602719 0.35 Q99880 EBI-21602719 0.35 Q92777 EBI-21602719 0.35 Q8NCB2 EBI-21602719 0.35 Q8IZL9 EBI-21602719 0.35 Q16623 EBI-21602719 0.35 Q16555 EBI-21602719 0.35 Q14847 EBI-21602719 0.35 Q14194 EBI-21602719 0.35 Q13554 EBI-21602719 0.35 Q12860 EBI-21602719 0.35 Q05193 EBI-21602719 0.35 Q01484 EBI-21602719 0.35 P84074 EBI-21602719 0.35 P62760 EBI-21602719 0.35 P61764 EBI-21602719 0.35 P61601 EBI-21602719 0.35 P61266 EBI-21602719 0.35 P59768 EBI-21602719 0.35 P43304 EBI-21602719 0.35 P42658 EBI-21602719 0.35 P42262 EBI-21602719 0.35 P37235 EBI-21602719 0.35 P32004 EBI-21602719 0.35 P31323 EBI-21602719 0.35 P22676 EBI-21602719 0.35 P21579 EBI-21602719 0.35 P20648 EBI-21602719 0.35 P20336 EBI-21602719 0.35 P17600 EBI-21602719 0.35 P16401 EBI-21602719 0.35 P11137 EBI-21602719 0.35 P09471 EBI-21602719 0.35 P05090 EBI-21602719 0.35 O60641 EBI-21602719 0.35 O43854 EBI-21602719 0.35 O43602 EBI-21602719 0.35 O15075 EBI-21602719 0.35 O00429 EBI-21602719 0.35 B7Z613 EBI-21602719 0.35 Q14195 EBI-21602719 0.35 P51674 EBI-21648883 0.35 O15126 EBI-21648858 0.35 Q9H4B6 EBI-16427846 0.74 Q96RS6 EBI-20723859 0.35 Q6ZNJ1 EBI-16749633 0.35 O95831 EBI-16786283 0.42 Q96I36 EBI-16791250 0.27 P13073 EBI-16791533 0.27 Q9HBL7 EBI-16797429 0.27 O75880 EBI-16799233 0.27 Q9H9B4 EBI-16799442 0.27 P11279 EBI-16795231 0.35 P08559 EBI-20306509 0.35 P46013 EBI-20562326 0.35 Q9BRX2 EBI-20567704 0.66 Q92844 EBI-20737201 0.35 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 Q15077 EBI-21262943 0.35 F5H1C8 EBI-21264930 0.35 X6RFA8 EBI-21265624 0.35 Q9H1C4 EBI-21266770 0.35 P03427 EBI-21268420 0.35 Q6ZRI8 EBI-25410669 0.35 P0DOF2 EBI-25603126 0.35 O95072 EBI-25483697 0.35 P59046 EBI-25499386 0.37 P0DTC5 EBI-25685699 0.35 Q8N4Q1 EBI-25744959 0.35 O43572 EBI-26451580 0.35 P61981 EBI-25902182 0.56 Q15047 EBI-25909133 0.56 Q92993 EBI-25912324 0.56 Q8TAP4 EBI-25926058 0.56 O43464 EBI-27049380 0.42 Q96LU5 EBI-27049466 0.27 P83111 EBI-27049642 0.27 Q96E52 EBI-27049801 0.27 Q9H300 EBI-27049982 0.27 Q96TA2 EBI-27050177 0.27 O14733 EBI-28930089 0.35 O14757 EBI-28930743 0.35 P04049 EBI-28931531 0.35 P22612 EBI-28934688 0.35 P43250 EBI-28935197 0.35 P51617 EBI-28935882 0.35 P53671 EBI-28938453 0.35 Q6P5Z2 EBI-28941754 0.35 Q7Z695 EBI-28941998 0.35 Q92918 EBI-28944233 0.35 Q9BXA6 EBI-28945972 0.35 Q9H3Y6 EBI-28946258 0.35 Q9NR20 EBI-28946409 0.35 Q9NRM7 EBI-28946455 0.35 Q9NSY0 EBI-28946547 0.35 O95476 EBI-27113178 0.35 O14595 EBI-27113200 0.35 O14830 EBI-27113806 0.35 P04626 EBI-32718334 0.35 P35916 EBI-32718614 0.42 P08069 EBI-32718669 0.35 P06213 EBI-32718777 0.35 P04629 EBI-32719115 0.35 Q16288 EBI-32719212 0.35 Q06418 EBI-32719716 0.35 GO:0015629 GO:0016324 GO:0005938 GO:0030136 GO:0005783 GO:0030027 GO:0005758 GO:0005741 GO:0005739 GO:0005635 GO:0031965 GO:0000932 GO:0016529 GO:0005667 GO:0019966 GO:0047485 GO:0071345 GO:0043066 GO:2000251 GO:0030854 GO:0033138 GO:0050731 GO:0014068 GO:0051897 GO:0045944 GO:0030833 GO:0042981 GO:1903146 GO:1903214 Peripheral UniProt Experimental Evidence {ECO:0000269|PubMed:26997484} MSLFDLFRGFFGFPGPRSHRDPFFGGMTRDEDDDEEEEEEGGSWGRGNPRFHSPQHPPEEFGFGFSFSPGGGIRFHDNFGFDDLVRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDWGSQRPFHRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSYFKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSSPRGDPESPRPPALDDAFSILDLFLGRWFRSR 279 O35387 HCLS1-associated Hax1 10090 None SL-0178 SL-0182 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}. UNIPROT O35387 UNIPROT Q542F8 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}. P42227 EBI-657283 0.37 Q8BWG8 EBI-649719 0.37 Q8CIH5 EBI-649769 0.37 Q13563 EBI-9635489 0.51 O14925 EBI-11010276 0.35 Q9H477 EBI-11010276 0.35 H3BS42 EBI-11010276 0.35 P56199 EBI-11010276 0.35 P10809 EBI-11010276 0.35 P37198 EBI-11010276 0.35 Q92604 EBI-11010276 0.35 P12236 EBI-11010276 0.35 Q9H061 EBI-11010276 0.35 Q7KZ85 EBI-11010276 0.35 O15066 EBI-11010276 0.35 Q9H078 EBI-11010276 0.35 O75165 EBI-11010276 0.35 G3XAN4 EBI-11010276 0.35 B4E1G1 EBI-11010276 0.35 Q5XJY4 EBI-15687233 0.52 Q9JIY5 EBI-15687275 0.52 Q9NRI5 EBI-26612017 0.35 GO:0015629 GO:0016324 GO:0005938 GO:0030136 GO:0005737 GO:0005783 GO:0043231 GO:0030027 GO:0005758 GO:0005741 GO:0005739 GO:0031965 GO:0000932 GO:0016529 GO:0005667 GO:0019966 GO:0019904 GO:0047485 GO:0007166 GO:0071345 GO:0043066 GO:2000251 GO:0030854 GO:0033138 GO:0050731 GO:0014068 GO:0051897 GO:0045944 GO:0030833 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:O00165} MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDDDDDDEAEEDRGAWGRESYAFDGSQPPEEFGFSFSPRGGMRFHGNFGFDDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESPKPAPDWGSQGPFHRLDDTWPVSPHSRAKEDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEERRTVVDSEGRRETTVTHQEAHDSSRSDPDSQRSSALDDPFSILDLLLGRWFRSR 280 Q7TSE9 HCLS1-associated Hax1 10116 None SL-0178 SL-0182 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}. UNIPROT Q7TSE9 UNIPROT Q5D1N3 UNIPROT Q5D1N4 UNIPROT Q7TSE7 UNIPROT Q7TSE8 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}. Q08201 EBI-930001 0.51 O70127 EBI-930049 0.60 Q6PSM0 EBI-930069 0.51 O70420 EBI-930391 0.40 GO:0015629 GO:0016324 GO:0005938 GO:0030136 GO:0005737 GO:0005783 GO:0043231 GO:0030027 GO:0005758 GO:0005741 GO:0005739 GO:0031965 GO:0000932 GO:0016529 GO:0005667 GO:0019966 GO:0019904 GO:0047485 GO:0071345 GO:0043066 GO:2000251 GO:0030854 GO:0033138 GO:0050731 GO:0014068 GO:0051897 GO:0045944 GO:0030833 Peripheral UniProt By Similarity {ECO:0000250|UniProtKB:O00165} MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDEDDEEEEDSGAWGRESYAFDGFHPTEEFGFSFSPRGGMRFHGNFGFDDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGVRLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESSKPAPDWGSQGPFHRLDDTWPVSPHSRAREDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEEHRTVVDSEGRRETTVTHQEAHDSSRSDPDPPRSSALDDPFSILDLLLGRWFRSR 278 Q5T447 E3 HECTD3 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5T447 UNIPROT B3KPV7 UNIPROT B3KRH4 UNIPROT Q5T448 UNIPROT Q9H783 Pfam PF03256 Pfam PF00632 PROSITE PS51284 PROSITE PS50237 OMIM 618638 DisGeNET 79654 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}. P0DTD1 EBI-27126088 0.35 Q15796 EBI-2691165 0.00 Q7Z434 EBI-6115727 0.35 P08238 EBI-6425955 0.40 Q8IUH5 EBI-9088791 0.37 O60437 EBI-24537202 0.56 D2XQB9 EBI-14063588 0.35 Q8N5F7 EBI-21520423 0.35 P82930 EBI-21521832 0.35 P13994 EBI-21552344 0.35 Q8N0V3 EBI-21561897 0.35 Q8IUX8 EBI-21565522 0.35 Q6UWQ5 EBI-21641185 0.35 Q7Z4W2 EBI-21670934 0.35 O75596 EBI-21674079 0.35 Q6IN84 EBI-21721548 0.35 Q96NG3 EBI-21726764 0.35 P05154 EBI-21730352 0.35 Q8N4T0 EBI-21731449 0.35 A8MT70 EBI-21738250 0.35 O15123 EBI-21738454 0.35 P01350 EBI-21738479 0.35 P15408 EBI-21738528 0.35 E7EPC3 EBI-21738429 0.35 Q2MKA7 EBI-21738795 0.35 Q9BU40 EBI-21739567 0.35 Q6NZI2 EBI-21738912 0.35 Q7L0Y3 EBI-21739027 0.35 Q8NBL1 EBI-21739323 0.35 Q8NBX0 EBI-21739378 0.35 Q96EL2 EBI-21739451 0.35 Q9BYG5 EBI-21739610 0.35 Q9H9Q2 EBI-21739689 0.35 Q9H1F0 EBI-21739868 0.35 Q99501 EBI-21832664 0.35 P62701 EBI-21876649 0.40 Q96PQ6 EBI-21890582 0.35 P11166 EBI-20903936 0.40 O84388 EBI-22302856 0.35 P0DOF2 EBI-25603126 0.35 P22607 EBI-25854798 0.56 Q14957 EBI-25862911 0.56 P06396 EBI-25864492 0.56 Q9Y649 EBI-25901376 0.56 Q9UMX0 EBI-25921251 0.56 Q6ZNK6 EBI-26453464 0.35 P34972 EBI-26880846 0.35 GO:0048471 GO:0019905 GO:0004842 GO:0043161 Unknown UniProt Sequence Analysis MAGPGPGAVLESPRQLLGRVRFLAEAARSLRAGRPLPAALAFVPREVLYKLYKDPAGPSRVLLPVWEAEGLGLRVGAAGPAPGTGSGPLRAARDSIELRRGACVRTTGEELCNGHGLWVKLTKEQLAEHLGDCGLQEGWLLVCRPAEGGARLVPIDTPNHLQRQQQLFGVDYRPVLRWEQVVDLTYSHRLGSRPQPAEAYAEAVQRLLYVPPTWTYECDEDLIHFLYDHLGKEDENLGSVKQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEGDNLKKLSDVSIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPTSLVRYPRLEGTDPEVLYRRAVLLQRFIKILDSVLHHLVPAWDHTLGTFSEIKQVKQFLLLSRQRPGLVAQCLRDSESSKPSFMPRLYINRRLAMEHRACPSRDPACKNAVFTQVYEGLKPSDKYEKPLDYRWPMRYDQWWECKFIAEGIIDQGGGFRDSLADMSEELCPSSADTPVPLPFFVRTANQGNGTGEARDMYVPNPSCRDFAKYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSKDFPAVDSVLVKLLEVMEGMDKETFEFKFGKELTFTTVLSDQQVVELIPGGAGIVVGYGDRSRFIQLVQKARLEESKEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLTRFEDFEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPARIYIYPDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYAAYNCVAIDTDMSPWEE 861 Q3U487 E3 Hectd3 10090 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:18821010}. UNIPROT Q3U487 UNIPROT B1AUL1 UNIPROT Q3TN76 UNIPROT Q641P3 UNIPROT Q8BQ74 UNIPROT Q8R1L6 Pfam PF03256 Pfam PF00632 PROSITE PS51284 PROSITE PS50237 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}. GO:0048471 GO:0019905 GO:0004842 GO:0043161 Unknown UniProt Sequence Analysis MAGPGPGAALESPRQLLGRVRFLAEAARSLRAGLPLPAALAFVPREVLYKLYKDPAGPSRVLLPVWEAEGLGLRVGAVGAAPGTGSGPLRAARDSIELRRGACVRTTGEELCNGHGLWVKLTKEQLAEHLSDCSLDEGWLLVCRPAEGGARLVPIDTPDHLQRQQQLFGVDYRPVLRWEQVVDLTYSHRLGSRPQPAEAYTEAIQRLLYVPPTWTYECDEDLIHFLYDHLGKEDENLGSVKQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEGDNLKKLSDVNIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPASLVRYPRLEGTDPEVLYRRAVLLQRFIKILDSVLHHLVPAWDHTLGTFSEIKQVKQFLLLSRQRPSLVAQCLRDSESSKPSFMPRLYINRRLAMEHRACPSRDPACKNAVFTQVYEGLKPSDKYEKPLDYRWPMRYDQWWECKFIAEGIIDQGGGFRDSLADMSEELCPSSADTPVPLPFFVRTANQGNGTGEARDMYVPNPSCRDFAKYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSKDFPAVDSVLVKLLEVMEGVDKETFEFKFGKELTFTTVLSDQQVVELIPGGTGIVVEYEDRSRFIQLVRKARLEESKEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLTRFEDFEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPARIYIYPDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYAAYNCVAIDTDMSPWEE 861 Q03281 Inner HEH2 559292 None SL-0178 SL-0179 SL-0182 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. UNIPROT Q03281 UNIPROT D6VT82 PDB 4PVZ Pfam PF12949 Pfam PF09402 P38181 EBI-10052697 0.44 P39929 EBI-10052667 0.58 Q02821 EBI-15598611 0.76 P32462 EBI-789522 0.35 P47088 EBI-856789 0.00 P11484 EBI-3689025 0.35 P32589 EBI-3805388 0.35 P02829 EBI-3811847 0.35 P52917 EBI-10053328 0.40 GO:0016021 GO:0005635 GO:0005637 GO:0034399 GO:0003682 Transmembrane UniProt Sequence Analysis {ECO:0000255} MDHRNLDPKTLKVSQLRRVLVENDVAFPANARKPVLVKLFEEKVRQRLQSSPEASKVRTSIQKVVKSGAKNADRKKTLKSKKLESSSSESKTVKDENVETNKRKREQISTDNEAKMQIQEEKSPKKKRKKRSSKANKPPESPPQSKSDGKATSADLTSELETVEELHKKDSSDDKPRVKELPKPELPNLKVSNEFLAQLNKELASAATENYDHSIKSTDLSSIRIETEEPVGPSTGAETRNESEVMENINLEVQPEVKEAKEELTKISETFDNQDEEDTSRLSSKKNIRSPKGRTRHFIANKTKRGIDIMKPFIAHLFIWLWNGAIFLSIICPILFGLWYREQRIQVGYCGHEKPLKSLAISAFPQTERVDSVLQAYRPNCLECPEHGICSSFMNVECEPGYEPKSSILETYGIIPFPKYCAKDESKEKEVDELVWKVNEYLKKKNAQHECGEGENLFESGETETKLYDIFSHSRPSWESQREFNDHWKNVLEILKKKDDIIWLPLDFETNGKREKSKSNNTNYIYRSTSKKWVTLQCHLEGDIQEYITKYGGSLFITLGVLFLIKKIQSTLDNYVQGEQIIEKLVKEAIDKLKDVKKNKGEEPFLTTVQLRATLLSDIPNIKEQNNLWAQTKEKIMKEQSENIELYLLEENGEIMTCWEWKE 663 Q9UII4 E3 HERC5 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:20542004}. Note=Associated with the polyribosomes, probably via the 60S subunit. UNIPROT Q9UII4 UNIPROT B2RTQ1 UNIPROT Q69G20 Pfam PF00632 Pfam PF00415 PROSITE PS50237 PROSITE PS00626 PROSITE PS50012 OMIM 608242 DisGeNET 51191 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}. P59595 EBI-27129966 0.35 Q8K4B0 EBI-11126052 0.35 Q9UKV8 EBI-7642941 0.35 P51965 EBI-2339545 0.37 Q96LR5 EBI-2339579 0.37 Q969T4 EBI-2339769 0.37 Q8WVJ2 EBI-9484933 0.40 Q12952 EBI-11321256 0.35 Q08050 EBI-11321374 0.35 P05412 EBI-11324725 0.35 Q9JJR9 EBI-11017700 0.35 P33981 EBI-11027245 0.35 P27635 EBI-11035646 0.35 F8VQC1 EBI-11054725 0.35 Q99PL5 EBI-11066888 0.35 Q00839 EBI-11088773 0.35 P37840 EBI-11113842 0.35 Q8TF76 EBI-11146909 0.35 Q76RH4 EBI-14063348 0.35 Q9GZY0 EBI-21528397 0.35 O43159 EBI-21627620 0.35 Q9P031 EBI-21664473 0.35 P15880 EBI-21677299 0.35 Q9BSG1 EBI-21680046 0.35 Q8WYQ5 EBI-21679517 0.35 Q5T3I0 EBI-21681508 0.35 Q07020 EBI-21680991 0.35 A2RU67 EBI-21694732 0.35 P50914 EBI-21741266 0.35 Q9Y3C1 EBI-21875103 0.35 P03495 EBI-15833966 0.54 A2A935 EBI-21022882 0.35 P14404 EBI-21026252 0.35 Q99558 EBI-21261374 0.35 Q4FZB7 EBI-25485626 0.40 A0A0F6B063 EBI-27033283 0.35 P0DTC9 EBI-27102259 0.53 P15130 EBI-27131516 0.35 Q0ZME3 EBI-27131755 0.35 Q6Q1R8 EBI-27132003 0.35 K9N4V7 EBI-27132270 0.35 P33469 EBI-27132272 0.35 P46108 EBI-30821447 0.44 GO:0005737 GO:0005829 GO:0048471 GO:0030332 GO:0042296 GO:0003723 GO:0061630 GO:0004842 GO:0051607 GO:0045087 GO:0032020 GO:0016567 GO:0000079 GO:0050688 GO:0006511 Unknown UniProt Sequence Analysis MERRSRRKSRRNGRSTAGKAAATQPAKSPGAQLWLFPSAAGLHRALLRRVEVTRQLCCSPGRLAVLERGGAGVQVHQLLAGSGGARTPKCIKLGKNMKIHSVDQGAEHMLILSSDGKPFEYDNYSMKHLRFESILQEKKIIQITCGDYHSLALSKGGELFAWGQNLHGQLGVGRKFPSTTTPQIVEHLAGVPLAQISAGEAHSMALSMSGNIYSWGKNECGQLGLGHTESKDDPSLIEGLDNQKVEFVACGGSHSALLTQDGLLFTFGAGKHGQLGHNSTQNELRPCLVAELVGYRVTQIACGRWHTLAYVSDLGKVFSFGSGKDGQLGNGGTRDQLMPLPVKVSSSEELKLESHTSEKELIMIAGGNQSILLWIKKENSYVNLKRTIPTLNEGTVKRWIADVETKRWQSTKREIQEIFSSPACLTGSFLRKRRTTEMMPVYLDLNKARNIFKELTQKDWITNMITTCLKDNLLKRLPFHSPPQEALEIFFLLPECPMMHISNNWESLVVPFAKVVCKMSDQSSLVLEEYWATLQESTFSKLVQMFKTAVICQLDYWDESAEENGNVQALLEMLKKLHRVNQVKCQLPESIFQVDELLHRLNFFVEVCRRYLWKMTVDASENVQCCVIFSHFPFIFNNLSKIKLLHTDTLLKIESKKHKAYLRSAAIEEERESEFALRPTFDLTVRRNHLIEDVLNQLSQFENEDLRKELWVSFSGEIGYDLGGVKKEFFYCLFAEMIQPEYGMFMYPEGASCMWFPVKPKFEKKRYFFFGVLCGLSLFNCNVANLPFPLALFKKLLDQMPSLEDLKELSPDLGKNLQTLLDDEGDNFEEVFYIHFNVHWDRNDTNLIPNGSSITVNQTNKRDYVSKYINYIFNDSVKAVYEEFRRGFYKMCDEDIIKLFHPEELKDVIVGNTDYDWKTFEKNARYEPGYNSSHPTIVMFWKAFHKLTLEEKKKFLVFLTGTDRLQMKDLNNMKITFCCPESWNERDPIRALTCFSVLFLPKYSTMETVEEALQEAINNNRGFG 1024 P59723 Hypoxia-inducible hif1an 7955 None SL-0198 Nucleus {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9NWT6}. UNIPROT P59723 UNIPROT B8A5K4 Pfam PF13621 PROSITE PS51184 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}. GO:0005737 GO:0005634 GO:0048471 GO:0016706 GO:0071532 GO:0031406 GO:0008198 GO:0102113 GO:0036140 GO:0036139 GO:0042803 GO:0008270 GO:0045746 GO:0061428 GO:1901343 GO:0042265 GO:0042264 GO:0036138 GO:0030947 Unknown UniProt Sequence Analysis MAETDGAAAFTELRDPDWDESQLRQYTFPTRQIPRLSHTDPRAEVLINNEEPVVLTDTSLVYPALKWDIPYLQENIGNGDFSVYIAENHKFLYYDEKKMVNFQDFVPKSRRIEMKFSEFVDKMHQTEEQGGKGRVYLQQTLNDTVGRKIVVDFLGFNWNWINKQQAKRNWGPLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGHKRCILFPPDQFDCLYPYPVHHPCDRQSQVDFENPDYDKFPNFKNAVGYEAVVGPGDVLYIPMYWWHHIESLLNGGETITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGDPHEVGPLLNMMIKGRYDHGLS 344 Q9NWT6 Hypoxia-inducible HIF1AN 9606 None SL-0198 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. UNIPROT Q9NWT6 UNIPROT D3DR69 UNIPROT Q5W147 UNIPROT Q969Q7 UNIPROT Q9NPV5 PDB 1H2K PDB 1H2L PDB 1H2M PDB 1H2N PDB 1IZ3 PDB 1MZE PDB 1MZF PDB 1YCI PDB 2CGN PDB 2CGO PDB 2ILM PDB 2W0X PDB 2WA3 PDB 2WA4 PDB 2XUM PDB 2Y0I PDB 2YC0 PDB 2YDE PDB 3D8C PDB 3KCX PDB 3KCY PDB 3OD4 PDB 3P3N PDB 3P3P PDB 4AI8 PDB 4B7E PDB 4B7K PDB 4BIO PDB 4JAA PDB 4NR1 PDB 4Z1V PDB 4Z2W PDB 5JWK PDB 5JWL PDB 5JWP PDB 5OP6 PDB 5OP8 PDB 5OPC PDB 6H9J PDB 6HA6 PDB 6HC8 PDB 6HKP PDB 6HL5 PDB 6HL6 PDB 6RUJ PDB 7A1J PDB 7A1K PDB 7A1L PDB 7A1M PDB 7A1N PDB 7A1O PDB 7A1P PDB 7A1Q PDB 7A1S Pfam PF13621 PROSITE PS51184 OMIM 606615 DisGeNET 55662 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}. O75190 EBI-12502476 0.35 O95271 EBI-8565753 0.78 O96018 EBI-15099018 0.75 P58546 EBI-15602804 0.44 Q06787 EBI-12502476 0.35 Q86UE4 EBI-16813719 0.35 Q8WXH0 EBI-12502476 0.35 Q9H4L5 EBI-21638930 0.35 Q9NUQ3 EBI-21638930 0.35 Q96DX5 EBI-754615 0.78 Q8WXK3 EBI-755812 0.55 Q9Y283 EBI-759370 0.64 Q16665 EBI-1035055 0.92 Q6GQQ9 EBI-2510717 0.56 Q9H2K2 EBI-8565642 0.74 Q8TAK5 EBI-8565789 0.44 Q9HBA0 EBI-8565771 0.44 Q8IY67 EBI-12502476 0.35 P54132 EBI-12502476 0.35 Q8NB46 EBI-12502476 0.64 Q05823 EBI-12502476 0.79 Q9NVH0 EBI-12502476 0.35 Q9NWX5 EBI-12502476 0.53 Q68DC2 EBI-12502476 0.35 Q9NU02 EBI-12502476 0.35 O95218 EBI-12502476 0.35 Q969S3 EBI-12502476 0.35 Q8N5A5 EBI-12502476 0.35 Q9NUD5 EBI-12502476 0.35 Q8WYQ9 EBI-12502476 0.35 Q86T24 EBI-12502476 0.35 Q9BQA1 EBI-12502476 0.35 Q96MT7 EBI-12502476 0.35 Q9P0L0 EBI-12502476 0.35 Q14157 EBI-12502476 0.35 Q9UPQ9 EBI-12502476 0.35 Q9UM00 EBI-12502476 0.35 Q9Y4G6 EBI-12502476 0.35 Q99081 EBI-12502476 0.35 Q15370 EBI-12502476 0.35 Q15369 EBI-12502476 0.35 Q92844 EBI-12502476 0.35 Q9UNL2 EBI-12502476 0.35 Q9Y2K2 EBI-12502476 0.35 P60468 EBI-12502476 0.35 O43159 EBI-12502476 0.35 P62847 EBI-12502476 0.35 P62841 EBI-12502476 0.35 Q5VT52 EBI-12502476 0.35 P61927 EBI-12502476 0.35 P61353 EBI-12502476 0.35 P57078 EBI-12502476 0.50 Q7L0Y3 EBI-12502476 0.35 Q04206 EBI-12502476 0.35 Q9HCJ3 EBI-12502476 0.35 Q2TAL8 EBI-12502476 0.35 O00487 EBI-12502476 0.35 Q9UNM6 EBI-12502476 0.35 O75832 EBI-12502476 0.59 P62195 EBI-12502476 0.35 P35998 EBI-12502476 0.35 Q5H9R7 EBI-12502476 0.35 Q9UPN7 EBI-12502476 0.35 O15355 EBI-12502476 0.35 P62875 EBI-12502476 0.35 P30876 EBI-12502476 0.35 Q4KWH8 EBI-12502476 0.35 O60733 EBI-12502476 0.35 Q8IZ21 EBI-12502476 0.35 P08237 EBI-12502476 0.35 Q8N3A8 EBI-12502476 0.35 Q9BXW6 EBI-12502476 0.53 Q9H857 EBI-12502476 0.35 Q9UM47 EBI-12502476 0.53 Q04721 EBI-12502476 0.35 Q9Y3T9 EBI-12502476 0.35 O00221 EBI-12502476 0.35 P25963 EBI-12502476 0.73 Q00653 EBI-12502476 0.53 Q9P032 EBI-12502476 0.35 Q9Y6Q9 EBI-12502476 0.35 Q9HCH0 EBI-12502476 0.35 P41227 EBI-12502476 0.35 Q9NZJ7 EBI-12502476 0.35 Q8TE76 EBI-12502476 0.35 Q5TCX8 EBI-12502476 0.64 Q15773 EBI-12502476 0.35 Q96AX9 EBI-12502476 0.35 O43318 EBI-12502476 0.35 Q7L5Y9 EBI-12502476 0.35 Q9BRK4 EBI-12502476 0.35 P83369 EBI-12502476 0.35 Q9ULH0 EBI-12502476 0.35 Q8N163 EBI-12502476 0.35 Q7LBC6 EBI-12502476 0.35 Q96SI1 EBI-12502476 0.35 Q13418 EBI-12502476 0.59 Q12894 EBI-12502476 0.35 Q9ULT8 EBI-12502476 0.64 Q00341 EBI-12502476 0.35 O15379 EBI-12502476 0.35 Q9Y450 EBI-12502476 0.35 Q9H6D7 EBI-12502476 0.35 Q8IYU2 EBI-12502476 0.35 Q9UKJ3 EBI-12502476 0.35 O60547 EBI-12502476 0.53 Q9NRA8 EBI-12502476 0.53 P06730 EBI-12502476 0.35 Q9H9B1 EBI-12502476 0.35 Q96F86 EBI-12502476 0.35 Q9Y678 EBI-12502476 0.35 A5YKK6 EBI-12502476 0.35 Q99439 EBI-12502476 0.35 Q96ST8 EBI-12502476 0.35 Q5VT06 EBI-12502476 0.35 Q12834 EBI-12502476 0.35 Q8WXE0 EBI-12502476 0.35 Q9UKZ1 EBI-12502476 0.35 Q9BY42 EBI-12502476 0.35 Q6ZUT1 EBI-12502476 0.35 P20290 EBI-12502476 0.35 Q9NVI7 EBI-12502476 0.35 Q8NBU5 EBI-12502476 0.35 Q9H765 EBI-12502476 0.64 P27540 EBI-12502476 0.35 Q92625 EBI-12502476 0.64 Q9ULJ7 EBI-24286767 0.56 Q8N8A2 EBI-12502476 0.35 O15084 EBI-12502476 0.35 Q96NW4 EBI-12502476 0.53 O75179 EBI-12502476 0.35 Q8IWZ3 EBI-12502476 0.35 Q9P2R3 EBI-12502476 0.35 Q96FW1 EBI-10770028 0.70 P46531 EBI-11473706 0.44 P19838 EBI-11322417 0.74 P47086 EBI-11532399 0.56 Q6P5F9 EBI-11603310 0.35 Q6PG48 EBI-24615512 0.56 Q7Z713 EBI-24425210 0.56 Q9H672 EBI-24534882 0.56 Q8NFD2 EBI-25272595 0.67 Q96P71 EBI-15098946 0.40 Q9Y575 EBI-21571836 0.35 Q9UPU5 EBI-21638930 0.35 Q9UHD2 EBI-21638930 0.35 Q9H6R7 EBI-21638930 0.35 Q9BQS8 EBI-21638930 0.53 Q8WXD9 EBI-21638930 0.35 Q8TES7 EBI-21638930 0.35 Q8TBX8 EBI-21638930 0.35 Q15653 EBI-21638930 0.53 Q05086 EBI-21638930 0.53 Q04864 EBI-21638930 0.35 Q01484 EBI-21638930 0.35 P78356 EBI-21638930 0.53 P55196 EBI-21638930 0.35 P47974 EBI-21638930 0.35 P40222 EBI-21638930 0.53 Q12955 EBI-21638930 0.35 Q8WXI3 EBI-21754620 0.35 Q9BW85 EBI-21758292 0.35 Q9Y574 EBI-21801297 0.35 Q8WVL7 EBI-21811862 0.69 Q3KP44 EBI-21876401 0.35 Q96NS5 EBI-21897846 0.35 Q495B1 EBI-21900536 0.40 Q9UK73 EBI-15602843 0.59 Q9BZF9 EBI-15602883 0.51 Q06547 EBI-15603005 0.44 P55273 EBI-15603110 0.44 O14974 EBI-15603359 0.44 Q9UL18 EBI-16813719 0.35 P09012 EBI-16813719 0.35 O14497 EBI-16813719 0.35 Q4U2R6 EBI-16813719 0.35 Q9Y2X3 EBI-16813719 0.35 Q9Y2T7 EBI-16813719 0.35 Q9UQ35 EBI-16813719 0.35 Q9H4B7 EBI-16813719 0.35 Q9BWF3 EBI-16813719 0.35 Q9BVA1 EBI-16813719 0.35 Q9BU76 EBI-16813719 0.35 Q9BPZ3 EBI-16813719 0.35 Q99700 EBI-16813719 0.35 Q96MR6 EBI-16813719 0.35 Q96EK7 EBI-16813719 0.35 Q92925 EBI-16813719 0.35 Q92784 EBI-16813719 0.35 Q92734 EBI-16813719 0.35 Q8WUZ0 EBI-16813719 0.35 Q8NFD5 EBI-16813719 0.35 Q8N5F7 EBI-16813719 0.35 Q6PKG0 EBI-16813719 0.35 Q4VC05 EBI-16813719 0.35 Q15020 EBI-16813719 0.35 Q13838 EBI-16813719 0.35 Q13283 EBI-16813719 0.35 Q13243 EBI-16813719 0.35 Q12926 EBI-16813719 0.35 Q07955 EBI-16813719 0.35 P82664 EBI-16813719 0.35 P51531 EBI-16813719 0.35 P51532 EBI-16813719 0.35 Q9BQE3 EBI-16814752 0.53 Q7L014 EBI-16814752 0.35 Q13772 EBI-16814752 0.35 P48668 EBI-16814752 0.35 Q969F8 EBI-21282024 0.40 Q71UM5 EBI-25479285 0.35 P50502 EBI-25479285 0.35 Q9Y6H1 EBI-25479285 0.35 P40763 EBI-25485488 0.40 Q59H18 EBI-28941654 0.35 GO:0005737 GO:0005829 GO:0005654 GO:0048471 GO:0016706 GO:0071532 GO:0031406 GO:0008198 GO:0102113 GO:0051059 GO:0005112 GO:0019826 GO:0036140 GO:0036139 GO:0042803 GO:0008270 GO:0045746 GO:0061428 GO:0042265 GO:0042264 GO:0036138 GO:0045663 GO:2001214 Unknown UniProt Sequence Analysis MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN 349 Q8BLR9 Hypoxia-inducible Hif1an 10090 None SL-0198 Nucleus {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9NWT6}. UNIPROT Q8BLR9 UNIPROT A1L3B7 UNIPROT Q3U3G4 Pfam PF13621 PROSITE PS51184 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}. Q07279 EBI-26677785 0.37 Q8VIM5 EBI-26677793 0.37 GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0048471 GO:0016706 GO:0071532 GO:0031406 GO:0008198 GO:0102113 GO:0051059 GO:0005112 GO:0036140 GO:0036139 GO:0042803 GO:0008270 GO:0045746 GO:0061428 GO:0042265 GO:0042264 GO:0036138 GO:0045663 Unknown UniProt Sequence Analysis MAATAAEVAASGSGEAREEAEAPGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMGNFQNFKPRSNREEIKFHEFVEKLQAIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGHKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFRNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN 349 O75146 Huntingtin-interacting HIP1R 9606 None SL-0198 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. UNIPROT O75146 UNIPROT A6NHQ6 UNIPROT Q6NXG8 UNIPROT Q9UED9 PDB 1R0D Pfam PF07651 Pfam PF16515 Pfam PF01608 PROSITE PS50942 PROSITE PS50945 OMIM 605613 DisGeNET 9026 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}. O14976 EBI-11150908 0.53 Q13573 EBI-7950968 0.35 Q99459 EBI-7954144 0.35 P19320 EBI-6189915 0.35 Q62925 EBI-9971384 0.00 Q13404 EBI-9971384 0.00 P22314 EBI-9971384 0.00 P61088 EBI-9971384 0.00 P60033 EBI-10766934 0.35 Q96H55 EBI-11031416 0.35 P60710 EBI-11045267 0.35 Q9ERG0 EBI-11054044 0.35 Q9UHB6 EBI-11058729 0.35 G3X972 EBI-11079358 0.35 P09497 EBI-11081190 0.35 Q9NYZ3 EBI-11081743 0.35 Q13492 EBI-11082344 0.35 Q00610 EBI-11082478 0.35 Q9WTI7 EBI-11093786 0.35 P35579 EBI-11098811 0.35 P47755 EBI-11117728 0.35 Q9UBB9 EBI-24361039 0.56 O14777 EBI-24400766 0.56 P14373 EBI-25262907 0.56 C5E519 EBI-12583021 0.35 P32970 EBI-21512742 0.35 Q6PJG9 EBI-21552126 0.35 P35414 EBI-21559824 0.35 P46059 EBI-21560916 0.35 Q14627 EBI-21561326 0.35 P21709 EBI-21595997 0.35 Q86VU5 EBI-21596714 0.35 Q8N6K0 EBI-21599984 0.35 O95274 EBI-21607810 0.35 P35813 EBI-21660332 0.35 Q96D71 EBI-21660332 0.35 Q15311 EBI-21660332 0.35 Q10567 EBI-21660332 0.35 P23246 EBI-21660332 0.35 O75688 EBI-21660332 0.35 O00291 EBI-21660332 0.35 Q96FJ0 EBI-21668214 0.35 O60939 EBI-21671922 0.35 A2RU67 EBI-21694732 0.35 Q9NZQ7 EBI-21740460 0.35 Q9NUM3 EBI-21748242 0.35 Q8N468 EBI-21785908 0.35 O75146 EBI-15564862 0.56 P03372 EBI-21301141 0.53 Q9BYP7 EBI-28946054 0.35 P0DTD8 EBI-27127141 0.35 GO:0016324 GO:0005938 GO:0005905 GO:0030136 GO:0030665 GO:0005856 GO:0005829 GO:0032839 GO:0043197 GO:0043231 GO:0005739 GO:0043025 GO:0048471 GO:0005886 GO:0014069 GO:0032587 GO:0097060 GO:0051015 GO:0035615 GO:0030276 GO:0032051 GO:0042802 GO:0035091 GO:0005547 GO:0043325 GO:0080025 GO:0005546 GO:0046982 GO:0042803 GO:0017124 GO:0007015 GO:0006919 GO:0006915 GO:0048268 GO:0055123 GO:0006897 GO:0030837 GO:0043066 GO:0034316 GO:0043065 GO:1905445 GO:0045742 GO:1901030 GO:2000588 GO:0032092 GO:0050821 GO:0006898 GO:0032956 GO:2000369 GO:0030100 GO:0060453 Unknown UniProt Sequence Analysis MNSIKNVPARVLSRRPGHSLEAEREQFDKTQAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIREIGDLWGHLHDRYGQLVNVYTKLLLTKISFHLKHPQFPAGLEVTDEVLEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLLFKLHSCLPADTLQGHRDRFHEQFHSLRNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEDEEPENLIEISTGPPAGEPVVVADLFDQTFGPPNGSVKDDRDLQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAERESQEQGLRQRLLDEQFAVLRGAAAEAAGILQDAVSKLDDPLHLRCTSSPDYLVSRAQEALDAVSTLEEGHAQYLTSLADASALVAALTRFSHLAADTIINGGATSHLAPTDPADRLIDTCRECGARALELMGQLQDQQALRHMQASLVRTPLQGILQLGQELKPKSLDVRQEELGAVVDKEMAATSAAIEDAVRRIEDMMNQARHASSGVKLEVNERILNSCTDLMKAIRLLVTTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVGWGATQLVEAADKVVLHTGKYEELIVCSHEIAASTAQLVAASKVKANKHSPHLSRLQECSRTVNERAANVVASTKSGQEQIEDRDTMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERMRLGELRKQHYVLAGASGSPGEEVAIRPSTAPRSVTTKKPPLAQKPSVAPRQDHQLDKKDGIYPAQLVNY 1068 Q9JKY5 Huntingtin-interacting Hip1r 10090 None SL-0198 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. UNIPROT Q9JKY5 UNIPROT Q3UJ14 Pfam PF07651 Pfam PF16515 Pfam PF01608 PROSITE PS50942 PROSITE PS50945 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. Q01279 EBI-27088765 0.40 P04973 EBI-7374625 0.37 P04975 EBI-7374604 0.57 Q61210 EBI-649779 0.37 Q60598 EBI-7285203 0.49 Q96B97 EBI-7167363 0.40 G3V6K6 EBI-27088754 0.52 GO:0016324 GO:0005938 GO:0005905 GO:0030136 GO:0030665 GO:0005856 GO:0005829 GO:0032839 GO:0043197 GO:0043231 GO:0016020 GO:0005739 GO:0043025 GO:0048471 GO:0005886 GO:0014069 GO:0032587 GO:0097060 GO:0003779 GO:0051015 GO:0035615 GO:0030276 GO:0032051 GO:0042802 GO:0035091 GO:0005547 GO:0043325 GO:0080025 GO:0005546 GO:0046982 GO:0042803 GO:0017124 GO:0007015 GO:0006919 GO:0006915 GO:0048268 GO:0055123 GO:0006897 GO:0061024 GO:0030837 GO:0043066 GO:0034316 GO:0043065 GO:1905445 GO:2000370 GO:0045742 GO:1901030 GO:2000588 GO:0032092 GO:0050821 GO:0006898 GO:0032956 GO:2000369 GO:0030100 GO:0060453 Unknown UniProt Sequence Analysis MNSIKNVPARVLSRRPGHSLEAEREQFDKTQAISISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLSSSSILSWKFCHVLHKVLRDGHPNVLHDYQRYRSNIREIGDLWGHLRDQYGHLVNIYTKLLLTKISFHLKHPQFPAGLEVTDEVLEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLMFKLHSCLPADTLQGHRDRFHEQFHSLKNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEEEEPENLIEISSAPPAGEPVVVADLFDQTFGPPNGSMKDDRDLQIENLKREVETLRAELEKIKMEAQRYISQLKGQVNGLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLREEAERKASATEARYSKLKEKHSELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQAKRESEMKMEEQSDQLEKLKRELAARAGELARAQEALSRTEQSGSELSSRLDTLNAEKEALSGVVRQREAELLAAQSLVREKEEALSQEQQRSSQEKGELRGQLAEKESQEQGLRQKLLDEQLAVLRSAAAEAEAILQDAVSKLDDPLHLRCTSSPDYLVSRAQAALDSVSGLEQGHTQYLASSEDASALVAALTRFSHLAADTIVNGAATSHLAPTDPADRLMDTCRECGARALELVGQLQDQTVLPRAQPSLMRAPLQGILQLGQDLKPKSLDVRQEELGAMVDKEMAATSAAIEDAVRRIEDMMSQARHESSGVKLEVNERILNSCTDLMKAIRLLVMTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVGWGATQLVESADKVVLHMGKYEELIVCSHEIAASTAQLVAASKVKANKNSPHLSRLQECSRTVNERAANVVASTKSGQEQIEDRDTMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERVRLGELRKQHYVLAGGMGTPSEEEPSRPSPAPRSGATKKPPLAQKPSIAPRTDNQLDKKDGVYPAQLVNY 1068 Q9SZN7 Heavy HIPP26 3702 None SL-0178 SL-0182 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}. UNIPROT Q9SZN7 UNIPROT Q8LGG1 UNIPROT Q9ZRE4 Pfam PF00403 PROSITE PS50846 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}. Q9STP8 EBI-2008217 0.58 Q9SEZ1 EBI-2027471 0.51 Q9LK09 EBI-9161847 0.35 Q9SZU7 EBI-25529995 0.56 Q9SQR3 EBI-25530237 0.56 GO:0031965 GO:0005886 GO:0009506 GO:0046870 GO:0005507 GO:0032791 GO:0010286 Lipid-Anchored UniProt Curator Inference {ECO:0000305|PubMed:18974936} MGVLDHVSEMFDCSHGHKIKKRKQLQTVEIKVKMDCEGCERKVRRSVEGMKGVSSVTLEPKAHKVTVVGYVDPNKVVARMSHRTGKKVELWPYVPYDVVAHPYAAGVYDKKAPSGYVRRVDDPGVSQLARASSTEVRYTTAFSDENPAACVVM 153 P12683 3-hydroxy-3-methylglutaryl-coenzyme HMG1 559292 None SL-0178 Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8744950}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:14562095}. UNIPROT P12683 UNIPROT D6W0K8 Pfam PF00368 Pfam PF13323 Pfam PF12349 PROSITE PS00066 PROSITE PS00318 PROSITE PS01192 PROSITE PS50065 PROSITE PS50156 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}. P33767 EBI-7745273 0.37 P07286 EBI-7745296 0.37 Q08421 EBI-786893 0.35 P38708 EBI-786893 0.35 Q12447 EBI-786893 0.35 P38219 EBI-786893 0.35 P16140 EBI-786893 0.35 P02557 EBI-786893 0.35 P09733 EBI-786893 0.35 P02994 EBI-786893 0.35 P10592 EBI-786893 0.35 P10659 EBI-786893 0.35 P33299 EBI-786893 0.35 P38764 EBI-786893 0.35 P41940 EBI-786893 0.35 P23641 EBI-786893 0.35 P40069 EBI-786893 0.35 P39993 EBI-786893 0.35 P43535 EBI-786893 0.35 P47912 EBI-786893 0.35 P30822 EBI-786893 0.35 P00330 EBI-786893 0.35 P53030 EBI-803408 0.35 P11484 EBI-803408 0.35 P38706 EBI-803408 0.44 P0C2I0 EBI-803408 0.35 P16370 EBI-803408 0.35 P25454 EBI-803408 0.44 P46985 EBI-803408 0.35 P12684 EBI-803408 0.67 P39925 EBI-812746 0.27 P32790 EBI-7494165 0.37 Q12329 EBI-3828992 0.35 P12683 EBI-21322239 0.37 GO:0005789 GO:0016021 GO:0005635 GO:0034399 GO:0005778 GO:0004420 GO:0015936 GO:0006696 GO:0019287 GO:0008299 GO:0016126 Transmembrane UniProt Sequence Analysis {ECO:0000255} MPPLFKGLKQMAKPIAYVSRFSAKRPIHIILFSLIISAFAYLSVIQYYFNGWQLDSNSVFETAPNKDSNTLFQECSHYYRDSSLDGWVSITAHEASELPAPHHYYLLNLNFNSPNETDSIPELANTVFEKDNTKYILQEDLSVSKEISSTDGTKWRLRSDRKSLFDVKTLAYSLYDVFSENVTQADPFDVLIMVTAYLMMFYTIFGLFNDMRKTGSNFWLSASTVVNSASSLFLALYVTQCILGKEVSALTLFEGLPFIVVVVGFKHKIKIAQYALEKFERVGLSKRITTDEIVFESVSEEGGRLIQDHLLCIFAFIGCSMYAHQLKTLTNFCILSAFILIFELILTPTFYSAILALRLEMNVIHRSTIIKQTLEEDGVVPSTARIISKAEKKSVSSFLNLSVVVIIMKLSVILLFVFINFYNFGANWVNDAFNSLYFDKERVSLPDFITSNASENFKEQAIVSVTPLLYYKPIKSYQRIEDMVLLLLRNVSVAIRDRFVSKLVLSALVCSAVINVYLLNAARIHTSYTADQLVKTEVTKKSFTAPVQKASTPVLTNKTVISGSKVKSLSSAQSSSSGPSSSSEEDDSRDIESLDKKIRPLEELEALLSSGNTKQLKNKEVAALVIHGKLPLYALEKKLGDTTRAVAVRRKALSILAEAPVLASDRLPYKNYDYDRVFGACCENVIGYMPLPVGVIGPLVIDGTSYHIPMATTEGCLVASAMRGCKAINAGGGATTVLTKDGMTRGPVVRFPTLKRSGACKIWLDSEEGQNAIKKAFNSTSRFARLQHIQTCLAGDLLFMRFRTTTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVRKVLKSDVSALVELNIAKNLVGSAMAGSVGGFNAHAANLVTAVFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGPHATAPGTNARQLARIVACAVLAGELSLCAALAAGHLVQSHMTHNRKPAEPTKPNNLDATDINRLKDGSVTCIKS 1054 P12684 3-hydroxy-3-methylglutaryl-coenzyme HMG2 559292 None SL-0178 Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8744950}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:14562095}. UNIPROT P12684 UNIPROT D6VZ84 UNIPROT E9P8X3 Pfam PF00368 Pfam PF13323 Pfam PF12349 PROSITE PS00066 PROSITE PS00318 PROSITE PS01192 PROSITE PS50065 PROSITE PS50156 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}. P12683 EBI-803408 0.67 Q06449 EBI-601343 0.37 P38219 EBI-787291 0.35 P16140 EBI-787291 0.35 P09733 EBI-787291 0.35 P36008 EBI-787291 0.35 P02994 EBI-787291 0.35 P11484 EBI-787291 0.35 P33299 EBI-787291 0.35 P40069 EBI-787291 0.35 P30822 EBI-787291 0.35 P00330 EBI-787291 0.35 P40341 EBI-806785 0.35 P16521 EBI-806785 0.35 P10592 EBI-806785 0.35 P26783 EBI-806785 0.35 P32905 EBI-806785 0.35 P26321 EBI-806785 0.35 P38706 EBI-806785 0.35 P41805 EBI-806785 0.35 P41940 EBI-806785 0.35 P12709 EBI-806785 0.35 P06169 EBI-806785 0.35 P04147 EBI-806785 0.35 P15108 EBI-806785 0.35 P39925 EBI-806785 0.35 Q02159 EBI-860875 0.00 P25694 EBI-1008636 0.35 P53044 EBI-1008636 0.35 Q04228 EBI-1008636 0.35 Q03010 EBI-6316649 0.00 P38837 EBI-6316638 0.00 P12684 EBI-21320996 0.55 Q12469 EBI-16282981 0.35 GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0034399 GO:0005778 GO:0000502 GO:0004420 GO:0015936 GO:0006696 GO:0008299 GO:0016126 Transmembrane UniProt Sequence Analysis {ECO:0000255} MSLPLKTIVHLVKPFACTARFSARYPIHVIVVAVLLSAAAYLSVTQSYLNEWKLDSNQYSTYLSIKPDELFEKCTHYYRSPVSDTWKLLSSKEAADIYTPFHYYLSTISFQSKDNSTTLPSLDDVIYSVDHTRYLLSEEPKIPTELVSENGTKWRLRNNSNFILDLHNIYRNMVKQFSNKTSEFDQFDLFIILAAYLTLFYTLCCLFNDMRKIGSKFWLSFSALSNSACALYLSLYTTHSLLKKPASLLSLVIGLPFIVVIIGFKHKVRLAAFSLQKFHRISIDKKITVSNIIYEAMFQEGAYLIRDYLFYISSFIGCAIYARHLPGLVNFCILSTFMLVFDLLLSATFYSAILSMKLEINIIHRSTVIRQTLEEDGVVPTTADIIYKDETASEPHFLRSNVAIILGKASVIGLLLLINLYVFTDKLNATILNTVYFDSTIYSLPNFINYKDIGNLSNQVIISVLPKQYYTPLKKYHQIEDSVLLIIDSVSNAIRDQFISKLLFFAFAVSISINVYLLNAAKIHTGYMNFQPQSNKIDDLVVQQKSATIEFSETRSMPASSGLETPVTAKDIIISEEIQNNECVYALSSQDEPIRPLSNLVELMEKEQLKNMNNTEVSNLVVNGKLPLYSLEKKLEDTTRAVLVRRKALSTLAESPILVSEKLPFRNYDYDRVFGACCENVIGYMPIPVGVIGPLIIDGTSYHIPMATTEGCLVASAMRGCKAINAGGGATTVLTKDGMTRGPVVRFPTLIRSGACKIWLDSEEGQNSIKKAFNSTSRFARLQHIQTCLAGDLLFMRFRTTTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVKSVLKSDVSALVELNISKNLVGSAMAGSVGGFNAHAANLVTALFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGPHPTEPGANARQLARIIACAVLAGELSLCSALAAGHLVQSHMTHNRKTNKANELPQPSNKGPPCKTSALL 1045 Q10283 3-hydroxy-3-methylglutaryl-coenzyme hmg1 284812 None SL-0178 Endoplasmic reticulum membrane {ECO:0000269|PubMed:19486165}; Multi-pass membrane protein {ECO:0000269|PubMed:19486165}. Nucleus envelope {ECO:0000269|PubMed:19486165}. UNIPROT Q10283 UNIPROT O74425 Pfam PF00368 Pfam PF12349 PROSITE PS00066 PROSITE PS00318 PROSITE PS50065 PROSITE PS50156 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}. GO:0005783 GO:0005789 GO:0016021 GO:0005635 GO:0031965 GO:0042175 GO:0005778 GO:0004420 GO:0015936 GO:0006696 GO:0010142 GO:0019287 GO:0008299 GO:0016126 Transmembrane UniProt Sequence Analysis {ECO:0000255} MIYKLAARYPIQVIAIVGILVSMAYFSFLEALTQEDFPVLIRALKRFGILDGFPNTRLPNEMILKLSSVQGEDASVWEQIPAAELGGEGFVDFDITQWYYPANAKVDVAQLVEPYRNDCIFHDASGACHFFFKEVGNWTVSSIALPSNLANPPIDYFLDSSSTVIQRILPAIREHGISWSWLLQLIARTWMNTLKIASQASKTELLIVGTAYACMLISIVSLYLKMRRLGSKFWLFFSVLLSTLFSVQFAMTLVRASGVRISLVSLIESLPFLINVVALDKAAELTRQVITRCSVSDSHSPMHEDIAKACRNAAPPILRHFSFGIVVLAIFSYCNFGIKQFFLFAAVMIYDLLLLFSFFVAILTLKLEMRRYNAKDDVRKVLIEEGLSESTARHVADGNDSSATTSAGSRYFKVRYGTKIILFIFIAFNLFELCSIPFKHYAATSAAAARLIPLVRSQYPDFKSQRLLDDGVFDDVLSAISSMSNIESPSVRLLPAVFYGAELSSTSFLSTIHSFINNWSHYISASFLSKWIVCALSLSIAVNVFLLNAARLNSIKEEPEKKVVEKVVEVVKYIPSSNSSSIDDIQKDEIAQESVVRSLEECITLYNNGQISTLNDEEVVQLTLAKKIPLYALERVLKDVTRAVVIRRTVVSRSSRTKTLESSNCPVYHYDYSRVLNACCENVIGYMPLPLGVAGPLIIDGKPFYIPMATTEGALVASTMRGCKAINAGGGAVTVLTRDQMSRGPCVAFPNLTRAGRAKIWLDSPEGQEVMKKAFNSTSRFARLQHIKTALAGTRLFIRFCTSTGDAMGMNMISKGVEHALVVMSNDAGFDDMQVISVSGNYCTDKKPAAINWIDGRGKSVIAEAIIPGDAVKSVLKTTVEDLVKLNVDKNLIGSAMAGSVGGFNAHAANIVTAVYLATGQDPAQNVESSNCITLMDNVDGNLQLSVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGAHMTSPGDNSRQLARVVAAAVMAGELSLCSALASGHLVKSHIGLNRSALNTPAMDSSAKKPATDALKSVNSRVPGR 1053 A8WUP2 Zygote zyg 6238 None SL-0178 SL-0182 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}. UNIPROT A8WUP2 Pfam PF19047 PROSITE PS50021 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}. GO:0005813 GO:0005737 GO:0016021 GO:0005874 GO:0031965 GO:0051959 GO:0008017 GO:0031122 GO:0030705 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLDLTNQESDSSENGNSKYADSTDGRGIGTSRRLDDEDLDERRKDLADLVFWMSGLKATTLPLDDHTSLCNGRAFAEILHEIDRSFFDERWLETMPEMRTSSNLVVKRSNLRKLWRKMSDYIQVLNRKVVSTRWTEIGDRLDGLDETDIPVAADLAMAVVSLAFIGKTQEKYIQYSQELPAGEHQHMMANVARLVQIVMEELPEVPTFHEISELDGSQNELNSSHVESSVITNGNGSAERRSTLSANDQVLVEAQLEIDELRSERDNLIKDVERLTKALESSQLDTSTCSEPNELSILEKQNEELRVKRRQAEERVLELEASMEHFQAIVVKLTDENDTLQSGQKELNMLKTHLDTAQSDVEEWRTIANKYQSDAEMLKKREKEVKELQGQVKSLTSRLEHHVKTATIDEDNKAGIVQLRSQIGTLTANNVELNVGLESKKRIVEQLELQLIQYKEKVKELEDRKEDLIAERNELENKLLFKESVTPRSLHESMFEAGHLSFDDKTKLPLEIENKRLTERIQELESLEPLKGEIIKMKSQNGVLEEEKLVITKQMEELERQVADLQEKLTKNQQHASGDVVELKVQLEKANVEVERMRETEMRTEAKLAGVEELLRKRNVEKEANETALQKAKAVIDELESRNRPVGEDNKTSVQDFKELKTENELLRQKNEALETALNTTTQSLEQENRLITSAAHQQILDRSSDSMMIMRAQAGSDHPQTLLDTQKMTRALPWRFGISSMLIIFMVWFFINTFCEVNAPPKA 764 Q23529 Zygote zyg 6239 None SL-0178 SL-0182 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. UNIPROT Q23529 UNIPROT Q2V4T6 UNIPROT Q7JPD4 Pfam PF19047 PROSITE PS50021 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}. Q23529 EBI-1570329 0.40 G5ECK7 EBI-1570311 0.37 Q9U2Z1 EBI-6457211 0.37 P91409 EBI-6457201 0.37 G5ED30 EBI-11465222 0.51 H2KYA1 EBI-11469957 0.37 Q93198 EBI-11471204 0.37 GO:0005813 GO:0005737 GO:0016021 GO:0005874 GO:0005635 GO:0031965 GO:0051959 GO:0008017 GO:0043621 GO:0051642 GO:0007059 GO:0031122 GO:0030705 GO:0009792 GO:0051647 GO:0035046 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLDLTNKESESSDNGNSKYEDSIDGREVGTSKPFKEERSLEDLQADLADMAVWMEGLDATKLPLNDPQLLCNGRAFSEVLHNVDKNFFTDGWLETMPENRTTNIMVFRSCTRKLWRKMFDYVNHINRTVVSSRWTDIHERIDGIYESDLPAMVNLGMAVVTLAHIGKNAKRFVDYSKALTSTHKSMMSNVAKMVTTVIDEMPENPCFHEISELHGSQSELNSLSESSGKLNGNGSSERRSNADQILVDAELEIERLRTETENQRKEIERLTKSFETAQHDMSSNSESGDISILEKQNEELRQKRRELEEKNLELDAAVDQFKGIVFELTNENDVLRRSDKERQRLQTVLDAAQSDLDEWKTVANQYQKEAELSKQQDKEIKELLSQNKALKSRLDHHVKSATLEDANKNGIAQLRTQVGGLTALNTELKASLDSKKRCVEQLEIQLIQHKEKVKELEDRKDELIEERNRLENQLIFKEAVTPRSLHESMFEAGNLSFEPFSEKNTLPLEIENKRLTERIQELESLEPLKGELITLKSKNGVLEEEKLFATKQIEELQQQIEDLQENLLKNQEHASGDVVGLKIQLEKAEVEAQQMREAKMRAETNQAQVDEILKKRTAELEVNATALQKAKAVIDELEYNSRPVSEDSMTSVQAFKEMKEENEKLRQKVEKLEIELNTVTQGFEQENRLLTSASHQQVLNRSIDEVMSMRAHAGSEEPQTLLDTQKMSGALPWRSLASETRRELPTAMASILVLGFLVFIAWMFININSALNAPPNA 777 Q23647 Hypersensitive hpo 6239 None SL-0198 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}. UNIPROT Q23647 GO:1990633 GO:0048471 Unknown UniProt Sequence Analysis MNSQQEWEHAYSLAERMYNKQAPTKREELNPTERVICSRFETIFDYDPFKDEYTFRDQALLFSTPVQPKCRTVAEADLHELKENTAKLNIPMPSYINICPIYALLPFTVLVFNNSQHAHKSLSDDMERAAATFRNPHESEIVPGAMYIFKQKHGKAYRCIILSEDGDMNIPDAERKYLVAFIDNVQIVSVKQKTLFVSDQFSIKDYPCALHCARIVGISAIRKSYVSGMNQFILNFYDAKEKRKAGMFAFIYKLDKEEKKLVIDYPSLLGTPKTTSTEIRTAVGHQIVASKDPVSLTFEQLNKKEVPEFKYLNSTDDDSDVELDLIEHDTKSVNPVASSHPTSSSMDDCPYGRASIARAKDYQLRLPPHSQKGLSSSSLLGSSYPVSNSIKNDITKQSESNRADATNISFSSFESTKSDISPQNNQNVEETSTPTVPPNSTIQENEEDEIMSPASIIRAPSRLAGSLNKVSIERPNTPLPTSSKNSEHNMSEISTYEASSISSHHLVPQSPSVPKTNYTVPVVQRPLTAPEKFRDPFGGPGSSDILNTKMLCSEKNIVPSNKFGRQISPGKDDKNENYQYSRMETKPQTLFAPVLDENQRQSSSSNMMCQIPDISSVAQGSNAPKTAPNDSVNSVAPDDIHETDKRGNHCKSVTEDPKDNKDPTAVTTLEDPDINDENFSVQSICSETFVETDQKLMEVETGADAFTESITDQFAQMSEGLKKLAINLADSVRTAAIEKNHDAFIANIHAMEIISKKVPDDIDKRFWKMKIVEARKLEAAFD 782 Q960X8 Hepatocyte Hrs 7227 None SL-0198 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. UNIPROT Q960X8 UNIPROT A4V018 UNIPROT Q8IGU6 UNIPROT Q9VQF2 UNIPROT Q9VQF3 PDB 1DVP Pfam PF01363 Pfam PF12210 Pfam PF00790 PROSITE PS50330 PROSITE PS50179 PROSITE PS50178 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}. Q8IQV9 EBI-509966 0.37 P23573 EBI-203520 0.00 Q9VNS1 EBI-236619 0.00 O46339 EBI-248743 0.00 Q9VLJ5 EBI-253365 0.00 Q9W4P5 EBI-259675 0.00 Q9VAD6 EBI-259680 0.00 Q9V397 EBI-259684 0.00 Q9XTL2 EBI-259688 0.00 O46036 EBI-259692 0.00 P68198 EBI-300719 0.40 Q9VVT5 EBI-509756 0.37 Q9Y103 EBI-509763 0.00 P18091 EBI-509770 0.00 Q8SXD4 EBI-509777 0.00 Q7KLE5 EBI-509784 0.00 Q9V595 EBI-509791 0.37 Q03017 EBI-509798 0.37 Q9VH60 EBI-509805 0.37 Q95RP4 EBI-509812 0.37 Q9VCB8 EBI-509819 0.37 Q23983 EBI-509826 0.37 Q9VEN1 EBI-509833 0.00 Q00963 EBI-509840 0.37 A1Z9J3 EBI-509847 0.37 Q9VN68 EBI-509854 0.00 Q9VXG4 EBI-509861 0.37 Q7YU91 EBI-509868 0.37 Q8SXA8 EBI-509875 0.00 Q9VW47 EBI-509882 0.37 P29742 EBI-509896 0.37 Q9VC36 EBI-509903 0.37 O44381 EBI-509917 0.37 Q9VPL5 EBI-509924 0.37 P54360 EBI-509931 0.37 P48608 EBI-509938 0.00 P07666 EBI-509945 0.37 Q8T987 EBI-509952 0.37 Q7KN74 EBI-509959 0.37 O02373 EBI-509973 0.37 Q9VM75 EBI-509980 0.37 P08953 EBI-15848965 0.35 Q9VUH6 EBI-15848965 0.35 GO:0005938 GO:0005829 GO:0005769 GO:0005768 GO:0048471 GO:0046872 GO:0035091 GO:0043130 GO:0045022 GO:0032456 GO:0006897 GO:0016197 GO:0032509 GO:1990182 GO:0045879 GO:0120177 GO:0016322 GO:1903688 GO:0045752 GO:0061357 GO:0031623 GO:0051726 GO:2000274 Unknown UniProt Sequence Analysis MFRSSFDKNLENATSHLRLEPDWPSILLICDEINQKDVTPKNAFAAIKKKMNSPNPHSSCYSLLVLESIVKNCGAPVHEEVFTKENCEMFSSFLESTPHENVRQKMLELVQTWAYAFRSSDKYQAIKDTMTILKAKGHTFPELREADAMFTADTAPNWADGRVCHRCRVEFTFTNRKHHCRNCGQVFCGQCTAKQCPLPKYGIEKEVRVCDGCFAALQRPTSGSGGAKSGPRPADSELPAEYLNSTLAQQVQTPARKTEQELKEEEELQLALALSQSEAEQQKPKLQSLPPAAYRMQQRSPSPEAPPEPKEYHQQPEEATNPELAKYLNRSYWEQRKISESSSMASPSAPSPMPPTPQPQQIMPLQVKSADEVQIDEFAANMRTQVEIFVNRMKSNSSRGRSISNDSSVQTLFMTLTSLHSQQLSYIKEMDDKRMWYEQLQDKLTQIKDSRAALDQLRQEHVEKLRRIAEEQERQRQMQMAQKLDIMRKKKQEYLQYQRQLALQRIQEQEREMQLRQEQQKAQYLMGQSAPPFPYMPPSAVPQHGSPSHQLNNVYNPYAAGVPGYLPQGPAPAPNGHGQFQAIPPGMYNPAIQQPMPPNLQPGGLMQQPAPPGNPQMMPPMPENQFANNPAAILQLPQQHSIAQPPQIPFQPQPQQIPGQQPQQIPGQQPQQIPGQQPQQIPGQQPQQIPVQQPQPQPQMGHVMLQQHQAPPAAQAPPVTEIANNQVQAVAAAPAPPQNEPGPAPVKAEEPATAELISFD 760 Q08DJ8 Heat HSF1 9913 None SL-0198 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}. UNIPROT Q08DJ8 Pfam PF00447 Pfam PF06546 PROSITE PS00434 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}. GO:0005813 GO:0101031 GO:0005737 GO:0000776 GO:0097431 GO:0097165 GO:0005654 GO:0005634 GO:0048471 GO:0016605 GO:1990904 GO:0031490 GO:0003677 GO:0001228 GO:0003700 GO:0031072 GO:0051879 GO:0042802 GO:0046982 GO:0043621 GO:0000978 GO:0043565 GO:0061770 GO:0071276 GO:0071280 GO:0072738 GO:0071480 GO:0034605 GO:1903936 GO:0034620 GO:0006281 GO:0000165 GO:0006397 GO:0051028 GO:2001033 GO:0031333 GO:0000122 GO:0045931 GO:1900365 GO:0045944 GO:0065003 GO:1900034 GO:0006357 Unknown UniProt Sequence Analysis MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVLDQGQFAKEVLPKYFKHSNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLRSEDIKIRQDSVTKLLTDVQLMKGKQESMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDGGPAHPMPKYGRQYSLEHIHGPGPYPAPSPAYSGSSLYSPDAVTSSGPIISDITELAPGSPVASSGGSVDERPLSSSPLVRVKEEPPSPPQSPRAEGASPGRPSSMVETPLSPTTLIDSILRESEPTPVASTTPLVDTGGRPPSPLPASAPEKCLSVACLDKTELSDHLDAMDSNLDNLQTMLTSHGFSVDTSTLLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPRPLEAEKSSPDSGKQLVHYTAQPLLLLDPGSVDVGSSDLPVLFELGEGSYFSEGDDYSDDPTISLLTGSEPPKAKDPTVS 525 P38529 Heat HSF1 9031 None SL-0198 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}. UNIPROT P38529 UNIPROT I7GGU6 Pfam PF00447 Pfam PF06546 PROSITE PS00434 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}. GO:0005813 GO:0101031 GO:0000785 GO:0005737 GO:0000776 GO:0097431 GO:0097165 GO:0005654 GO:0005634 GO:0048471 GO:0016605 GO:0031490 GO:0001046 GO:0003677 GO:0001228 GO:0003700 GO:0031072 GO:0042803 GO:0043621 GO:0000978 GO:0043565 GO:0071276 GO:0071480 GO:0034605 GO:0006281 GO:0000165 GO:0006397 GO:0051028 GO:2001033 GO:0031333 GO:0000122 GO:1902808 GO:1902751 GO:0008284 GO:0010628 GO:0045931 GO:1900365 GO:0045944 GO:0070207 GO:0006357 GO:0009408 GO:0009416 Unknown UniProt Sequence Analysis MEGPGAAAAAVGAGPGGSNVSAFLTKLWTLVEDPETDPLICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPEKDDTEFQHPYFIRGQEHLLENIKRKVTSVSSIKNEDIKVRQDNVTKLLTDIQVMKGKQESMDSKLIAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSSSAHSMPKYSRQYSLEHVHGSSPYAASSPAYSGSNIYSPDSSTNSGPIISDVTELAQSSPSASPSGSLDERSSPVVRIKEEPPSPSRSPKENEPSTTTAAAGNSTEQPQPQEKCLSVACLDKNELNDHLDTIDSNLDNLQTMLSTHGFSVDTTALLDLFSPSMTVTDMNLPDLDSSLASIQDLLSSQEQQKPSEADAAAADTGKQLVHYTAQPLFLVDSSAVDVGSGDLPIFFELGEGSYFTDGDEYNEDPTISLLSGTEQPKPKDPTVS 491 Q00613 Heat HSF1 9606 None SL-0198 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}. UNIPROT Q00613 UNIPROT A8K4L0 UNIPROT A8MW26 UNIPROT Q53XT4 PDB 2LDU PDB 5D5U PDB 5D5V PDB 5HDG PDB 5HDN PDB 7DCJ PDB 7DCS PDB 7DCT Pfam PF00447 Pfam PF06546 PROSITE PS00434 OMIM 140580 DisGeNET 3297 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}. O60271 EBI-11911387 0.00 P02545 EBI-10682932 0.35 P22392 EBI-9394221 0.35 P63165 EBI-15799774 0.44 P09104 EBI-734427 0.00 Q9UNE7 EBI-7902188 0.40 P49137 EBI-993295 0.60 Q8N0Z6 EBI-7909995 0.40 Q9CQU5 EBI-2556745 0.40 Q81JT7 EBI-2832104 0.00 Q81VE1 EBI-2832111 0.00 P62258 EBI-6994351 0.53 O43529 EBI-3910513 0.37 P26641 EBI-6954536 0.40 Q00534 EBI-5293131 0.44 Q04759 EBI-6512722 0.54 O00505 EBI-9394221 0.64 O95817 EBI-9394221 0.64 O95757 EBI-9394221 0.35 Q9NZL4 EBI-9394221 0.64 Q03933 EBI-9394221 0.73 P04792 EBI-9394221 0.35 O00629 EBI-9394221 0.64 Q9ULV5 EBI-9394268 0.35 P14618 EBI-9355222 0.44 P54645 EBI-10682831 0.40 Q8N4C8 EBI-10816412 0.54 Q5VY09 EBI-10816421 0.59 Q9UKX3 EBI-11141047 0.35 Q53FA3 EBI-12450308 0.35 Q8NET4 EBI-12450281 0.51 Q5VZK9 EBI-12450281 0.51 P34931 EBI-12450281 0.51 O43683 EBI-12450281 0.51 Q96SB8 EBI-12450281 0.51 Q15029 EBI-12450281 0.51 Q8NEH6 EBI-12451193 0.51 P53350 EBI-12451475 0.51 Q9UKN8 EBI-11911558 0.00 Q9UBC2 EBI-11911549 0.00 Q15555 EBI-11911495 0.00 Q14C86 EBI-11911477 0.00 Q14683 EBI-11911468 0.00 Q14566 EBI-11911459 0.00 P61962 EBI-11911450 0.00 P51157 EBI-11911432 0.00 P49736 EBI-11911423 0.00 P33991 EBI-11911405 0.00 Q9Y4E8 EBI-11911567 0.00 Q9Y6Y0 EBI-11911585 0.00 Q9Y6A4 EBI-11911576 0.00 Q8IV03 EBI-21503643 0.35 P11142 EBI-21714606 0.35 O95429 EBI-21788135 0.35 Q00613 EBI-16190425 0.57 P45983 EBI-16203579 0.35 Q96MT8 EBI-21379247 0.00 Q6ZMY6 EBI-25869741 0.56 Q96CM3 EBI-25869733 0.56 Q8NFB2 EBI-25869723 0.56 Q9UIH9 EBI-25869715 0.56 Q13352 EBI-25869705 0.56 Q14693 EBI-25869697 0.56 O14744 EBI-25869689 0.56 Q9UNY5 EBI-25869681 0.56 P11684 EBI-25869673 0.56 GO:0005813 GO:0101031 GO:0000785 GO:0005737 GO:0005829 GO:0000791 GO:0000792 GO:0000776 GO:0097431 GO:0097165 GO:0005654 GO:0005634 GO:0048471 GO:0016605 GO:1990904 GO:0031490 GO:0003677 GO:0001228 GO:0003700 GO:0000981 GO:0001227 GO:0140296 GO:0031072 GO:0051879 GO:0042802 GO:1990841 GO:0046982 GO:0019901 GO:0043621 GO:0000978 GO:0001162 GO:0043565 GO:1990837 GO:0098847 GO:0097677 GO:0000976 GO:0061770 GO:1904385 GO:0071276 GO:0071280 GO:0072738 GO:0071392 GO:0071480 GO:0034605 GO:0070301 GO:1904845 GO:0071222 GO:1904843 GO:0035865 GO:1903936 GO:0034620 GO:0071466 GO:0006952 GO:0006281 GO:0000165 GO:0006397 GO:0009299 GO:0051028 GO:0010667 GO:2001033 GO:0010629 GO:0090084 GO:1901215 GO:0031333 GO:0000122 GO:1902512 GO:0120162 GO:0043280 GO:0051091 GO:0010628 GO:0090261 GO:0045651 GO:1904528 GO:0045931 GO:1900365 GO:0045944 GO:0042531 GO:0065003 GO:1900034 GO:0006357 GO:0014823 GO:1990910 GO:0007584 GO:1990911 GO:0033574 Unknown UniProt Sequence Analysis MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEEPPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPRPPEAENSSPDSGKQLVHYTAQPLFLLDPGSVDTGSNDLPVLFELGEGSYFSEGDGFAEDPTISLLTGSEPPKAKDPTVS 529 P38532 Heat Hsf1 10090 None SL-0198 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}. UNIPROT P38532 UNIPROT O70462 Pfam PF00447 Pfam PF06546 PROSITE PS00434 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}. Q9UNE7 EBI-7902106 0.44 P11142 EBI-7902157 0.44 Q969M3 EBI-11091232 0.35 O75665 EBI-11091232 0.35 Q9UP38 EBI-11091232 0.35 Q9HDC5 EBI-11091232 0.35 Q8TDY2 EBI-11091232 0.35 Q8WYQ5 EBI-11091232 0.35 O75771 EBI-11091232 0.35 Q4VC44 EBI-11091232 0.35 Q13573 EBI-11091232 0.35 P19404 EBI-11091232 0.35 Q9UHR4 EBI-11091232 0.35 GO:0005813 GO:0101031 GO:0005737 GO:0005829 GO:0000791 GO:0000792 GO:0000776 GO:0097431 GO:0097165 GO:0005654 GO:0005634 GO:0048471 GO:0016605 GO:0045120 GO:0032991 GO:1990904 GO:0003682 GO:0031490 GO:0003677 GO:0001228 GO:0003700 GO:0000981 GO:0001227 GO:0140296 GO:0031072 GO:0051879 GO:0042802 GO:1990841 GO:0046982 GO:0019901 GO:0043621 GO:0000978 GO:0001162 GO:0043565 GO:1990837 GO:0098847 GO:0097677 GO:0000976 GO:0061770 GO:0008283 GO:0071230 GO:1904385 GO:0071276 GO:0071280 GO:0072738 GO:0071392 GO:0071480 GO:0034605 GO:0070301 GO:0071407 GO:0071478 GO:1903936 GO:0034620 GO:0006952 GO:0006281 GO:0001892 GO:0060136 GO:0050673 GO:0007143 GO:0001701 GO:0000165 GO:0006397 GO:0009299 GO:0051028 GO:0010667 GO:2001033 GO:0050680 GO:0010629 GO:0090084 GO:1901215 GO:0031333 GO:0000122 GO:0032720 GO:1902512 GO:0008284 GO:0120162 GO:0043280 GO:0051091 GO:0010628 GO:0090261 GO:0045651 GO:1904528 GO:0045931 GO:1900365 GO:0040018 GO:0045944 GO:0061408 GO:0042531 GO:0006468 GO:0065003 GO:1900034 GO:0006357 GO:0032355 GO:0009408 GO:0032496 GO:0033574 GO:0007283 Unknown UniProt Sequence Analysis MDLAVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTRLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLSDSNSAHSVPKYGRQYSLEHVHGPGPYSAPSPAYSSSSLYSSDAVTSSGPIISDITELAPTSPLASPGRSIDERPLSSSTLVRVKQEPPSPPHSPRVLEASPGRPSSMDTPLSPTAFIDSILRESEPTPAASNTAPMDTTGAQAPALPTPSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLTSHGFSVDTSALLDLFSPSVTMPDMSLPDLDSSLASIQELLSPQEPPRPIEAENSNPDSGKQLVHYTAQPLFLLDPDAVDTGSSELPVLFELGESSYFSEGDDYTDDPTISLLTGTEPHKAKDPTVS 525 P11147 Heat Hsc70 7227 None SL-0198 Cytoplasm, perinuclear region. Nucleus. Note=Localized to a meshwork of cytoplasmic fibers around the nucleus. Translocates to the nucleus after thermal stress. UNIPROT P11147 UNIPROT Q3KN45 UNIPROT Q8SXQ4 UNIPROT Q9VFB0 Pfam PF00012 PROSITE PS00297 PROSITE PS00329 PROSITE PS01036 O96757 EBI-75193 0.37 Q9VI55 EBI-208882 0.00 Q9VMA3 EBI-211214 0.00 Q9VNV2 EBI-215710 0.00 Q9VLI5 EBI-222379 0.00 Q9VVC2 EBI-226363 0.00 Q9VRQ6 EBI-228980 0.00 Q9VC50 EBI-231555 0.00 Q9VJB0 EBI-241955 0.00 Q9VIY9 EBI-250829 0.00 Q8IR79 EBI-254487 0.00 Q9W3N7 EBI-255184 0.00 Q9VNE0 EBI-259860 0.00 Q9I7H9 EBI-262585 0.00 Q9VU81 EBI-265621 0.00 Q8IRH9 EBI-266258 0.00 Q9VLG9 EBI-268283 0.00 Q24216 EBI-268762 0.00 Q9W5G1 EBI-271186 0.00 Q9V3F2 EBI-272607 0.00 Q9XYW6 EBI-273001 0.00 P40301 EBI-273005 0.00 Q7JXC4 EBI-273009 0.00 Q9VUQ1 EBI-273014 0.00 Q5BI03 EBI-273022 0.00 Q9W0B2 EBI-273018 0.00 Q9VRV9 EBI-273026 0.00 Q9VIJ0 EBI-273030 0.00 P29413 EBI-273034 0.00 Q9XZC2 EBI-507718 0.37 Q24570 EBI-508174 0.37 Q9VZF4 EBI-508300 0.37 Q9VWE4 EBI-508930 0.37 Q9VML8 EBI-512430 0.37 Q9VRQ2 EBI-468896 0.00 Q03751 EBI-872154 0.27 P83949 EBI-878253 0.48 P25439 EBI-1368536 0.40 Q24459 EBI-7591079 0.35 P42124 EBI-7591102 0.35 Q24133 EBI-2110992 0.37 P92177 EBI-8283416 0.35 O97143 EBI-15878339 0.35 Q24592 EBI-16151646 0.35 GO:0071013 GO:0005737 GO:0005829 GO:0005634 GO:0005726 GO:0048471 GO:0005886 GO:0071011 GO:0098793 GO:0005524 GO:0016887 GO:0140662 GO:0051087 GO:0031072 GO:0051787 GO:0044183 GO:0051082 GO:0007411 GO:0007413 GO:0035967 GO:0034620 GO:0051085 GO:0061077 GO:0061738 GO:0097753 GO:0000398 GO:0007399 GO:0007269 GO:0030707 GO:0035194 GO:0042026 GO:0070922 GO:0016192 Unknown UniProt Sequence Analysis MSKAPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTQTIFDAKRLIGRKFDDAAVQSDMKHWPFEVVSADGKPKIEVTYKDEKKTFFPEEISSMVLTKMKETAEAYLGKTVTNAVITVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKAVGERNVLIFDLGGGTFDVSILSIDDGIFEVKSTAGDTHLGGEDFDNRLVTHFVQEFKRKHKKDLTTNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGTDFYTSITRARFEELNADLFRSTMDPVEKALRDAKLDKSVIHDIVLVGGSTRIPKVQRLLQDLFNGKELNKSINPDEAVAYGAAVQAAILHGDKSQEVQDLLLLDVTPLSLGIETAGGVMSVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVTALERSTNKENKITITNDKGRLSKEDIERMVNEAEKYRNEDEKQKETIAAKNGLESYCFNMKATLDEDNLKTKISDSDRTTILDKCNETIKWLDANQLADKEEYEHRQKELEGVCNPIITKLYQGAGFPPGGMPGGPGGMPGAAGAAGAAGAGGAGPTIEEVD 651 Q61W58 Heat daf 6238 None SL-0198 Cytoplasm, perinuclear region. Note=Perinuclear region of somatic cells. {ECO:0000250}. UNIPROT Q61W58 UNIPROT A8WXX6 Pfam PF02518 Pfam PF00183 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}. GO:0005829 GO:1990565 GO:0048471 GO:0005886 GO:0032991 GO:0005524 GO:0016887 GO:0140662 GO:0097718 GO:0042802 GO:0035259 GO:1990634 GO:0051082 GO:0007049 GO:0034605 GO:0061077 GO:0006935 GO:0040024 GO:0050829 GO:0008340 GO:0032516 GO:0006470 GO:0006611 GO:0006457 GO:0050821 GO:0050920 GO:0045859 Unknown UniProt Sequence Analysis MSENAETFAFQAEIAQLMSLIINTFYSNKEIYLRELISNASDALDKIRYQALTEPSELDTGKELFIKITPNKEEKTLTIMDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAFLVADKVVVTSKNNDDDSYQWESSAGGSFVVRPYNDPELTRGTKITMYIKEDQVDFLEERKIKEIVKKHSQFIGYPIKLVVEKEREKEVEDEEAVESKDEEKKEGDVENVGEDADAEKDKKKTKKIKEKYFEDEELNKTKPIWTRNPDDISNEEYAEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFAPQRAPFDLFENKKSKNSIKLYVRRVFIMENCEELMPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCMELFDEIAEDKDNFKKFYEQFGKNLKLGIHEDSTNRKKLSEFLRYATSAGEEPTSLKEYVSRMKENQTQIYYITGESKEVVAASAFVERVKSRGFEVLYMCDPIDEYCVQQLKEYDGKKLVSVTKEGLELPETEEEKKKFEEDKVAYENLCKVIKDILEKKIEKVAVSNRLVSSPCCIVTSEYGWSANMERIMKAQALRDSSTMGYMAAKKHLEINPDHAIMKTLRERVEADKNDKTVKDLVVLLFETALLSSGFSLEEPQSHASRIYRMIKLGLDIGDEDIEESAVPSSCTAEAKIEGADEDASRMEEVD 706 Q18688 Heat daf 6239 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:12950278}. Note=Perinuclear region of somatic cells. UNIPROT Q18688 PDB 4GQT PDB 4I2Z Pfam PF02518 Pfam PF00183 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}. G5EG62 EBI-8086780 0.74 P02566 EBI-8086901 0.61 G5EGG2 EBI-336695 0.37 Q21829 EBI-339860 0.37 Q03563 EBI-332975 0.00 Q9XVV3 EBI-333605 0.00 O76840 EBI-334535 0.00 Q20308 EBI-337241 0.00 O17218 EBI-338108 0.00 O17927 EBI-338816 0.00 P45897 EBI-340136 0.00 G5EFL5 EBI-341354 0.00 O02108 EBI-6460076 0.55 Q9XWG3 EBI-344915 0.00 P90978 EBI-345344 0.00 Q27535 EBI-345398 0.00 P20792 EBI-360290 0.51 Q18688 EBI-360299 0.63 P50488 EBI-360536 0.37 Q20234 EBI-2916414 0.00 Q11184 EBI-3864453 0.51 O16259 EBI-6514170 0.66 P09446 EBI-6918699 0.40 P34447 EBI-21396671 0.40 GO:0101031 GO:0005737 GO:0005829 GO:1990565 GO:0045121 GO:0048471 GO:0005886 GO:0008287 GO:0032991 GO:0005524 GO:0016887 GO:0140662 GO:0097718 GO:0042802 GO:0035259 GO:1990634 GO:0051082 GO:0007049 GO:0034605 GO:0061077 GO:0006935 GO:0040024 GO:0050829 GO:0008340 GO:0002119 GO:0032516 GO:0006470 GO:0006611 GO:0006457 GO:0022417 GO:0050821 GO:0050920 GO:0045859 GO:0009408 Unknown UniProt Sequence Analysis MSENAETFAFQAEIAQLMSLIINTFYSNKEIYLRELISNASDALDKIRYQALTEPSELDTGKELFIKITPNKEEKTLTIMDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAFLVADKVVVTSKNNDDDSYQWESSAGGSFVVRPFNDPEVTRGTKIVMHIKEDQIDFLEERKIKEIVKKHSQFIGYPIKLVVEKEREKEVEDEEAVEAKDEEKKEGEVENVADDADKKKTKKIKEKYFEDEELNKTKPIWTRNPDDISNEEYAEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPQRAPFDLFENKKSKNSIKLYVRRVFIMENCEELMPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCMELIDEVAEDKDNFKKFYEQFGKNLKLGIHEDSTNRKKLSDFLRYSTSAGDEPTSLKEYVSRMKENQTQIYYITGESKDVVAASAFVERVKSRGFEVLYMCDPIDEYCVQQLKEYDGKKLVSVTKEGLELPETEEEKKKFEEDKVAYENLCKVIKDILEKKVEKVGVSNRLVSSPCCIVTSEYGWSANMERIMKAQALRDSSTMGYMAAKKHLEINPDHAIMKTLRDRVEVDKNDKTVKDLVVLLFETALLASGFSLEEPQSHASRIYRMIKLGLDIGDDEIEDSAVPSSCTAEAKIEGAEEDASRMEEVD 702 A1YER2 Oxidoreductase HTATIP2 9595 None SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT A1YER2 Pfam PF13460 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}. GO:0005737 GO:0005829 GO:0005635 GO:0016491 GO:0004674 GO:0001525 GO:0006915 GO:0030154 GO:0051170 GO:0043068 GO:0045944 GO:0046777 GO:0045765 Unknown UniProt Sequence Analysis MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYASAFQGHDVGFCCLGTTRGKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSKFLYLQVKGEVEAKVEELKFDRYSVFRPGVLLCDRQESRPGEWLVRKFFGSLPESWASGHSVPVVTVVRAMLNNVVRPRDKQMELLENKAIHDLGKAHGSLKP 242 Q9BUP3 Oxidoreductase HTATIP2 9606 None SL-0178 Cytoplasm {ECO:0000269|PubMed:15282309}. Nucleus envelope {ECO:0000269|PubMed:15282309}. UNIPROT Q9BUP3 UNIPROT A8K7S7 UNIPROT D3DQY8 UNIPROT O15383 UNIPROT O60520 UNIPROT O95345 UNIPROT Q53GC1 UNIPROT Q53GG2 UNIPROT Q6IBI3 PDB 2BKA Pfam PF13460 OMIM 605628 DisGeNET 10553 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}. Q5JX71 EBI-24643959 0.56 Q9NQG6 EBI-24671087 0.56 Q08426 EBI-24683997 0.56 Q8N6M3 EBI-24694273 0.56 Q86VR2 EBI-24700038 0.56 Q8NBQ5 EBI-24722966 0.56 Q99541 EBI-24727205 0.56 Q12893 EBI-24741240 0.56 Q9H6H4 EBI-24754940 0.56 Q3KNW5 EBI-23834757 0.56 O00258 EBI-24780762 0.56 Q9HDC5 EBI-24570639 0.56 Q9UKF7 EBI-24650569 0.56 Q8TB40 EBI-24758449 0.56 Q9Y371 EBI-24759832 0.56 Q9Y320 EBI-25185978 0.56 Q13520 EBI-25202074 0.56 Q9H2K0 EBI-24799964 0.56 Q8N5M9 EBI-25270050 0.56 P03427 EBI-14405248 0.35 Q53F39 EBI-21694305 0.35 Q9Y2J4 EBI-21884579 0.35 Q9HCD5 EBI-21884579 0.35 Q13510 EBI-21884579 0.35 O75208 EBI-21930142 0.35 P54852 EBI-21194685 0.54 P0DTD8 EBI-25687199 0.35 Q7TFA1 EBI-25688644 0.35 GO:0005737 GO:0005829 GO:0016020 GO:0005635 GO:0005634 GO:0016491 GO:0004674 GO:0003713 GO:0001525 GO:0006915 GO:0030154 GO:0051170 GO:0043066 GO:0043068 GO:0045944 GO:0046777 GO:0045765 GO:0006357 Unknown UniProt Sequence Analysis MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYASAFQGHDVGFCCLGTTRGKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSNFLYLQVKGEVEAKVEELKFDRYSVFRPGVLLCDRQESRPGEWLVRKFFGSLPDSWASGHSVPVVTVVRAMLNNVVRPRDKQMELLENKAIHDLGKAHGSLKP 242 Q9Z2G9 Oxidoreductase Htatip2 10090 None SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT Q9Z2G9 UNIPROT Q810Y5 UNIPROT Q99KN6 UNIPROT Q9D5F8 UNIPROT Q9D804 PDB 2FMU Pfam PF13460 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}. GO:0005737 GO:0005829 GO:0005635 GO:0051287 GO:0016620 GO:0004674 GO:0001525 GO:0006915 GO:0030154 GO:0051170 GO:0043068 GO:0045944 GO:0046777 GO:0045765 Unknown UniProt Sequence Analysis MADKEALPKLREDFKMQNKSVFILGASGETGKVLLKEILGQNLFSKVTLIGRRKLTFEEEAYKNVNQEVVDFEKLDVYASAFQGHDVGFCCLGTTRSKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSRGADKSSSFLYLQVKGEVEAKVEELKFDRLSVFRPGVLLCDRQESRPGEWLARKFFGSLPDSWASGYAVPVVTVVRAMLNNLVSPSSGQMELLENKAILHLGKDRDVPKL 242 A1YFX9 Oxidoreductase HTATIP2 9597 None SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT A1YFX9 Pfam PF13460 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}. GO:0005737 GO:0005635 GO:0051287 GO:0016620 GO:0001525 GO:0006915 GO:0030154 Unknown UniProt Sequence Analysis MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYASAFQGHDVGFCCLGTTRGKAGAEGFARVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSNFLYLQVKGEVEAKVEELKFDRYSVFRPGVXLCDRQESRPGEWLVRKFFGSLPDSWASGHSVPVVTVVRAMLNNVVRPRDKQMELLENKAIHDLGKAHGSLKP 242 A2T7G9 Oxidoreductase HTATIP2 9600 None SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT A2T7G9 Pfam PF13460 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}. GO:0005737 GO:0005635 GO:0051287 GO:0016620 GO:0001525 GO:0006915 GO:0030154 Unknown UniProt Sequence Analysis MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYASAFQGHDVGFCCLGTTRVKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSNFLYLQVKGEVEAKVEELKFDRYSVFRPGVLLCDRQESRPGEWLVRKFFGSLPESWASGYSVPVVTVVRAMLNNMVRPRDKQMELLENKAIHDLGKVHGSLKP 242 Q9P2D3 HEAT HEATR5B 9606 None SL-0198 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}. UNIPROT Q9P2D3 UNIPROT B5MDU8 UNIPROT Q7Z3B2 UNIPROT Q9NVL7 OMIM 619627 DisGeNET 54497 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}. Q9P0L0 EBI-21550773 0.35 A0A6H3A739 EBI-2832030 0.00 P56377 EBI-11037753 0.35 Q6P5F9 EBI-11603310 0.35 P26045 EBI-14024867 0.42 O95292 EBI-21550215 0.35 O14965 EBI-21639587 0.35 Q9Y6Q5 EBI-21760726 0.35 Q14160 EBI-20731245 0.44 Q12959 EBI-20731998 0.44 O00213 EBI-21017901 0.35 P03372 EBI-21301141 0.35 GO:0030136 GO:0005829 GO:0030139 GO:0043231 GO:0016020 GO:0016607 GO:0048471 GO:0006897 GO:0008104 GO:0015031 GO:0042147 Unknown UniProt Sequence Analysis MELAHSLLLNEEALAQITEAKRPVFIFEWLRFLDKVLVAANKTDVKEKQKKLVEQLTGLISSSPGPPTRKLLAKNLAALYSIGDTFTVFQTLDKCNDIIRNKDDTAAYLPTKLAAVACVGAFYEKMGRMLGSAFPETVNNLLKSLKSAESQGRSEILMSLQKVLSGLGGAAASSHRDIYKNARSLLTDRSMAVRCAVAKCLLELQNEAVFMWTAELENIATLCFKALENSNYGVRVAVSKLLGTVMATALMPKQATVMRQNVKRATFDEVLELMATGFLRGGSGFLKSGGEMLKVGGSVNREVRVGVTQAYVVFVTTLGGQWLERSFATFLSHVLDLVSHPRATQTHVEAVYSRRCVSFILRATVGSLLGEKAQIAAAKEICQAIGKQMKAVEAVVNDTSGENKSGAADIAASQHVMVCALQELGSLVQSLNATASPLIQEASIGLLEIVTSVLLHPSMAARLAAAWCLRCVAVALPFQLTPFLDRCAERLNNLKTSPEAVSGYSFAMAALLGGVHQCPLGIPHAKGKMVVSIAEDLLRTAAQNSRLSLQRTQAGWLLLGALMTLGPSVVRYHLPKMLLLWRNVFPRSLKELEAEKARGDSFTWQVTLEGRAGALCAMRSFVAHCPELLTEDVIRKLMTPIECAMTMMSHIPSVMKAHGAHLKASAAMVRLRLYDILALLPPKTYEGSFNALLRELVAEFTLTDNSANTTTSLLRSLCHYDDSVLLGSWLQETDHKSIEDQLQPNSASGSGALEHDPSSIYLRIPAGEAVPGPLPLGVSVIDASVALFGVVFPHVSYKHRLQMLDHFAECVKQAKGVRQQAVQLNIFTAVLSALKGLAENKSTLGPEEVRKSALTLVMGPLDNPNPILRCAAGEALGRMAQVVGEATFIARMAQYSFDKLKSARDVVSRTGHSLALGCLHRYVGGIGSGQHLKTSVSILLALAQDGTSPEVQTWSLHSLALIVDSSGPMYRGYVEPTLSLVLTLLLTVPPSHTEVHQCLGRCLGAIITTVGPELQGNGATTSTIRSSCLVGCAITQDHSDSLVQAAAISCLQQLHMFAPRHVNLSSLVPSLCVHLCSSHLLLRRAAVACLRQLAQREAAEVCEYAMSLAKNTGDKESSSANVSPFAPGVSSRTDIHCRHQGVNITETGLEGLLFGMLDRETDRKLCSDIHDTLGHMLSSLAVEKLSHWLMLCKDVLAASSDMSTATLLSSGKDEEAEKKDEMDDDTMFTTLGEEDKSKPFVAPRWATRVFAADCLCRIINLCENADQAHFDLALARSAKLRNPTNDLLVLHLSDLIRMAFMAATDHSNQLRMAGLQALEDIIKKFASVPEPEFPGHVILEQYQANVGAALRPAFSQDTPSDIIAKACQVCSTWIGSGVVSDLNDLRRVHNLLVSSLDKVQAGKGSSSQLYRESATTMEKLAVLKAWAEVYVVAMNIKKEAESKPKRAIKNTDDDDDDCGTIDELPPDSLITLVQPELPTLSRLWLAALKDYALLTLPAEFSSQLPPDGGAFYTPETIDTARLHYRNSWAPILHAVALWLNSTGFTCSESTEAAAISGLQKRSTSVNLNQASGAVGSAKSLPEINKDRMHLILGVSIQFLCSPRPEEPIEHVTACLQALHTLLDSPYARVHIAEDQLIGVELLSVLHRLLLTWNPSSVQLLVTGVVQQIVRAAQDYLQEKRNTLNEDDMEKEACTVLGEGGDSGGLIPGKSLVFATMELLMFILVRHMPHLSTKVSDSPSHIATKTRLSEESARLVAATVTILSDLPSLCSPAGCMTILPTILFLIARILKDTAIKSADNQVPPPVSAALQGIKSIVTLSMAKTEAGVQKQWTALIRSTLACILEYSQPEDSVPTPDEVSMLTAIALFLWSASNEIIGVQSLQNGCMNRFKNALNSCDPWVQAKCYQLLLSVFQHSNRALSTPYIHSLAPIVVEKLKAVERNRPASNIELLAVQEGIKVLETLVALGEEQNRVQLLALLVPTLISYLLDENSFASASSASKDLHEFALQNLMHIGPLYPHAFKTVMGAAPELKVRLETAVRASQASKAKAAARQPAPAIHSAPTIKLKTSFF 2071 Q8C547 HEAT Heatr5b 10090 None SL-0198 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}. UNIPROT Q8C547 UNIPROT Q3TPS4 UNIPROT Q5DTY0 UNIPROT Q5PRF1 UNIPROT Q8C6W1 UNIPROT Q8C773 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}. P61027 EBI-11567802 0.35 P62158 EBI-911456 0.35 GO:0030136 GO:0005829 GO:0030139 GO:0043231 GO:0016607 GO:0048471 GO:0006897 GO:0008104 GO:0015031 GO:0042147 Unknown UniProt Sequence Analysis MELAHSLLLNEEALAQITEAKRPVFIFEWLRFLDKVLVAANKTDVKEKQKKLVEQLTGLISSSPGPPTRKLLAKNLAALYSIGDTYTVFQTLDKCNDIIRSKDDTAAYLPTKLAAVACVGAFYEKMGRMLGSAFPETVNNLLKSLKSAESQGRSEILMSLQKVLTGLGGAAASSHRDIYKNARSLLTDRSMAVRCAVAKCLLELQNEAVFMWTAELENVATLCFKALENSNYGVRVAVSKLLGTVMATALMPKQATVMRQNVKRATFDEVLELMATGFLRGGSGFLKSGGEMLKVGGSVNREVRVGVTQAYVVFVTTLGGQWLERSFATFLSHVLDLVSHPRATQTHVDAVYSRRCVSFMLRATVGSLLGEKAQIAAAKEICQAIGKQMKAVEAVVNDTSSENKSGTADIAASQHVMVCALQELGSLVQSLNATASPLIQEASIGLLEIVTSVLLHPSMAARLAAAWCLRCVAVALPFQLTPFLDRCAERLNNLKTSPEAVSGYSFAMAALLGGVHQCPLGIPHAKGKMVVSIAEDLLRTAAQNSRLSLQRTQAGWLLLGALMTLGPSVVRYHLPKMLLLWRNVFPRSLKELEAEKARGDSFTWQVTLEGRAGALCAMRSFVAHCPELLTEDAIRKLMTPIECAMTMMSHIPSVIKAHGAHLKASAAMVRLRLYDILALLPPKTYEGSFNALLRELVAEFTLTDNSANTTTSLLRSLCHYDDSVLLGSWLQETDHKSIEDQLQPNSASGSGALEHDPSSIYLRIPAGEAVPGPLPLGVSVIDASVALFGVVFPHVSYKHRLQMLDHFAECVKQAKGVRQQAVQLNIFTAVLSALKGLAENKSTLGPEEVRKSALTLVMGALDNPNPILRCAAGEALGRMAQVVGEASFIARMAQYSFDKLKSARDVVSRTGHSLALGCLHRYVGGIGSGQHLKTSVSILLALAQDGTSPEVQTWSLHSLALIVDSSGPMYRGYVEPTLSLVLTLLLTVPPSHTEVHQCLGRCLGAIITTVGPELQGNAATISTIRSSCLVGCAITQDHSDSLVQAAAISCLQQLHMFAPRHVNLSSLVPSLCVHLCSSHLLLRRAAVACLRQLAQREAAEVCEYAMSLAKNAGDKEISGGNVNPFTPGVSSRSDVHCRHQGVNITDTGLEGLLFGMLDRETDRKLCSDIHDTLGHMLSSLAVEKLSHWLMLCKDVLAASSDMSAATLLSSGKDEESEKKDEMDDDAMFTTLGEEDKSKPFVAPRWATRVFAADCLCRIINLCENSDQAHFDLALARSAKLRNPKNDLLVLHLSDLIRMAFMAATDHSNQLRMAGLQALEDIIKKFASVPEPEFPGHVILEQYQANVGAALRPAFSQDTPSDIIAKACQVCSTWIGSGVVSDLNDLRRVHNLLVSSLDTVQAGKGSSSQLYRESATTMEKLAVLKAWAEVYVVAMNIKKEAESKPKRAMNNPDDDDDDYGTIDELPPDSLITLVQPELPTLSRLWLAALKDYALLTLPAEFSSQLPPDGGAFYTPETIDTARLHYRNSWAPILHAVALWLNSTGFISQESTEATTVSGVQKRSPAVSLNQVPGAMASAKPLPEVNKDRMHLILGVSIQFLCSPRPEEPIEHVTACLQALHTLLGSPYARIHIAEDQLIGVELLSVLHRLLLTWNPPSIQLLVTGVVQQIVRAAQDYLQEKRNALNEEDMEKESCPTLGEGGDTGGLIPGKSLVFATMELLMFILVRHMPHLSTKMLDSPSHTAMKTQLSEESARLVAATVAILSDLPSLCSPAGCMTILPTILFLIARILKDTAIKSADNQVPPPVSAALQGIKSIVTLSMAKTEDTQKQWTTLIRSTLACILEYSQPDDCMPAPDEVSTLTAIALFLWSASSEIIGVQSLQNGCMNRFKSALNSCDPWVQAKCYQLLLSVFQHSNRALSTPYIHSLAPLVVGKLKAVERHRPASSTELLAVQEGIKVLETLVALGEEQNRVQLLALLVPTLISYLLDENSFASASSISKDLHEFALQNLMHIGPLYPHAFKTVMGAAPELKARLETAVRASQASKAKAAARQPAPTTHSTPTIKLKTSFF 2070 Q13261 Soluble IL15RA 9606 None SL-0178 SL-0182 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}. UNIPROT Q13261 UNIPROT B4E2C2 UNIPROT Q3B769 UNIPROT Q5JVA1 UNIPROT Q5JVA2 UNIPROT Q5JVA4 UNIPROT Q6B0J2 UNIPROT Q7LDR4 UNIPROT Q7Z609 PDB 2ERS PDB 2Z3Q PDB 2Z3R PDB 4GS7 PROSITE PS50923 OMIM 601070 DisGeNET 3601 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}. O95999 EBI-3910825 0.37 P11802 EBI-3906693 0.37 P40933 EBI-980314 0.66 P24941 EBI-3906648 0.37 P35243 EBI-3910805 0.37 O14936 EBI-3910815 0.37 Q8N2W9 EBI-3918941 0.37 P14784 EBI-6858800 0.59 P31785 EBI-6858800 0.52 GO:0009986 GO:0030659 GO:0005789 GO:0005768 GO:0005615 GO:0000139 GO:0016021 GO:0031965 GO:0005886 GO:0004896 GO:0042010 GO:0019901 GO:0035723 GO:0001779 GO:0032825 GO:0050766 Transmembrane UniProt Sequence Analysis {ECO:0000255} MAPRRARGCRTLGLPALLLLLLLRPPATRGITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPAASSPSSNNTAATTAAIVPGSQLMPSKSPSTGTTEISSHESSHGTPSQTTAKNWELTASASHQPPGVYPQGHSDTTVAISTSTVLLCGLSAVSLLACYLKSRQTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL 267 Q60819 Soluble Il15ra 10090 None SL-0178 SL-0182 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}. UNIPROT Q60819 UNIPROT A2AP35 UNIPROT A2AP36 UNIPROT A2AP37 UNIPROT Q80Z90 UNIPROT Q80Z91 UNIPROT Q80Z92 UNIPROT Q8R5E4 PDB 2PSM Pfam PF00084 PROSITE PS50923 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}. GO:0009986 GO:0031410 GO:0005615 GO:0016021 GO:0031965 GO:0005886 GO:0042010 GO:0019901 GO:0035723 GO:0001779 GO:0010977 GO:0032825 GO:0050766 GO:0007259 Transmembrane UniProt Sequence Analysis {ECO:0000255} MASPQLRGYGVQAIPVLLLLLLLLLLPLRVTPGTTCPPPVSIEHADIRVKNYSVNSRERYVCNSGFKRKAGTSTLIECVINKNTNVAHWTTPSLKCIRDPSLAHYSPVPTVVTPKVTSQPESPSPSAKEPEAFSPKSDTAMTTETAIMPGSRLTPSQTTSAGTTGTGSHKSSRAPSLAATMTLEPTASTSLRITEISPHSSKMTKVAISTSVLLVGAGVVMAFLAWYIKSRQPSQPCRVEVETMETVPMTVRASSKEDEDTGA 263 Q8R412 Interferon Ifi27l2a 10090 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000305|PubMed:22427340}; Multi-pass membrane protein {ECO:0000255}. UNIPROT Q8R412 Pfam PF06140 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}. GO:0016021 GO:0031966 GO:0005739 GO:0005635 GO:0005637 GO:0042802 GO:0007568 GO:0097190 GO:0009615 Transmembrane UniProt Sequence Analysis {ECO:0000255} MLGTLFGSAIGGALAVAGAPVALAAMGFTGTGIAAASIAAKMMSAAAIANGGGVAAGSLVATLQSAGVLGLSTSTNAILGAAGAAVGALL 90 O42254 Insulin-like IGF2BP1 9031 None SL-0198 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. UNIPROT O42254 PDB 2N8L PDB 2N8M Pfam PF00013 Pfam PF00076 PROSITE PS50084 PROSITE PS50102 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}. GO:0070937 GO:0005737 GO:0010494 GO:0005829 GO:0030175 GO:0030426 GO:0030027 GO:0005634 GO:0000932 GO:0048471 GO:0003730 GO:0003729 GO:1990247 GO:0070934 GO:0051028 GO:0017148 GO:0007399 GO:0010976 GO:0010468 GO:0051252 Unknown UniProt Sequence Analysis MNKLYIGNLNESVTPADLEKVFNDHKISFSGQFLVKSGYAFVDCPDEQWAMKAIETFSGKVELHGKQLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDGLLAQYGTVENCEQVNTDSETAVVNVTYTNREQTRQAIMKLNGHQLENHVLKVSYIPDEQSVQGPENGRRGGFGARGAPRQGSPVTAGAPVKQQPVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISIHSTPEGCSAACKMILEIMQKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGSIENCCKAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSNAVPPPPSSVSGAAPYSSFMPPEQETVHVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVVITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENEQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSGQLQARRK 576 Q08CK7 Insulin-like igf2bp1 7955 None SL-0198 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}. UNIPROT Q08CK7 Pfam PF00013 Pfam PF00076 PROSITE PS50084 PROSITE PS50102 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}. GO:0070937 GO:0005737 GO:0010494 GO:0005829 GO:0030175 GO:0030426 GO:0030027 GO:0005634 GO:0000932 GO:0048471 GO:0003730 GO:0003729 GO:1990247 GO:0070934 GO:0051028 GO:0007399 GO:0003407 GO:0010468 GO:0051252 GO:0006417 Unknown UniProt Sequence Analysis MNKLYIGNLNEKVTAEDLVKTFEDYKIPYSGQFLMKTGYASVDCPDDQWAMKAIETFSGKVELHGKRIEVEHSVPKKQRTRKLQIRNIPPHLQWEVLDGLLAQYGTVENCEQVNTDSETAVVNVTYGTREQARQAIQKLNGYQFDNNALRVSYIPDENSEVDSQRGPDNGRRPGYGPRGTSRQMSPGSGIPSKHQHADIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKPISIHSTPEGCSAACRMILEIMNQEAKDTKTADEVPLKVLAHNNFVGRLIGKEGRNLKKVEQDTDTKITISPLQDLTLYNPERTITVKGSIEACCLAEQEIMKKVREAYDNDIAAMNQQTHLIPGLNLGAIGLFPPSSAMPPPALGNSVPGPPYGPMGASEQETVHVYIPAQAVGALIGKKGQHIKQLSRFAGASIKIAPAEAPDSKMRMVIVTGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIKVAAAAAGRVIGKGGKTVNELQNLTAAEVVVPREQTPDEHDQVIVKIIGHFYASQLAQRKIRDILTQVKQQQKGGGMGTPQGPHPQGMTELGSPQGLAQEPRRK 598 Q9NZI8 Insulin-like IGF2BP1 9606 None SL-0198 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}. UNIPROT Q9NZI8 UNIPROT C9JT33 PDB 3KRM PDB 6QEY Pfam PF00013 Pfam PF00076 PROSITE PS50084 PROSITE PS50102 OMIM 608288 DisGeNET 10642 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}. O75569 EBI-1081716 0.00 P42704 EBI-13949271 0.35 Q06787 EBI-26367348 0.35 Q8NC51 EBI-13949271 0.35 Q92905 EBI-21325777 0.35 Q9NX58 EBI-1059651 0.00 P62633 EBI-1060912 0.00 Q9UHX1 EBI-1061218 0.00 Q9NRG4 EBI-1063796 0.00 P49841 EBI-1064100 0.00 P78330 EBI-1064352 0.00 Q9UET6 EBI-1067710 0.00 Q13418 EBI-1076453 0.00 P01889 EBI-1076582 0.00 Q14164 EBI-1082794 0.00 P52565 EBI-1084000 0.00 P01106 EBI-1237540 0.35 Q9UL18 EBI-7641579 0.35 Q9UKV8 EBI-7642941 0.35 P32121 EBI-1642567 0.35 Q9HCK5 EBI-2269711 0.35 P62960 EBI-2560211 0.40 Q9H492 EBI-3044058 0.35 Q9GZQ8 EBI-3045543 0.35 P60520 EBI-3046676 0.35 Q9H0R8 EBI-3048562 0.35 O95166 EBI-3050465 0.35 O95503 EBI-3951754 0.35 Q9HC52 EBI-3951861 0.35 P62993 EBI-3964621 0.35 Q6QDQ4 EBI-5276631 0.35 P67809 EBI-5325180 0.58 P03496 EBI-6154589 0.35 Q99AU3 EBI-6157083 0.35 O56264 EBI-6157161 0.35 P04487 EBI-6157560 0.35 D1LN35 EBI-6159328 0.35 P19320 EBI-6189915 0.35 Q5U5Q3 EBI-8011718 0.35 Q86VP6 EBI-21322532 0.35 Q13616 EBI-21323857 0.35 Q13619 EBI-21324822 0.35 Q13617 EBI-21327106 0.35 Q13620 EBI-21327757 0.35 Q15843 EBI-21328206 0.35 Q13618 EBI-21329068 0.35 Q93034 EBI-21331078 0.35 Q4VGL6 EBI-8759371 0.35 P0C090 EBI-8759987 0.35 P41218 EBI-9996028 0.35 P19838 EBI-11322719 0.35 P05412 EBI-11324725 0.35 P03211 EBI-11722110 0.35 Q6VGS8 EBI-11733617 0.35 F8VQC1 EBI-11054725 0.35 Q00839 EBI-11088773 0.58 P60229 EBI-11148789 0.35 P19712 EBI-10901375 0.35 Q6P5F9 EBI-11603310 0.35 Q9UBX2 EBI-11601780 0.35 O00571 EBI-13949286 0.35 O95793 EBI-13949286 0.54 Q15366 EBI-13949405 0.43 Q9NUL3 EBI-13949405 0.35 Q15717 EBI-13949405 0.43 Q12906 EBI-13949405 0.35 P11940 EBI-13949405 0.35 Q9UKA9 EBI-13949405 0.35 O60506 EBI-13949405 0.43 Q08211 EBI-13949405 0.43 P0DJD3 EBI-13949271 0.35 P51991 EBI-13949271 0.35 P61978 EBI-13949271 0.35 Q99729 EBI-13949271 0.35 Q01826 EBI-13949271 0.35 Q9Y2W6 EBI-13949271 0.35 P16989 EBI-13949271 0.35 Q2VIK8 EBI-13949271 0.35 Q96PU8 EBI-13949271 0.35 Q14103 EBI-13949271 0.35 P26599 EBI-13949271 0.35 P22626 EBI-13949271 0.35 O00425 EBI-13949271 0.35 Q9Y6M1 EBI-13949271 0.35 Q6IQ23 EBI-16398399 0.35 P82930 EBI-21521832 0.35 Q12926 EBI-21666158 0.35 Q8IYD1 EBI-21666681 0.35 Q15050 EBI-21678544 0.35 P54645 EBI-16361875 0.35 P80386 EBI-16362252 0.35 Q8VDS3 EBI-16248011 0.50 Q9HCE1 EBI-16248043 0.40 Q9UPY3 EBI-20621391 0.35 P51957 EBI-20721387 0.35 Q5T7N2 EBI-20993270 0.35 Q5S007 EBI-21360986 0.35 Q15646 EBI-21262435 0.35 P0DOF2 EBI-25603126 0.35 Q9H9Z2 EBI-25480521 0.35 O43572 EBI-26451580 0.35 Q53F19 EBI-26396827 0.35 P14240 EBI-26968430 0.35 Q99608 EBI-26955247 0.27 P0DTC9 EBI-26994159 0.35 Q9BZB8 EBI-29019560 0.42 Q9UIH9 EBI-29019642 0.35 Q9BXK1 EBI-29019783 0.35 O43474 EBI-29020028 0.35 O60248 EBI-29371942 0.42 P48431 EBI-29373058 0.35 P35711 EBI-29375677 0.35 P35712 EBI-29384845 0.35 P31314 EBI-29607649 0.35 O43763 EBI-29612789 0.35 Q8TDD2 EBI-29740517 0.27 P17948 EBI-32722433 0.27 GO:0070161 GO:0070937 GO:0005737 GO:0010494 GO:0005829 GO:0043197 GO:0030175 GO:0030426 GO:0030027 GO:0043025 GO:0005654 GO:0005634 GO:0000932 GO:0048471 GO:1990904 GO:0003730 GO:0048027 GO:0003729 GO:1990247 GO:0003723 GO:0045182 GO:0070934 GO:0140059 GO:0051028 GO:1900152 GO:0017148 GO:0007399 GO:0097150 GO:0022013 GO:2000767 GO:0001817 GO:0010468 GO:0010610 GO:0051252 Unknown UniProt Sequence Analysis MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIAQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQQVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVIITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNQAQARRK 577 O88477 Insulin-like Igf2bp1 10090 None SL-0198 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}. UNIPROT O88477 UNIPROT Q80US9 UNIPROT Q8BRH1 Pfam PF00013 Pfam PF00076 PROSITE PS50084 PROSITE PS50102 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}. Q8CJG0 EBI-9030750 0.35 A2AG06 EBI-11664104 0.35 Q9P2S5 EBI-11694751 0.35 Q8K3Y3 EBI-15801841 0.35 GO:0070161 GO:0030424 GO:0070937 GO:0005737 GO:0010494 GO:0005829 GO:0030425 GO:0043197 GO:0030175 GO:0030426 GO:0030027 GO:0043025 GO:0005654 GO:0005634 GO:0000932 GO:0048471 GO:1990904 GO:0003730 GO:0048027 GO:0003729 GO:1990247 GO:0045182 GO:0070934 GO:0140059 GO:0051028 GO:1900152 GO:0017148 GO:0007399 GO:0097150 GO:0022013 GO:2000767 GO:0010468 GO:0010610 GO:0051252 GO:0006403 Unknown UniProt Sequence Analysis MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQITQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQPVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVVITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNLAQARRK 577 Q8CGX0 Insulin-like Igf2bp1 10116 None SL-0198 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}. UNIPROT Q8CGX0 UNIPROT B1WBP3 Pfam PF00013 Pfam PF00076 PROSITE PS50084 PROSITE PS50102 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}. GO:0070161 GO:0030424 GO:0070937 GO:0005737 GO:0010494 GO:0005829 GO:0030425 GO:0043197 GO:0030175 GO:0030426 GO:0030027 GO:0043025 GO:0005654 GO:0005634 GO:0000932 GO:0048471 GO:1990904 GO:0003730 GO:0048027 GO:0003729 GO:1990247 GO:0045182 GO:0070934 GO:0140059 GO:0051028 GO:1900152 GO:0017148 GO:0007399 GO:0097150 GO:0022013 GO:2000767 GO:0010468 GO:0010610 GO:0051252 GO:0006403 Unknown UniProt Sequence Analysis MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIAQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQQVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYGSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVVITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNQAQARRK 577 O61955 Eukaryotic ife 6239 None SL-0198 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}. UNIPROT O61955 UNIPROT Q8MNX5 UNIPROT Q95X31 PDB 5ABX PDB 5ABY Pfam PF01652 PROSITE PS00813 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}. Q9XW13 EBI-2411755 0.62 Q20898 EBI-2411740 0.62 Q22497 EBI-2411744 0.62 Q09293 EBI-21449250 0.52 Q1ZXS5 EBI-6457351 0.37 G5EDU4 EBI-6458345 0.37 Q19541 EBI-21448974 0.46 O76616 EBI-21449031 0.35 Q20057 EBI-21449069 0.35 Q9N405 EBI-21449322 0.35 G5EC16 EBI-21449322 0.35 O01871 EBI-21449322 0.35 G5ED26 EBI-21449322 0.35 O45551 EBI-21449322 0.35 Q18603 EBI-21449322 0.35 Q94279 EBI-21449322 0.35 Q18244 EBI-21449322 0.35 Q21323 EBI-21449322 0.35 P48166 EBI-21449322 0.35 Q18490 EBI-21449322 0.35 Q22624 EBI-21449322 0.35 GO:0016281 GO:0048471 GO:0034518 GO:0070992 GO:0000340 GO:0003743 GO:0034585 GO:0009792 GO:0031047 GO:0006413 Unknown UniProt Sequence Analysis MSTSVAENKALSASGDVNASDASVPPELLTRHPLQNRWALWYLKADRNKEWEDCLKMVSLFDTVEDFWSLYNHIQSAGGLNWGSDYYLFKEGIKPMWEDVNNVQGGRWLVVVDKQKLQRRTQLLDHYWLELLMAIVGEQFDEYGDYICGAVVNVRQKGDKVSLWTRDATRDDVNLRIGQVLKQKLSIPDTEILRYEVHKDSSARTSSTVKPRICLPAKDPAPVKEKGPAATTSPSNPGTEATGTSPATPTP 251 Q10475 Eukaryotic tif471 284812 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:12581158}. Note=Localized to the perinuclear region, the growing tips and septum. UNIPROT Q10475 UNIPROT P78832 Pfam PF12152 Pfam PF02854 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}. Q9UUB7 EBI-2477389 0.35 Q9USV1 EBI-2478191 0.35 GO:0005737 GO:0010494 GO:0005829 GO:0016281 GO:0005634 GO:0048471 GO:0003729 GO:0005198 GO:0003743 GO:0002183 GO:0042273 Unknown UniProt Sequence Analysis MSSKPPSNTPKFSYARALASSQSNKSNSTKASENNTATAEKQAVKPSGVEPTNTSRANAQKKTESTGKITSEADTEKYNSSKSPVNKEGSVEKKSSEKSSTNNKPWRGDNTSKPSANSSAERTSSQHQKPETSSQIGKDNAAPVENVNEKSTSQETAPPVSTVPIQFGSITRNAAIPSKPKVSGNMQNKSGVSSYSSKSQSVNSSVTSNPPHTEEPVAAKPEASSTATKGPRPTTSASNTNTSPANGAPTNKPSTDINTTDPATQTTQVSASNSPALSGSSTPSNTSSRSNRQNHGNFSEKRHYDRYGNSHPSYNKYSHYQHGFNYNNSGNNRNESGHPRFRNSRRNYNNQGAYPTYMSNGRSANQSPRNNPQNVNNGSTPIQIPVSLQTPYGQVYGQPQYIVDPNMVQYGPILQPGYVPQYYPVYHQTPYTQNFPNMSRSGSQVSDQVVESPNSSTLSPRNGFAPIVKQQKKSSALKIVNPVTHTEVVVPQKNASSPNPSETNSRAETPTAAPPQISEEEASQRKDAIKLAIQQRIQEKAEAEAKRKAEEKARLEAEENAKREAEEQAKREAEEKAKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEENAKREAEEKVKRETEENAKRKAEEEGKREADKNPEIKSSAPLASSEANVDTSKQTNATEPEVVDKTKVEKLKASEGKSTSSLSSPSHSTSSKRDLLSGLESLSLKTNPKSEQCLESLLNSQFITDFSALVYPSTIKPPSTEEALKAGKYEYDVPFLLQFQSVYTDKPMKGWDERMKETVASAFSDKSSRGMYSSSRQSSRSGSNTHSHAGPGFGGPSERKGISRLGIDRGFSSSGAGFGSGSNYKSAPSRGVSHHGHGGMSGSHRGSQRGSRRGGGERDKPDPSSLTIPVDQVAPLQLSANRWQPKKLTEKPAETKGEDEEALLPPEVVQRKVKGSLNKMTLEKFDKISDQILEIAMQSRKENDGRTLKQVIQLTFEKATDEPNFSNMYARFARKMMDSIDDSIRDEGVLDKNNQPVRGGLLFRKYLLSRCQEDFERGWKANLPSGKAGEAEIMSDEYYVAAAIKRRGLGLVRFIGELFKLSMLSEKIMHECIKRLLGNVTDPEEEEIESLCRLLMTVGVNIDATEKGHAAMDVYVLRMETITKIPNLPSRIKFMLMDVMDSRKNGWAVKNEVEKGPKTIAEIHEEAERKKALAESQRPSSGRMHGRDMNRGDSRMGGRGSNPPFSSSDWSNNKDGYARLGQGIRGLKSGTQGSHGPTSLSSMLKGGSVSRTPSRQNSALRREQSVRAPPSNVAVTSANSFELLEEHDHDNDGGQKDSNSKTSS 1403 Q1JPH6 Eukaryotic EIF4H 9913 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q1JPH6 UNIPROT A5D959 Pfam PF00076 PROSITE PS50102 Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). {ECO:0000250}. GO:0048471 GO:0043024 GO:0033592 GO:0034057 GO:0003743 GO:0097010 GO:0001731 Unknown UniProt Sequence Analysis MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGFRDDFLGGRGGSRPGDRRTGPPMGSRFRDGPPLRGPNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVHKEQE 228 Q15056 Eukaryotic EIF4H 9606 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q15056 UNIPROT A8K3R1 UNIPROT D3DXF6 UNIPROT D3DXF8 Pfam PF00076 PROSITE PS50102 OMIM 603431 DisGeNET 7458 Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA. {ECO:0000269|PubMed:10585411, ECO:0000269|PubMed:11418588}. 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}. P0DTD1 EBI-25491191 0.64 Q9H3H3 EBI-756607 0.74 P23508 EBI-1065071 0.00 O60739 EBI-1065818 0.00 Q14164 EBI-1075879 0.00 Q6MZP7 EBI-1389994 0.35 P60842 EBI-2267802 0.54 A0A6L7H7R4 EBI-2831788 0.00 A0A5P8YEZ8 EBI-2867095 0.00 P10225 EBI-6155523 0.35 P19320 EBI-6189915 0.35 P02751 EBI-6285956 0.35 Q8TBB1 EBI-10235782 0.67 Q96FW1 EBI-10770198 0.35 Q91W50 EBI-11079890 0.35 Q9NRD5 EBI-24336001 0.56 Q9NZD8 EBI-24518067 0.56 Q96D03 EBI-25265649 0.56 Q92796 EBI-24436218 0.56 Q96EF6 EBI-24559599 0.56 P62807 EBI-25471348 0.27 P04156 EBI-21014477 0.35 P12004 EBI-21237916 0.37 P0DOF2 EBI-25603126 0.35 Q8TB24 EBI-26518569 0.35 Q9NRI5 EBI-26610537 0.35 F1PAA9 EBI-27079701 0.27 P35226 EBI-27108918 0.35 P36507 EBI-28935019 0.35 Q5W0V3 EBI-34574999 0.27 GO:0005829 GO:0016281 GO:0016020 GO:0048471 GO:0045296 GO:0043024 GO:0003723 GO:0033592 GO:0034057 GO:0008135 GO:0003743 GO:0048589 GO:0097010 GO:0001731 GO:0006446 GO:0019953 Unknown UniProt Sequence Analysis MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGSSRESRGGWDSRDDFNSGFRDDFLGGRGGSRPGDRRTGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE 248 Q9WUK2 Eukaryotic Eif4h 10090 None SL-0198 Cytoplasm, perinuclear region. UNIPROT Q9WUK2 UNIPROT Q9WUK3 PDB 2DNG Pfam PF00076 PROSITE PS50102 Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). {ECO:0000250}. GO:0048471 GO:0043024 GO:0033592 GO:0034057 GO:0003743 GO:0048589 GO:0097010 GO:0001731 GO:0019953 Unknown UniProt Sequence Analysis MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGGSRESRGGWDSRDDFNSGYRDDFLGGRGGSRPGDRRAGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE 248 Q5RBR8 Eukaryotic EIF4H 9601 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5RBR8 Pfam PF00076 PROSITE PS50102 Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). {ECO:0000250}. GO:0048471 GO:0003723 GO:0003743 Unknown UniProt Sequence Analysis MADFDTYDDRAYNSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGFRDDFLGGRGGSRPGDRRTGPAMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE 228 Q5XI72 Eukaryotic Eif4h 10116 None SL-0198 Cytoplasm, perinuclear region {ECO:0000250}. UNIPROT Q5XI72 Pfam PF00076 PROSITE PS50102 Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). {ECO:0000250}. Q9UI08 EBI-22238608 0.35 P27361 EBI-22238588 0.35 P15498 EBI-22241288 0.35 P07332 EBI-22243434 0.35 P08069 EBI-22245613 0.35 P18031 EBI-22255654 0.35 Q96RT1 EBI-22258042 0.35 O75096 EBI-22258804 0.35 GO:0048471 GO:0043024 GO:0033592 GO:0034057 GO:0003743 GO:0048589 GO:0097010 GO:0001731 GO:0019953 Unknown UniProt Sequence Analysis MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGGSREPRGGWDSRDDFSSGYRDDFLGGRGGSRPGDRRAGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE 248 Q09121 Eukaryotic EIF5A1 9031 None SL-0178 SL-0185 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}. UNIPROT Q09121 UNIPROT Q5ZLI6 Pfam PF01287 PROSITE PS00302 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}. GO:0005789 GO:0005643 GO:0043022 GO:0003723 GO:0003746 GO:0051028 GO:0045901 GO:0045905 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRCDFQLIGIQDGFLSLLQDSGEVREDLRLPEGELGREIEQKYDCGEEIITIHGARFTTS 144 Q07460 Eukaryotic EIF5A2 9031 None SL-0178 SL-0185 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}. UNIPROT Q07460 Pfam PF01287 PROSITE PS00302 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}. GO:0005789 GO:0005643 GO:0043022 GO:0003723 GO:0003746 GO:0051028 GO:0045901 GO:0045905 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MADELDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFNGKKYEDICPSTHNMDVPNIKRNDYQLIGIQDGYLSLLTESGEVREDLKLPEGDLGKEIEGKFNANEDVQISVISAMNEECAVAIKPCK 153 Q9GZV4 Eukaryotic EIF5A2 9606 None SL-0178 SL-0185 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}. UNIPROT Q9GZV4 UNIPROT B2R4V5 Pfam PF01287 PROSITE PS00302 OMIM 605782 DisGeNET 56648 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}. Q96CV9 EBI-6115969 0.35 P49366 EBI-756238 0.78 P43146 EBI-2678596 0.35 Q9H492 EBI-3044058 0.35 Q9H0R8 EBI-3048562 0.35 Q15771 EBI-3924283 0.37 Q9UKA9 EBI-3924886 0.37 P03496 EBI-6158649 0.35 Q13620 EBI-21327757 0.35 Q13618 EBI-21329068 0.35 O00560 EBI-10304015 0.72 Q04864 EBI-10304037 0.56 Q9GZT8 EBI-10304047 0.56 Q9UJX2 EBI-10304057 0.56 Q9BU89 EBI-21850571 0.35 P51957 EBI-20721387 0.35 Q9UQC2 EBI-25384304 0.35 P69479 EBI-25568051 0.35 GO:0005829 GO:0005789 GO:0043231 GO:0005643 GO:0043022 GO:0003723 GO:0003746 GO:0051028 GO:0010509 GO:0045901 GO:0045905 GO:0015031 GO:0007283 Peripheral UniProt By Similarity {ECO:0000250} MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK 153 Q8BGY2 Eukaryotic Eif5a2 10090 None SL-0178 SL-0185 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}. UNIPROT Q8BGY2 Pfam PF01287 PROSITE PS00302 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}. GO:0005789 GO:0043231 GO:0005643 GO:0043022 GO:0003723 GO:0003746 GO:0051028 GO:0045901 GO:0045905 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK 153 Q5R898 Eukaryotic EIF5A2 9601 None SL-0178 SL-0185 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}. UNIPROT Q5R898 Pfam PF01287 PROSITE PS00302 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}. GO:0005789 GO:0005643 GO:0043022 GO:0003723 GO:0003746 GO:0051028 GO:0045901 GO:0045905 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK 153 Q6IS14 Eukaryotic EIF5AL1 9606 None SL-0178 SL-0185 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}. UNIPROT Q6IS14 Pfam PF01287 PROSITE PS00302 DisGeNET 143244 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}. P03496 EBI-6158649 0.35 Q99963 EBI-25376320 0.35 Q9UQC2 EBI-25384304 0.35 P0DOF2 EBI-25603126 0.35 A0A0H3NFP4 EBI-27055452 0.35 Q92630 EBI-28952196 0.27 GO:0005789 GO:0005643 GO:0043022 GO:0003723 GO:0003746 GO:0051028 GO:0045901 GO:0045905 GO:0015031 Peripheral UniProt By Similarity {ECO:0000250} MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGWPCKIVEMSASKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVPEDLRLPEGDLGKEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK 154 Q0D2I5 Non-homologous IFFO1 9606 None SL-0178 SL-0179 SL-0182 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}. UNIPROT Q0D2I5 UNIPROT Q24JT6 UNIPROT Q7L5J9 UNIPROT Q7Z5X4 UNIPROT Q9BQ46 PDB 6ABO PROSITE PS51842 OMIM 610495 DisGeNET 25900 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}. P02545 EBI-26498092 0.58 P0C6X4 EBI-27128759 0.35 Q13426 EBI-753355 0.71 Q96D59 EBI-756262 0.37 Q15027 EBI-759763 0.37 Q9H6Z9 EBI-12503146 0.35 Q99608 EBI-21251050 0.37 A0JNW5 EBI-11898643 0.00 Q86UE8 EBI-11911984 0.00 Q53SF7 EBI-11916115 0.00 Q6NT76 EBI-11917716 0.00 Q8IY63 EBI-11921623 0.00 Q8NEL9 EBI-11922796 0.00 Q9BWV3 EBI-11930488 0.00 Q9UN30 EBI-11939244 0.00 Q96KS9 EBI-21503766 0.35 O15460 EBI-21563604 0.35 Q9NQX6 EBI-21675860 0.35 P46779 EBI-21676629 0.35 Q9UBP4 EBI-21684976 0.35 Q6ZN55 EBI-21720777 0.35 A8MT70 EBI-21738250 0.35 Q9H1K0 EBI-21777075 0.35 Q86XE0 EBI-21777996 0.35 Q6XPS3 EBI-21801323 0.35 Q9UP83 EBI-21866024 0.35 Q9NPF7 EBI-21882357 0.35 P0DOF2 EBI-25603126 0.35 Q9H9Q4 EBI-26498051 0.35 P49917 EBI-26564737 0.40 P78527 EBI-26564743 0.40 P13010 EBI-26564743 0.40 Q93009 EBI-30842093 0.44 GO:0005882 GO:0005637 GO:0016363 GO:0005654 GO:0035861 GO:1990683 GO:0006303 GO:1990166 Unknown UniProt Sequence Analysis MNPLFGPNLFLLQQEQQGLAGPLGDSLGGDHFAGGGDLPPAPLSPAGPAAYSPPGPGPAPPAAMALRNDLGSNINVLKTLNLRFRCFLAKVHELERRNRLLEKQLQQALEEGKQGRRGLGRRDQAVQTGFVSPIRPLGLQLGARPAAVCSPSARVLGSPARSPAGPLAPSAASLSSSSTSTSTTYSSSARFMPGTIWSFSHARRLGPGLEPTLVQGPGLSWVHPDGVGVQIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQDRVNELQEEAQEADACQEELALKVEQLKAELVVFKGLMSNNLSELDTKIQEKAMKVDMDICRRIDITAKLCDVAQQRNCEDMIQMFQVPSMGGRKRERKAAVEEDTSLSESEGPRQPDGDEEESTALSINEEMQRMLNQLREYDFEDDCDSLTWEETEETLLLWEDFSGYAMAAAEAQGEQEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKNDMNRHLHEYMEMCSMKRGLDVQMETCRRLITQSGDRKSPAFTAVPLSDPPPPPSEAEDSDRDVSSDSSMR 559 Q8BXL9 Non-homologous Iffo1 10090 None SL-0178 SL-0179 SL-0182 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}. UNIPROT Q8BXL9 UNIPROT Q3TQI1 UNIPROT Q6PFE6 UNIPROT Q8BXS3 UNIPROT Q8C1D6 PROSITE PS51842 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}. GO:0005882 GO:0005637 GO:0016363 GO:0005654 GO:0035861 GO:1990683 GO:0006303 GO:1990166 Unknown UniProt Sequence Analysis MNPLFGPNLFLLQQEQQGLAGPLGDPLGGDHFAGGGDLASAPLASAGPSAYSPPGPGPAPPAAMALRNDLGSNINVLKTLNLRFRCFLAKVHELERRNRLLEKQLQQALEEGKQGRRGLARRDQAVQTGFISPIRPLGLPLSSRPAAVCPPSARVLGSPSRSPAGPLASSAACHTSSSTSTSTAFSSSTRFMPGTIWSFSHARRLGPGLEPTLVQGPGLSWVHPDGVGVQIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLMSNNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQRNCEDMIQMFQKKLVPSMGGRKRERKAAVEEDTSLSESDGPRQPEGAEEESTALSINEEMQRMLSQLREYDFEDDCDSLTWEETEETLLLWEDFSGYAMAAAEAQGEQEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKNDMNRHLHEYMEMCSMKRGLDVQMETCRRLITQSGDRKSPAFTAVPLSDPPPPPSETEDSDRDVSSDSSMR 562 P40305 Interferon IFI27 9606 None SL-0178 SL-0179 SL-0182 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}. UNIPROT P40305 UNIPROT A0A087WZF8 UNIPROT A8K0H0 UNIPROT Q53YA6 UNIPROT Q6IEC1 UNIPROT Q7Z5R0 UNIPROT Q7Z5R1 UNIPROT Q7Z5R2 UNIPROT Q96BK3 UNIPROT Q9H4B1 Pfam PF06140 OMIM 600009 DisGeNET 3429 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}. P02545 EBI-27124576 0.40 Q5NGF6 EBI-2805959 0.00 Q81KT8 EBI-2831742 0.00 A0A6H3ABE4 EBI-2831749 0.00 A0A6L7HHX2 EBI-2831761 0.00 A0A6L7HB40 EBI-2831768 0.00 Q8ZCW0 EBI-2847220 0.00 A0A5P8YAW1 EBI-2867067 0.00 A0A380PNP6 EBI-2867060 0.00 P17778 EBI-2867046 0.00 A0A3N4BEU0 EBI-2867053 0.00 Q8ZG09 EBI-2867074 0.00 Q8ZHF1 EBI-2867081 0.00 P05549 EBI-9679979 0.37 Q92754 EBI-9680053 0.37 P55056 EBI-24754759 0.56 P22736 EBI-27124261 0.61 GO:0005789 GO:0016021 GO:0031966 GO:0005741 GO:0005739 GO:0005635 GO:0005637 GO:0042802 GO:0005521 GO:0061629 GO:0006915 GO:0097190 GO:0051607 GO:0097191 GO:0045087 GO:0044827 GO:0000122 GO:0043161 GO:0070936 GO:0046825 GO:0060337 Transmembrane UniProt Sequence Analysis {ECO:0000255} MEASALTSSAVTSVAKVVRVASGSAVVLPLARIATVVIGGVVAMAAVPMVLSAMGFTAAGIASSSIAAKMMSAAAIANGGGVASGSLVATLQSLGATGLSGLTKFILGSIGSAIAAVIARFY 122 Q01628 Interferon-induced IFITM3 9606 None SL-0198 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}. UNIPROT Q01628 UNIPROT Q53Y76 UNIPROT Q96HK8 UNIPROT Q96J15 Pfam PF04505 OMIM 605579 OMIM 614680 DisGeNET 10410 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}. O95415 EBI-25503997 0.54 P43490 EBI-7932891 0.51 P06460 EBI-11723082 0.35 P06927 EBI-11724813 0.35 P35372 EBI-24521211 0.56 P43628 EBI-24670376 0.56 O60669 EBI-23704678 0.56 O95870 EBI-24691282 0.56 O95470 EBI-24700847 0.56 Q9NXB9 EBI-24702045 0.56 Q9Y680 EBI-24738925 0.56 Q9NZD1 EBI-24748139 0.56 Q9Y282 EBI-24756591 0.56 Q6UWN5 EBI-24779968 0.56 P60201 EBI-24783936 0.56 O15552 EBI-24797538 0.56 Q96KR6 EBI-25276379 0.56 Q86VR2 EBI-25280796 0.56 Q8N661 EBI-25282350 0.56 Q14973 EBI-24642589 0.56 Q9NUH8 EBI-24792170 0.56 Q96HJ5 EBI-24801917 0.56 P19397 EBI-24808633 0.56 Q13520 EBI-24811070 0.56 Q12908 EBI-25269791 0.56 Q9H6H4 EBI-25272718 0.56 O15354 EBI-20808121 0.37 P25105 EBI-20811134 0.37 O43490 EBI-21451704 0.37 GO:0031901 GO:0016021 GO:0031902 GO:0005765 GO:0048471 GO:0005886 GO:0032991 GO:0051607 GO:0006955 GO:0046597 GO:0045071 GO:0032897 GO:0035455 GO:0035456 GO:0034341 GO:0009615 GO:0060337 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNHTVQTFFSPVNSGQPPNYEMLKEEHEVAVLGAPHNPAPPTSTVIHIRSETSVPDHVVWSLFNTLFMNPCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTILLIVIPVLIFQAYG 133 Q9CQW9 Interferon-induced Ifitm3 10090 None SL-0198 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}. UNIPROT Q9CQW9 UNIPROT Q9D8L6 Pfam PF04505 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}. GO:0045177 GO:0009986 GO:0005737 GO:0031410 GO:0031901 GO:0005783 GO:0016021 GO:0031902 GO:0005765 GO:0005634 GO:0048471 GO:0005886 GO:0032991 GO:0051607 GO:0008285 GO:0046597 GO:0045071 GO:0006898 GO:0035455 GO:0035456 GO:0034341 GO:0009615 GO:0060337 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNHTSQAFITAASGGQPPNYERIKEEYEVAEMGAPHGSASVRTTVINMPREVSVPDHVVWSLFNTLFMNFCCLGFIAYAYSVKSRDRKMVGDVTGAQAYASTAKCLNISTLVLSILMVVITIVSVIIIVLNAQNLHT 137 P26376 Interferon-induced ifitm3 10116 None SL-0198 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}. UNIPROT P26376 UNIPROT B5DER6 Pfam PF04505 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}. P15127 EBI-21297848 0.35 GO:0031901 GO:0016021 GO:0031902 GO:0005765 GO:0048471 GO:0005886 GO:0051607 GO:0046597 GO:0045071 GO:0035455 GO:0035456 GO:0034341 GO:0060337 Transmembrane UniProt Sequence Analysis {ECO:0000255} MNHTSQAFVNAATGGQPPNYERIKEEYEVSELGAPHGSASVRTTVINMPREVSVPDHVVWSLFNTLFMNFCCLGFIAYAYSVKSRDRKMVGDMTGAQAYASTAKCLNISSLVLSILMVIITIVTVVIIALNAPRLQT 137 Q9QZ85 Interferon-inducible Iigp1 10090 None SL-0178 SL-0182 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. UNIPROT Q9QZ85 UNIPROT Q9Z1M3 PDB 1TPZ PDB 1TQ2 PDB 1TQ4 PDB 1TQ6 PDB 1TQD PDB 4LV5 PDB 4LV8 PDB 5FPH Pfam PF05049 PROSITE PS51716 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}. Q6P542 EBI-6909752 0.35 A1E140 EBI-15902276 0.54 Q9QZ85 EBI-15902301 0.54 GO:0005737 GO:0005789 GO:0032580 GO:0031965 GO:0020005 GO:0019003 GO:0005525 GO:0003924 GO:0042802 GO:0035458 GO:0019221 GO:0006952 GO:0050829 GO:0042832 GO:0045087 GO:0010506 GO:0009617 Lipid-Anchored UniProt Curator Inference {ECO:0000305} MGQLFSSPKSDENNDLPSSFTGYFKKFNTGRKIISQEILNLIELRMRKGNIQLTNSAISDALKEIDSSVLNVAVTGETGSGKSSFINTLRGIGNEEEGAAKTGVVEVTMERHPYKHPNIPNVVFWDLPGIGSTNFPPNTYLEKMKFYEYDFFIIISATRFKKNDIDIAKAISMMKKEFYFVRTKVDSDITNEADGKPQTFDKEKVLQDIRLNCVNTFRENGIAEPPIFLLSNKNVCHYDFPVLMDKLISDLPIYKRHNFMVSLPNITDSVIEKKRQFLKQRIWLEGFAADLVNIIPSLTFLLDSDLETLKKSMKFYRTVFGVDETSLQRLARDWEIEVDQVEAMIKSPAVFKPTDEETIQERLSRYIQEFCLANGYLLPKNSFLKEIFYLKYYFLDMVTEDAKTLLKEICLRN 413 O13681 Integral IMA1 284812 None SL-0178 SL-0179 SL-0182 Nucleus inner membrane {ECO:0000269|PubMed:18692466}; Multi-pass membrane protein {ECO:0000269|PubMed:18692466}. UNIPROT O13681 Pfam PF09779 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}. GO:0034506 GO:0005783 GO:0016021 GO:0034992 GO:0044732 GO:0005635 GO:0005637 GO:0031965 GO:0071765 Transmembrane UniProt Sequence Analysis {ECO:0000255} MESSRLFTLGLGNSDDGLKSTFGDKTVTCFYCNKKKEKIRDGTSTWTCSICEATNHIDEKGDILDYRPPTPTQDKGVGPFYAIRDFPSSSSFQSPFCEKCQMNQLIVNRMLADYLPDSSHPDYQAYEKALPEYKKSIEEKFPIVCSECYDSVQDQLDANDYEAKNQVLGYWLQKSKEQLNAKVPHHYPKASFVLWLLRGFGFSFFYLQSIVWHLYHSMIISLLPDGIRNLFLKAISYFLLDGSSSKIFYFNWLGFFVVFWNPYWYKMMDNPSWELFGRDQYIQCQALYLIIRLTCLYLLSCYESEILNLSSDTNLESDFLLRQIHAAFFFVTICFTWISISCLKPSPPPEVHLTGEILKPRKKRQESTSSVHRIGKESSDRKDGISGQNKLQQFATISILNNTNATSHLGNQSVRERAPEESPMTFLQKKMAALPTSSPVRPMLKPTLQLQNSPLSKLVPQEVGNKVNDSIHTTSNQPSKFSLNPSISLKGDNVIEKNLPFSVSTLKSTAKKDTGKAGDGQNREIQNEPVSLESHFSKSLALQNDPTEVIQVKNVLHRNRRNAKLLIAFTILFLVGLICGWRLNRFTMFIYYLCILVLATYYVMKHNFYPLRKVA 615 Q557F4 Probable DDB_G0273595 44689 None SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT Q557F4 UNIPROT Q869V5 Pfam PF00514 Pfam PF16186 Pfam PF01749 PROSITE PS50176 PROSITE PS51214 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}. GO:0005737 GO:0005635 GO:0005634 GO:0061608 GO:0008139 GO:0006607 Unknown UniProt Sequence Analysis MSSRDKQDSRKKEFKKSLDSETARRKREENSIGIRKNAREELMLKRRGIVQPNPSTSYQIIVPPEVQEQFQKYENETMENKIKNLPGLVTALNSNDQAYVYSSLVQFRKLLSIHAYPPIDQVIECGIIPKLNQLLQCNNPKVQFESAWALTNIASGNNRQTQTVMESGSVPIFIQLLCAETTDEVKEQCAWALGNIAGDTVDSRNYLLKYGAMNALIPLLHYGEDNGATTTSANSERKIGLIQNVVWTISNLCRGKPQPDFSVVSQCLPAINELIRIENLPSEIYGDLCWALSYLCDGPNTKIQAVIDSGVVPRLVKLLEYPDSIVFTPALRAVGNIVTGESSQTQIVIDNNGVELITRLLAVQKKSIRKESCWALSNITAGEPSQIDVVVSNPKTVTTLISLLSHSEHDIKREACWALSNSTNNSSTKSIQTLVRHNILKHFIDLLNSQDLVILKIVLEGLINIIKEGEKTKTKTGVNPYVNLISEMQGESIIYDLQEHQSKDVYKKAFELIEFFESSDYSDSENSEPNINQNGQYEFSSNYNSNSINI 550 Q71VM4 Importin Os01g0253300 39947 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:9727027}. UNIPROT Q71VM4 UNIPROT O82783 PDB 2YNS PDB 4B8J PDB 4B8O PDB 4B8P PDB 4BPL PDB 4BQK Pfam PF00514 Pfam PF16186 Pfam PF01749 PROSITE PS50176 PROSITE PS51214 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}. Q8S7W1 EBI-628940 0.37 Q3HM11 EBI-8014436 0.44 GO:0005634 GO:0048471 GO:0061608 GO:0008139 GO:0006607 Unknown UniProt Sequence Analysis MSLRPSERVEVRRNRYKVAVDAEEGRRRREDNMVEIRKSRREESLLKKRREGLQAQAPVPASAATGVDKKLESLPAMIGGVYSDDNNLQLEATTQFRKLLSIERSPPIEEVIQSGVVPRFVQFLTREDFPQLQFEAAWALTNIASGTSENTKVVIDHGAVPIFVKLLGSSSDDVREQAVWALGNVAGDSPKCRDLVLANGALLPLLAQLNEHTKLSMLRNATWTLSNFCRGKPQPSFEQTRPALPALARLIHSNDEEVLTDACWALSYLSDGTNDKIQAVIEAGVCPRLVELLLHPSPSVLIPALRTVGNIVTGDDAQTQCIIDHQALPCLLSLLTQNLKKSIKKEACWTISNITAGNKDQIQAVINAGIIGPLVNLLQTAEFDIKKEAAWAISNATSGGSHDQIKYLVSEGCIKPLCDLLICPDIRIVTVCLEGLENILKVGETDKTLAAGDVNVFSQMIDEAEGLEKIENLQSHDNNEIYEKAVKILEAYWMDEEDDTMGATTVAAPQGATFDFGQGGGAAQFK 526 Q9SLX0 Importin Os05g0155601 39947 None SL-0198 Cytoplasm, perinuclear region {ECO:0000269|PubMed:11124253}. UNIPROT Q9SLX0 Pfam PF00514 Pfam PF16186 Pfam PF01749 PROSITE PS50176 PROSITE PS51214 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}. GO:0005634 GO:0048471 GO:0061608 GO:0008139 GO:0006607 Unknown UniProt Sequence Analysis MSLRPSERAEVRRSRYKVAVDADEGRRRREDNMVEIRKSRREESLLKKRRDGLPAAAAAAAAASPLLAHSSALQQKLEGLPAMVQAVQSDDSAVQLEATTQFRKLLSIERSPPIEEVINTGVVPRFIAFLQREDYPQLQFEAAWALTNIASGTSDNTKVVVESGAVPIFVKLLSSPSEDVREQAVWALGNVAGDSPKCRDLVLASGGLYPLLQQLNEHAKLSMLRNATWTLSNFCRGKPQPNFEQVKPALSALQRLIHSQDEEVLTDACWALSYLSDGTNDKIQAVIESGVFPRLVELLMHPSASVLIPALRTVGNIVTGDDMQTQCVIDHQALPCLLNLLTNNHKKSIKKEACWTISNITAGNREQIQAVINANIIAPLVHLLQTAEFDIKKEAAWAISNATSGGTHDQIKYLVAQGCIKPLCDLLVCPDPRIVTVCLEGLENILKVGEAEKNLGAGDVNSYAQMIDDAEGLEKIENLQSHDNTEIYEKAVKMLESYWLEEEDDAMPSGDNAQNGFNFGNQQPNVPSGGFNFG 534 Q02821 Importin SRP1 559292 None SL-0198 Cytoplasm, perinuclear region. Note=Mainly localized at the periphery of the nucleus. UNIPROT Q02821 UNIPROT D6W0Z8 PDB 1BK5 PDB 1BK6 PDB 1EE4 PDB 1EE5 PDB 1UN0 PDB 1WA5 PDB 2C1T PDB 4PVZ PDB 4XZR PDB 5H2W PDB 5H2X PDB 5T94 Pfam PF00514 Pfam PF16186 Pfam PF01749 PROSITE PS50176 PROSITE PS51214 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}. P20591 EBI-11534426 0.56 P20676 EBI-789997 0.69 P32499 EBI-801825 0.78 P34160 EBI-806268 0.69 P39705 EBI-802293 0.69 P40069 EBI-804491 0.53 P22768 EBI-391461 0.37 P00812 EBI-391464 0.37 P33317 EBI-391467 0.37 Q12178 EBI-391470 0.37 P28240 EBI-391473 0.37 P06106 EBI-391476 0.37 P53081 EBI-391479 0.37 P19881 EBI-391482 0.37 P36068 EBI-391485 0.37 P35497 EBI-391488 0.37 P41835 EBI-391491 0.37 P34760 EBI-391494 0.37 P47165 EBI-391497 0.37 P38749 EBI-391500 0.37 P43543 EBI-391503 0.37 P53215 EBI-391506 0.37 Q05016 EBI-391509 0.37 P15108 EBI-708957 0.56 Q06142 EBI-784458 0.94 P46948 EBI-789541 0.35 P38792 EBI-791854 0.53 P32799 EBI-792386 0.35 P53859 EBI-792516 0.35 P27466 EBI-793512 0.35 P36124 EBI-794754 0.53 Q12149 EBI-796196 0.67 Q02724 EBI-797293 0.59 Q12124 EBI-797390 0.35 Q08278 EBI-799246 0.35 P53833 EBI-799459 0.35 P13259 EBI-799593 0.69 P53256 EBI-800712 0.35 P53881 EBI-800899 0.35 P50111 EBI-803477 0.35 P22215 EBI-804242 0.35 P53866 EBI-804491 0.35 P32337 EBI-804491 0.35 P41940 EBI-804491 0.35 P00330 EBI-804491 0.35 Q12449 EBI-807743 0.35 Q08285 EBI-808713 0.35 Q05636 EBI-809094 0.35 Q08920 EBI-810994 0.77 Q12464 EBI-811656 0.53 P28003 EBI-815383 0.27 Q06218 EBI-817288 0.27 Q12277 EBI-6963562 0.40 P25359 EBI-6964469 0.56 Q05543 EBI-6995482 0.56 Q12460 EBI-7021190 0.40 P22579 EBI-7021237 0.67 Q06697 EBI-7044996 0.40 P53072 EBI-7153795 0.40 Q05900 EBI-7156793 0.40 P47108 EBI-7162569 0.44 P38806 EBI-7181311 0.40 P53911 EBI-7184902 0.40 Q08162 EBI-7271310 0.56 P32324 EBI-7286906 0.56 P19659 EBI-7307988 0.40 Q12499 EBI-7435045 0.40 P53261 EBI-7436958 0.56 P53397 EBI-7440707 0.44 P22216 EBI-7509953 0.69 Q04779 EBI-7512888 0.40 P53552 EBI-7519241 0.56 P49723 EBI-7582150 0.40 P06843 EBI-7751879 0.56 Q01476 EBI-7792448 0.40 Q04500 EBI-7810284 0.40 P22936 EBI-7900920 0.40 P36036 EBI-8226241 0.22 P33307 EBI-1041382 0.57 P32562 EBI-2112894 0.53 P06700 EBI-2212712 0.40 Q04087 EBI-2212766 0.40 Q08904 EBI-2344792 0.37 P53184 EBI-2345292 0.37 P51601 EBI-2345314 0.37 P25367 EBI-2345326 0.37 P08536 EBI-2345887 0.37 Q03063 EBI-2345890 0.37 P17423 EBI-2345893 0.37 P60010 EBI-2346004 0.37 P38821 EBI-2346115 0.37 Q02895 EBI-2346118 0.37 Q12306 EBI-2346577 0.37 Q06549 EBI-2346610 0.37 P32318 EBI-2346619 0.37 P43619 EBI-2346747 0.37 Q03373 EBI-2346812 0.55 P09201 EBI-2346852 0.37 Q12189 EBI-2347997 0.37 P15202 EBI-2348000 0.37 P18759 EBI-2348009 0.37 P38716 EBI-2348021 0.37 Q12206 EBI-2348042 0.37 P37366 EBI-2611238 0.35 P13365 EBI-2611665 0.35 P32350 EBI-2612391 0.35 P40187 EBI-2612903 0.35 P38089 EBI-2613131 0.35 Q12224 EBI-2613375 0.35 P38255 EBI-2613514 0.35 P32447 EBI-2881693 0.00 Q12495 EBI-16280136 0.53 Q02796 EBI-2885546 0.00 Q04116 EBI-2889029 0.00 P25303 EBI-3659819 0.35 P10591 EBI-3677844 0.35 P11484 EBI-3784104 0.35 P50875 EBI-4376349 0.35 P50102 EBI-4380099 0.35 P38129 EBI-4380674 0.35 Q05027 EBI-4382094 0.35 P35177 EBI-4383599 0.35 Q03330 EBI-4385804 0.35 P53131 EBI-10903607 0.35 O00635 EBI-11534408 0.56 Q7Z6G3 EBI-11534397 0.56 A0A0C4DGF1 EBI-11534388 0.56 Q96A10 EBI-11534379 0.56 P60709 EBI-11534454 0.56 P35520 EBI-11534444 0.56 P22234 EBI-11534435 0.56 P13196 EBI-11534417 0.56 Q13557 EBI-11534487 0.56 Q13137 EBI-11534474 0.56 P63261 EBI-11534464 0.56 Q9NS73 EBI-11534541 0.56 Q9HAN9 EBI-11534532 0.56 Q8WVF5 EBI-11534523 0.56 Q15041 EBI-11534514 0.56 Q15038 EBI-11534505 0.56 Q13867 EBI-11534496 0.56 Q9NVV9 EBI-11534559 0.56 Q14974 EBI-13942487 0.44 Q03281 EBI-15598611 0.76 Q03707 EBI-16159762 0.68 P05221 EBI-16159838 0.56 P33322 EBI-16265066 0.35 P47027 EBI-16268315 0.35 P34252 EBI-16268369 0.35 P21268 EBI-16269078 0.35 P40316 EBI-16275395 0.35 P40348 EBI-16279429 0.35 Q12749 EBI-16279839 0.35 P22470 EBI-16281382 0.35 P11978 EBI-16282672 0.35 Q00916 EBI-16283579 0.35 Q03010 EBI-16284085 0.35 P38811 EBI-16284085 0.35 P15019 EBI-16284085 0.35 P0CS90 EBI-16284085 0.35 Q03782 EBI-16284085 0.35 P38262 EBI-16284085 0.35 P39954 EBI-16284085 0.35 Q02555 EBI-16284085 0.35 P21538 EBI-16284085 0.35 P12709 EBI-16284085 0.35 P06169 EBI-16284085 0.35 P29468 EBI-16284085 0.35 Q00539 EBI-16284085 0.35 P33441 EBI-16284085 0.35 P05694 EBI-16284085 0.35 P00958 EBI-16284085 0.35 P17629 EBI-16284085 0.35 Q03532 EBI-16284085 0.35 Q07623 EBI-16284085 0.35 P45976 EBI-16284085 0.35 P14540 EBI-16284085 0.35 Q12432 EBI-16284085 0.35 P54115 EBI-16284085 0.35 P19414 EBI-16284085 0.35 Q12476 EBI-16287516 0.35 Q07930 EBI-16290646 0.35 Q00416 EBI-16421063 0.35 GO:0005737 GO:0005829 GO:0042564 GO:0005635 GO:0005654 GO:0005634 GO:0048471 GO:0032991 GO:0097718 GO:0061608 GO:0008139 GO:0044877 GO:0051170 GO:0006607 GO:0031144 GO:0006606 GO:0006612 Unknown UniProt Sequence Analysis MDNGTDSSTSKFVPEYRRTNFKNKGRFSADELRRRRDTQQVELRKAKRDEALAKRRNFIPPTDGADSDEEDESSVSADQQFYSQLQQELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEMLQLEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDYRDYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLIYSMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPALRAVGNIVTGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPPLVKLLEVAEYKTKKEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEVTLDALENILKMGEADKEARGLNINENADFIEKAGGMEKIFNCQQNENDKIYEKAYKIIETYFGEEEDAVDETMAPQNAGNTFGFGSNVNQQFNFN 542 P91276 Importin ima 6239 None SL-0178 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}. UNIPROT P91276 Pfam PF00514 Pfam PF16186 Pfam PF01749 PROSITE PS50176 PROSITE PS51214 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}. V6CLJ5 EBI-338966 0.00 G5ECL3 EBI-343463 0.00 Q9N2K7 EBI-344852 0.00 O44761 EBI-6458140 0.37 GO:0005737 GO:0005635 GO:0005643 GO:0005654 GO:0005634 GO:0061608 GO:0008139 GO:0009792 GO:0051177 GO:0007084 GO:0006607 GO:0006606 GO:0051983 Unknown UniProt Sequence Analysis MTLTETSLSHNAEEGKDEGGRLQQYKNLTKHEELRRRRTECSVEIRKQKGADMMMKRRNIVDVDEGGNSESELEEPEKISHQQSSTRLSNDEIRAILSNNPSEDDMVRCFESLRKSLSKTKNPPIDEVIHCGLLQALVQALSVENERVQYEAAWALTNIVSGSTEQTIAAVEAGVTIPLIHLSVHQSAQISEQALWAVANIAGDSSQLRDYVIKCHGVEALMHLMEKVDQLGDSHVRTIAWAFSNMCRHKNPHAPLEVLRVLSKGLVKLVQHTDRQVRQDACWAVSYLTDGPDEQIELARESGVLPHVVAFFKEAENLVAPALRTLGNVATGNDSLTQAVIDLGSLDEILPLMEKTRSSSIVKECCWLVSNIIAGTQKQIQAVLDANLLPVLINVLKSGDHKCQFEASWALSNLAQGGTNRQVVAMLEDNVVPALCQALLQTNTDMLNNTLETLYTLMLTVQNGYPHKVDILHDQVEENGGLDSLERLQESQSEQIYTQAYRIITQFFTDDDAGEKESHENADPQDNKWSF 531 O59809 Probable SPCC550 284812 None SL-0178 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}. UNIPROT O59809 Pfam PF08506 Pfam PF03810 PROSITE PS50166 Active in protein import into the nucleus. {ECO:0000250}. GO:0005829 GO:0005635 GO:0005643 GO:0005634 GO:0005525 GO:0005049 GO:0061608 GO:0031267 GO:0006406 GO:0006606 Unknown UniProt Sequence Analysis MSLVEHFDATLSADPNTRTKAELSLKQLEKEPSFVLAVLQLLSSQEISLPTQQAAVIYLKNRVSRSWSSIDDAPSPLDIPEEQKALFRQNILPVLLQSPMSTRSHLMAILNIILSTDFPEYWPGFSEYTSNLVHSTERCEVYAGLICFHELAKVYRWRLDDRQRDIGPLVAALFPTILQLGQGLINLEDNDSAEMLRLILKTFKSVIALELPPELLANDMILSWIQLLLAVVQKPLPESLMSLEPEVRQSHVWHKCKKWAYYSLNRIFTRYGEPSSLVGDSANKYRAFAKNFITNVVPNILETYIQQTILWTQGQLWLSPRVLYFLGCFYEECVKPKSTWALLKPHLQLLIGSFVFPQLCMSEEDEELWELDPVEFIHKYIDIYDDFNSADVAASRFLVKLASKRKKYTFMGILSFASDILNQYAASPPNEKNPRQKEGALRMVAAVSNSILSKNSPVAGMMQDFLVAHVMPEFTSPVGYLRSRACEMINRFSEIDWSDKSQLLNAYQAVLNCLQDNDLPVRIQAALALQPLMRHLEVHDVMTAHVPIIMQNLLFLANEVDIDALSSCMEEFVSSFSHELTPFASQLAKQLRNTFVKLMQETMDESTTVDDFDSLVDDKSIAAIGILNTLSTMILSLENTVDVLREIEAILLPMINFVLDNNIFDVYAELFEIIDGCTFASKEISPIMWGVYEKLQKVLKESGIEFVEEATPALSNFITYGGKEFASRPDYIAVMVDIIMQVFNSEHLAVNDRVSACKLTELLMLNYRGLLDQYVPAFIEVAGNLLLVTEKPTSQTYRVFLLEVIINALYYNPSMSLGVLEMHQWTLPFFALWFENIPSFTRVHDKKLSLVAILSVISLGAQQVAVAIQDSWGNIMKVMITLLNTLPEALAARAELEKEYDGETFNLSGSGWNDGIDWEADDDEGVDDFAVEYGGPDLGGEISADVVDDFDEFEHFQGNYLLDEDPLFHTLLDQVDPFSLFQEFMVHLKDNSPVTLQDLVKNLEASEQQSLQRLVTEKPSTLAVASDKT 1029 Q76P29 Importin DDB_G0272318 44689 None SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT Q76P29 UNIPROT Q55A47 Pfam PF00514 Pfam PF16186 Pfam PF01749 PROSITE PS50176 PROSITE PS51214 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}. GO:0005737 GO:0005635 GO:0005634 GO:0061608 GO:0008139 GO:0006607 Unknown UniProt Sequence Analysis MQRSKQETRKSQYKKSIDSDESRRKREEASLSIRKNKREESLLKKRTQAVPGSTPVKVDSLINQRLEQLPSLVAEINSENPDLILKSTTAFRKLLSIEKSPPIEEVIKTGIVPRLVKFLYMQDFPQLQFEAAWALTNIASGTPEQTRVVIENGAIQVFVLLLSSPHDDVREQAVWALGNIAGDSHYCRDLVLSHNALPPLLSLLQNPAAIKVSMVRNATWTLSNFCRGKPQPPFEIVRASLPVLAKLIYYQDEEVLIDACWALSYLSDGSNERIQEVIDAKVCRKMVELLGHPTIAVQTPALRTIGNIVTGDDNQTQIVLSVQALSHLLNLLQSPKRAIRKEACWTISNITAGDKNQIQQVIDANIIPSLVYLLANAEFEIQKEAAWAISNATSCGTPQQIHFLVSQGCVKPLCDLLKVSDPRIINVALEGIENILVAGKKEAQVTGVNPYKKIIEDADGLGKIYDLQHHMNKDTFEKVSRIISTYLEDEQEDEGDLMPEGSSFSFSNQTNSNFNL 516 Q9FYP9 Importin P0011G08 39947 None SL-0198 Cytoplasm, perinuclear region. UNIPROT Q9FYP9 UNIPROT O80332 UNIPROT Q0JQJ0 Pfam PF00514 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}. GO:0005634 GO:0048471 GO:0061608 GO:0008139 GO:0006607 Unknown UniProt Sequence Analysis MADDSASPSPSSASPLQHHREALKSSVRNTAASRRREQAIAIGKERREALIRAKRVCRAPISGSDEAEMEEGDMVVDEEKACLEAKTAHAVEELKSALSIQGKGVQKKKIEALRDLRRLLSQPEVPLVDTAIKAGAVPLLVQYLSFGSSDEQLLEAAWCLTNIAAGEPEETKSLLPALPLLIAHLGEKSSTLVAEQCAWAIGNVAGEGAELRSTLLAQGALRPLTRLMFSSKGSTARTAAWAMSNLIKGPDPKAANELITIDGVLNAIIASLEKEDEELATEVAWVVVYLSALSDRGISLIVRSSVPQLLIGRLFSSENLQLLIPVLRGLGNLIAADDYMVDSVLTVGHNIIDQALSGLIKCLKSDNRVLRKESSWALSNIAAGSFEHKKLIFASEATPVLIRLVTSMQFDIRREAAYTLGNLCVVPTGNCELPKIIVEHLVAIVDGGALPGFIHLVRSADVDTAGLGLQFLELVMRGYPNKQGPKLVEMEDGIEAMERFQFHENEQMRNMANGLVDEYFGEDYGLDE 528 Q14974 Importin KPNB1 9606 None SL-0178 Cytoplasm {ECO:0000269|PubMed:11891849}. Nucleus envelope {ECO:0000269|PubMed:11891849}. UNIPROT Q14974 UNIPROT B7ZAV6 UNIPROT D3DTT3 UNIPROT Q14637 UNIPROT Q53XN2 UNIPROT Q96J27 PDB 1F59 PDB 1IBR PDB 1M5N PDB 1O6O PDB 1O6P PDB 1QGK PDB 1QGR PDB 2P8Q PDB 2Q5D PDB 2QNA PDB 3LWW PDB 3W5K PDB 6N88 PDB 6N89 Pfam PF03810 PROSITE PS50077 PROSITE PS50166 OMIM 602738 DisGeNET 3837 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}. A0A142I5B9 EBI-20625330 0.35 A6NF01 EBI-30827108 0.44 A8CG34 EBI-11115566 0.59 O14524 EBI-11115566 0.35 O15504 EBI-11115566 0.35 O95295 EBI-5664409 0.00 P00533 EBI-702075 0.35 P02545 EBI-16795756 0.27 P04626 EBI-4373084 0.57 P14907 EBI-1034546 0.62 P35658 EBI-30827243 0.44 P46060 EBI-11115566 0.35 P49790 EBI-11076796 0.77 P49792 EBI-11115566 0.35 P52948 EBI-11115566 0.35 P57740 EBI-11115566 0.35 P62826 EBI-11115566 0.53 P63165 EBI-11115566 0.35 P63279 EBI-11105225 0.35 P70168 EBI-2555147 0.40 P78406 EBI-11115566 0.35 Q02821 EBI-13942487 0.44 Q12769 EBI-11115566 0.35 P52292 EBI-286795 0.93 Q9GK30 EBI-8580826 0.44 Q9NRA8 EBI-301394 0.35 Q01201 EBI-363445 0.00 P20333 EBI-364543 0.00 Q15628 EBI-364816 0.00 Q9Y4K3 EBI-365110 0.00 P60709 EBI-353790 0.40 Q16637 EBI-464895 0.52 O75940 EBI-464916 0.40 Q12873 EBI-474956 0.37 Q8N2W9 EBI-475005 0.37 P21246 EBI-475012 0.37 Q15796 EBI-7224889 0.37 P51178 EBI-7795361 0.60 O92837 EBI-8512780 0.40 P03087 EBI-8512862 0.44 P03126 EBI-8592423 0.44 P03107 EBI-7362635 0.44 P03101 EBI-7362692 0.62 P63104 EBI-7194971 0.40 P13569 EBI-1171566 0.64 P01106 EBI-1237540 0.35 P32121 EBI-1642843 0.35 Q00005 EBI-2211497 0.35 Q9Z0E3 EBI-2549710 0.35 Q9ERU9 EBI-2555617 0.56 Q9QWT9 EBI-2558911 0.40 E9PVX6 EBI-2561030 0.40 Q9D4G9 EBI-2561931 0.40 Q9D0T1 EBI-2563541 0.40 Q8N0X7 EBI-2643801 0.35 Q5NEH1 EBI-2805872 0.00 Q14974 EBI-7166773 0.44 Q13573 EBI-7950968 0.35 Q99459 EBI-7954144 0.35 Q5EWX9 EBI-8070469 0.35 Q16658 EBI-2893273 0.35 Q9UH99 EBI-8021405 0.40 O00629 EBI-8291902 0.74 Q8K4J6 EBI-8292094 0.52 Q00610 EBI-4373239 0.35 Q15075 EBI-4373273 0.35 P42566 EBI-4373380 0.40 P50570 EBI-4373384 0.35 Q14696 EBI-7246101 0.37 Q5TAQ9 EBI-7817974 0.40 P0C1C7 EBI-6157992 0.35 P0C1C6 EBI-6158469 0.35 Q05322 EBI-6159823 0.35 P19320 EBI-6191068 0.53 Q77M19 EBI-6270503 0.35 P02751 EBI-6285956 0.35 P49761 EBI-6380381 0.35 Q9UBE8 EBI-6381385 0.35 Q9UQ88 EBI-6381526 0.35 Q86VP6 EBI-21322532 0.35 Q92905 EBI-21325777 0.35 Q13618 EBI-21329068 0.35 Q5S007 EBI-9515510 0.53 Q13043 EBI-10049645 0.35 Q13418 EBI-10103376 0.35 O60674 EBI-10103554 0.35 Q96FW1 EBI-10770198 0.35 P05412 EBI-11323169 0.35 P04620 EBI-10687139 0.58 P03225 EBI-11722220 0.35 P0C739 EBI-11725101 0.35 Q6PFD9 EBI-10994876 0.35 Q8BH74 EBI-10997196 0.35 E9PUA5 EBI-11016929 0.35 Q8VE37 EBI-11043815 0.35 P63280 EBI-11044140 0.35 P34022 EBI-11080066 0.35 Q15398 EBI-11083028 0.53 Q6PFD6 EBI-11093571 0.35 Q9R1K9 EBI-11111151 0.35 P18754 EBI-11115566 0.35 Q9HCK8 EBI-11115566 0.35 Q96JN0 EBI-11115566 0.35 Q69YN4 EBI-11115566 0.35 P52294 EBI-11115566 0.69 Q96JA3 EBI-11115566 0.35 Q5SRE5 EBI-11115566 0.35 Q9NRG9 EBI-11115566 0.35 Q15544 EBI-11115566 0.35 P62495 EBI-11115566 0.35 O60684 EBI-11115566 0.59 Q96G23 EBI-11115566 0.35 Q8WUM0 EBI-11115566 0.35 I3L0N3 EBI-11115566 0.35 Q96EE3 EBI-11115566 0.35 Q8TEP8 EBI-11115566 0.35 O14715 EBI-11115566 0.35 O15541 EBI-11115566 0.35 Q92621 EBI-11115566 0.35 Q96P63 EBI-11115566 0.35 Q8NI27 EBI-11115566 0.35 Q92750 EBI-11115566 0.35 P51648 EBI-11115566 0.35 J3QR07 EBI-11115566 0.35 Q6NUQ4 EBI-11115566 0.35 Q9BXS6 EBI-11115566 0.35 Q69YH5 EBI-11115566 0.35 Q9UDW1 EBI-11115566 0.35 Q8NFH5 EBI-11115566 0.35 Q9UKX7 EBI-11115566 0.35 Q8N1F7 EBI-11115566 0.35 Q86VU5 EBI-11115566 0.35 Q9BW19 EBI-11115566 0.35 Q9NXE4 EBI-11115566 0.35 Q8NFH4 EBI-11115566 0.35 E9PF10 EBI-11115566 0.35 O75448 EBI-11115566 0.35 Q96SK2 EBI-11115566 0.35 Q8NFH3 EBI-11115566 0.35 Q9P0U3 EBI-11115566 0.35 P43487 EBI-11115566 0.35 Q8TEM1 EBI-11115566 0.35 Q9BTX1 EBI-11115566 0.35 Q53EZ4 EBI-11115566 0.35 Q8N2Y8 EBI-11115566 0.35 P55084 EBI-11115566 0.35 O95373 EBI-11115566 0.59 Q99567 EBI-11115566 0.35 O00505 EBI-11115566 0.71 Q9UBU9 EBI-11115566 0.35 Q6PJT7 EBI-11115566 0.35 Q9BW27 EBI-11115566 0.35 O14975 EBI-11115566 0.35 Q9HB58 EBI-11115566 0.35 Q53GS7 EBI-11115566 0.35 O75909 EBI-11115566 0.35 Q86VQ0 EBI-11363336 0.35 P48039 EBI-11577056 0.00 Q9WMX2 EBI-11513409 0.50 O96017 EBI-11579031 0.35 P27105 EBI-12452286 0.51 Q71U36 EBI-11897791 0.35 P03427 EBI-14404759 0.35 P46531 EBI-13915571 0.35 A9QM74 EBI-13950021 0.44 O15355 EBI-14023765 0.35 O15297 EBI-14024588 0.53 P36873 EBI-14025388 0.42 P56180 EBI-14025693 0.42 P62140 EBI-14026087 0.42 Q6IQ23 EBI-16398399 0.59 P10275 EBI-15187911 0.40 O43524 EBI-15187932 0.35 Q9NPC8 EBI-21617697 0.35 P61769 EBI-21675069 0.35 Q5SSJ5 EBI-21734720 0.35 Q2NL82 EBI-21815364 0.35 P54645 EBI-16361875 0.35 P80386 EBI-16362252 0.35 O95149 EBI-15577065 0.44 P52298 EBI-15798493 0.52 Q09161 EBI-15798552 0.40 Q9BUR4 EBI-15892338 0.35 P03950 EBI-16363282 0.35 Q14684 EBI-16686997 0.35 P62753 EBI-16799122 0.35 O94776 EBI-16803315 0.35 P09622 EBI-20304669 0.35 P36957 EBI-20305285 0.35 O00429 EBI-20305770 0.35 Q99714 EBI-20306067 0.35 P08559 EBI-20306509 0.35 P31040 EBI-20306992 0.35 P35610 EBI-20307233 0.35 P00441 EBI-20307497 0.35 P21796 EBI-20307902 0.35 Q9UPY3 EBI-20621330 0.35 P51957 EBI-20722397 0.35 P10636 EBI-20799058 0.35 A2A935 EBI-21024514 0.35 P14404 EBI-21026252 0.35 P56817 EBI-20992725 0.35 P04156 EBI-21014477 0.35 P04233 EBI-21258980 0.50 Q99558 EBI-21261374 0.50 Q15077 EBI-21262943 0.50 F5H1C8 EBI-21264930 0.50 Q9Y275 EBI-21266480 0.50 Q9H1C4 EBI-21266770 0.50 P42858 EBI-21132926 0.35 P12004 EBI-21236861 0.37 Q9NRI5 EBI-30827879 0.59 P09613 EBI-21497303 0.35 Q16526 EBI-21981854 0.35 Q13164 EBI-25374538 0.35 P11234 EBI-25376255 0.35 Q92934 EBI-25378368 0.35 P0DOF2 EBI-25603126 0.35 Q9BY14 EBI-25505396 0.35 A0A3G5BIZ0 EBI-25565269 0.43 Q9C0B5 EBI-25636144 0.35 B3CRR2 EBI-26357604 0.50 B3CTB0 EBI-26357616 0.35 Q53F19 EBI-26396827 0.35 P35226 EBI-27109494 0.35 Q8N488 EBI-27111302 0.35 Q99592 EBI-27093179 0.35 Q8NCK7 EBI-27103180 0.35 Q05D32 EBI-27113232 0.35 P0DTC4 EBI-28955127 0.35 Q5HYC2 EBI-30827309 0.44 O96028 EBI-30827207 0.44 Q6ZQQ2 EBI-30827357 0.44 Q6ZUB0 EBI-30827368 0.44 Q702N8 EBI-30827379 0.44 Q7RTY1 EBI-30827390 0.44 Q7Z6M1 EBI-30827401 0.44 Q8N398 EBI-30827412 0.44 O15397 EBI-30827163 0.44 O43307 EBI-30827174 0.44 O43520 EBI-30827185 0.44 O15321 EBI-30827152 0.44 O00750 EBI-30827141 0.44 Q15642 EBI-30827298 0.44 P0C874 EBI-30827232 0.44 Q5XG87 EBI-30827320 0.44 Q9H207 EBI-30827679 0.44 Q9C0D9 EBI-30827646 0.44 Q9BZ95 EBI-30827635 0.44 Q96R08 EBI-30827624 0.44 Q96HA1 EBI-30827588 0.44 Q92615 EBI-30827577 0.44 Q8NGY0 EBI-30827566 0.44 Q8NGI9 EBI-30827537 0.44 Q8NGA6 EBI-30827526 0.44 Q8N7C0 EBI-30827423 0.44 Q8NCP5 EBI-30827434 0.44 Q9H208 EBI-30827709 0.44 Q8NGA2 EBI-30827490 0.44 Q8NG92 EBI-30827464 0.44 Q9H6Z4 EBI-30827857 0.44 Q9NRD1 EBI-30827868 0.44 Q9Y399 EBI-30827920 0.44 Q9NZP0 EBI-30827909 0.44 GO:0005737 GO:0010494 GO:0005829 GO:0071782 GO:0070062 GO:0005576 GO:1904813 GO:0016020 GO:0042564 GO:0005635 GO:0031965 GO:0005643 GO:0005654 GO:0005634 GO:0035580 GO:0019899 GO:0051879 GO:0061676 GO:0061608 GO:0008139 GO:0019904 GO:0003723 GO:0031267 GO:0008270 GO:0030953 GO:0040001 GO:0045184 GO:0007079 GO:0007080 GO:0090307 GO:0006607 GO:0006606 GO:0031291 GO:0006610 GO:0006404 Unknown UniProt Sequence Analysis MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDPSVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKNYAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDIALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA 876 P70168 Importin Kpnb1 10090 None SL-0178 Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. UNIPROT P70168 UNIPROT Q62117 UNIPROT Q6GTI5 PDB 1GCJ PDB 1UKL Pfam PF03810 PROSITE PS50077 PROSITE PS50166 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}. P17955 EBI-15732706 0.36 P35922 EBI-16728828 0.35 P37198 EBI-16128776 0.44 P49790 EBI-15732587 0.52 P49792 EBI-15732742 0.36 P62826 EBI-15732723 0.44 P46527 EBI-540594 0.50 A3KGF7 EBI-688094 0.37 P11798 EBI-652692 0.37 Q12772 EBI-1037525 0.44 P01580 EBI-7892295 0.40 P03070 EBI-7892542 0.40 Q9Z0E3 EBI-2549816 0.35 Q14974 EBI-2555147 0.40 P49452 EBI-8573213 0.35 Q8BP00 EBI-4283417 0.35 Q8CG73 EBI-4284701 0.35 Q6AXH7 EBI-6876709 0.35 P52927 EBI-9986179 0.35 Q9P2S5 EBI-11694751 0.35 O54957 EBI-12602113 0.35 P32835 EBI-15558546 0.44 Q61712 EBI-15558601 0.44 P83953 EBI-16128832 0.44 Q61584 EBI-16729686 0.35 Q9NRI5 EBI-26612017 0.35 GO:0010494 GO:0005829 GO:0071782 GO:0042564 GO:0005635 GO:0031965 GO:0005643 GO:0005654 GO:0005634 GO:0032991 GO:0019899 GO:0051879 GO:0061676 GO:0019894 GO:0061608 GO:0008139 GO:0019904 GO:0044877 GO:0031267 GO:0030953 GO:0040001 GO:0045184 GO:0007079 GO:0007080 GO:0090307 GO:0006606 GO:0031291 GO:0006610 GO:0006404 Unknown UniProt Sequence Analysis MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVSQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLSTCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGSILEGPEPNQLKPLVIQAMPTLIELMKDPSVVVRDTTAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKNYAEYQVCLAAVGLVGDLCRALQSNILPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDIALAIGGEFKKYLEVVLNTLQQASQAQVDKSDFDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA 876 P52296 Importin Kpnb1 10116 None SL-0178 Cytoplasm {ECO:0000269|PubMed:7604027}. Nucleus envelope {ECO:0000269|PubMed:7604027}. UNIPROT P52296 Pfam PF03810 PROSITE PS50077 PROSITE PS50166 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}. P19357 EBI-921030 0.35 P21708 EBI-7621986 0.35 A0A142I9X8 EBI-11701393 0.35 P16310 EBI-15651327 0.40 P09619 EBI-22247316 0.35 P19332 EBI-26374040 0.35 GO:0010494 GO:0071782 GO:0042564 GO:0005635 GO:0005643 GO:0005634 GO:0032991 GO:0019899 GO:0051879 GO:0061676 GO:0019894 GO:0061608 GO:0008139 GO:0019904 GO:0044877 GO:0031267 GO:0030953 GO:0040001 GO:0045184 GO:0007079 GO:0007080 GO:0090307 GO:0006606 GO:0031291 GO:0006610 GO:0006404 Unknown UniProt Sequence Analysis MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIRLLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVSQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLSTCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGSILEGPEPNQLKPLVIQAMPTLIELMKDPSVVVRDTTAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLWKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKNYAECQVCLAAVGLVGDLCRALQSNILPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDITLAIGGEFKKYLEVVLNTLQQASQAQVDKSDFDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA 875 O13864 Importin kap95 284812 None SL-0178 SL-0185 Cytoplasm {ECO:0000250|UniProtKB:Q06142}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q06142}. UNIPROT O13864 Pfam PF03810 PROSITE PS50077 PROSITE PS50166 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}. GO:0005737 GO:1990023 GO:0005635 GO:0034399 GO:0005643 GO:0005634 GO:0005525 GO:0061608 GO:0008139 GO:0031267 GO:0051028 GO:0006606 Unknown UniProt Sequence Analysis MNAGEFLAQTLSPDANVRLNAEKQLENAARTDFAQYMVLLAQELANDNSMPYIRMAAGLALKNAITAREEARKLEYQQLWQSLPVEIKQQVKSLALQTLGSSEHQAGQSAAQLVAAIAAYELATNQWPDLMVTLVANVGEGQPSALKQHSLQTIGYICESVSPEVLSAQSNAILTAVVAGARKEEPDAAVRLAALGALYDSLEFVRENFNNEYERNYIMQVVCEATQSPEASIQTAAFGCLVKIMHLYYDTMPFYMEKALFALTTQGMYNTNEQVALQAVEFWSTVCEEEIEVNLEIQEAQDLNEVPARQNHGFARAAAADILPVLLKLLCNQDEDADEDDWNISMAAATCLQLFAQVVGDLIVNPVLAFVEQNIQNPDWHQREAAVMAFGSVLEGPNVAMLTPLVNQALPVLINMMVDPVIFVKDTTAWALGQISSFVADAINPEIHLSPMVSALLQGLTDNPRIVANCCWAFMNLVCHFAPVDNHQTSVMTPFYEAIIGSLLHVTDQKGNENNSRTSGYETLGTLITFSSDSVLPMIANVLSIILTRLETSIQMQSQILDVEDRANHDELQSNLCNVLTSIIRRFGPDIRTSSDQIMNLLLQTMQTAPKQSVVHEDVLLAIGAMMNSLEEQFEVYVPSFVPFLSSALSNEQEYQLCSVAVGLVGDLARALNAKILPYCDDFMTRLVQDLQSSVLDRNVKPAILSCFSDIALAIGAAFQTYLEAVMVLLQQASSVQAPPGANFSMIDYVDALRLGIVEAYVGITQAVRTDNRLDLIQPYVHSMFTLLNMITADPECSESLTRAALGLLGDLAESFPKGELKSYFAADWVAALLNSGKTKISSQQTKDLARWATEQVKRQARA 863 Q06142 Importin KAP95 559292 None SL-0178 SL-0185 Cytoplasm {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:9321403}. Nucleus {ECO:0000269|PubMed:9321403}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. UNIPROT Q06142 UNIPROT D6VYY6 PDB 2BKU PDB 3EA5 PDB 3ND2 PDB 5OWU Pfam PF03810 PROSITE PS50077 PROSITE PS50166 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}. P14907 EBI-1173482 0.72 P20676 EBI-789997 0.77 P32499 EBI-784458 0.78 P34160 EBI-806268 0.35 P39705 EBI-802293 0.77 P40069 EBI-784458 0.35 P40477 EBI-1173489 0.61 P48837 EBI-1269406 0.00 P49686 EBI-1266067 0.00 P49687 EBI-1269395 0.00 Q02199 EBI-1269417 0.00 Q02629 EBI-1566666 0.82 Q02630 EBI-1566676 0.67 Q02821 EBI-784458 0.94 Q03790 EBI-1269428 0.00 Q05166 EBI-1269439 0.00 P53911 EBI-531265 0.56 P53261 EBI-7108298 0.59 P53552 EBI-7108332 0.59 P10863 EBI-7108362 0.40 Q06142 EBI-7108412 0.40 Q12149 EBI-7108426 0.69 P43609 EBI-7108460 0.59 P06103 EBI-7108489 0.40 Q12499 EBI-7108547 0.40 P38219 EBI-784458 0.35 P07259 EBI-784458 0.35 P02557 EBI-784458 0.35 P02994 EBI-784458 0.35 P00359 EBI-784458 0.35 P11484 EBI-784458 0.53 P10592 EBI-784458 0.53 P18888 EBI-784458 0.35 P19358 EBI-784458 0.35 P10659 EBI-784458 0.35 P46654 EBI-784458 0.35 P26755 EBI-784458 0.35 P32337 EBI-784458 0.35 P41940 EBI-784458 0.35 P33892 EBI-784458 0.35 Q04673 EBI-786726 0.35 Q00578 EBI-787928 0.35 P38262 EBI-788896 0.35 P28496 EBI-793629 0.35 P36124 EBI-794754 0.53 Q12504 EBI-795637 0.35 Q12476 EBI-796671 0.35 Q02724 EBI-797293 0.56 P38703 EBI-799064 0.35 P53833 EBI-799459 0.35 P13259 EBI-799593 0.35 Q04779 EBI-801204 0.35 Q04182 EBI-802063 0.35 P50111 EBI-803477 0.35 P22336 EBI-804782 0.35 P39004 EBI-806863 0.35 Q08920 EBI-810994 0.67 P38111 EBI-813321 0.27 P28003 EBI-815383 0.27 P14832 EBI-816973 0.27 Q06218 EBI-817288 0.27 P19414 EBI-819202 0.27 P47077 EBI-854045 0.35 P47026 EBI-854100 0.35 Q05543 EBI-6995831 0.40 Q12460 EBI-7021174 0.40 P53072 EBI-7153942 0.40 Q05900 EBI-7156472 0.40 P47108 EBI-7162619 0.40 P38806 EBI-7181361 0.40 P19659 EBI-7308345 0.40 P53397 EBI-7440746 0.40 P22216 EBI-7510088 0.67 P49723 EBI-7582061 0.40 P0CG63 EBI-7613913 0.40 P0CX31 EBI-7651644 0.40 Q08446 EBI-7691677 0.40 Q03782 EBI-7728183 0.40 Q01476 EBI-7791695 0.40 P32357 EBI-7893646 0.40 P38991 EBI-8082572 0.40 P05694 EBI-8435372 0.40 P15019 EBI-6317331 0.00 P32562 EBI-2112894 0.53 P06700 EBI-2212712 0.40 P37366 EBI-2611238 0.35 P40187 EBI-2612903 0.35 Q12224 EBI-2613375 0.35 P32447 EBI-2881693 0.00 Q12495 EBI-16280136 0.53 P53687 EBI-2884664 0.00 Q12529 EBI-2887496 0.00 P39723 EBI-2887969 0.00 P27692 EBI-2888169 0.00 Q04116 EBI-2889003 0.00 P39101 EBI-3653413 0.35 P32527 EBI-3656017 0.35 P10591 EBI-3671852 0.35 P40150 EBI-3721078 0.35 P39079 EBI-3740059 0.35 P33416 EBI-3745091 0.35 P32589 EBI-3757079 0.35 P15108 EBI-3809579 0.35 P32835 EBI-16270361 0.35 Q08773 EBI-16271699 0.35 P42838 EBI-16272625 0.35 Q07623 EBI-16287594 0.35 Q00416 EBI-16421063 0.35 GO:0005737 GO:0005829 GO:0042564 GO:0005635 GO:0005643 GO:0005634 GO:0097718 GO:0005085 GO:0061676 GO:0061608 GO:0008139 GO:0044877 GO:0031267 GO:0051170 GO:0051028 GO:0006607 GO:0051292 GO:0006656 GO:0006606 GO:0006612 GO:0046822 GO:0060188 Unknown UniProt Sequence Analysis MSTAEFAQLLENSILSPDQNIRLTSETQLKKLSNDNFLQFAGLSSQVLIDENTKLEGRILAALTLKNELVSKDSVKTQQFAQRWITQVSPEAKNQIKTNALTALVSIEPRIANAAAQLIAAIADIELPHGAWPELMKIMVDNTGAEQPENVKRASLLALGYMCESADPQSQALVSSSNNILIAIVQGAQSTETSKAVRLAALNALADSLIFIKNNMEREGERNYLMQVVCEATQAEDIEVQAAAFGCLCKIMSLYYTFMKPYMEQALYALTIATMKSPNDKVASMTVEFWSTICEEEIDIAYELAQFPQSPLQSYNFALSSIKDVVPNLLNLLTRQNEDPEDDDWNVSMSAGACLQLFAQNCGNHILEPVLEFVEQNITADNWRNREAAVMAFGSIMDGPDKVQRTYYVHQALPSILNLMNDQSLQVKETTAWCIGRIADSVAESIDPQQHLPGVVQACLIGLQDHPKVATNCSWTIINLVEQLAEATPSPIYNFYPALVDGLIGAANRIDNEFNARASAFSALTTMVEYATDTVAETSASISTFVMDKLGQTMSVDENQLTLEDAQSLQELQSNILTVLAAVIRKSPSSVEPVADMLMGLFFRLLEKKDSAFIEDDVFYAISALAASLGKGFEKYLETFSPYLLKALNQVDSPVSITAVGFIADISNSLEEDFRRYSDAMMNVLAQMISNPNARRELKPAVLSVFGDIASNIGADFIPYLNDIMALCVAAQNTKPENGTLEALDYQIKVLEAVLDAYVGIVAGLHDKPEALFPYVGTIFQFIAQVAEDPQLYSEDATSRAAVGLIGDIAAMFPDGSIKQFYGQDWVIDYIKRTRSGQLFSQATKDTARWAREQQKRQLSL 861 O14089 Importin kap104 284812 None SL-0178 Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. UNIPROT O14089 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}. GO:0005829 GO:1990023 GO:0005635 GO:0034399 GO:0005634 GO:0032991 GO:0005525 GO:0061608 GO:0008139 GO:0051028 GO:0006606 Unknown UniProt Sequence Analysis MGDNPWVLQEQVLVELSEVIKNSLSENSQTRNAALNLLEKAKDIPDLNNYLTCILINATELSVSIRSAAGLLLKNNVRVSSLESGSGLQSLDYTKSTVIRGLCDPEQLIRGISGNVITTIISRWGISTWPEVLPQLMEMLSSPASTTQEGAFSALTKICEDSAQELDRDFNGTRPLDFMIPRFIELARHENPKIRTDALFCLNQFVLIQSQSLYAHIDTFLETCYALATDVSPNVRKNVCQALVYLLDVRPDKIAPSLGSIVEYMLYSTQDSDQNVALEACEFWLAIAEQPDLCSALGPYLDKIVPMLLQGMVYSDMDLLLLGNDADDYDVEDREEDIRPQHAKGKSRITLNTQGPITQQGSSNADADELEDEDEDDDEFDEDDDAFMDWNLRKCSAAALDVLSSFWKQRLLEIILPHLKQSLTSEDWKVQEAGVLAVGAIAEGCMDGMVQYLPELYPYFLSLLDSKKPLVRTITCWTLGRYSKWASCLESEEDRQKYFVPLLQGLLRMVVDNNKKVQEAGCSAFAILEEQAGPSLVPYLEPILTNLAFAFQKYQRKNVLILYDAVQTLADYVGSALNDKRYIELLITPLLQKWSMIPDDDPNLFPLFECLSSVAVALRDGFAPFAAETYARTFRILRNTLYLITTAQNDPTVDVPDRDFLVTTLDLVSGIIQALGSQVSPLLAQADPPLGQIIGICAKDEVPEVRQSAYALLGDMCMYCFDQIRPYCDALLVDMLPQMQLPLLHVSASNNAIWSAGEMALQLGKDMQQWVKPLLERLICILKSKKSNTTVLENVAITIGRLGVYNPELVAPHLELFYQPWFEIIKTVGENEEKDSAFRGFCNILACNPQALSYLLPMFVLCVAEYENPSAELRDMFQKILQGSVELFNGKASWQASPEVLAQIQAQYGV 910 P38217 Importin KAP104 559292 None SL-0178 SL-0185 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}. UNIPROT P38217 UNIPROT D6VQ19 Pfam PF02985 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 t