Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O94855
|
SC24D_HUMAN
|
MSQQGYVATPPYSQPQPGIGLSPPHYGHYGDPSHTASPTGMMKPAGPLGATATRGMLPPGPPPPGPHQFGQNGAHATGHPPQRFPGPPPVNNVASSHAPYQPSAQSSYPGPISTSSVTQLGSQLSAMQINSYGSGMAPPSQGPPGPLSATSLQTPPRPPQPSILQPGSQVLPPPPTTLNGPGASPLPLPMYRPDGLSGPPPPNAQYQPPPLPGQTLGAGYPPQQANSGPQMAGAQLSYPGGFPGGPAQMAGPPQPQKKLDPDSIPSPIQVIENDRASRGGQVYATNTRGQIPPLVTTDCMIQDQGNASPRFIRCTTYCFPCTSDMAKQAQIPLAAVIKPFATIPSNESPLYLVNHGESGPVRCNRCKAYMCPFMQFIEGGRRYQCGFCNCVNDVPPFYFQHLDHIGRRLDHYEKPELSLGSYEYVATLDYCRKSKPPNPPAFIFMIDVSYSNIKNGLVKLICEELKTMLEKIPKEEQEETSAIRVGFITYNKVLHFFNVKSNLAQPQMMVVTDVGEVFVPLLDGFLVNYQESQSVIHNLLDQIPDMFADSNENETVFAPVIQAGMEALKAADCPGKLFIFHSSLPTAEAPGKLKNRDDKKLVNTDKEKILFQPQTNVYDSLAKDCVAHGCSVTLFLFPSQYVDVASLGLVPQLTGGTLYKYNNFQMHLDRQQFLNDLRNDIEKKIGFDAIMRVRTSTGFRATDFFGGILMNNTTDVEMAAIDCDKAVTVEFKHDDKLSEDSGALIQCAVLYTTISGQRRLRIHNLGLNCSSQLADLYKSCETDALINFFAKSAFKAVLHQPLKVIREILVNQTAHMLACYRKNCASPSAASQLILPDSMKVLPVYMNCLLKNCVLLSRPEISTDERAYQRQLVMTMGVADSQLFFYPQLLPIHTLDVKSTMLPAAVRCSESRLSEEGIFLLANGLHMFLWLGVSSPPELIQGIFNVPSFAHINTDMTLLPEVGNPYSQQLRMIMGIIQQKRPYSMKLTIVKQREQPEMVFRQFLVEDKGLYGGSSYVDFLCCVHKEICQLLN
| null | null |
COPII-coated vesicle cargo loading [GO:0090110]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; in utero embryonic development [GO:0001701]; intracellular protein transport [GO:0006886]
|
COPII vesicle coat [GO:0030127]; cytosol [GO:0005829]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; intracellular membrane-bounded organelle [GO:0043231]
|
SNARE binding [GO:0000149]; zinc ion binding [GO:0008270]
|
PF00626;PF08033;PF04815;PF04811;PF04810;
|
2.60.40.1670;1.20.120.730;3.40.20.10;3.40.50.410;2.30.30.380;
|
SEC23/SEC24 family, SEC24 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:10329445}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53992}; Cytoplasmic side {ECO:0000250|UniProtKB:P53992}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:10329445}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53992}; Cytoplasmic side {ECO:0000250|UniProtKB:P53992}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P53992}.
| null | null | null | null | null |
FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex (PubMed:17499046, PubMed:18843296, PubMed:20427317). Plays a central role in cargo selection within the COPII complex and together with SEC24C may have a different specificity compared to SEC24A and SEC24B (PubMed:17499046, PubMed:18843296, PubMed:20427317). May more specifically package GPI-anchored proteins through the cargo receptor TMED10 (PubMed:20427317). May also be specific for IxM motif-containing cargos like the SNAREs GOSR2 and STX5 (PubMed:18843296). {ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
|
Homo sapiens (Human)
|
O94856
|
NFASC_HUMAN
|
MARQPPPPWVHAAFLLCLLSLGGAIEIPMDPSIQNELTQPPTITKQSAKDHIVDPRDNILIECEAKGNPAPSFHWTRNSRFFNIAKDPRVSMRRRSGTLVIDFRSGGRPEEYEGEYQCFARNKFGTALSNRIRLQVSKSPLWPKENLDPVVVQEGAPLTLQCNPPPGLPSPVIFWMSSSMEPITQDKRVSQGHNGDLYFSNVMLQDMQTDYSCNARFHFTHTIQQKNPFTLKVLTTRGVAERTPSFMYPQGTASSQMVLRGMDLLLECIASGVPTPDIAWYKKGGDLPSDKAKFENFNKALRITNVSEEDSGEYFCLASNKMGSIRHTISVRVKAAPYWLDEPKNLILAPGEDGRLVCRANGNPKPTVQWMVNGEPLQSAPPNPNREVAGDTIIFRDTQISSRAVYQCNTSNEHGYLLANAFVSVLDVPPRMLSPRNQLIRVILYNRTRLDCPFFGSPIPTLRWFKNGQGSNLDGGNYHVYENGSLEIKMIRKEDQGIYTCVATNILGKAENQVRLEVKDPTRIYRMPEDQVARRGTTVQLECRVKHDPSLKLTVSWLKDDEPLYIGNRMKKEDDSLTIFGVAERDQGSYTCVASTELDQDLAKAYLTVLADQATPTNRLAALPKGRPDRPRDLELTDLAERSVRLTWIPGDANNSPITDYVVQFEEDQFQPGVWHDHSKYPGSVNSAVLRLSPYVNYQFRVIAINEVGSSHPSLPSERYRTSGAPPESNPGDVKGEGTRKNNMEITWTPMNATSAFGPNLRYIVKWRRRETREAWNNVTVWGSRYVVGQTPVYVPYEIRVQAENDFGKGPEPESVIGYSGEDYPRAAPTEVKVRVMNSTAISLQWNRVYSDTVQGQLREYRAYYWRESSLLKNLWVSQKRQQASFPGDRLRGVVSRLFPYSNYKLEMVVVNGRGDGPRSETKEFTTPEGVPSAPRRFRVRQPNLETINLEWDHPEHPNGIMIGYTLKYVAFNGTKVGKQIVENFSPNQTKFTVQRTDPVSRYRFTLSARTQVGSGEAVTEESPAPPNEATPTAAPPTLPPTTVGATGAVSSTDATAIAATTEATTVPIIPTVAPTTIATTTTVATTTTTTAAATTTTESPPTTTSGTKIHESAPDEQSIWNVTVLPNSKWANITWKHNFGPGTDFVVEYIDSNHTKKTVPVKAQAQPIQLTDLYPGMTYTLRVYSRDNEGISSTVITFMTSTAYTNNQADIATQGWFIGLMCAIALLVLILLIVCFIKRSRGGKYPVREKKDVPLGPEDPKEEDGSFDYSDEDNKPLQGSQTSLDGTIKQQESDDSLVDYGEGGEGQFNEDGSFIGQYTVKKDKEETEGNESSEATSPVNAIYSLA
| null | null |
axon guidance [GO:0007411]; brain development [GO:0007420]; cell-cell adhesion [GO:0098609]; myelination [GO:0042552]; peripheral nervous system development [GO:0007422]
|
axon [GO:0030424]; axon initial segment [GO:0043194]; ficolin-1-rich granule membrane [GO:0101003]; focal adhesion [GO:0005925]; node of Ranvier [GO:0033268]; paranodal junction [GO:0033010]; plasma membrane [GO:0005886]
|
cell-cell adhesion mediator activity [GO:0098632]
|
PF13882;PF00041;PF07679;PF00047;PF13927;
|
2.60.40.10;
|
Immunoglobulin superfamily, L1/neurofascin/NgCAM family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30850329}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 8]: Cell junction, paranodal septate junction {ECO:0000269|PubMed:30124836}.
| null | null | null | null | null |
FUNCTION: Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions. {ECO:0000250}.
|
Homo sapiens (Human)
|
O94864
|
ST65G_HUMAN
|
MNLQRYWGEIPISSSQTNRSSFDLLPREFRLVEVHDPPLHQPSANKPKPPTMLDIPSEPCSLTIHTIQLIQHNRRLRNLIATAQAQNQQQTEGVKTEESEPLPSCPGSPPLPDDLLPLDCKNPNAPFQIRHSDPESDFYRGKGEPVTELSWHSCRQLLYQAVATILAHAGFDCANESVLETLTDVAHEYCLKFTKLLRFAVDREARLGQTPFPDVMEQVFHEVGIGSVLSLQKFWQHRIKDYHSYMLQISKQLSEEYERIVNPEKATEDAKPVKIKEEPVSDITFPVSEELEADLASGDQSLPMGVLGAQSERFPSNLEVEASPQASSAEVNASPLWNLAHVKMEPQESEEGNVSGHGVLGSDVFEEPMSGMSEAGIPQSPDDSDSSYGSHSTDSLMGSSPVFNQRCKKRMRKI
| null | null |
maintenance of protein location in nucleus [GO:0051457]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA repair [GO:0006282]; regulation of RNA splicing [GO:0043484]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SAGA complex [GO:0000124]
|
protein heterodimerization activity [GO:0046982]; transcription coactivator activity [GO:0003713]
|
PF07524;
|
1.10.20.10;
| null |
PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O94868
|
FCSD2_HUMAN
|
MQPPPRKVKVTQELKNIQVEQMTKLQAKHQAECDLLEDMRTFSQKKAAIEREYAQGMQKLASQYLKRDWPGVKADDRNDYRSMYPVWKSFLEGTMQVAQSRMNICENYKNFISEPARTVRSLKEQQLKRCVDQLTKIQTELQETVKDLAKGKKKYFETEQMAHAVREKADIEAKSKLSLFQSRISLQKASVKLKARRSECNSKATHARNDYLLTLAAANAHQDRYYQTDLVNIMKALDGNVYDHLKDYLIAFSRTELETCQAVQNTFQFLLENSSKVVRDYNLQLFLQENAVFHKPQPFQFQPCDSDTSRQLESETGTTEEHSLNKEARKWATRVAREHKNIVHQQRVLNDLECHGAAVSEQSRAELEQKIDEARENIRKAEIIKLKAEARLDLLKQIGVSVDTWLKSAMNQVMEELENERWARPPAVTSNGTLHSLNADTEREEGEEFEDNMDVFDDSSSSPSGTLRNYPLTCKVVYSYKASQPDELTIEEHEVLEVIEDGDMEDWVKARNKVGQVGYVPEKYLQFPTSNSLLSMLQSLAALDSRSHTSSNSTEAELVSGSLNGDASVCFVKALYDYEGQTDDELSFPEGAIIRILNKENQDDDGFWEGEFNGRIGVFPSVLVEELSASENGDTPWMREIQISPSPKPHASLPPLPLYDQPPSSPYPSPDKRSSLYFPRSPSANEKSLHAESPGFSQASRHTPETSYGKLRPVRAAPPPPTQNHRRPAEKIEDVEITLV
| null | null |
clathrin-dependent endocytosis [GO:0072583]; membrane organization [GO:0061024]; neuromuscular synaptic transmission [GO:0007274]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of Arp2/3 complex-mediated actin nucleation [GO:2000601]; protein transport [GO:0015031]; regulation of actin filament polymerization [GO:0030833]
|
anchoring junction [GO:0070161]; clathrin-coated pit [GO:0005905]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; stereocilium shaft [GO:0120043]
|
phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]
|
PF00611;PF00018;PF14604;
|
1.20.1270.60;2.30.30.40;
| null |
PTM: Phosphorylated. Phosphorylation on a Ser residue is important for recruitment to the cell membrane and for its role in promoting endocytosis. {ECO:0000269|PubMed:30249660}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3USJ8}. Cell junction {ECO:0000269|PubMed:14627983}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:29887380, ECO:0000269|PubMed:30249660}. Cell membrane {ECO:0000269|PubMed:14627983, ECO:0000269|PubMed:29887380, ECO:0000269|PubMed:30249660}; Peripheral membrane protein {ECO:0000269|PubMed:14627983, ECO:0000269|PubMed:30249660}; Cytoplasmic side {ECO:0000269|PubMed:14627983, ECO:0000269|PubMed:30249660}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q3USJ8}. Note=Partially localized at clathrin-coated pits at the cell membrane (PubMed:30249660). Detected at the cell membrane at sites around clathrin-coated pits, very close to the clathrin-coated pits but not an intrinsic part of the clathrin-coated pits (PubMed:29887380). Colocalizes at cell-cell contacts with CDH1, but is not detected at tight junctions (PubMed:14627983). {ECO:0000269|PubMed:14627983, ECO:0000269|PubMed:29887380, ECO:0000269|PubMed:30249660}.
| null | null | null | null | null |
FUNCTION: Adapter protein that plays a role in endocytosis via clathrin-coated pits. Contributes to the internalization of cell surface receptors, such as integrin ITGB1 and transferrin receptor (PubMed:29887380). Promotes endocytosis of EGFR in cancer cells, and thereby contributes to the down-regulation of EGFR signaling (PubMed:30249660). Recruited to clathrin-coated pits during a mid-to-late stage of assembly, where it is required for normal progress from U-shaped intermediate stage pits to terminal, omega-shaped pits (PubMed:29887380). Binds to membranes enriched in phosphatidylinositol 3,4-bisphosphate or phosphatidylinositol 3,4,5-trisphosphate (PubMed:29887380). When bound to membranes, promotes actin polymerization via its interaction with WAS and/or WASL which leads to the activation of the Arp2/3 complex. Does not promote actin polymerisation in the absence of membranes (PubMed:29887380). {ECO:0000269|PubMed:29887380, ECO:0000269|PubMed:30249660}.
|
Homo sapiens (Human)
|
O94874
|
UFL1_HUMAN
|
MADAWEEIRRLAADFQRAQFAEATQRLSERNCIEIVNKLIAQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQVINVDLIHIENRIGDIIKSEKHVQLVLGQLIDENYLDRLAEEVNDKLQESGQVTISELCKTYDLPGNFLTQALTQRLGRIISGHIDLDNRGVIFTEAFVARHKARIRGLFSAITRPTAVNSLISKYGFQEQLLYSVLEELVNSGRLRGTVVGGRQDKAVFVPDIYSRTQSTWVDSFFRQNGYLEFDALSRLGIPDAVSYIKKRYKTTQLLFLKAACVGQGLVDQVEASVEEAISSGTWVDIAPLLPTSLSVEDAAILLQQVMRAFSKQASTVVFSDTVVVSEKFINDCTELFRELMHQKAEKEMKNNPVHLITEEDLKQISTLESVSTSKKDKKDERRRKATEGSGSMRGGGGGNAREYKIKKVKKKGRKDDDSDDESQSSHTGKKKPEISFMFQDEIEDFLRKHIQDAPEEFISELAEYLIKPLNKTYLEVVRSVFMSSTTSASGTGRKRTIKDLQEEVSNLYNNIRLFEKGMKFFADDTQAALTKHLLKSVCTDITNLIFNFLASDLMMAVDDPAAITSEIRKKILSKLSEETKVALTKLHNSLNEKSIEDFISCLDSAAEACDIMVKRGDKKRERQILFQHRQALAEQLKVTEDPALILHLTSVLLFQFSTHSMLHAPGRCVPQIIAFLNSKIPEDQHALLVKYQGLVVKQLVSQSKKTGQGDYPLNNELDKEQEDVASTTRKELQELSSSIKDLVLKSRKSSVTEE
|
2.3.2.-
| null |
DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; erythrocyte differentiation [GO:0030218]; hematopoietic stem cell differentiation [GO:0060218]; negative regulation of apoptotic process [GO:0043066]; negative regulation of IRE1-mediated unfolded protein response [GO:1903895]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein ubiquitination [GO:0031397]; osteoblast differentiation [GO:0001649]; positive regulation of autophagy [GO:0010508]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of glial cell proliferation [GO:0060252]; protein K69-linked ufmylation [GO:1990592]; protein ufmylation [GO:0071569]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of inflammatory response [GO:0050727]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; regulation of protein localization [GO:0032880]; response to endoplasmic reticulum stress [GO:0034976]; response to L-glutamate [GO:1902065]; reticulophagy [GO:0061709]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; neuron projection [GO:0043005]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; site of double-strand break [GO:0035861]
|
protein kinase binding [GO:0019901]; UFM1 ligase activity [GO:0061666]; UFM1 transferase activity [GO:0071568]
|
PF09743;
| null |
UFL1 family
|
PTM: Ubiquitinated, leading to its degradation by the proteasome (PubMed:20164180). Interaction with CDK5RAP3 protects both proteins against ubiquitination and degradation via the proteasome (PubMed:20164180). {ECO:0000269|PubMed:20164180}.; PTM: Phosphorylated at Ser-462 by ATM, enhancing protein ligase activity and promoting ATM activation in a positive feedback loop. {ECO:0000269|PubMed:30886146}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:20164180, ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:32160526}. Cytoplasm, cytosol {ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:30886146}. Nucleus {ECO:0000269|PubMed:30886146}. Chromosome {ECO:0000269|PubMed:30886146}. Note=Recruited to double-strand breaks by the MRE11-RAD50-NBN (MRN) complex following DNA damage. {ECO:0000269|PubMed:30886146}.
| null | null | null | null | null |
FUNCTION: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (PubMed:20018847, PubMed:20164180, PubMed:20228063, PubMed:25219498, PubMed:30783677, PubMed:32160526, PubMed:37311461). In response to endoplasmic reticulum stress, recruited to the endoplasmic reticulum membrane by DDRGK1, and mediates ufmylation of proteins such as RPN1 and RPL26/uL24, thereby promoting reticulophagy of endoplasmic reticulum sheets (PubMed:32160526). Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) via ERN1/IRE1-alpha (PubMed:23152784, PubMed:32160526). Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis, blood vessel morphogenesis or inflammatory response (PubMed:32050156). Regulates inflammation in response to endoplasmic reticulum stress by promoting reticulophagy, leading to inhibit the activity of the NF-kappa-B transcription factor (By similarity). Mediates ufmylation of DDRGK1 and CDK5RAP3; the role of these modifications is however unclear: as both DDRGK1 and CDK5RAP3 act as substrate adapters for ufmylation, it is uncertain whether ufmylation of these proteins is a collateral effect or is required for ufmylation (PubMed:20018847, PubMed:20531390). Catalyzes ufmylation of various subunits of the ribosomal complex or associated components, such as RPS3/uS3, RPS20/uS10, RPL10/uL16, RPL26/uL24 and EIF6 (By similarity). Anchors CDK5RAP3 in the cytoplasm, preventing its translocation to the nucleus which allows expression of the CCND1 cyclin and progression of cells through the G1/S transition (PubMed:20531390). Also involved in the response to DNA damage: recruited to double-strand break sites following DNA damage and mediates monoufmylation of histone H4 and ufmylation of MRE11 (PubMed:30783677, PubMed:30886146). Catalyzes ufmylation of TRIP4, thereby playing a role in nuclear receptor-mediated transcription (PubMed:25219498). Required for hematopoietic stem cell function and hematopoiesis (By similarity). Required for cardiac homeostasis (By similarity). {ECO:0000250|UniProtKB:A1A4I9, ECO:0000250|UniProtKB:Q8CCJ3, ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:20164180, ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:20531390, ECO:0000269|PubMed:23152784, ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:30783677, ECO:0000269|PubMed:30886146, ECO:0000269|PubMed:32050156, ECO:0000269|PubMed:32160526, ECO:0000269|PubMed:37311461}.
|
Homo sapiens (Human)
|
O94875
|
SRBS2_HUMAN
|
MSYYQRPFSPSAYSLPASLNSSIVMQHGTSLDSTDTYPQHAQSLDGTTSSSIPLYRSSEEEKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDDDTDMYNTPYTYNAGLYNPPYSAQSHPAAKTQTYRPLSKSHSDNSPNAFKDASSPVPPPHVPPPVPPLRPRDRSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQHERPASLYQSSIDRSLERPMSSASMASDFRKRRKSEPAVGPPRGLGDQSASRTSPGRVDLPGSSTTLTKSFTSSSPSSPSRAKGGDDSKICPSLCSYSGLNGNPSSELDYCSTYRQHLDVPRDSPRAISFKNGWQMARQNAEIWSSTEETVSPKIKSRSCDDLLNDDCDSFPDPKVKSESMGSLLCEEDSKESCPMAWGSPYVPEVRSNGRSRIRHRSARNAPGFLKMYKKMHRINRKDLMNSEVICSVKSRILQYESEQQHKDLLRAWSQCSTEEVPRDMVPTRISEFEKLIQKSKSMPNLGDDMLSPVTLEPPQNGLCPKRRFSIEYLLEEENQSGPPARGRRGCQSNALVPIHIEVTSDEQPRAHVEFSDSDQDGVVSDHSDYIHLEGSSFCSESDFDHFSFTSSESFYGSSHHHHHHHHHHHRHLISSCKGRCPASYTRFTTMLKHERARHENTEEPRRQEMDPGLSKLAFLVSPVPFRRKKNSAPKKQTEKAKCKASVFEALDSALKDICDQIKAEKKRGSLPDNSILHRLISELLPDVPERNSSLRALRRSPLHQPLHPLPPDGAIHCPPYQNDCGRMPRSASFQDVDTANSSCHHQDRGGALQDRESPRSYSSTLTDMGRSAPRERRGTPEKEKLPAKAVYDFKAQTSKELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKLTPPEKAQPARPPPPAQPGEIGEAIAKYNFNADTNVELSLRKGDRVILLKRVDQNWYEGKIPGTNRQGIFPVSYVEVVKKNTKGAEDYPDPPIPHSYSSDRIHSLSSNKPQRPVFTHENIQGGGEPFQALYNYTPRNEDELELRESDVIDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
| null | null |
cell growth involved in cardiac muscle cell development [GO:0061049]; Notch signaling pathway [GO:0007219]
|
actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; dendrite [GO:0030425]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; synapse [GO:0045202]; Z disc [GO:0030018]
|
cytoskeletal anchor activity [GO:0008093]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307]
|
PF00018;PF14604;PF02208;
|
2.30.30.40;
| null |
PTM: Ubiquitinated by CBL. {ECO:0000269|PubMed:12475393}.; PTM: Dephosphorylated by PTPN12. {ECO:0000269|PubMed:18559503}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16125169, ECO:0000269|PubMed:9211900}. Apical cell membrane {ECO:0000269|PubMed:18559503}. Cell junction, focal adhesion {ECO:0000269|PubMed:18559503}. Cell projection, lamellipodium {ECO:0000269|PubMed:18559503}. Note=Found at the Z-disk sarcomeres, stress fibers, dense bodies and focal adhesion. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells. {ECO:0000269|PubMed:18559503}.
| null | null | null | null | null |
FUNCTION: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269|PubMed:12475393, ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:9211900}.
|
Homo sapiens (Human)
|
O94876
|
TMCC1_HUMAN
|
MEPSGSEQLFEDPDPGGKSQDAEARKQTESEQKLSKMTHNALENINVIGQGLKHLFQHQRRRSSVSPHDVQQIQADPEPEMDLESQNACAEIDGVPTHPTALNRVLQQIRVPPKMKRGTSLHSRRGKPEAPKGSPQINRKSGQEMTAVMQSGRPRSSSTTDAPTSSAMMEIACAAAAAAAACLPGEEGTAERIERLEVSSLAQTSSAVASSTDGSIHTDSVDGTPDPQRTKAAIAHLQQKILKLTEQIKIAQTARDDNVAEYLKLANSADKQQAARIKQVFEKKNQKSAQTILQLQKKLEHYHRKLREVEQNGIPRQPKDVFRDMHQGLKDVGAKVTGFSEGVVDSVKGGFSSFSQATHSAAGAVVSKPREIASLIRNKFGSADNIPNLKDSLEEGQVDDAGKALGVISNFQSSPKYGSEEDCSSATSGSVGANSTTGGIAVGASSSKTNTLDMQSSGFDALLHEIQEIRETQARLEESFETLKEHYQRDYSLIMQTLQEERYRCERLEEQLNDLTELHQNEILNLKQELASMEEKIAYQSYERARDIQEALEACQTRISKMELQQQQQQVVQLEGLENATARNLLGKLINILLAVMAVLLVFVSTVANCVVPLMKTRNRTFSTLFLVVFIAFLWKHWDALFSYVERFFSSPR
| null | null |
endoplasmic reticulum organization [GO:0007029]; endosomal transport [GO:0016197]; endosome fission [GO:0140285]; endosome membrane tubulation [GO:0097750]; membrane fission [GO:0090148]
|
cytosol [GO:0005829]; endomembrane system [GO:0012505]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-endosome membrane contact site [GO:0140284]; rough endoplasmic reticulum [GO:0005791]
|
identical protein binding [GO:0042802]
|
PF10267;
| null |
TEX28 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24454821, ECO:0000269|PubMed:30220460}; Multi-pass membrane protein {ECO:0000255}. Note=Specifically localizes to contact sites between the endoplasmic reticulum and endosomes that are spatially and temporally linked to endosome fission. {ECO:0000269|PubMed:30220460}.
| null | null | null | null | null |
FUNCTION: Endoplasmic reticulum membrane protein that promotes endoplasmic reticulum-associated endosome fission (PubMed:30220460). Localizes to contact sites between the endoplasmic reticulum and endosomes and acts by promoting recruitment of the endoplasmic reticulum to endosome tubules for fission (PubMed:30220460). Endosome membrane fission of early and late endosomes is essential to separate regions destined for lysosomal degradation from carriers to be recycled to the plasma membrane (PubMed:30220460). {ECO:0000269|PubMed:30220460}.
|
Homo sapiens (Human)
|
O94880
|
PHF14_HUMAN
|
MDRSSKRRQVKPLAASLLEALDYDSSDDSDFKVGDASDSEGSGNGSEDASKDSGEGSCSDSEENILEEELNEDIKVKEEQLKNSAEEEVLSSEKQLIKMEKKEEEENGERPRKKKEKEKEKEKEKEKEKEREKEKEKATVSENVAASAAATTPATSPPAVNTSPSVPTTTTATEEQVSEPKKWNLRRNRPLLDFVSMEELNDMDDYDSEDDNDWRPTVVKRKGRSASQKEGSDGDNEDDEDEGSGSDEDENDEGNDEDHSSPASEGGCKKKKSKVLSRNSADDEELTNDSLTLSQSKSNEDSLILEKSQNWSSQKMDHILICCVCLGDNSEDADEIIQCDNCGITVHEGCYGVDGESDSIMSSASENSTEPWFCDACKCGVSPSCELCPNQDGIFKETDAGRWVHIVCALYVPGVAFGDIDKLRPVTLTEMNYSKYGAKECSFCEDPRFARTGVCISCDAGMCRAYFHVTCAQKEGLLSEAAAEEDIADPFFAYCKQHADRLDRKWKRKNYLALQSYCKMSLQEREKQLSPEAQARINARLQQYRAKAELARSTRPQAWVPREKLPRPLTSSASAIRKLMRKAELMGISTDIFPVDNSDTSSSVDGRRKHKQPALTADFVNYYFERNMRMIQIQENMAEQKNIKDKLENEQEKLHVEYNKLCESLEELQNLNGKLRSEGQGIWALLGRITGQKLNIPAILRAPKERKPSKKEGGTQKTSTLPAVLYSCGICKKNHDQHLLLLCDTCKLHYHLGCLDPPLTRMPRKTKNSYWQCSECDQAGSSDMEADMAMETLPDGTKRSRRQIKEPVKFVPQDVPPEPKKIPIRNTRTRGRKRSFVPEEEKHEERVPRERRQRQSVLQKKPKAEDLRTECATCKGTGDNENLVRCDECRLCYHFGCLDPPLKKSPKQTGYGWICQECDSSSSKEDENEAERKNISQELNMEQKNPKK
| null | null |
germinal center B cell differentiation [GO:0002314]; lung alveolus development [GO:0048286]; mesenchymal cell proliferation [GO:0010463]; mesenchymal cell proliferation involved in lung development [GO:0060916]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of mesenchymal cell proliferation [GO:0072201]; negative regulation of mesenchymal cell proliferation involved in lung development [GO:2000791]; negative regulation of platelet-derived growth factor receptor-alpha signaling pathway [GO:2000584]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
histone binding [GO:0042393]; histone reader activity [GO:0140566]; zinc ion binding [GO:0008270]
|
PF00628;PF13831;PF13832;
|
2.30.30.1150;3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:23688586}. Chromosome {ECO:0000269|PubMed:23688586}. Note=Mainly localized in the nucleus of interphase cells. In mitotic cells, colocalizes with condensed chromatin during metaphase and anaphase. {ECO:0000269|PubMed:23688586}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:23688586}.
| null | null | null | null | null |
FUNCTION: Histone-binding protein (PubMed:23688586). Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity). Represses PDGFRA expression, thus playing a role in regulation of mesenchymal cell proliferation (By similarity). Suppresses the expression of CDKN1A/p21 by reducing the level of trimethylation of histone H3 'Lys-4', leading to enhanced proliferation of germinal center B cells (By similarity). {ECO:0000250|UniProtKB:A0A286Y9D1, ECO:0000250|UniProtKB:Q9D4H9, ECO:0000269|PubMed:23688586}.
|
Homo sapiens (Human)
|
O94885
|
SASH1_HUMAN
|
MEDAGAAGPGPEPEPEPEPEPEPAPEPEPEPKPGAGTSEAFSRLWTDVMGILDGSLGNIDDLAQQYADYYNTCFSDVCERMEELRKRRVSQDLEVEKPDASPTSLQLRSQIEESLGFCSAVSTPEVERKNPLHKSNSEDSSVGKGDWKKKNKYFWQNFRKNQKGIMRQTSKGEDVGYVASEITMSDEERIQLMMMVKEKMITIEEALARLKEYEAQHRQSAALDPADWPDGSYPTFDGSSNCNSREQSDDETEESVKFKRLHKLVNSTRRVRKKLIRVEEMKKPSTEGGEEHVFENSPVLDERSALYSGVHKKPLFFDGSPEKPPEDDSDSLTTSPSSSSLDTWGAGRKLVKTFSKGESRGLIKPPKKMGTFFSYPEEEKAQKVSRSLTEGEMKKGLGSLSHGRTCSFGGFDLTNRSLHVGSNNSDPMGKEGDFVYKEVIKSPTASRISLGKKVKSVKETMRKRMSKKYSSSVSEQDSGLDGMPGSPPPSQPDPEHLDKPKLKAGGSVESLRSSLSGQSSMSGQTVSTTDSSTSNRESVKSEDGDDEEPPYRGPFCGRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVLSEDEEKPKRPTRRRRKGRPPQPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEYDSNSDQSGSQEKLLVDSQGLSGCSPRDSGCYESSENLENGKTRKASLLSAKSSTEPSLKSFSRNQLGNYPTLPLMKSGDALKQGQEEGRLGGGLAPDTSKSCDPPGVTGLNKNRRSLPVSICRSCETLEGPQTVDTWPRSHSLDDLQVEPGAEQDVPTEVTEPPPQIVPEVPQKTTASSTKAQPLEQDSAVDNALLLTQSKRFSEPQKLTTKKLEGSIAASGRGLSPPQCLPRNYDAQPPGAKHGLARTPLEGHRKGHEFEGTHHPLGTKEGVDAEQRMQPKIPSQPPPVPAKKSRERLANGLHPVPMGPSGALPSPDAPCLPVKRGSPASPTSPSDCPPALAPRPLSGQAPGSPPSTRPPPWLSELPENTSLQEHGVKLGPALTRKVSCARGVDLETLTENKLHAEGIDLTEEPYSDKHGRCGIPEALVQRYAEDLDQPERDVAANMDQIRVKQLRKQHRMAIPSGGLTEICRKPVSPGCISSVSDWLISIGLPMYAGTLSTAGFSTLSQVPSLSHTCLQEAGITEERHIRKLLSAARLFKLPPGPEAM
| null | null |
positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of lipopolysaccharide-mediated signaling pathway [GO:0031666]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of p38MAPK cascade [GO:1900745]; protein polyubiquitination [GO:0000209]; regulation of epithelial cell migration [GO:0010632]; regulation of protein autoubiquitination [GO:1902498]; regulation of protein K63-linked ubiquitination [GO:1900044]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; protein-containing complex [GO:0032991]
|
G-protein alpha-subunit binding [GO:0001965]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]
|
PF00536;PF07647;PF07653;PF12485;
|
2.30.30.40;1.10.150.50;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23333244}.
| null | null | null | null | null |
FUNCTION: Is a positive regulator of NF-kappa-B signaling downstream of TLR4 activation. It acts as a scaffold molecule to assemble a molecular complex that includes TRAF6, MAP3K7, CHUK and IKBKB, thereby facilitating NF-kappa-B signaling activation (PubMed:23776175). Regulates TRAF6 and MAP3K7 ubiquitination (PubMed:23776175). Involved in the regulation of cell mobility (PubMed:23333244, PubMed:23776175, PubMed:25315659). Regulates lipolysaccharide (LPS)-induced endothelial cell migration (PubMed:23776175). Is involved in the regulation of skin pigmentation through the control of melanocyte migration in the epidermis (PubMed:23333244). {ECO:0000269|PubMed:23333244, ECO:0000269|PubMed:23776175, ECO:0000269|PubMed:25315659}.
|
Homo sapiens (Human)
|
O94886
|
CSCL1_HUMAN
|
MMDSPFLELWQSKAVSIREQLGLGDRPNDSYCYNSAKNSTVLQGVTFGGIPTVLLIDVSCFLFLILVFSIIRRRFWDYGRIALVSEADSESRFQRLSSTSSSGQQDFENELGCCPWLTAIFRLHDDQILEWCGEDAIHYLSFQRHIIFLLVVVSFLSLCVILPVNLSGDLLDKDPYSFGRTTIANLQTDNDLLWLHTIFAVIYLFLTVGFMRHHTQSIKYKEENLVRRTLFITGLPRDARKETVESHFRDAYPTCEVVDVQLCYNVAKLIYLCKEKKKTEKSLTYYTNLQVKTGQRTLINPKPCGQFCCCEVLGCEWEDAISYYTRMKDRLLERITEEERHVQDQPLGMAFVTFQEKSMATYILKDFNACKCQSLQCKGEPQPSSHSRELYTSKWTVTFAADPEDICWKNLSIQGLRWWLQWLGINFTLFLGLFFLTTPSIILSTMDKFNVTKPIHALNNPIISQFFPTLLLWSFSALLPSIVYYSTLLESHWTKSGENQIMMTKVYIFLIFMVLILPSLGLTSLDFFFRWLFDKTSSEASIRLECVFLPDQGAFFVNYVIASAFIGNGMELLRLPGLILYTFRMIMAKTAADRRNVKQNQAFQYEFGAMYAWMLCVFTVIVAYSITCPIIAPFGLIYILLKHMVDRHNLYFVYLPAKLEKGIHFAAVNQALAAPILCLFWLYFFSFLRLGMKAPATLFTFLVLLLTILVCLAHTCFGCFKHLSPLNYKTEEPASDKGSEAEAHMPPPFTPYVPRILNGLASERTALSPQQQQQQTYGAIHNISGTIPGQCLAQSATGSVAAAPQEA
| null | null | null |
centriolar satellite [GO:0034451]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579]; tertiary granule membrane [GO:0070821]
|
calcium-activated cation channel activity [GO:0005227]; mechanosensitive monoatomic ion channel activity [GO:0008381]; nucleic acid binding [GO:0003676]; osmolarity-sensing monoatomic cation channel activity [GO:1990760]
|
PF14703;PF02714;PF13967;
|
3.30.70.330;
|
CSC1 (TC 1.A.17) family
|
PTM: N-Glycosylated. {ECO:0000269|PubMed:37543036}.
|
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:20957757}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:37543036}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Acts as an osmosensitive calcium-permeable cation channel (PubMed:30382938, PubMed:31587869). Mechanosensitive ion channel that converts mechanical stimuli into a flow of ion (PubMed:30382938, PubMed:31587869, PubMed:37543036). {ECO:0000250|UniProtKB:Q91YT8, ECO:0000269|PubMed:30382938, ECO:0000269|PubMed:31587869, ECO:0000269|PubMed:37543036}.
|
Homo sapiens (Human)
|
O94887
|
FARP2_HUMAN
|
MGEIEGTYRVLQTAGMRLGAQTPVGVSTLEPGQTLLPRMQEKHLHLRVKLLDNTMEIFDIEPKCDGQVLLTQVWKRLNLVECDYFGMEFQNTQSYWIWLEPMKPIIRQIRRPKNVVLRLAVKFFPPDPGQLQEEYTRYLFALQLKRDLLEERLTCADTTAALLTSHLLQSEIGDYDETLDREHLKVNEYLPGQQHCLEKILEFHQKHVGQTPAESDFQVLEIARKLEMYGIRFHMASDREGTKIQLAVSHMGVLVFQGTTKINTFNWSKVRKLSFKRKRFLIKLHPEVHGPYQDTLEFLLGSRDECKNFWKICVEYHTFFRLLDQPKPKAKAVFFSRGSSFRYSGRTQKQLVDYFKDSGMKRIPYERRHSKTHTSVRALTADLPKQSISFPEGLRTPASPSSANAFYSLSPSTLVPSGLPEFKDSSSSLTDPQVSYVKSPAAERRSGAVAGGPDTPSAQPLGPPALQPGPGLSTKSPQPSPSSRKSPLSLSPAFQVPLGPAEQGSSPLLSPVLSDAGGAGMDCEEPRHKRVPADEAYFIVKEILATERTYLKDLEVITVWFRSAVVKEDAMPATLMTLLFSNIDPIYEFHRGFLREVEQRLALWEGPSKAHTKGSHQRIGDILLRNMRQLKEFTSYFQRHDEVLTELEKATKRCKKLEAVYKEFELQKVCYLPLNTFLLKPIQRLLHYRLLLRRLCGHYSPGHHDYADCHDALKAITEVTTTLQHILIRLENLQKLTELQRDLVGIENLIAPGREFIREGCLHKLTKKGLQQRMFFLFSDMLLYTSKGVAGTSHFRIRGLLPLQGMLVEESDNEWSVPHCFTIYAAQKTIVVAASTRLEKEKWMLDLNSAIQAAKSGGDTAPALPGRTVCTRPPRSPNEVSLEQESEDDARGVRSSLEGHGQHRANTTMHVCWYRNTSVSRADHSAAVENQLSGYLLRKFKNSHGWQKLWVVFTNFCLFFYKTHQDDYPLASLPLLGYSVSIPREADGIHKDYVFKLQFKSHVYFFRAESKYTFERWMEVIQGASSSAGRAPSIVQDGPQPSSGLEGMVRGKEE
| null | null |
actin cytoskeleton organization [GO:0030036]; cell adhesion [GO:0007155]; hair cycle process [GO:0022405]; neuron remodeling [GO:0016322]; osteoclast differentiation [GO:0030316]; podosome assembly [GO:0071800]; Rac protein signal transduction [GO:0016601]; regulation of integrin activation [GO:0033623]; semaphorin-plexin signaling pathway [GO:0071526]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]
|
cytoskeletal protein binding [GO:0008092]; guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF08736;PF09380;PF00373;PF09379;PF00169;PF00621;
|
1.20.80.10;1.20.900.10;2.30.29.30;
| null | null | null | null | null | null | null | null |
FUNCTION: Functions as a guanine nucleotide exchange factor that activates RAC1. May have relatively low activity. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton. Plays a role in TNFSF11-mediated osteoclast differentiation, especially in podosome rearrangement and reorganization of the actin cytoskeleton. Regulates the activation of ITGB3, integrin signaling and cell adhesion (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O94888
|
UBXN7_HUMAN
|
MAAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPVRTDPGTATNHQGLPAVDSEILEMPPEKADGVVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN
| null | null |
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]
|
RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]
|
PF13899;PF14555;PF00789;
|
1.10.8.10;3.40.30.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22537386}.
| null | null | null | null | null |
FUNCTION: Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates. {ECO:0000269|PubMed:22537386}.
|
Homo sapiens (Human)
|
O94892
|
ZN432_HUMAN
|
MINAQELLTLEDVTVEFTWEEWQLLGPFQKDLYRDVMLEIYSNLLSMGYQVSKPDALSKLERGEEPWTMEDERHSRICPENNEVDDHLQDHLENQRMLKSVEQYHEHNAFGNTASQTKSLCLFRENHDTFELYIKTLKSNLSLVNQNKSCEINNSTKFSGDGKSFLHGNYEELYSAAKFSVSTKANSTKSQVSKHQRTHEIEKNHVCSECGKAFVKKSQLTDHERVHTGEKPYGCTLCAKVFSRKSRLNEHQRIHKREKSFICSECGKVFTMKSRLIEHQRTHTGEKPYICNECGKGFPGKRNLIVHQRNHTGEKSYICSECGKGFTGKSMLIIHQRTHTGEKPYICSECGKGFTTKHYVIIHQRNHTGEKPYICNECGKGFTMKSRMIEHQRTHTGEKPYICSECGKGFPRKSNLIVHQRNHTVEKSYLCSECGKGFTVKSMLIIHQRTHTGEKPYTCSECGKGFPLKSRLIVHQRTHTGEKPYRCSECGKGFIVNSGLMLHQRTHTGEKPYICNECGKGFAFKSNLVVHQRTHTGEKPFMCSECGKGFTMKRYLIVHQQIHTEEKSCICSECGRGFAKETELALHKQVHTGEKPYGCNECGKGFTMKSRLIVHQRTHTGEKPFVCSECRKAFSSKRNLIVHQRTHNGNKP
| null | null |
DNA damage response [GO:0006974]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
damaged DNA binding [GO:0003684]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF01352;PF00096;
|
6.10.140.140;3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:37823600}. Note=Excluded from nucleolus (PubMed:37823600). Responds to DNA damage by relocating to damage sites, this relocation is PAR-dependent (PubMed:37823600). {ECO:0000269|PubMed:37823600}.
| null | null | null | null | null |
FUNCTION: Homologous recombination repressor that functions as a poly(ADP-ribose) (PAR) reader regulating DNA damage response and PARP inhibition. Once recruited to DNA lesions via DNA-, in a PAR-dependent mechanism, stimulates PARP1 activity (PubMed:37823600). Binds preferentially ssDNA and inhibits EXO1-mediated resection, probably through a PAR-independent DNA-binding mechanism (PubMed:37823600). {ECO:0000269|PubMed:37823600}.
|
Homo sapiens (Human)
|
O94898
|
LRIG2_HUMAN
|
MAPAPLGVPEEQLLGCRSRVLSRLLFIAQTALLLLPAAGAGLCPAPCSCRIPLLDCSRRKLPAPSWRALSGLLPPDTAILDFSHNRLSNWNISLESQTLQEVKMNYNELTEIPYFGEPTSNITLLSLVHNIIPEINAQALQFYPALESLDLSSNIISEIKTSSFPRMQLKYLNLSNNRITTLEAGCFDNLSSSLLVVKLNRNRMSMIPPKIFKLPHLQFLELKRNRIKIVEGLTFQGLDSLRSLKMQRNGISKLKDGAFFGLNNMEELELEHNNLTRVNKGWLYGLRMLQQLYVSQNAIERISPDAWEFCQRLSELDLSYNQLTRLDESAFVGLSLLERLNLGDNRVTHIADGVFRFLSNLQTLDLRNNEISWAIEDASEAFAGLTSLTKLILQGNQIKSITKKAFIGLESLEHLDLNNNAIMSIQENAFSQTHLKELILNTSSLLCDCHLKWLLQWLVDNNFQHSVNVSCAHPEWLAGQSILNVDLKDFVCDDFLKPQIRTHPETIIALRGMNVTLTCTAVSSSDSPMSTVWRKDSEILYDVDTENFVRYWQQAGEALEYTSILHLFNVNFTDEGKYQCIVTNHFGSNYSQKAKLTVNEMPSFLKTPMDLTIRTGAMARLECAAEGHPAPQISWQKDGGTDFPAARERRMHVMPEDDVFFIANVKIEDMGIYSCMAQNTAGGLSANASLTVLETPSFIRPLEDKTVTRGETAVLQCIAGGSPAPRLNWTKDDGPLLVTERHFFAAANQLLIIVDAGLEDAGKYTCIMSNTLGTERGHIYLNVISSPNCDSSQSSIGHEDDGWTTVGIVIIVVVCCVVGTSLIWVIVIYHMRRKNEDYSITNTEELNLPADIPSYLSSQGTLSEPQEGYSNSEAGSHQQLMPPANGYIHKGTDGGTGTRVICSDCYDNANIYSRTREYCPYTYIAEEDVLDQTLSSLMVQMPKETYLVHPPQDTTALESLIPSANREPSAFPTNHERISEKKLPSTQMSGETLQRPVWNINRELGLPHPPFSQQPVHESPQLHQNEGLAGREPDCSASSMSCHRLQDHAFDFSRTRNIQDGSEGT
| null | null |
innervation [GO:0060384]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of axon regeneration [GO:0048681]; negative regulation of membrane protein ectodomain proteolysis [GO:0051045]; positive regulation of protein localization to cell surface [GO:2000010]; protein localization to cell surface [GO:0034394]; regulation of neuron migration [GO:2001222]; regulation of platelet-derived growth factor receptor signaling pathway [GO:0010640]; sensory perception of sound [GO:0007605]
|
cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; growth cone [GO:0030426]; intracellular vesicle [GO:0097708]; plasma membrane [GO:0005886]
|
signaling receptor binding [GO:0005102]
|
PF07679;PF13927;PF13855;PF01463;
|
2.60.40.10;3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15145052}; Single-pass type I membrane protein {ECO:0000269|PubMed:15145052}. Cytoplasm {ECO:0000269|PubMed:15145052}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O94900
|
TOX_HUMAN
|
MDVRFYPPPAQPAAAPDAPCLGPSPCLDPYYCNKFDGENMYMSMTEPSQDYVPASQSYPGPSLESEDFNIPPITPPSLPDHSLVHLNEVESGYHSLCHPMNHNGLLPFHPQNMDLPEITVSNMLGQDGTLLSNSISVMPDIRNPEGTQYSSHPQMAAMRPRGQPADIRQQPGMMPHGQLTTINQSQLSAQLGLNMGGSNVPHNSPSPPGSKSATPSPSSSVHEDEGDDTSKINGGEKRPASDMGKKPKTPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDGLGEEQKQVYKKKTEAAKKEYLKQLAAYRASLVSKSYSEPVDVKTSQPPQLINSKPSVFHGPSQAHSALYLSSHYHQQPGMNPHLTAMHPSLPRNIAPKPNNQMPVTVSIANMAVSPPPPLQISPPLHQHLNMQQHQPLTMQQPLGNQLPMQVQSALHSPTMQQGFTLQPDYQTIINPTSTAAQVVTQAMEYVRSGCRNPPPQPVDWNNDYCSSGGMQRDKALYLT
| null | null |
CD4-positive, alpha-beta T cell lineage commitment [GO:0043373]; CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment [GO:0002362]; CD8-positive, alpha-beta T cell lineage commitment [GO:0043375]; cerebral cortex neuron differentiation [GO:0021895]; chromatin organization [GO:0006325]; leukocyte differentiation [GO:0002521]; lymph node development [GO:0048535]; natural killer cell differentiation [GO:0001779]; NK T cell lineage commitment [GO:0002364]; Peyer's patch development [GO:0048541]; positive regulation of natural killer cell differentiation [GO:0032825]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of neuron projection development [GO:0010976]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of positive thymic T cell selection [GO:1902232]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
chromatin DNA binding [GO:0031490]
|
PF00505;
|
1.10.30.10;
|
High motility group (HMG) box superfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator with a major role in neural stem cell commitment and corticogenesis as well as in lymphoid cell development and lymphoid tissue organogenesis (By similarity). Binds to GC-rich DNA sequences in the proximity of transcription start sites and may alter chromatin structure, modifying access of transcription factors to DNA. During cortical development, controls the neural stem cell pool by inhibiting the switch from proliferative to differentiating progenitors. Beyond progenitor cells, promotes neurite outgrowth in newborn neurons migrating to reach the cortical plate. May activate or repress critical genes for neural stem cell fate such as SOX2, EOMES and ROBO2 (By similarity). Plays an essential role in the development of lymphoid tissue-inducer (LTi) cells, a subset necessary for the formation of secondary lymphoid organs: peripheral lymph nodes and Peyer's patches. Acts as a developmental checkpoint and regulates thymocyte positive selection toward T cell lineage commitment. Required for the development of various T cell subsets, including CD4-positive helper T cells, CD8-positive cytotoxic T cells, regulatory T cells and CD1D-dependent natural killer T (NKT) cells. Required for the differentiation of common lymphoid progenitors (CMP) to innate lymphoid cells (ILC) (By similarity). May regulate the NOTCH-mediated gene program, promoting differentiation of the ILC lineage. Required at the progenitor phase of NK cell development in the bone marrow to specify NK cell lineage commitment (By similarity) (PubMed:21126536). Upon chronic antigen stimulation, diverts T cell development by promoting the generation of exhaustive T cells, while suppressing effector and memory T cell programming. May regulate the expression of genes encoding inhibitory receptors such as PDCD1 and induce the exhaustion program, to prevent the overstimulation of T cells and activation-induced cell death (By similarity). {ECO:0000250|UniProtKB:Q66JW3, ECO:0000269|PubMed:21126536}.
|
Homo sapiens (Human)
|
O94901
|
SUN1_HUMAN
|
MDFSRLHMYSPPQCVPENTGYTYALSSSYSSDALDFETEHKLDPVFDSPRMSRRSLRLATTACTLGDGEAVGADSGTSSAVSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGVSHGGTVSLQDAVTRRPPVLDESWIREQTTVDHFWGLDDDGDLKGGNKAAIQGNGDVGAAAATAHNGFSCSNCSMLSERKDVLTAHPAAPGPVSRVYSRDRNQKCYFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGKAASGVFWWLGIGWYQFVTLISWLNVFLLTRCLRNICKFLVLLIPLFLLLAGLSLRGQGNFFSFLPVLNWASMHRTQRVDDPQDVFKPTTSRLKQPLQGDSEAFPWHWMSGVEQQVASLSGQCHHHGENLRELTTLLQKLQARVDQMEGGAAGPSASVRDAVGQPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQLLPTVEHLQLELDQLKSELSSWRHVKTGCETVDAVQERVDVQVREMVKLLFSEDQQGGSLEQLLQRFSSQFVSKGDLQTMLRDLQLQILRNVTHHVSVTKQLPTSEAVVSAVSEAGASGITEAQARAIVNSALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALMSLFGIPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTLEHIPKTLSPTGNISSAPKDFAVYGLENEYQEEGQLLGQFTYDQDGESLQMFQALKRPDDTAFQIVELRIFSNWGHPEYTCLYRFRVHGEPVK
| null | null |
centrosome localization [GO:0051642]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic attachment of telomere to nuclear envelope [GO:0070197]; nuclear matrix anchoring at nuclear membrane [GO:0090292]; nucleokinesis involved in cell motility in cerebral cortex radial glia guided migration [GO:0021817]; ossification [GO:0001503]; response to mechanical stimulus [GO:0009612]; spermatogenesis [GO:0007283]
|
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; meiotic nuclear membrane microtubule tethering complex [GO:0034993]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear membrane [GO:0031965]
|
cytoskeleton-nuclear membrane anchor activity [GO:0140444]; identical protein binding [GO:0042802]; lamin binding [GO:0005521]; protein-membrane adaptor activity [GO:0043495]
|
PF18580;PF09387;PF07738;
|
2.60.120.260;
| null |
PTM: The disulfide bond with KASH domain-containing nesprins is required for stability of the respective LINC complexes under tensile forces. {ECO:0000250|UniProtKB:Q9UH99}.
|
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19933576}. Note=At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. {ECO:0000250|UniProtKB:Q9D666}.
| null | null | null | null | null |
FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (PubMed:18039933, PubMed:18396275). The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration (By similarity). Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly (By similarity). Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis (By similarity). Helps to define the distribution of nuclear pore complexes (NPCs) (By similarity). Required for efficient localization of SYNE4 in the nuclear envelope (By similarity). May be involved in nuclear remodeling during sperm head formation in spermatogenesis (By similarity). May play a role in DNA repair by suppressing non-homologous end joining repair to facilitate the repair of DNA cross-links (PubMed:24375709). {ECO:0000250|UniProtKB:Q9D666, ECO:0000269|PubMed:18039933, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:24375709}.
|
Homo sapiens (Human)
|
O94905
|
ERLN2_HUMAN
|
MAQLGAVVAVASSFFCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDSAGSVSKQFEGLADKLSFGLEDEPLETATKEN
| null | null |
cholesterol metabolic process [GO:0008203]; ERAD pathway [GO:0036503]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of fatty acid biosynthetic process [GO:0045717]; regulation of cholesterol biosynthetic process [GO:0045540]; SREBP signaling pathway [GO:0032933]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
cholesterol binding [GO:0015485]; ubiquitin protein ligase binding [GO:0031625]
|
PF01145;
|
3.30.479.30;
|
Band 7/mec-2 family
|
PTM: Deubiquitinated by USP25; leading to stabilization. {ECO:0000250|UniProtKB:O75477}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031}; Single-pass type II membrane protein {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031}. Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane.
| null | null | null | null | null |
FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs) such as ITPR1 (PubMed:17502376, PubMed:19240031). Promotes sterol-accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin ligase complex (PubMed:21343306). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. May promote ER retention of the SCAP-SREBF complex (PubMed:24217618). {ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031, ECO:0000269|PubMed:21343306, ECO:0000269|PubMed:24217618}.
|
Homo sapiens (Human)
|
O94906
|
PRP6_HUMAN
|
MNKKKKPFLGMPAPLGYVPGLGRGATGFTTRSDIGPARDANDPVDDRHAPPGKRTVGDQMKKNQAADDDDEDLNDTNYDEFNGYAGSLFSSGPYEKDDEEADAIYAALDKRMDERRKERREQREKEEIEKYRMERPKIQQQFSDLKRKLAEVTEEEWLSIPEVGDARNKRQRNPRYEKLTPVPDSFFAKHLQTGENHTSVDPRQTQFGGLNTPYPGGLNTPYPGGMTPGLMTPGTGELDMRKIGQARNTLMDMRLSQVSDSVSGQTVVDPKGYLTDLNSMIPTHGGDINDIKKARLLLKSVRETNPHHPPAWIASARLEEVTGKLQVARNLIMKGTEMCPKSEDVWLEAARLQPGDTAKAVVAQAVRHLPQSVRIYIRAAELETDIRAKKRVLRKALEHVPNSVRLWKAAVELEEPEDARIMLSRAVECCPTSVELWLALARLETYENARKVLNKARENIPTDRHIWITAAKLEEANGNTQMVEKIIDRAITSLRANGVEINREQWIQDAEECDRAGSVATCQAVMRAVIGIGIEEEDRKHTWMEDADSCVAHNALECARAIYAYALQVFPSKKSVWLRAAYFEKNHGTRESLEALLQRAVAHCPKAEVLWLMGAKSKWLAGDVPAARSILALAFQANPNSEEIWLAAVKLESENDEYERARRLLAKARSSAPTARVFMKSVKLEWVQDNIRAAQDLCEEALRHYEDFPKLWMMKGQIEEQKEMMEKAREAYNQGLKKCPHSTPLWLLLSRLEEKIGQLTRARAILEKSRLKNPKNPGLWLESVRLEYRAGLKNIANTLMAKALQECPNSGILWSEAIFLEARPQRRTKSVDALKKCEHDPHVLLAVAKLFWSQRKITKAREWFHRTVKIDSDLGDAWAFFYKFELQHGTEEQQEEVRKRCESAEPRHGELWCAVSKDIANWQKKIGDILRLVAGRIKNTF
| null | null |
mRNA splicing, via spliceosome [GO:0000398]; positive regulation of miRNA metabolic process [GO:2000630]; positive regulation of primary miRNA processing [GO:2000636]; positive regulation of transcription by RNA polymerase II [GO:0045944]; RNA localization [GO:0006403]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal complex assembly [GO:0000245]; spliceosomal tri-snRNP complex assembly [GO:0000244]
|
catalytic step 2 spliceosome [GO:0071013]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]
|
identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; ribonucleoprotein complex binding [GO:0043021]; RNA binding [GO:0003723]
|
PF06424;PF13432;PF14559;
|
1.25.40.10;
| null |
PTM: Phosphorylated by PRP4K during spliceosome assembly. {ECO:0000269|PubMed:20118938}.
|
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:10561546, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:34023904}. Nucleus speckle {ECO:0000269|PubMed:21549338}. Note=Localized in splicing speckles. {ECO:0000269|PubMed:21549338}.
| null | null | null | null | null |
FUNCTION: Involved in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome (PubMed:20118938, PubMed:21549338, PubMed:28781166). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation. {ECO:0000269|PubMed:12039962, ECO:0000269|PubMed:20118938, ECO:0000269|PubMed:21549338, ECO:0000269|PubMed:28781166}.
|
Homo sapiens (Human)
|
O94907
|
DKK1_HUMAN
|
MMALGAAGATRVFVAMVAAALGGHPLLGVSATLNSVLNSNAIKNLPPPLGGAAGHPGSAVSAAPGILYPGGNKYQTIDNYQPYPCAEDEECGTDEYCASPTRGGDAGVQICLACRKRRKRCMRHAMCCPGNYCKNGICVSSDQNHFRGEIEETITESFGNDHSTLDGYSRRTTLSSKMYHTKGQEGSVCLRSSDCASGLCCARHFWSKICKPVLKEGQVCTKHRRKGSHGLEIFQRCYCGEGLSCRIQKDHHQASNSSRLHTCQRH
| null | null |
canonical Wnt signaling pathway [GO:0060070]; cell morphogenesis [GO:0000902]; embryonic limb morphogenesis [GO:0030326]; endocardial cushion development [GO:0003197]; endoderm formation [GO:0001706]; face morphogenesis [GO:0060325]; forebrain development [GO:0030900]; hair follicle development [GO:0001942]; heart induction [GO:0003129]; heart valve development [GO:0003170]; learning or memory [GO:0007611]; limb development [GO:0060173]; mesoderm formation [GO:0001707]; motor learning [GO:0061743]; negative regulation of apoptotic process [GO:0043066]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cardiac muscle cell differentiation [GO:2000726]; negative regulation of mesodermal cell fate specification [GO:0042662]; negative regulation of neuron projection development [GO:0010977]; negative regulation of ossification [GO:0030279]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of presynapse assembly [GO:1905607]; negative regulation of protein binding [GO:0032091]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of Wnt signaling pathway [GO:0030178]; negative regulation of Wnt-Frizzled-LRP5/6 complex assembly [GO:1904723]; positive regulation of gene expression [GO:0010628]; positive regulation of JNK cascade [GO:0046330]; positive regulation of midbrain dopaminergic neuron differentiation [GO:1904958]; positive regulation of Wnt signaling pathway, calcium modulating pathway [GO:0045813]; positive regulation of Wnt signaling pathway, planar cell polarity pathway [GO:2000096]; regulation of dopaminergic neuron differentiation [GO:1904338]; regulation of endodermal cell fate specification [GO:0042663]; regulation of neuron apoptotic process [GO:0043523]; regulation of receptor internalization [GO:0002090]; regulation of synaptic transmission, glutamatergic [GO:0051966]; response to retinoic acid [GO:0032526]; synapse pruning [GO:0098883]; Wnt signaling pathway involved in somitogenesis [GO:0090244]
|
early endosome membrane [GO:0031901]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
co-receptor binding [GO:0039706]; growth factor activity [GO:0008083]; low-density lipoprotein particle receptor binding [GO:0050750]; receptor antagonist activity [GO:0048019]
|
PF04706;PF21481;PF21479;
|
2.10.80.10;
|
Dickkopf family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6 (PubMed:22000856). DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (PubMed:17143291). Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity (By similarity). {ECO:0000250|UniProtKB:O54908, ECO:0000269|PubMed:22000856, ECO:0000303|PubMed:17143291}.
|
Homo sapiens (Human)
|
O94910
|
AGRL1_HUMAN
|
MARLAAVLWNLCVTAVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELVFPQEEYPRKNSIQLSAKTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGPGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEDKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGTHGSLKTSAMRSNTRYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGGPEPPRGRNLADAAAFEKMIISELVHNNLRGSSSAAKGPPPPEPPVPPVPGGGGEEEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPSEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPGLEGPGPDGDGQMQLVTSL
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell surface receptor signaling pathway [GO:0007166]; G protein-coupled receptor signaling pathway [GO:0007186]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; positive regulation of synapse maturation [GO:0090129]
|
axon [GO:0030424]; growth cone [GO:0030426]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; synapse [GO:0045202]
|
carbohydrate binding [GO:0030246]; cell adhesion molecule binding [GO:0050839]; G protein-coupled receptor activity [GO:0004930]; latrotoxin receptor activity [GO:0016524]
|
PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191;
|
1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10;
|
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
|
PTM: Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus (By similarity). {ECO:0000250|UniProtKB:O88917}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35907405}; Multi-pass membrane protein. Cell projection, axon {ECO:0000250|UniProtKB:O88917}. Cell projection, growth cone {ECO:0000250|UniProtKB:O88917}. Synapse {ECO:0000250|UniProtKB:O88917}. Presynaptic cell membrane {ECO:0000250|UniProtKB:O88917}. Synapse, synaptosome {ECO:0000250|UniProtKB:O88917}. Note=Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts. {ECO:0000250|UniProtKB:O88917}.
| null | null | null | null | null |
FUNCTION: Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells (PubMed:35907405). Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor probably implicated in the regulation of exocytosis (By similarity). {ECO:0000250|UniProtKB:O88917, ECO:0000269|PubMed:35907405}.
|
Homo sapiens (Human)
|
O94911
|
ABCA8_HUMAN
|
MRKRKISVCQQTWALLCKNFLKKWRMKRESLMEWLNSLLLLLCLYIYPHSHQVNDFSSLLTMDLGRVDTFNESRFSVVYTPVTNTTQQIMNKVASTPFLAGKEVLGLPDEESIKEFTANYPEEIVRVTFTNTYSYHLKFLLGHGMPAKKEHKDHTAHCYETNEDVYCEVSVFWKEGFVALQAAINAAIIEITTNHSVMEELMSVTGKNMKMHSFIGQSGVITDLYLFSCIISFSSFIYYASVNVTRERKRMKALMTMMGLRDSAFWLSWGLLYAGFIFIMALFLALVIRSTQFIILSGFMVVFSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLTVFWGCLGFTSLYRHLPASLEWILSLLSPFAFMLGMAQLLHLDYDLNSNAFPHPSDGSNLIVATNFMLAFDTCLYLALAIYFEKILPNEYGHRRPPLFFLKSSFWSQTQKTDHVALEDEMDADPSFHDSFEQAPPEFQGKEAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWGIGYHLSLQLNEICVEENITSLVKQHIPDAKLSAKSEGKLIYTLPLERTNKFPELYKDLDSYPDLGIENYGVSMTTLNEVFLKLEGKSTINESDIAILGEVQAEKADDTERLVEMEQVLSSLNKMRKTIGGVALWRQQICAIARVRLLKLKHERKALLALLLILMAGFCPLLVEYTMVKIYQNSYTWELSPHLYFLAPGQQPHDPLTQLLIINKTGASIDDFIQSVEHQNIALEVDAFGTRNGTDDPSYNGAITVCCNEKNYSFSLACNAKRLNCFPVLMDIVSNGLLGMVKPSVHIRTERSTFLENGQDNPIGFLAYIMFWLVLTSSCPPYIAMSSIDDYKNRARSQLRISGLSPSAYWFGQALVDVSLYFLVFVFIYLMSYISNFEDMLLTIIHIIQIPCAVGYSFSLIFMTYVISFIFRKGRKNSGIWSFCFYVVTVFSVAGFAFSIFESDIPFIFTFLIPPATMIGCLFLSSHLLFSSLFSEERMDVQPFLVFLIPFLHFIIFLFTLRCLEWKFGKKSMRKDPFFRISPRSSDVCQNPEEPEGEDEDVQMERVRTANALNSTNFDEKPVIIASCLRKEYAGKRKGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKVKNLAQVEPLHAEILRLFPQAARQERYSSLMVYKLPVEDVQPLAQAFFKLEKVKQSFDLEEYSLSQSTLEQVFLELSKEQELGDFEEDFDPSVKWKLLPQEEP
|
7.6.2.-
| null |
cholesterol efflux [GO:0033344]; cholesterol transport [GO:0030301]; lipid transport [GO:0006869]; positive regulation of cholesterol efflux [GO:0010875]; regulation of cholesterol efflux [GO:0010874]; sphingomyelin biosynthetic process [GO:0006686]; transmembrane transport [GO:0055085]; xenobiotic transport [GO:0042908]
|
basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; plasma membrane [GO:0005886]
|
ABC-type transporter activity [GO:0140359]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; lipid transporter activity [GO:0005319]
|
PF12698;PF00005;
|
3.40.50.300;
|
ABC transporter superfamily, ABCA family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28882873, ECO:0000269|PubMed:29300488}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8K440}. Note=Predominantly expressed on the sinusoidal plasma membrane. {ECO:0000250|UniProtKB:Q8K440}.
|
CATALYTIC ACTIVITY: [Isoform 3]: Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate + taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:29300488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053; Evidence={ECO:0000305|PubMed:29300488}; CATALYTIC ACTIVITY: Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) + phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:23560799, ECO:0000269|PubMed:28882873, ECO:0000269|PubMed:29300488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052; Evidence={ECO:0000269|PubMed:28882873, ECO:0000269|PubMed:29300488}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + estrone 3-sulfate(out) + H2O = ADP + estrone 3-sulfate(in) + H(+) + phosphate; Xref=Rhea:RHEA:65956, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60050, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:12379217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65957; Evidence={ECO:0000305|PubMed:12379217}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + H2O + leukotriene C4(out) = ADP + H(+) + leukotriene C4(in) + phosphate; Xref=Rhea:RHEA:65960, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57973, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:12379217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65961; Evidence={ECO:0000305|PubMed:12379217}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + H2O + taurocholate(out) = ADP + H(+) + phosphate + taurocholate(in); Xref=Rhea:RHEA:65964, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:12379217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65965; Evidence={ECO:0000305|PubMed:12379217}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:65968, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82961, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:12379217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65969; Evidence={ECO:0000305|PubMed:12379217};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30.4 uM for estradiol-beta-glucuronide {ECO:0000269|PubMed:12379217}; KM=0.1 uM for LTC4 {ECO:0000269|PubMed:12379217}; KM=10.3 uM for taurochlorate {ECO:0000269|PubMed:12379217}; KM=5 uM for PAH {ECO:0000269|PubMed:12379217}; KM=0.5 uM for estrone sulfate {ECO:0000269|PubMed:12379217}; KM=0.4 uM for ochratoxin A {ECO:0000269|PubMed:12379217};
| null | null | null |
FUNCTION: [Isoform 1]: Catalyzes ATP-dependent import of organic anions such as taurocholate and estrone sulfate (PubMed:12379217). In vitro, also imports ochratoxin A (PubMed:12379217). Also mediates cholesterol efflux independent of apolipoprotein, and plays a role in sphingomyelin production in oligodendrocytes (PubMed:23560799). {ECO:0000269|PubMed:12379217, ECO:0000269|PubMed:23560799}.; FUNCTION: [Isoform 3]: Catalyzes ATP-dependent efflux of cholesterol and taurocholate (PubMed:29300488). Interaction with ABCA1 potentiates cholesterol efflux to lipid-free APOA1, which regulates high-density lipoprotein cholesterol levels (PubMed:28882873). {ECO:0000269|PubMed:28882873, ECO:0000269|PubMed:29300488}.
|
Homo sapiens (Human)
|
O94913
|
PCF11_HUMAN
|
MSEQTPAEAGAAGAREDACRDYQSSLEDLTFNSKPHINMLTILAEENLPFAKEIVSLIEAQTAKAPSSEKLPVMYLMDSIVKNVGREYLTAFTKNLVATFICVFEKVDENTRKSLFKLRSTWDEIFPLKKLYALDVRVNSLDPAWPIKPLPPNVNTSSIHVNPKFLNKSPEEPSTPGTVVSSPSISTPPIVPDIQKNLTQEQLIRQQLLAKQKQLLELQQKKLELELEQAKAQLAVSLSVQQETSNLGPGSAPSKLHVSQIPPMAVKAPHQVPVQSEKSRPGPSLQIQDLKGTNRDPRLNRISQHSHGKDQSHRKEFLMNTLNQSDTKTSKTIPSEKLNSSKQEKSKSGEKITKKELDQLDSKSKSKSKSPSPLKNKLSHTKDLKNQESESMRLSDMNKRDPRLKKHLQDKTDGKDDDVKEKRKTAEKKDKDEHMKSSEHRLAGSRNKIINGIVQKQDTITEESEKQGTKPGRSSTRKRSRSRSPKSRSPIIHSPKRRDRRSPKRRQRSMSPTSTPKAGKIRQSGAKQSHMEEFTPPSREDRNAKRSTKQDIRDPRRMKKTEEERPQETTNQHSTKSGTEPKENVENWQSSKSAKRWKSGWEENKSLQQVDEHSKPPHLRHRESWSSTKGILSPRAPKQQQHRLSVDANLQIPKELTLASKRELLQKTSERLASGEITQDDFLVVVHQIRQLFQYQEGVREEQRSPFNDRFPLKRPRYEDSDKPFVDSPASRFAGLDTNQRLTALAEDRPLFDGPSRPSVARDGPTKMIFEGPNKLSPRIDGPPTPASLRFDGSPGQMGGGGPLRFEGPQGQLGGGCPLRFEGPPGPVGTPLRFEGPIGQAGGGGFRFEGSPGLRFEGSPGGLRFEGPGGQPVGGLRFEGHRGQPVGGLRFEGPHGQPVGGLRFDNPRGQPVGGLRFEGGHGPSGAAIRFDGPHGQPGGGIRFEGPLLQQGVGMRFEGPHGQSVAGLRFEGQHNQLGGNLRFEGPHGQPGVGIRFEGPLVQQGGGMRFEGPSVPGGGLRIEGPLGQGGPRFEGCHALRFDGQPGQPSLLPRFDGLHGQPGPRFERTPGQPGPQRFDGPPGQQVQPRFDGVPQRFDGPQHQQASRFDIPLGLQGTRFDNHPSQRLESVSFNQTGPYNDPPGNAFNAPSQGLQFQRHEQIFDSPQGPNFNGPHGPGNQSFSNPLNRASGHYFDEKNLQSSQFGNFGNIPAPMTVGNIQASQQVLSGVAQPVAFGQGQQFLPVHPQNPGFVQNPSGALPKAYPDNHLSQVDVNELFSKLLKTGILKLSQTDSATTQVSEVTAQPPPEEEEDQNEDQDVPDLTNFTVEELKQRYDSVINRLYTGIQCYSCGMRFTTSQTDVYADHLDWHYRQNRTEKDVSRKVTHRRWYYSLTDWIEFEEIADLEERAKSQFFEKVHEEVVLKTQEAAKEKEFQSVPAGPAGAVESCEICQEQFEQYWDEEEEEWHLKNAIRVDGKIYHPSCYEDYQNTSSFDCTPSPSKTPVENPLNIMLNIVKNELQEPCDSPKVKEERIDTPPACTEESIATPSEIKTENDTVESV
| null | null |
co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway [GO:0180010]; mRNA polyadenylation [GO:0006378]; termination of RNA polymerase II transcription [GO:0006369]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; mRNA cleavage factor complex [GO:0005849]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
mRNA binding [GO:0003729]; RNA polymerase II complex binding [GO:0000993]
|
PF11526;PF04818;PF20827;PF20845;PF20844;
|
1.25.40.90;
| null |
PTM: Phosphorylation at Ser-120 and/or Thr-121 by WNK1 weakens its association with POLR2A/RNA polymerase II, promoting transcript release from the chromatin template and mRNA export to the cytoplasm. {ECO:0000269|PubMed:29196535}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29196535}.
| null | null | null | null | null |
FUNCTION: Component of pre-mRNA cleavage complex II, which promotes transcription termination by RNA polymerase II. {ECO:0000269|PubMed:11060040, ECO:0000269|PubMed:29196535}.
|
Homo sapiens (Human)
|
O94915
|
FRYL_HUMAN
|
MSNITIDPDVKPGEYVIKSLFAEFAVQAEKKIEVVMAEPLEKLLSRSLQRGEDLQFDQLISSMSSVAEHCLPSLLRTLFDWYRRQNGTEDESYEYRPRSSTKSKGDEQQRERDYLLERRDLAVDFIFCLVLVEVLKQIPVHPVPDPLVHEVLNLAFKHFKHKEGYSGTNTGNVHIIADLYAEVIGVLAQSKFQAVRKKFVTELKELRQKEQSPHVVQSVISLIMGMKFFRVKMYPVEDFEASFQFMQECAQYFLEVKDKDIKHALAGLFVEILIPVAAAVKNEVNVPCLKNFVEMLYQTTFELSSRKKHSLALYPLITCLLCVSQKQFFLNNWHIFLQNCLSHLKNKDPKMSRVALESLYRLLWVYVIRIKCESNTVTQSRLMSIVSALFPKGSRSVVPRDTPLNIFVKIIQFIAQERLDFAMKEIIFDLLSVGKSTKTFTINPERMNIGLRVFLVIADSLQQKDGEPPMPTTGVILPSGNTLRVKKIFLNKTLTDEEAKVIGMSVYYPQVRKALDSILRHLDKEVGRPMCMTSVQMSNKEPEDMITGERKPKIDLFRTCIAAIPRLIPDGMSRTDLIELLARLTIHMDEELRALAFNTLQALMLDFPDWREDVLSGFVYFIVREVTDVHPTLLDNAVKMLVQLINQWKQAAQMHNKNQDTQHGVANGASHPPPLERSPYSNVFHVVEGFALVILCSSRPATRRLAVSVLREIRALFALLEIPKGDDELAIDVMDRLSPSILESFIHLTGADQTTLLYCPSSIDLQTLAEWNSSPISHQFDVISPSHIWIFAHVTQGQDPWIISLSSFLKQENLPKHCSTAVSYAWMFAYTRLQLLSPQVDINSPINAKKVNTTTSSDSYIGLWRNYLILCCSAATSSSSTSAGSVRCSPPETLASTPDSGYSIDSKIIGIPSPSSLFKHIVPMMRSESMEITESLVLGLGRTNPGAFRELIEELHPIIKEALERRPENMKRRRRRDILRVQLVRIFELLADAGVISHSASGGLDNETHFLNNTLLEYVDLTRQLLEAENEKDSDTLKDIRCHFSALVANIIQNVPVHQRRSIFPQQSLRHSLFMLFSHWAGPFSIMFTPLDRYSDRNMQINRHQYCALKAMSAVLCCGPVADNVGLSSDGYLYKWLDNILDSLDKKVHQLGCEAVTLLLELNPDQSNLMYWAVDRCYTGSGRVAAGCFKAIANVFQNRDYQCDTVMLLNLILFKAADSSRSIYEVAMQLLQILEPKMFRYAHKLEVQRTDGVLSQLSPLPHLYSVSYYQLSEELARAYPELTLAIFSEISQRIQTAHPAGRQVMLHYLLPWMNNIELVDLKPLPTARRHDEDEDDSLKDRELMVTSRRWLRGEGWGSPQATAMVLNNLMYMTAKYGDELAWSEVENVWTTLADGWPKNLKIILHFLISICGVNSEPSLLPYVKKVIVYLGRDKTMQLLEELVSELQLTDPVSSGVTHMDNPPYYRITSSYKIPSVTSGTTSSSNTMVAPTDGNPDNKPIKENIEESYVHLDIYSGLNSHLNRQHHRLESRYSSSSGGSYEEEKSDSMPLYSNWRLKVMEHNQGEPLPFPPAGGCWSPLVDYVPETSSPGLPLHRCNIAVILLTDLIIDHSVKVEWGSYLHLLLHAIFIGFDHCHPEVYEHCKRLLLHLLIVMGPNSNIRTVASVLLRNKEFNEPRVLTVKQVAHLDYNFTAGINDFIPDYQPSPMTDSGLSSSSTSSSISLGNNSAAISHLHTTILNEVDISVEQDGKVKTLMEFITSRKRGPLWNHEDVSAKNPSIKSAEQLTTFLKHVVSVFKQSSSEGIHLEHHLSEVALQTALSCSSRHYAGRSFQIFRALKQPLTATTLSDVLSRLVETVGDPGEDAQGFVIELLLTLESAIDTLAETMKHYDLLSALSQTSYHDPIMGNKYAANRKSTGQLNLSTSPINSSSYLGYNSNARSNSLRLSLIGDRRGDRRRSNTLDIMDGRINHSSSLARTRSLSSLREKGMYDVQSTTEPTNLMATIFWIAASLLESDYEYEYLLALRLLNKLLIHLPLDKSESREKIENVQSKLKWTNFPGLQQLFLKGFTSASTQEMTVHLLSKLISVSKHTLVDPSQLSGFPLNILCLLPHLIQHFDSPTQFCKETASRIAKVCAEEKCPTLVNLAHMMSLYSTHTYSRDCSNWINVVCRYLHDSFSDTTFNLVTYLAELLEKGLSSMQQSLLQIIYSLLSHIDLSAAPAKQFNLEIIKIIGKYVQSPYWKEALNILKLVVSRSASLVVPSDIPKTYGGDTGSPEISFTKIFNNVSKELPGKTLDFHFDISETPIIGNKYGDQHSAAGRNGKPKVIAVTRSTSSTSSGSNSNALVPVSWKRPQLSQRRTREKLMNVLSLCGPESGLPKNPSVVFSSNEDLEVGDQQTSLISTTEDINQEEEVAVEDNSSEQQFGVFKDFDFLDVELEDAEGESMDNFNWGVRRRSLDSIDKGDTPSLQEYQCSSSTPSLNLTNQEDTDESSEEEAALTASQILSRTQMLNSDSATDETIPDHPDLLLQSEDSTGSITTEEVLQIRDETPTLEASLDNANSRLPEDTTSVLKEEHVTTFEDEGSYIIQEQQESLVCQGILDLEETEMPEPLAPESYPESVCEEDVTLALKELDERCEEEEADFSGLSSQDEEEQDGFPEVQTSPLPSPFLSAIIAAFQPVAYDDEEEAWRCHVNQMLSDTDGSSAVFTFHVFSRLFQTIQRKFGEITNEAVSFLGDSLQRIGTKFKSSLEVMMLCSECPTVFVDAETLMSCGLLETLKFGVLELQEHLDTYNVKREAAEQWLDDCKRTFGAKEDMYRINTDAQQMEILAELELCRRLYKLHFQLLLLFQAYCKLINQVNTIKNEAEVINMSEELAQLESILKEAESASENEEIDISKAAQTTIETAIHSLIETLKNKEFISAVAQVKAFRSLWPSDIFGSCEDDPVQTLLHIYFHHQTLGQTGSFAVIGSNLDMSEANYKLMELNLEIRESLRMVQSYQLLAQAKPMGNMVSTGF
| null | null |
cell morphogenesis [GO:0000902]; neuron projection development [GO:0031175]
|
cell cortex [GO:0005938]; site of polarized growth [GO:0030427]
| null |
PF19421;PF14225;PF14228;PF14222;
| null |
Furry protein family
| null | null | null | null | null | null | null |
FUNCTION: Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). May function as a transcriptional activator. {ECO:0000250, ECO:0000269|PubMed:16061630}.
|
Homo sapiens (Human)
|
O94916
|
NFAT5_HUMAN
|
MPSDFISLLSADLDLESPKSLYSRESVYDLLPKELQLPPSRETSVASMSQTSGGEAGSPPPAVVAADASSAPSSSSMGGACSSFTTSSSPTIYSTSVTDSKAMQVESCSSAVGVSNRGVSEKQLTSNTVQQHPSTPKRHTVLYISPPPEDLLDNSRMSCQDEGCGLESEQSCSMWMEDSPSNFSNMSTSSYNDNTEVPRKSRKRNPKQRPGVKRRDCEESNMDIFDADSAKAPHYVLSQLTTDNKGNSKAGNGTLENQKGTGVKKSPMLCGQYPVKSEGKELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKEVDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNIMRKDGSTLTLQTPSSPILCTQPAGVPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSDENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSVGIYVVTNAGRSHDVQPFTYTPDPAAAGALNVNVKKEISSPARPCSFEEAMKAMKTTGCNLDKVNIIPNALMTPLIPSSMIKSEDVTPMEVTAEKRSSTIFKTTKSVGSTQQTLENISNIAGNGSFSSPSSSHLPSENEKQQQIQPKAYNPETLTTIQTQDISQPGTFPAVSASSQLPNSDALLQQATQFQTRETQSREILQSDGTVVNLSQLTEASQQQQQSPLQEQAQTLQQQISSNIFPSPNSVSQLQNTIQQLQAGSFTGSTASGSSGSVDLVQQVLEAQQQLSSVLFSAPDGNENVQEQLSADIFQQVSQIQSGVSPGMFSSTEPTVHTRPDNLLPGRAESVHPQSENTLSNQQQQQQQQQQVMESSAAMVMEMQQSICQAAAQIQSELFPSTASANGNLQQSPVYQQTSHMMSALSTNEDMQMQCELFSSPPAVSGNETSTTTTQQVATPGTTMFQTSSSGDGEETGTQAKQIQNSVFQTMVQMQHSGDNQPQVNLFSSTKSMMSVQNSGTQQQGNGLFQQGNEMMSLQSGNFLQQSSHSQAQLFHPQNPIADAQNLSQETQGSLFHSPNPIVHSQTSTTSSEQMQPPMFHSQSTIAVLQGSSVPQDQQSTNIFLSQSPMNNLQTNTVAQEAFFAAPNSISPLQSTSNSEQQAAFQQQAPISHIQTPMLSQEQAQPPQQGLFQPQVALGSLPPNPMPQSQQGTMFQSQHSIVAMQSNSPSQEQQQQQQQQQQQQQQQQQSILFSNQNTMATMASPKQPPPNMIFNPNQNPMANQEQQNQSIFHQQSNMAPMNQEQQPMQFQSQSTVSSLQNPGPTQSESSQTPLFHSSPQIQLVQGSPSSQEQQVTLFLSPASMSALQTSINQQDMQQSPLYSPQNNMPGIQGATSSPQPQATLFHNTAGGTMNQLQNSPGSSQQTSGMFLFGIQNNCSQLLTSGPATLPDQLMAISQPGQPQNEGQPPVTTLLSQQMPENSPLASSINTNQNIEKIDLLVSLQNQGNNLTGSF
| null | null |
calcineurin-NFAT signaling cascade [GO:0033173]; cellular hyperosmotic response [GO:0071474]; cellular response to cytokine stimulus [GO:0071345]; DNA damage response [GO:0006974]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of gene expression [GO:0010628]; positive regulation of leukocyte adhesion to vascular endothelial cell [GO:1904996]; positive regulation of transcription by RNA polymerase II [GO:0045944]; R-loop processing [GO:0062176]; regulation of calcineurin-NFAT signaling cascade [GO:0070884]; regulation of transcription by RNA polymerase II [GO:0006357]; signal transduction [GO:0007165]; transcription by RNA polymerase II [GO:0006366]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF16179;PF00554;
|
2.60.40.10;2.60.40.340;
| null |
PTM: Phosphorylated (PubMed:10377394). Phosphorylated at Thr-135 by CDK5 in response to osmotic stress; this phosphorylation mediates its rapid nuclear localization (PubMed:21209322). {ECO:0000269|PubMed:10377394, ECO:0000269|PubMed:21209322}.; PTM: Poly-ADP-ribosylated by PARP1 in response to DNA damage, promoting recruitment to sites of R-loop-associated DNA damage. {ECO:0000269|PubMed:34049076}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10377394}. Cytoplasm {ECO:0000250|UniProtKB:Q9WV30}. Chromosome {ECO:0000269|PubMed:34049076}. Note=Nuclear distribution increases under hypertonic conditions (By similarity). Recruited to sites of R-loop-associated DNA damage following poly-ADP-ribosylation by PARP1 (PubMed:34049076). {ECO:0000250|UniProtKB:Q9WV30, ECO:0000269|PubMed:34049076}.
| null | null | null | null | null |
FUNCTION: Transcription factor involved, among others, in the transcriptional regulation of osmoprotective and inflammatory genes. Binds the DNA consensus sequence 5'-[ACT][AG]TGGAAA[CAT]A[TA][ATC][CA][ATG][GT][GAC][CG][CT]-3' (PubMed:10377394). Mediates the transcriptional response to hypertonicity (PubMed:10051678). Positively regulates the transcription of LCN2 and S100A4 genes; optimal transactivation of these genes requires the presence of DDX5/DDX17 (PubMed:22266867). Also involved in the DNA damage response by preventing formation of R-loops; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (PubMed:34049076). {ECO:0000269|PubMed:10051678, ECO:0000269|PubMed:10377394, ECO:0000269|PubMed:22266867, ECO:0000269|PubMed:34049076}.
|
Homo sapiens (Human)
|
O94919
|
ENDD1_HUMAN
|
MGTARWLALGSLFALAGLLEGRLVGEEEAGFGECDKFFYAGTPPAGLAADSHVKICQRAEGAERFATLYSTRDRIPVYSAFRAPRPAPGGAEQRWLVEPQIDDPNSNLEEAINEAEAITSVNSLGSKQALNTDYLDSDYQRGQLYPFSLSSDVQVATFTLTNSAPMTQSFQERWYVNLHSLMDRALTPQCGSGEDLYILTGTVPSDYRVKDKVAVPEFVWLAACCAVPGGGWAMGFVKHTRDSDIIEDVMVKDLQKLLPFNPQLFQNNCGETEQDTEKMKKILEVVNQIQDEERMVQSQKSSSPLSSTRSKRSTLLPPEASEGSSSFLGKLMGFIATPFIKLFQLIYYLVVAILKNIVYFLWCVTKQVINGIESCLYRLGSATISYFMAIGEELVSIPWKVLKVVAKVIRALLRILCCLLKAICRVLSIPVRVLVDVATFPVYTMGAIPIVCKDIALGLGGTVSLLFDTAFGTLGGLFQVVFSVCKRIGYKVTFDNSGEL
|
3.1.30.-
| null |
innate immune response [GO:0045087]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane [GO:0016020]
|
endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]
|
PF01223;
|
3.40.570.10;
|
DNA/RNA non-specific endonuclease family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May act as a DNase and a RNase. Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26. {ECO:0000269|PubMed:32614325}.
|
Homo sapiens (Human)
|
O94921
|
CDK14_HUMAN
|
MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKDDTTFDEICVTKMSTRNCQGMDSVIKPLDTIPEDKKVRVQRTQSTFDPFEKPANQVKRVHSENNACINFKTSSTGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPDNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLGTPNEDTWPGVHSLPHFKPERFTLYSSKNLRQAWNKLSYVNHAEDLASKLLQCSPKNRLSAQAALSHEYFSDLPPRLWELTDMSSIFTVPNVRLQPEAGESMRAFGKNNSYGKSLSNSKH
|
2.7.11.22
| null |
cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; phosphorylation [GO:0016310]; regulation of canonical Wnt signaling pathway [GO:0060828]; Wnt signaling pathway [GO:0016055]
|
cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytoplasmic cyclin-dependent protein kinase holoenzyme complex [GO:0000308]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cytoplasm. Nucleus. Note=Recruited to the cell membrane by CCNY.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport. {ECO:0000269|PubMed:16461467, ECO:0000269|PubMed:17517622, ECO:0000269|PubMed:19524571, ECO:0000269|PubMed:20059949}.
|
Homo sapiens (Human)
|
O94923
|
GLCE_HUMAN
|
MRCLAARVNYKTLIIICALFTLVTVLLWNKCSSDKAIQFPRRSSSGFRVDGFEKRAAASESNNYMNHVAKQQSEEAFPQEQQKAPPVVGGFNSNVGSKVLGLKYEEIDCLINDEHTIKGRREGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFEFSHSYSKVYAQRAPYHPDGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPHIEVYETAEDRDKNKPNDWTVPKGCFMANVADKSRFTNVKQFIAPETSEGVSLQLGNTKDFIISFDLKFLTNGSVSVVLETTEKNQLFTIHYVSNAQLIAFKERDIYYGIGPRTSWSTVTRDLVTDLRKGVGLSNTKAVKPTKIMPKKVVRLIAKGKGFLDNITISTTAHMAAFFAASDWLVRNQDEKGGWPIMVTRKLGEGFKSLEPGWYSAMAQGQAISTLVRAYLLTKDHIFLNSALRATAPYKFLSEQHGVKAVFMNKHDWYEEYPTTPSSFVLNGFMYSLIGLYDLKETAGEKLGKEARSLYERGMESLKAMLPLYDTGSGTIYDLRHFMLGIAPNLARWDYHTTHINQLQLLSTIDESPVFKEFVKRWKSYLKGSRAKHN
|
5.1.3.17
| null |
heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparin biosynthetic process [GO:0030210]; negative regulation of cell projection organization [GO:0031345]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of SMAD protein signal transduction [GO:0060391]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
calcium ion binding [GO:0005509]; heparosan-N-sulfate-glucuronate 5-epimerase activity [GO:0047464]; protein homodimerization activity [GO:0042803]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857]
|
PF06662;PF21174;
| null |
D-glucuronyl C5-epimerase family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9EPS3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9EPS3}.
|
CATALYTIC ACTIVITY: Reaction=[heparosan-N-sulfate](n) = [heparan-N-sulfate](n); Xref=Rhea:RHEA:20197, Rhea:RHEA-COMP:9556, Rhea:RHEA-COMP:9557, ChEBI:CHEBI:58041, ChEBI:CHEBI:58287; EC=5.1.3.17; Evidence={ECO:0000269|PubMed:20118238, ECO:0000269|PubMed:22528493, ECO:0000269|PubMed:30872481};
| null |
PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. {ECO:0000305|PubMed:22528493, ECO:0000305|PubMed:30872481}.; PATHWAY: Glycan metabolism; heparin biosynthesis. {ECO:0000305}.
| null | null |
FUNCTION: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins. {ECO:0000269|PubMed:20118238, ECO:0000269|PubMed:22528493, ECO:0000269|PubMed:30872481}.
|
Homo sapiens (Human)
|
O94925
|
GLSK_HUMAN
|
MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGGGGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEGKELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTVHKNLDGLL
|
3.5.1.2
| null |
chemical synaptic transmission [GO:0007268]; glutamate biosynthetic process [GO:0006537]; glutamine catabolic process [GO:0006543]; intracellular glutamate homeostasis [GO:0090461]; protein homotetramerization [GO:0051289]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; suckling behavior [GO:0001967]
|
cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; synapse [GO:0045202]
|
glutaminase activity [GO:0004359]
|
PF12796;PF17959;PF04960;
|
1.10.238.210;1.25.40.20;3.40.710.10;
|
Glutaminase family
|
PTM: Synthesized as a 74-kDa cytosolic precursor which is proteolytically processed by the mitochondrial-processing peptidase (MPP) via a 72-kDa intermediate to yield the mature mitochondrial 68- and 65-kDa subunits. {ECO:0000250|UniProtKB:P13264}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000250|UniProtKB:P13264}. Cytoplasm, cytosol {ECO:0000269|PubMed:22228304}. Note=The 74-kDa cytosolic precursor is translocated into the mitochondria and processed via a 72-kDa intermediate to yield the mature 68- and 65-kDa subunits. {ECO:0000250|UniProtKB:P13264}.; SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion {ECO:0000269|PubMed:22228304}.; SUBCELLULAR LOCATION: [Glutaminase kidney isoform, mitochondrial 68 kDa chain]: Mitochondrion matrix {ECO:0000250|UniProtKB:P13264}. Note=Produced by the proteolytic processing of the 74-kDa cytosolic precursor. {ECO:0000250|UniProtKB:P13264}.; SUBCELLULAR LOCATION: [Glutaminase kidney isoform, mitochondrial 65 kDa chain]: Mitochondrion matrix {ECO:0000250|UniProtKB:P13264}. Note=Produced by the proteolytic processing of the 74-kDa cytosolic precursor. {ECO:0000250|UniProtKB:P13264}.
|
CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000269|PubMed:24451979, ECO:0000269|PubMed:26988803, ECO:0000269|PubMed:28526749, ECO:0000269|PubMed:29317493};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for glutamine (isoform 1) {ECO:0000269|PubMed:22049910}; KM=1.4 mM for glutamine (isoform 3) {ECO:0000269|PubMed:22049910};
| null | null | null |
FUNCTION: Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain (PubMed:30239721, PubMed:30575854, PubMed:30970188). {ECO:0000269|PubMed:30239721, ECO:0000269|PubMed:30575854, ECO:0000269|PubMed:30970188}.; FUNCTION: [Isoform 2]: Lacks catalytic activity. {ECO:0000269|PubMed:11015561}.
|
Homo sapiens (Human)
|
O94927
|
HAUS5_HUMAN
|
MELAQEARELGCWAVEEMGVPVAARAPESTLRRLCLGQGADIWAYILQHVHSQRTVKKIRGNLLWYGHQDSPQVRRKLELEAAVTRLRAEIQELDQSLELMERDTEAQDTAMEQARQHTQDTQRRALLLRAQAGAMRRQQHTLRDPMQRLQNQLRRLQDMERKAKVDVTFGSLTSAALGLEPVVLRDVRTACTLRAQFLQNLLLPQAKRGSLPTPHDDHFGTSYQQWLSSVETLLTNHPPGHVLAALEHLAAEREAEIRSLCSGDGLGDTEISRPQAPDQSDSSQTLPSMVHLIQEGWRTVGVLVSQRSTLLKERQVLTQRLQGLVEEVERRVLGSSERQVLILGLRRCCLWTELKALHDQSQELQDAAGHRQLLLRELQAKQQRILHWRQLVEETQEQVRLLIKGNSASKTRLCRSPGEVLALVQRKVVPTFEAVAPQSRELLRCLEEEVRHLPHILLGTLLRHRPGELKPLPTVLPSIHQLHPASPRGSSFIALSHKLGLPPGKASELLLPAAASLRQDLLLLQDQRSLWCWDLLHMKTSLPPGLPTQELLQIQASQEKQQKENLGQALKRLEKLLKQALERIPELQGIVGDWWEQPGQAALSEELCQGLSLPQWRLRWVQAQGALQKLCS
| null | null |
cell division [GO:0051301]; centrosome cycle [GO:0007098]; regulation of microtubule nucleation [GO:0010968]; spindle assembly [GO:0051225]
|
centrosome [GO:0005813]; cytosol [GO:0005829]; HAUS complex [GO:0070652]; mitotic spindle microtubule [GO:1990498]
| null |
PF14817;
| null |
HAUS5 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
| null | null | null | null | null |
FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.
|
Homo sapiens (Human)
|
O94929
|
ABLM3_HUMAN
|
MNTSIPYQQNPYNPRGSSNVIQCYRCGDTCKGEVVRVHNNHFHIRCFTCQVCGCGLAQSGFFFKNQEYICTQDYQQLYGTRCDSCRDFITGEVISALGRTYHPKCFVCSLCRKPFPIGDKVTFSGKECVCQTCSQSMASSKPIKIRGPSHCAGCKEEIKHGQSLLALDKQWHVSCFKCQTCSVILTGEYISKDGVPYCESDYHAQFGIKCETCDRYISGRVLEAGGKHYHPTCARCVRCHQMFTEGEEMYLTGSEVWHPICKQAARAEKKLKHRRTSETSISPPGSSIGSPNRVICAKVDNEILNYKDLAALPKVKSIYEVQRPDLISYEPHSRYMSDEMLERCGYGESLGTLSPYSQDIYENLDLRQRRASSPGYIDSPTYSRQGMSPTFSRSPHHYYRSGPESGRSSPYHSQLDVRSSTPTSYQAPKHFHIPAGDSNIYRKPPIYKRHGDLSTATKSKTSEDISQTSKYSPIYSPDPYYASESEYWTYHGSPKVPRARRFSSGGEEDDFDRSMHKLQSGIGRLILKEEMKARSSSYADPWTPPRSSTSSREALHTAGYEMSLNGSPRSHYLADSDPLISKSASLPAYRRNGLHRTPSADLFHYDSMNAVNWGMREYKIYPYELLLVTTRGRNRLPKDVDRTRLERHLSQEEFYQVFGMTISEFDRLALWKRNELKKQARLF
| null | null |
cilium assembly [GO:0060271]; cytoskeleton organization [GO:0007010]; lamellipodium assembly [GO:0030032]; positive regulation of protein targeting to mitochondrion [GO:1903955]; positive regulation of transcription by RNA polymerase II [GO:0045944]; transcription by RNA polymerase II [GO:0006366]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; stress fiber [GO:0001725]
|
actin filament binding [GO:0051015]; metal ion binding [GO:0046872]
|
PF16182;PF00412;PF02209;
|
2.10.110.10;1.10.950.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. {ECO:0000269|PubMed:17194709}.
|
Homo sapiens (Human)
|
O94933
|
SLIK3_HUMAN
|
MKPSIAEMLHRGRMLWIILLSTIALGWTTPIPLIEDSEEIDEPCFDPCYCEVKESLFHIHCDSKGFTNISQITEFWSRPFKLYLQRNSMRKLYTNSFLHLNNAVSINLGNNALQDIQTGAFNGLKILKRLYLHENKLDVFRNDTFLGLESLEYLQADYNVIKRIESGAFRNLSKLRVLILNDNLIPMLPTNLFKAVSLTHLDLRGNRLKVLFYRGMLDHIGRSLMELQLEENPWNCTCEIVQLKSWLERIPYTALVGDITCETPFHFHGKDLREIRKTELCPLLSDSEVEASLGIPHSSSSKENAWPTKPSSMLSSVHFTASSVEYKSSNKQPKPTKQPRTPRPPSTSQALYPGPNQPPIAPYQTRPPIPIICPTGCTCNLHINDLGLTVNCKERGFNNISELLPRPLNAKKLYLSSNLIQKIYRSDFWNFSSLDLLHLGNNRISYVQDGAFINLPNLKSLFLNGNDIEKLTPGMFRGLQSLHYLYFEFNVIREIQPAAFSLMPNLKLLFLNNNLLRTLPTDAFAGTSLARLNLRKNYFLYLPVAGVLEHLNAIVQIDLNENPWDCTCDLVPFKQWIETISSVSVVGDVLCRSPENLTHRDVRTIELEVLCPEMLHVAPAGESPAQPGDSHLIGAPTSASPYEFSPPGGPVPLSVLILSLLVLFFSAVFVAAGLFAYVLRRRRKKLPFRSKRQEGVDLTGIQMQCHRLFEDGGGGGGGSGGGGRPTLSSPEKAPPVGHVYEYIPHPVTQMCNNPIYKPREEEEVAVSSAQEAGSAERGGPGTQPPGMGEALLGSEQFAETPKENHSNYRTLLEKEKEWALAVSSSQLNTIVTVNHHHPHHPAVGGVSGVVGGTGGDLAGFRHHEKNGGVVLFPPGGGCGSGSMLLDRERPQPAPCTVGFVDCLYGTVPKLKELHVHPPGMQYPDLQQDARLKETLLFSAGKGFTDHQTQKSDYLELRAKLQTKPDYLEVLEKTTYRF
| null | null |
axonogenesis [GO:0007409]; gephyrin clustering involved in postsynaptic density assembly [GO:0097116]; neurotransmitter-gated ion channel clustering [GO:0072578]; positive regulation of synapse assembly [GO:0051965]; regulation of presynapse assembly [GO:1905606]; synaptic membrane adhesion [GO:0099560]; synaptic transmission, GABAergic [GO:0051932]; terminal button organization [GO:0072553]
|
cell surface [GO:0009986]; GABA-ergic synapse [GO:0098982]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; postsynaptic specialization membrane [GO:0099634]
| null |
PF13855;
|
3.80.10.10;
|
SLITRK family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Suppresses neurite outgrowth. {ECO:0000250}.
|
Homo sapiens (Human)
|
O94941
|
RNF37_HUMAN
|
MVINLCLPQFRPRIHCNKISADGYEVENLISEDLTKRSHGFRTEYFIKPPVYVTVSFPFNVEICRINIDLTAGGGQNVTGLEMYTSASSSRVSWNTPQCRTLGPAEPSVPDKEAFTLVGKVLLKNQSQVVFSHRGFKARPPFGAMEATLPSPAVVAQELWNKGALSLSHVAHLRICITHVTGGGIPCIKRLEVWGQPAKTCSQEVIDSILLVTSENLPQDVALQAPALPMESDCDPGDQPESQQAPSSLQKLAEIIQDVPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWGRVPSDPFTGVAFTPHSQPLPHPSLKARIDHFLLQHSIPGCHLLGRAQTALAVIPSSIVLPSQKRKIEQAEHVPDSNFGVNASCFSATSPLVLPTTSEHTAKKMKATNEPSLTHMDCSTGPLSHEQKLSQSLEIALASTLGSMPSFTARLTRGQLQHLGTRGSNTSWRPGTGSEQPGSILGPECASCKRVFSPYFKKEPVYQLPCGHLLCRPCLGEKQRSLPMTCTACQRPVASQDVLRVHF
|
2.3.2.27
| null |
protein polyubiquitination [GO:0000209]
|
focal adhesion [GO:0005925]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-ubiquitin ligase activity [GO:0034450]
|
PF19318;PF04564;PF14634;
|
3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11274149, ECO:0000269|PubMed:11435423}. Note=Enriched in nuclear bodies. {ECO:0000269|PubMed:11274149}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q925F4};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q925F4}.
| null | null |
FUNCTION: May have a ubiquitin-protein ligase activity acting as an E3 ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. {ECO:0000250|UniProtKB:Q925F4}.
|
Homo sapiens (Human)
|
O94953
|
KDM4B_HUMAN
|
MGSEDHGAQNPSCKIMTFRPTMEEFKDFNKYVAYIESQGAHRAGLAKIIPPKEWKPRQTYDDIDDVVIPAPIQQVVTGQSGLFTQYNIQKKAMTVGEYRRLANSEKYCTPRHQDFDDLERKYWKNLTFVSPIYGADISGSLYDDDVAQWNIGSLRTILDMVERECGTIIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAIGFFPGSSQGCDAFLRHKMTLISPIILKKYGIPFSRITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATLRWIDYGKVATQCTCRKDMVKISMDVFVRILQPERYELWKQGKDLTVLDHTRPTALTSPELSSWSASRASLKAKLLRRSHRKRSQPKKPKPEDPKFPGEGTAGAALLEEAGGSVKEEAGPEVDPEEEEEEPQPLPHGREAEGAEEDGRGKLRPTKAKSERKKKSFGLLPPQLPPPPAHFPSEEALWLPSPLEPPVLGPGPAAMEESPLPAPLNVVPPEVPSEELEAKPRPIIPMLYVVPRPGKAAFNQEHVSCQQAFEHFAQKGPTWKEPVSPMELTGPEDGAASSGAGRMETKARAGEGQAPSTFSKLKMEIKKSRRHPLGRPPTRSPLSVVKQEASSDEEASPFSGEEDVSDPDALRPLLSLQWKNRAASFQAERKFNAAAARTEPYCAICTLFYPYCQALQTEKEAPIASLGKGCPATLPSKSRQKTRPLIPEMCFTSGGENTEPLPANSYIGDDGTSPLIACGKCCLQVHASCYGIRPELVNEGWTCSRCAAHAWTAECCLCNLRGGALQMTTDRRWIHVICAIAVPEARFLNVIERHPVDISAIPEQRWKLKCVYCRKRMKKVSGACIQCSYEHCSTSFHVTCAHAAGVLMEPDDWPYVVSITCLKHKSGGHAVQLLRAVSLGQVVITKNRNGLYYRCRVIGAASQTCYEVNFDDGSYSDNLYPESITSRDCVQLGPPSEGELVELRWTDGNLYKAKFISSVTSHIYQVEFEDGSQLTVKRGDIFTLEEELPKRVRSRLSLSTGAPQEPAFSGEEAKAAKRPRVGTPLATEDSGRSQDYVAFVESLLQVQGRPGAPF
|
1.14.11.66
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
|
brain development [GO:0007420]; chromatin remodeling [GO:0006338]; regulation of gene expression [GO:0010468]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
histone demethylase activity [GO:0032452]; histone H3K36 demethylase activity [GO:0051864]; histone H3K9 demethylase activity [GO:0032454]; histone H3K9me2/H3K9me3 demethylase activity [GO:0140684]; metal ion binding [GO:0046872]
|
PF02373;PF02375;PF13831;PF18104;PF13832;
|
2.30.30.140;3.10.330.70;2.60.120.650;3.30.40.10;
|
JHDM3 histone demethylase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:15927959}.
|
CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.66; Evidence={ECO:0000269|PubMed:16603238};
| null | null | null | null |
FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate (PubMed:16603238, PubMed:28262558). Plays a critical role in the development of the central nervous system (CNS). {ECO:0000250|UniProtKB:Q91VY5, ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:28262558}.
|
Homo sapiens (Human)
|
O94955
|
RHBT3_HUMAN
|
MSIHIVALGNEGDTFHQDNRPSGLIRTYLGRSPLVSGDESSLLLNAASTVARPVFTEYQASAFGNVKLVVHDCPVWDIFDSDWYTSRNLIGGADIIVIKYNVNDKFSFHEVKDNYIPVIKRALNSVPVIIAAVGTRQNEELPCTCPLCTSDRGSCVSTTEGIQLAKELGATYLELHSLDDFYIGKYFGGVLEYFMIQALNQKTSEKMKKRKMSNSFHGIRPPQLEQPEKMPVLKAEASHYNSDLNNLLFCCQCVDVVFYNPNLKKVVEAHKIVLCAVSHVFMLLFNVKSPTDIQDSSIIRTTQDLFAINRDTAFPGASHESSGNPPLRVIVKDALFCSCLSDILRFIYSGAFQWEELEEDIRKKLKDSGDVSNVIEKVKCILKTPGKINCLRNCKTYQARKPLWFYNTSLKFFLNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGIFQAMCLLICAEMYQVSRLQHICELFIITQLQSMPSRELASMNLDIVDLLKKAKFHHSDCLSTWLLHFIATNYLIFSQKPEFQDLSVEERSFVEKHRWPSNMYLKQLAEYRKYIHSRKCRCLVM
|
3.6.1.-
| null |
male gonad development [GO:0008584]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of proteolysis [GO:0030162]; retrograde transport, endosome to Golgi [GO:0042147]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; trans-Golgi network membrane [GO:0032588]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; GTPase activity [GO:0003924]; small GTPase binding [GO:0031267]; ubiquitin protein ligase binding [GO:0031625]
|
PF00651;PF00071;
|
3.40.50.300;
| null | null |
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:19490898}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48 uM for ATP {ECO:0000269|PubMed:19490898};
| null | null | null |
FUNCTION: Rab9-regulated ATPase required for endosome to Golgi transport. Involved in transport vesicle docking at the Golgi complex, possibly by participating in release M6PRBP1/TIP47 from vesicles to permit their efficient docking and fusion at the Golgi. Specifically binds Rab9, but not other Rab proteins. Has low intrinsic ATPase activity due to autoinhibition, which is relieved by Rab9. {ECO:0000269|PubMed:19490898}.
|
Homo sapiens (Human)
|
O94956
|
SO2B1_HUMAN
|
MGPRIGPAGEVPQVPDKETKATMGTENTPGGKASPDPQDVRPSVFHNIKLFVLCHSLLQLAQLMISGYLKSSISTVEKRFGLSSQTSGLLASFNEVGNTALIVFVSYFGSRVHRPRMIGYGAILVALAGLLMTLPHFISEPYRYDNTSPEDMPQDFKASLCLPTTSAPASAPSNGNCSSYTETQHLSVVGIMFVAQTLLGVGGVPIQPFGISYIDDFAHNSNSPLYLGILFAVTMMGPGLAFGLGSLMLRLYVDINQMPEGGISLTIKDPRWVGAWWLGFLIAAGAVALAAIPYFFFPKEMPKEKRELQFRRKVLAVTDSPARKGKDSPSKQSPGESTKKQDGLVQIAPNLTVIQFIKVFPRVLLQTLRHPIFLLVVLSQVCLSSMAAGMATFLPKFLERQFSITASYANLLIGCLSFPSVIVGIVVGGVLVKRLHLGPVGCGALCLLGMLLCLFFSLPLFFIGCSSHQIAGITHQTSAHPGLELSPSCMEACSCPLDGFNPVCDPSTRVEYITPCHAGCSSWVVQDALDNSQVFYTNCSCVVEGNPVLAGSCDSTCSHLVVPFLLLVSLGSALACLTHTPSFMLILRGVKKEDKTLAVGIQFMFLRILAWMPSPVIHGSAIDTTCVHWALSCGRRAVCRYYNNDLLRNRFIGLQFFFKTGSVICFALVLAVLRQQDKEARTKESRSSPAVEQQLLVSGPGKKPEDSRV
| null | null |
bile acid and bile salt transport [GO:0015721]; heme catabolic process [GO:0042167]; monoatomic ion transport [GO:0006811]; organic anion transport [GO:0015711]; sodium-independent organic anion transport [GO:0043252]; transmembrane transport [GO:0055085]; transport across blood-brain barrier [GO:0150104]; xenobiotic metabolic process [GO:0006805]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886]
|
bile acid transmembrane transporter activity [GO:0015125]; organic anion transmembrane transporter activity [GO:0008514]; prostaglandin transmembrane transporter activity [GO:0015132]; sodium-independent organic anion transmembrane transporter activity [GO:0015347]; transmembrane transporter activity [GO:0022857]
|
PF03137;
|
1.20.1250.20;
|
Organo anion transporter (TC 2.A.60) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25132355}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000269|PubMed:11159893, ECO:0000269|PubMed:11932330, ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:28408210}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:12724351, ECO:0000269|PubMed:28408210}; Multi-pass membrane protein {ECO:0000305}. Note=Expressed at the basal membrane of hepatocytes, syncytiotrophoblast and Sertoli cells (PubMed:11159893, PubMed:11932330, PubMed:12409283, PubMed:35307651). Localized to the basolateral membrane of enterocytes (PubMed:28408210). Also found at the apical membrane of enterocytes (PubMed:12724351, PubMed:28408210). {ECO:0000269|PubMed:11159893, ECO:0000269|PubMed:11932330, ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:12724351, ECO:0000269|PubMed:28408210, ECO:0000269|PubMed:35307651}.
|
CATALYTIC ACTIVITY: Reaction=dehydroepiandrosterone 3-sulfate(out) = dehydroepiandrosterone 3-sulfate(in); Xref=Rhea:RHEA:71839, ChEBI:CHEBI:57905; Evidence={ECO:0000305|PubMed:11159893, ECO:0000305|PubMed:14610227, ECO:0000305|PubMed:16908597, ECO:0000305|PubMed:18501590, ECO:0000305|PubMed:23531488, ECO:0000305|PubMed:26277985, ECO:0000305|PubMed:34628357}; CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in); Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050; Evidence={ECO:0000269|PubMed:28408210, ECO:0000305|PubMed:10873595, ECO:0000305|PubMed:11159893, ECO:0000305|PubMed:11932330, ECO:0000305|PubMed:12724351, ECO:0000305|PubMed:14610227, ECO:0000305|PubMed:16908597, ECO:0000305|PubMed:18501590, ECO:0000305|PubMed:19129463, ECO:0000305|PubMed:20507927, ECO:0000305|PubMed:22201122, ECO:0000305|PubMed:23531488, ECO:0000305|PubMed:26277985, ECO:0000305|PubMed:26383540, ECO:0000305|PubMed:27576593, ECO:0000305|PubMed:29871943, ECO:0000305|PubMed:34628357, ECO:0000305|Ref.25}; CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) + hydrogencarbonate(in) = estrone 3-sulfate(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:73055, ChEBI:CHEBI:17544, ChEBI:CHEBI:60050; Evidence={ECO:0000269|PubMed:19129463}; CATALYTIC ACTIVITY: Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703, ChEBI:CHEBI:36257; Evidence={ECO:0000305|PubMed:14610227, ECO:0000305|PubMed:29871943}; CATALYTIC ACTIVITY: Reaction=coproporphyrin III(out) = coproporphyrin III(in); Xref=Rhea:RHEA:74363, ChEBI:CHEBI:131725; Evidence={ECO:0000305|PubMed:26383540}; CATALYTIC ACTIVITY: Reaction=substance P(out) = substance P(in); Xref=Rhea:RHEA:74367, ChEBI:CHEBI:190692; Evidence={ECO:0000305|PubMed:25132355}; CATALYTIC ACTIVITY: Reaction=pregnenolone sulfate(out) = pregnenolone sulfate(in); Xref=Rhea:RHEA:73023, ChEBI:CHEBI:133000; Evidence={ECO:0000305|PubMed:16908597, ECO:0000305|PubMed:34628357}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000305|PubMed:10873595, ECO:0000305|Ref.25}; CATALYTIC ACTIVITY: Reaction=prostaglandin D2(out) = prostaglandin D2(in); Xref=Rhea:RHEA:50976, ChEBI:CHEBI:57406; Evidence={ECO:0000250|UniProtKB:Q9JHI3}; CATALYTIC ACTIVITY: Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819, ChEBI:CHEBI:58448; Evidence={ECO:0000305|PubMed:19129463};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.1 uM for estrone 3-sulfate (at pH 5.0) {ECO:0000269|PubMed:14610227}; KM=9.36 uM for estrone-3-sulfate (at pH 6.5) {ECO:0000269|PubMed:19129463}; KM=35 uM for estrone 3-sulfate (at pH 7.2) {ECO:0000269|PubMed:11932330}; KM=14 uM for estrone 3-sulfate (at pH 7.3) {ECO:0000269|PubMed:16908597}; KM=6.4 uM for estrone 3-sulfate (at pH 7.4) {ECO:0000269|PubMed:29871943}; KM=19.1 uM for estrone 3-sulfate (at pH 7.4) {ECO:0000269|PubMed:18501590}; KM=8.09 uM for estrone 3-sulfate (at pH 7.4) {ECO:0000269|PubMed:14610227}; KM=7.1 uM for estrone 3-sulfate (at pH 7.4) {ECO:0000269|PubMed:27576593}; KM=6.76 uM for estrone 3-sulfate (at pH 7.4) {ECO:0000269|PubMed:27576593}; KM=16 uM for estrone 3-sulfate (at pH 7.4) {ECO:0000269|PubMed:20507927}; KM=6.3 uM for estrone 3-sulfate (at pH 7.5) {ECO:0000269|PubMed:11159893}; KM=17.7 uM for estrone-3-sulfate (at pH 8.0) {ECO:0000269|PubMed:19129463}; KM=29.9 uM for estrone 3-sulfate for the low-affinity site (at pH 6.5) {ECO:0000269|PubMed:22201122}; KM=51.4 uM for estrone 3-sulfate for the low-affinity site (at pH 6.5) {ECO:0000269|Ref.25}; KM=0.1 uM for estrone 3-sulfate for the high-affinity site (at pH 6.5) {ECO:0000269|PubMed:22201122}; KM=0.463 uM for estrone 3-sulfate for the high-affinity site (at pH 6.5) {ECO:0000269|Ref.25}; KM=201.8 uM for dehydroepiandrosterone sulfate (at pH 7.4) {ECO:0000269|PubMed:18501590}; KM=0.31 uM for L-thyroxine (at pH 6.5) {ECO:0000269|PubMed:19129463}; KM=0.77 uM for L-thyroxine (at pH 8.0) {ECO:0000269|PubMed:19129463}; KM=71.8 uM for taurocholate (at pH 5.0) {ECO:0000269|PubMed:14610227}; KM=84 uM for substance P/TAC1 (at pH 7.5) {ECO:0000269|PubMed:25132355}; KM=94 uM for vasoactive intestinal peptide/VIP (at pH 7.5) {ECO:0000269|PubMed:25132355}; KM=0.31 uM for coproporphyrin III (at pH 7.4) {ECO:0000269|PubMed:26383540}; Vmax=2135 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at pH 5.0) {ECO:0000269|PubMed:14610227}; Vmax=1293 pmol/min/mg enzyme with estrone-3-sulfate as substrate (at pH 6.5) {ECO:0000269|PubMed:19129463}; Vmax=12300 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at pH 7.2) {ECO:0000269|PubMed:11932330}; Vmax=169 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at pH 7.3) {ECO:0000269|PubMed:16908597}; Vmax=585 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at pH 7.4) {ECO:0000269|PubMed:18501590}; Vmax=351 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at pH 7.4) {ECO:0000269|PubMed:29871943}; Vmax=300 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at pH 7.4) {ECO:0000269|PubMed:14610227}; Vmax=182 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at pH 7.4) {ECO:0000269|PubMed:27576593}; Vmax=209 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at pH 7.4) {ECO:0000269|PubMed:20507927}; Vmax=1400 pmol/min/mg enzyme with estrone-3-sulfate as substrate (at pH 8.0) {ECO:0000269|PubMed:19129463}; Vmax=602 pmol/min/mg enzyme with dehydroepiandrosterone sulfate as substrate (at pH 7.4) {ECO:0000269|PubMed:18501590}; Vmax=5.76 pmol/min/mg enzyme with L-thyroxine as substrate (at pH 6.5) {ECO:0000269|PubMed:19129463}; Vmax=7.28 pmol/min/mg enzyme with L-thyroxine as substrate (at pH 8.0) {ECO:0000269|PubMed:19129463}; Vmax=546 pmol/min/mg enzyme with taurocholate as substrate (at pH 5.0) {ECO:0000269|PubMed:14610227}; Vmax=19 pmol/min/mg enzyme with coproporphyrin III as substrate (at pH 7.4) {ECO:0000269|PubMed:26383540}; Note=Estrone 3-sulfate transport exhibits a biphasic saturation kinetics, with Km and Vmax values of high- and low-affinity sites due to the presence of multiple binding sites. {ECO:0000269|PubMed:22201122, ECO:0000269|Ref.25};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 5.0 with estrone 3-sulfate, dehydroepiandrosterone sulfate and taurocholate as substrates (PubMed:12724351, PubMed:14610227, PubMed:20507927, PubMed:22201122). The high-affinity site for estrone 3-sulfate binding is pH-dependent with increased transport at lower pH, while the low-affinity site is pH-independent (PubMed:22201122). Taurocholate is only transported at acidic pH (PubMed:14610227). {ECO:0000269|PubMed:12724351, ECO:0000269|PubMed:14610227, ECO:0000269|PubMed:20507927, ECO:0000269|PubMed:22201122};
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BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius with estrone 3-sulfate as substrate. {ECO:0000269|PubMed:11932330};
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FUNCTION: Mediates the Na(+)-independent transport of steroid sulfate conjugates and other specific organic anions (PubMed:10873595, PubMed:11159893, PubMed:11932330, PubMed:12724351, PubMed:14610227, PubMed:16908597, PubMed:18501590, PubMed:20507927, PubMed:22201122, PubMed:23531488, PubMed:25132355, PubMed:26383540, PubMed:27576593, PubMed:28408210, PubMed:29871943, PubMed:34628357). Responsible for the transport of estrone 3-sulfate (E1S) through the basal membrane of syncytiotrophoblast, highlighting a potential role in the placental absorption of fetal-derived sulfated steroids including the steroid hormone precursor dehydroepiandrosterone sulfate (DHEA-S) (PubMed:11932330, PubMed:12409283). Also facilitates the uptake of sulfated steroids at the basal/sinusoidal membrane of hepatocytes, therefore accounting for the major part of organic anions clearance of liver (PubMed:11159893). Mediates the intestinal uptake of sulfated steroids (PubMed:12724351, PubMed:28408210). Mediates the uptake of the neurosteroids DHEA-S and pregnenolone sulfate (PregS) into the endothelial cells of the blood-brain barrier as the first step to enter the brain (PubMed:16908597, PubMed:25132355). Also plays a role in the reuptake of neuropeptides such as substance P/TAC1 and vasoactive intestinal peptide/VIP released from retinal neurons (PubMed:25132355). May act as a heme transporter that promotes cellular iron availability via heme oxygenase/HMOX2 and independently of TFRC (PubMed:35714613). Also transports heme by-product coproporphyrin III (CPIII), and may be involved in their hepatic disposition (PubMed:26383540). Mediates the uptake of other substrates such as prostaglandins D2 (PGD2), E1 (PGE1) and E2 (PGE2), taurocholate, L-thyroxine, leukotriene C4 and thromboxane B2 (PubMed:10873595, PubMed:14610227, PubMed:19129463, PubMed:29871943, Ref.25). May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable). Shows a pH-sensitive substrate specificity which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment (PubMed:14610227, PubMed:19129463, PubMed:22201122). The exact transport mechanism has not been yet deciphered but most likely involves an anion exchange, coupling the cellular uptake of organic substrate with the efflux of an anionic compound (PubMed:19129463, PubMed:20507927, PubMed:26277985). Hydrogencarbonate/HCO3(-) acts as a probable counteranion that exchanges for organic anions (PubMed:19129463). Cytoplasmic glutamate may also act as counteranion in the placenta (PubMed:26277985). An inwardly directed proton gradient has also been proposed as the driving force of E1S uptake with a (H(+):E1S) stoichiometry of (1:1) (PubMed:20507927). {ECO:0000269|PubMed:10873595, ECO:0000269|PubMed:11159893, ECO:0000269|PubMed:11932330, ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:12724351, ECO:0000269|PubMed:14610227, ECO:0000269|PubMed:16908597, ECO:0000269|PubMed:18501590, ECO:0000269|PubMed:19129463, ECO:0000269|PubMed:20507927, ECO:0000269|PubMed:22201122, ECO:0000269|PubMed:23531488, ECO:0000269|PubMed:25132355, ECO:0000269|PubMed:26277985, ECO:0000269|PubMed:26383540, ECO:0000269|PubMed:27576593, ECO:0000269|PubMed:29871943, ECO:0000269|PubMed:34628357, ECO:0000269|PubMed:35714613, ECO:0000269|Ref.25, ECO:0000305|PubMed:35307651}.; FUNCTION: [Isoform 3]: Has estrone 3-sulfate (E1S) transport activity comparable with the full-length isoform 1. {ECO:0000269|PubMed:23531488}.
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Homo sapiens (Human)
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O94964
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MTCL2_HUMAN
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MEAPAAEPPVRGCGPQPAPAPAPAPERKKSHRAPSPARPKDVAGWSLAKGRRGPGPGSAVACSAAFSSRPDKKGRAVAPGARGAGVRVAGVRTGVRAKGRPRSGAGPRPPPPPPSLTDSSSEVSDCASEEARLLGLELALSSDAESAAGGPAGVRTGQPAQPAPSAQQPPRPPASPDEPSVAASSVGSSRLPLSASLAFSDLTEEMLDCGPSGLVRELEELRSENDYLKDEIEELRAEMLEMRDVYMEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVDGELIRGLEQDVKVSKDISMRLHKELEVVEKKRARLEEENEELRQRLIETELAKQVLQTELERPREHSLKKRGTRSLGKADKKTLVQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDSALSAEELADAPHSRETELKVHLKLVEEEANLLSRRIVELEVENRGLRAEMDDMKDHGGGCGGPEARLAFSALGGGECGESLAELRRHLQFVEEEAELLRRSSAELEDQNKLLLNELAKFRSEHELDVALSEDSCSVLSEPSQEELAAAKLQIGELSGKVKKLQYENRVLLSNLQRCDLASCQSTRPMLETDAEAGDSAQCVPAPLGETHESHAVRLCRAREAEVLPGLREQAALVSKAIDVLVADANGFTAGLRLCLDNECADFRLHEAPDNSEGPRDTKLIHAILVRLSVLQQELNAFTRKADAVLGCSVKEQQESFSSLPPLGSQGLSKEILLAKDLGSDFQPPDFRDLPEWEPRIREAFRTGDLDSKPDPSRSFRPYRAEDNDSYASEIKELQLVLAEAHDSLRGLQEQLSQERQLRKEEADNFNQKMVQLKEDQQRALLRREFELQSLSLQRRLEQKFWSQEKNMLVQESQQFKHNFLLLFMKLRWFLKRWRQGKVLPSEGDDFLEVNSMKELYLLMEEEEINAQHSDNKACTGDSWTQNTPNEYIKTLADMKVTLKELCWLLRDERRGLTELQQQFAKAKATWETERAELKGHTSQMELKTGKGAGERAGPDWKAALQREREEQQHLLAESYSAVMELTRQLQISERNWSQEKLQLVERLQGEKQQVEQQVKELQNRLSQLQKAADPWVLKHSELEKQDNSWKETRSEKIHDKEAVSEVELGGNGLKRTKSVSSMSEFESLLDCSPYLAGGDARGKKLPNNPAFGFVSSEPGDPEKDTKEKPGLSSRDCNHLGALACQDPPGRQMQRSYTAPDKTGIRVYYSPPVARRLGVPVVHDKEGKIIIEPGFLFTTAKPKESAEADGLAESSYGRWLCNFSRQRLDGGSAGSPSAAGPGFPAALHDFEMSGNMSDDMKEITNCVRQAMRSGSLERKVKSTSSQTVGLASVGTQTIRTVSVGLQTDPPRSSLHGKAWSPRSSSLVSVRSKQISSSLDKVHSRIERPCCSPKYGSPKLQRRSVSKLDSSKDRSLWNLHQGKQNGSAWARSTTTRDSPVLRNINDGLSSLFSVVEHSGSTESVWKLGMSETRAKPEPPKYGIVQEFFRNVCGRAPSPTSSAGEEGTKKPEPLSPASYHQPEGVARILNKKAAKLGSSEEVRLTMLPQVGKDGVLRDGDGAVVLPNEDAVCDCSTQSLTSCFARSSRSAIRHSPSKCRLHPSESSWGGEERALPPSE
| null | null |
cell division [GO:0051301]; chromosome segregation [GO:0007059]; insulin receptor signaling pathway [GO:0008286]; negative regulation of gluconeogenesis [GO:0045721]; regulation of autophagy [GO:0010506]
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extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; microtubule [GO:0005874]; midbody [GO:0030496]
| null |
PF14818;PF11365;
| null |
MTCL family
|
PTM: Proteolytically cleaved in primary hepatocytes into a C-terminal 80 kDa form (By similarity). Proteolytically cleaved into a C-terminal SOGA 25 kDa form that is detected in plasma. {ECO:0000250|UniProtKB:E1U8D0, ECO:0000269|PubMed:20813965}.; PTM: Phosphorylated during mitosis in a CDK1-dependent manner. {ECO:0000269|PubMed:33587225}.
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SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33587225}. Golgi apparatus membrane {ECO:0000250|UniProtKB:E1U8D0}. Midbody {ECO:0000269|PubMed:33587225}. Note=Associates with microtubules during late mitosis and interphase. {ECO:0000269|PubMed:33587225}.; SUBCELLULAR LOCATION: [C-terminal 80 kDa form]: Secreted {ECO:0000250|UniProtKB:E1U8D0}. Note=Secreted in primary hepatocyte-conditioned media. {ECO:0000250|UniProtKB:E1U8D0}.
| null | null | null | null | null |
FUNCTION: Microtubule-associated factor that enables integration of the centrosomal and Golgi-associated microtubules on the Golgi membrane, supporting directional migration. Preferentially acts on the perinuclear microtubules accumulated around the Golgi. Associates with the Golgi membrane through the N-terminal coiled-coil region and directly binds microtubules through the C-terminal domain (By similarity). Required for faithful chromosome segregation during mitosis (PubMed:33587225). Regulates autophagy by playing a role in the reduction of glucose production in an adiponectin- and insulin-dependent manner (By similarity). {ECO:0000250|UniProtKB:E1U8D0, ECO:0000269|PubMed:33587225}.
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Homo sapiens (Human)
|
O94966
|
UBP19_HUMAN
|
MSGGASATGPRRGPPGLEDTTSKKKQKDRANQESKDGDPRKETGSRYVAQAGLEPLASGDPSASASHAAGITGSRHRTRLFFPSSSGSASTPQEEQTKEGACEDPHDLLATPTPELLLDWRQSAEEVIVKLRVGVGPLQLEDVDAAFTDTDCVVRFAGGQQWGGVFYAEIKSSCAKVQTRKGSLLHLTLPKKVPMLTWPSLLVEADEQLCIPPLNSQTCLLGSEENLAPLAGEKAVPPGNDPVSPAMVRSRNPGKDDCAKEEMAVAADAATLVDEPESMVNLAFVKNDSYEKGPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLHPGCGPHTTFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEAPAARVGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVTPKPETHLASPKPTCMVPPMPHSPVSGDSVEEEEEEEKKVCLPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEVVAEEAWQRHKMRNDSFIVDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKVLPVFYFAREPHSKPIKFLVSVSKENSTASEVLDSLSQSVHVKPENLRLAEVIKNRFHRVFLPSHSLDTVSPSDTLLCFELLSSELAKERVVVLEVQQRPQVPSVPISKCAACQRKQQSEDEKLKRCTRCYRVGYCNQLCQKTHWPDHKGLCRPENIGYPFLVSVPASRLTYARLAQLLEGYARYSVSVFQPPFQPGRMALESQSPGCTTLLSTGSLEAGDSERDPIQPPELQLVTPMAEGDTGLPRVWAAPDRGPVPSTSGISSEMLASGPIEVGSLPAGERVSRPEAAVPGYQHPSEAMNAHTPQFFIYKIDSSNREQRLEDKGDTPLELGDDCSLALVWRNNERLQEFVLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRNLDLSKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSSQRSDVGWRLFDDSTVTTVDESQVVTRYAYVLFYRRRNSPVERPPRAGHSEHHPDLGPAAEAAASQASRIWQELEAEEEPVPEGSGPLGPWGPQDWVGPLPRGPTTPDEGCLRYFVLGTVAALVALVLNVFYPLVSQSRWR
|
3.4.19.12
| null |
ERAD pathway [GO:0036503]; negative regulation of skeletal muscle tissue development [GO:0048642]; positive regulation of cell cycle process [GO:0090068]; protein deubiquitination [GO:0016579]; protein stabilization [GO:0050821]; regulation of cellular response to hypoxia [GO:1900037]; regulation of ERAD pathway [GO:1904292]; regulation of protein stability [GO:0031647]; response to endoplasmic reticulum stress [GO:0034976]
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cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]
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cysteine-type deubiquitinase activity [GO:0004843]; Hsp90 protein binding [GO:0051879]; metal ion binding [GO:0046872]
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PF04969;PF00443;PF16602;PF01753;
|
2.60.40.790;6.10.140.2220;3.90.70.10;
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Peptidase C19 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19465887}; Single-pass membrane protein {ECO:0000269|PubMed:19465887}.
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CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
| null | null | null | null |
FUNCTION: Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked ubiquitin chains. {ECO:0000269|PubMed:19465887, ECO:0000269|PubMed:21849505, ECO:0000269|PubMed:22128162, ECO:0000269|PubMed:22689415}.
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Homo sapiens (Human)
|
O94967
|
WDR47_HUMAN
|
MTAEETVNVKEVEIIKLILDFLNSKKLHISMLALEKESGVINGLFSDDMLFLRQLILDGQWDEVLQFIQPLECMEKFDKKRFRYIILKQKFLEALCVNNAMSAEDEPQHLEFTMQEAVQCLHALEEYCPSKDDYSKLCLLLTLPRLTNHAEFKDWNPSTARVHCFEEACVMVAEFIPADRKLSEAGFKASNNRLFQLVMKGLLYECCVEFCQSKATGEEITESEVLLGIDLLCGNGCDDLDLSLLSWLQNLPSSVFSCAFEQKMLNIHVDKLLKPTKAAYADLLTPLISKLSPYPSSPMRRPQSADAYMTRSLNPALDGLTCGLTSHDKRISDLGNKTSPMSHSFANFHYPGVQNLSRSLMLENTECHSIYEESPERDTPVDAQRPIGSEILGQSSVSEKEPANGAQNPGPAKQEKNELRDSTEQFQEYYRQRLRYQQHLEQKEQQRQIYQQMLLEGGVNQEDGPDQQQNLTEQFLNRSIQKLGELNIGMDGLGNEVSALNQQCNGSKGNGSNGSSVTSFTTPPQDSSQRLTHDASNIHTSTPRNPGSTNHIPFLEESPCGSQISSEHSVIKPPLGDSPGSLSRSKGEEDDKSKKQFVCINILEDTQAVRAVAFHPAGGLYAVGSNSKTLRVCAYPDVIDPSAHETPKQPVVRFKRNKHHKGSIYCVAWSPCGQLLATGSNDKYVKVLPFNAETCNATGPDLEFSMHDGTIRDLAFMEGPESGGAILISAGAGDCNIYTTDCQRGQGLHALSGHTGHILALYTWSGWMIASGSQDKTVRFWDLRVPSCVRVVGTTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPHSSDVRSVRFSPGAHYLLTGSYDMKIKVTDLQGDLTKQLPIMVVGEHKDKVIQCRWHTQDLSFLSSSADRTVTLWTYNG
| null | null |
adult locomotory behavior [GO:0008344]; anterior commissure morphogenesis [GO:0021960]; autophagy [GO:0006914]; cerebral cortex radial glia-guided migration [GO:0021801]; corpus callosum development [GO:0022038]; detection of hot stimulus involved in thermoception [GO:0120168]; microtubule cytoskeleton organization [GO:0000226]; motor behavior [GO:0061744]; negative regulation of microtubule depolymerization [GO:0007026]; neural precursor cell proliferation [GO:0061351]; neuronal stem cell population maintenance [GO:0097150]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; growth cone [GO:0030426]; microtubule [GO:0005874]; neuronal cell body [GO:0043025]
| null |
PF17814;PF00400;
|
2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localization along microtubules is mediated by MAP1S. {ECO:0000250}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O94972
|
TRI37_HUMAN
|
MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQLCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILRFQVRSPTFFQKSRDQHWYITQLEAAQTSYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDALETRAKKSACSDMLLEGGPTTASVREAKEDEEDEEKIQNEDYHHELSDGDLDLDLVYEDEVNQLDGSSSSASSTATSNTEENDIDEETMSGENDVEYNNMELEEGELMEDAAAAGPAGSSHGYVGSSSRISRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSIENLWGLQPRPPASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKNTLSEIKSSSAASGDMQTSLFSADQAALAACGTENSGRLQDLGMELLAKSSVANCYIRNSTNKKSNSPKPARSSVAGSLSLRRAVDPGENSRSKGDCQTLSEGSPGSSQSGSRHSSPRALIHGSIGDILPKTEDRQCKALDSDAVVVAVFSGLPAVEKRRKMVTLGANAKGGHLEGLQMTDLENNSETGELQPVLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSVGGFHDSFMVMTQPPDEDTHSSFPDGEQIGPEDLSFNTDENSGR
|
2.3.2.27
| null |
aggresome assembly [GO:0070842]; negative regulation of centriole replication [GO:0046600]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein autoubiquitination [GO:0051865]; protein import into peroxisome matrix [GO:0016558]; protein monoubiquitination [GO:0006513]; protein stabilization [GO:0050821]
|
aggresome [GO:0016235]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]
|
chromatin binding [GO:0003682]; histone H2AK119 ubiquitin ligase activity [GO:0140862]; protein homodimerization activity [GO:0042803]; transcription coactivator activity [GO:0003713]; tumor necrosis factor receptor binding [GO:0005164]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
|
PF00917;PF00643;
|
3.30.160.60;3.30.40.10;
|
TRIM/RBCC family
|
PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:15885686}.
|
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:25470042}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15885686}. Peroxisome membrane {ECO:0000269|PubMed:11938494, ECO:0000269|PubMed:28724525}; Peripheral membrane protein {ECO:0000269|PubMed:28724525}. Note=Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation. {ECO:0000269|PubMed:15885686}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:28724525};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:25470042, ECO:0000269|PubMed:28724525}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase required to prevent centriole reduplication (PubMed:15885686, PubMed:23769972). Probably acts by ubiquitinating positive regulators of centriole reduplication (PubMed:23769972). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes (PubMed:25470042). Also acts as a positive regulator of peroxisome import by mediating monoubiquitination of PEX5 at 'Lys-472': monoubiquitination promotes PEX5 stabilitation by preventing its polyubiquitination and degradation by the proteasome (PubMed:28724525). Has anti-HIV activity (PubMed:24317724). {ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:23769972, ECO:0000269|PubMed:24317724, ECO:0000269|PubMed:25470042, ECO:0000269|PubMed:28724525}.
|
Homo sapiens (Human)
|
O94973
|
AP2A2_HUMAN
|
MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIASVGSREMAEAFAGEIPKVLVAGDTMDSVKQSAALCLLRLYRTSPDLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPDPAVRGRLTECLETILNKAQEPPKSKKVQHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAPQIVAEMLSYLETADYSIREEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAAKTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFHLLHSKFHLCSVPTRALLLSTYIKFVNLFPEVKPTIQDVLRSDSQLRNADVELQQRAVEYLRLSTVASTDILATVLEEMPPFPERESSILAKLKKKKGPSTVTDLEDTKRDRSVDVNGGPEPAPASTSAVSTPSPSADLLGLGAAPPAPAGPPPSSGGSGLLVDVFSDSASVVAPLAPGSEDNFARFVCKNNGVLFENQLLQIGLKSEFRQNLGRMFIFYGNKTSTQFLNFTPTLICSDDLQPNLNLQTKPVDPTVEGGAQVQQVVNIECVSDFTEAPVLNIQFRYGGTFQNVSVQLPITLNKFFQPTEMASQDFFQRWKQLSNPQQEVQNIFKAKHPMDTEVTKAKIIGFGSALLEEVDPNPANFVGAGIIHTKTTQIGCLLRLEPNLQAQMYRLTLRTSKEAVSQRLCELLSAQF
| null | null |
clathrin-dependent endocytosis [GO:0072583]; intracellular protein transport [GO:0006886]; postsynaptic neurotransmitter receptor internalization [GO:0098884]; vesicle-mediated transport [GO:0016192]
|
AP-2 adaptor complex [GO:0030122]; clathrin-coated endocytic vesicle [GO:0045334]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; endolysosome membrane [GO:0036020]; ficolin-1-rich granule membrane [GO:0101003]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; secretory granule membrane [GO:0030667]
|
clathrin adaptor activity [GO:0035615]; disordered domain specific binding [GO:0097718]; lipid binding [GO:0008289]; protein kinase binding [GO:0019901]
|
PF01602;PF02296;PF02883;
|
2.60.40.1230;1.25.10.10;3.30.310.10;
|
Adaptor complexes large subunit family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17427}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17427}; Cytoplasmic side {ECO:0000250|UniProtKB:P17427}. Membrane, coated pit {ECO:0000250|UniProtKB:P17427}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17427}; Cytoplasmic side {ECO:0000250|UniProtKB:P17427}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000250|UniProtKB:P17427}.
| null | null | null | null | null |
FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). {ECO:0000250, ECO:0000269|PubMed:12960147, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23676497}.
|
Homo sapiens (Human)
|
O94979
|
SC31A_HUMAN
|
MKLKEVDRTAMQAWSPAQNHPIYLATGTSAQQLDATFSTNASLEIFELDLSDPSLDMKSCATFSSSHRYHKLIWGPYKMDSKGDVSGVLIAGGENGNIILYDPSKIIAGDKEVVIAQNDKHTGPVRALDVNIFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCSGLAWHPDVATQMVLASEDDRLPVIQMWDLRFASSPLRVLENHARGILAIAWSMADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSAASFDGRISVYSIMGGSTDGLRQKQVDKLSSSFGNLDPFGTGQPLPPLQIPQQTAQHSIVLPLKKPPKWIRRPVGASFSFGGKLVTFENVRMPSHQGAEQQQQQHHVFISQVVTEKEFLSRSDQLQQAVQSQGFINYCQKKIDASQTEFEKNVWSFLKVNFEDDSRGKYLELLGYRKEDLGKKIALALNKVDGANVALKDSDQVAQSDGEESPAAEEQLLGEHIKEEKEESEFLPSSGGTFNISVSGDIDGLITQALLTGNFESAVDLCLHDNRMADAIILAIAGGQELLARTQKKYFAKSQSKITRLITAVVMKNWKEIVESCDLKNWREALAAVLTYAKPDEFSALCDLLGTRLENEGDSLLQTQACLCYICAGNVEKLVACWTKAQDGSHPLSLQDLIEKVVILRKAVQLTQAMDTSTVGVLLAAKMSQYANLLAAQGSIAAALAFLPDNTNQPNIMQLRDRLCRAQGEPVAGHESPKIPYEKQQLPKGRPGPVAGHHQMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSNAYPNTPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPASQRTGPQNGWNDPPALNRVPKKKKMPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPVPLSSQSSFPQPHLPGGQPFHGVQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEHLILKTTFEDLIQRCLSSATDPQTKRKLDDASKRLEFLYDKLREQTLSPTITSGLHNIARSIETRNYSEGLTMHTHIVSTSNFSETSAFMPVLKVVLTQANKLGV
| null | null |
COPII-coated vesicle cargo loading [GO:0090110]; endoplasmic reticulum organization [GO:0007029]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; response to calcium ion [GO:0051592]
|
COPII vesicle coat [GO:0030127]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]; vesicle coat [GO:0030120]
|
calcium-dependent protein binding [GO:0048306]; structural molecule activity [GO:0005198]
|
PF12931;
|
1.25.40.1030;1.20.940.10;2.130.10.10;
|
WD repeat SEC31 family
|
PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex, leading to regulate the size of COPII coats. {ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:27565346}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:10788476, ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:27716508}; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:17428803}. Note=Associates with membranes in a GTP-dependent manner (By similarity). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:17428803, PubMed:25201882, PubMed:28442536). {ECO:0000250|UniProtKB:Q9Z2Q1, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:28442536}.
| null | null | null | null | null |
FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER) (PubMed:10788476). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity). {ECO:0000250|UniProtKB:Q9Z2Q1, ECO:0000269|PubMed:10788476}.
|
Homo sapiens (Human)
|
O94983
|
CMTA2_HUMAN
|
MNTKDTTEVAENSHHLKIFLPKKLLECLPRCPLLPPERLRWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKYRKDGYLWKKRKDGKTTREDHMKLKVQGMECLYGCYVHSSIVPTFHRRCYWLLQNPDIVLVHYLNVPALEDCGKGCSPIFCSISSDRREWLKWSREELLGQLKPMFHGIKWSCGNGTEEFSVEHLVQQILDTHPTKPAPRTHACLCSGGLGSGSLTHKCSSTKHRIISPKVEPRALTLTSIPHAHPPEPPPLIAPLPPELPKAHTSPSSSSSSSSSGFAEPLEIRPSPPTSRGGSSRGGTAILLLTGLEQRAGGLTPTRHLAPQADPRPSMSLAVVVGTEPSAPPAPPSPAFDPDRFLNSPQRGQTYGGGQGVSPDFPEAEAAHTPCSALEPAAALEPQAAARGPPPQSVAGGRRGNCFFIQDDDSGEELKGHGAAPPIPSPPPSPPPSPAPLEPSSRVGRGEALFGGPVGASELEPFSLSSFPDLMGELISDEAPSIPAPTPQLSPALSTITDFSPEWSYPEGGVKVLITGPWTEAAEHYSCVFDHIAVPASLVQPGVLRCYCPAHEVGLVSLQVAGREGPLSASVLFEYRARRFLSLPSTQLDWLSLDDNQFRMSILERLEQMEKRMAEIAAAGQVPCQGPDAPPVQDEGQGPGFEARVVVLVESMIPRSTWKGPERLAHGSPFRGMSLLHLAAAQGYARLIETLSQWRSVETGSLDLEQEVDPLNVDHFSCTPLMWACALGHLEAAVLLFRWNRQALSIPDSLGRLPLSVAHSRGHVRLARCLEELQRQEPSVEPPFALSPPSSSPDTGLSSVSSPSELSDGTFSVTSAYSSAPDGSPPPAPLPASEMTMEDMAPGQLSSGVPEAPLLLMDYEATNSKGPLSSLPALPPASDDGAAPEDADSPQAVDVIPVDMISLAKQIIEATPERIKREDFVGLPEAGASMRERTGAVGLSETMSWLASYLENVDHFPSSTPPSELPFERGRLAVPSAPSWAEFLSASTSGKMESDFALLTLSDHEQRELYEAARVIQTAFRKYKGRRLKEQQEVAAAVIQRCYRKYKQLTWIALKFALYKKMTQAAILIQSKFRSYYEQKRFQQSRRAAVLIQQHYRSYRRRPGPPHRTSATLPARNKGSFLTKKQDQAARKIMRFLRRCRHRMRELKQNQELEGLPQPGLAT
| null | null |
cardiac muscle hypertrophy in response to stress [GO:0014898]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; histone deacetylase binding [GO:0042826]; sequence-specific DNA binding [GO:0043565]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]
|
PF03859;PF01833;
|
1.20.5.190;1.25.40.20;2.60.40.10;
|
CAMTA family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11925432}.
| null | null | null | null | null |
FUNCTION: Transcription activator. May act as tumor suppressor. {ECO:0000269|PubMed:11925432}.
|
Homo sapiens (Human)
|
O94985
|
CSTN1_HUMAN
|
MLRRPAPALAPAARLLLAGLLCGGGVWAARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAESFEVTVTKEGEICGFKIHGQNVPFDAVVVDKSTGEGVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNVKKSHKATVHIQVNDVNEYAPVFKEKSYKATVIEGKQYDSILRVEAVDADCSPQFSQICSYEIITPDVPFTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKPTCTPGWQGWNNRIEYEPGTGALAVFPNIHLETCDEPVASVQATVELETSHIGKGCDRDTYSEKSLHRLCGAAAGTAELLPSPSGSLNWTMGLPTDNGHDSDQVFEFNGTQAVRIPDGVVSVSPKEPFTISVWMRHGPFGRKKETILCSSDKTDMNRHHYSLYVHGCRLIFLFRQDPSEEKKYRPAEFHWKLNQVCDEEWHHYVLNVEFPSVTLYVDGTSHEPFSVTEDYPLHPSKIETQLVVGACWQEFSGVENDNETEPVTVASAGGDLHMTQFFRGNLAGLTLRSGKLADKKVIDCLYTCKEGLDLQVLEDSGRGVQIQAHPSQLVLTLEGEDLGELDKAMQHISYLNSRQFPTPGIRRLKITSTIKCFNEATCISVPPVDGYVMVLQPEEPKISLSGVHHFARAASEFESSEGVFLFPELRIISTITREVEPEGDGAEDPTVQESLVSEEIVHDLDTCEVTVEGEELNHEQESLEVDMARLQQKGIEVSSSELGMTFTGVDTMASYEEVLHLLRYRNWHARSLLDRKFKLICSELNGRYISNEFKVEVNVIHTANPMEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSFLVFMIILGVFRIRAAHRRTMRDQDTGKENEMDWDDSALTITVNPMETYEDQHSSEEEEEEEEEEESEDGEEEDDITSAESESSEEEEGEQGDPQNATRQQQLEWDDSTLSY
| null | null |
cell adhesion [GO:0007155]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; neurotransmitter receptor transport to postsynaptic membrane [GO:0098969]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission [GO:0050806]; regulation of cell growth [GO:0001558]; regulation of synapse maturation [GO:0090128]; vesicle-mediated transport in synapse [GO:0099003]
|
cell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; neuron projection [GO:0043005]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]; postsynaptic endosome [GO:0098845]; postsynaptic membrane [GO:0045211]
|
amyloid-beta binding [GO:0001540]; calcium ion binding [GO:0005509]; kinesin binding [GO:0019894]; X11-like protein binding [GO:0042988]
|
PF00028;PF19699;PF13385;
|
2.60.120.200;2.60.40.60;
|
Calsyntenin family
|
PTM: Proteolytically processed under normal cellular conditions (PubMed:15037614). A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1) (PubMed:15037614). A secondary cleavage catalyzed by presenilin gamma-secretase within the transmembrane domain releases the beta-Alc-alpha chain in the extracellular milieu and produces an intracellular fragment (AlcICD) (PubMed:15037614). This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with PSEN1 (PubMed:15037614). {ECO:0000269|PubMed:15037614}.
|
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9EPL2}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17332754}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:17332754, ECO:0000269|PubMed:21385839}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, neuron projection {ECO:0000269|PubMed:17332754}. Note=Localized in the postsynaptic membrane of both excitatory and inhibitory synapses. {ECO:0000250|UniProtKB:Q9EPL2}.; SUBCELLULAR LOCATION: [Soluble Alc-alpha]: Nucleus {ECO:0000269|PubMed:17332754}. Note=The AlcICD fragment is translocated to the nucleus upon interaction with APBB1. {ECO:0000269|PubMed:17332754}.
| null | null | null | null | null |
FUNCTION: Postsynaptic adhesion molecule that binds to presynaptic neurexins to mediate both excitatory and inhibitory synapse formation (By similarity). Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with neurexin-alpha at the presynaptic membrane (By similarity). Also functions as a cargo in axonal anterograde transport by acting as a molecular adapter that promotes KLC1 association with vesicles (PubMed:21385839). Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation (PubMed:12972431). {ECO:0000250|UniProtKB:Q99JH7, ECO:0000250|UniProtKB:Q9EPL2, ECO:0000269|PubMed:12972431, ECO:0000269|PubMed:21385839}.; FUNCTION: [Soluble Alc-alpha]: As intracellular fragment AlcICD, suppresses APBB1-dependent transactivation stimulated by APP C-terminal intracellular fragment (AICD), most probably by competing with AICD for APBB1-binding (PubMed:15037614). {ECO:0000305|PubMed:15037614}.; FUNCTION: [CTF1-alpha]: In complex with APBA2 and C99, a C-terminal APP fragment, abolishes C99 interaction with PSEN1 and thus APP C99 cleavage by gamma-secretase, most probably through stabilization of the direct interaction between APBA2 and APP (PubMed:15037614). {ECO:0000305|PubMed:15037614}.
|
Homo sapiens (Human)
|
O94986
|
CE152_HUMAN
|
MSLDFGSVALPVQNEDEEYDEEDYEREKELQQLLTDLPHDMLDDDLSSPELQYSDCSEDGTDGQPHHPEQLEMSWNEQMLPKSQSVNGYNEIQSLYAGEKCGNVWEENRSKTEDRHPVYHPEEGGDEGGSGYSPPSKCEQTDLYHLPENFRPYTNGQKQEFNNQATNVIKFSDPQWNHFQGPSCQGLEPYNKVTYKPYQSSAQNNGSPAQEITGSDTFEGLQQQFLGANENSAENMQIIQLQVLNKAKERQLENLIEKLNESERQIRYLNHQLVIIKDEKDGLTLSLRESQKLFQNGKEREIQLEAQIKALETQIQALKVNEEQMIKKSRTTEMALESLKQQLVDLHHSESLQRAREQHESIVMGLTKKYEEQVLSLQKNLDATVTALKEQEDICSRLKDHVKQLERNQEAIKLEKTEIINKLTRSLEESQKQCAHLLQSGSVQEVAQLQFQLQQAQKAHAMSANMNKALQEELTELKDEISLYESAAKLGIHPSDSEGELNIELTESYVDLGIKKVNWKKSKVTSIVQEEDPNEELSKDEFILKLKAEVQRLLGSNSMKRHLVSQLQNDLKDCHKKIEDLHQVKKDEKSIEVETKTDTSEKPKNQLWPESSTSDVVRDDILLLKNEIQVLQQQNQELKETEGKLRNTNQDLCNQMRQMVQDFDHDKQEAVDRCERTYQQHHEAMKTQIRESLLAKHALEKQQLFEAYERTHLQLRSELDKLNKEVTAVQECYLEVCREKDNLELTLRKTTEKEQQTQEKIKEKLIQQLEKEWQSKLDQTIKAMKKKTLDCGSQTDQVTTSDVISKKEMAIMIEEQKCTIQQNLEQEKDIAIKGAMKKLEIELELKHCENITKQVEIAVQNAHQRWLGELPELAEYQALVKAEQKKWEEQHEVSVNKRISFAVSEAKEKWKSELENMRKNILPGKELEEKIHSLQKELELKNEEVPVVIRAELAKARSEWNKEKQEEIHRIQEQNEQDYRQFLDDHRNKINEVLAAAKEDFMKQKTELLLQKETELQTCLDQSRREWTMQEAKRIQLEIYQYEEDILTVLGVLLSDTQKEHISDSEDKQLLEIMSTCSSKWMSVQYFEKLKGCIQKAFQDTLPLLVENADPEWKKRNMAELSKDSASQGTGQGDPGPAAGHHAQPLALQATEAEADKKKVLEIKDLCCGHCFQELEKAKQECQDLKGKLEKCCRHLQHLERKHKAVVEKIGEENNKVVEELIEENNDMKNKLEELQTLCKTPPRSLSAGAIENACLPCSGGALEELRGQYIKAVKKIKCDMLRYIQESKERAAEMVKAEVLRERQETARKMRKYYLICLQQILQDDGKEGAEKKIMNAASKLATMAKLLETPISSKSQSKTTQSALPLTSEMLIAVKKSKRNDVNQKIPCCIESKSNSVNTITRTLCEQAPKRRAACNLQRLLENSEHQSIKHVGSKETHLEFQFGDGSCKHLNSLPRNVSPEFVPCEGEGGFGLHKKKDLLSDNGSESLPHSAAYPFLGTLGNKPSPRCTPGPSESGCMHITFRDSNERLGLKVYKCNPLMESENAASEKSQGLDVQEPPVKDGGDLSDCLGWPSSSATLSFDSREASFVHGRPQGTLEIPSESVKSKQFSPSGYLSDTEESNMICQTMKCQRYQTPYLSEETTYLEPGKISVNCGHPSRHKADRLKSDFKKLSSTLPSSVCQQPSRKLIVPLSSQQDSGFDSPFVNLD
| null | null |
cell projection organization [GO:0030030]; centriole replication [GO:0007099]; centrosome duplication [GO:0051298]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]
|
centriole [GO:0005814]; centrosome [GO:0005813]; cytosol [GO:0005829]; deuterosome [GO:0098536]; nucleoplasm [GO:0005654]; pericentriolar material [GO:0000242]; procentriole [GO:0120098]; procentriole replication complex [GO:0120099]
|
protein kinase binding [GO:0019901]
| null | null |
CEP152 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20598275, ECO:0000269|PubMed:21059844, ECO:0000269|PubMed:21131973, ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:30804208}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:22020124, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:26337392, ECO:0000269|PubMed:32060285}. Note=Colocalizes with CDK5RAP2, WDR62 and CEP63 in a discrete ring around the proximal end of the parental centriole. At this site, a cohesive structure is predicted to engage parental centrioles and procentrioles (PubMed:21983783, PubMed:26297806). Localizes to the deuterosome (By similarity). Localizes to pericentriolar material (PCM) (PubMed:26337392). {ECO:0000250|UniProtKB:Q498G2, ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:26337392}.
| null | null | null | null | null |
FUNCTION: Necessary for centrosome duplication; the function seems also to involve CEP63, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). Acts as a molecular scaffold facilitating the interaction of PLK4 and CENPJ, 2 molecules involved in centriole formation (PubMed:20852615, PubMed:21059844). Proposed to snatch PLK4 away from PLK4:CEP92 complexes in early G1 daughter centriole and to reposition PLK4 at the outer boundary of a newly forming CEP152 ring structure (PubMed:24997597). Also plays a key role in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles (By similarity). Overexpression of CEP152 can drive amplification of centrioles (PubMed:20852615). {ECO:0000250|UniProtKB:A2AUM9, ECO:0000250|UniProtKB:Q498G2, ECO:0000269|PubMed:20852615, ECO:0000269|PubMed:21059844, ECO:0000269|PubMed:21131973}.
|
Homo sapiens (Human)
|
O94989
|
ARHGF_HUMAN
|
MSAQSLPAATPPTQKPPRIIRPRPPSRSRAAQSPGPPHNGSSPQELPRNSNDAPTPMCTPIFWEPPAASLKPPALLPPSASRASLDSQTSPDSPSSTPTPSPVSRRSASPEPAPRSPVPPPKPSGSPCTPLLPMAGVLAQNGSASAPGTVRRLAGRFEGGAEGRAQDADAPEPGLQARADVNGEREAPLTGSGSQENGAPDAGLACPPCCPCVCHTTRPGLELRWVPVGGYEEVPRVPRRASPLRTSRSRPHPPSIGHPAVVLTSYRSTAERKLLPLLKPPKPTRVRQDATIFGDPPQPDLDLLSEDGIQTGDSPDEAPQNTPPATVEGREEEGLEVLKEQNWELPLQDEPLYQTYRAAVLSEELWGVGEDGSPSPANAGDAPTFPRPPGPRNTLWQELPAVQASGLLDTLSPQERRMQESLFEVVTSEASYLRSLRLLTDTFVLSQALRDTLTPRDHHTLFSNVQRVQGVSERFLATLLSRVRSSPHISDLCDVVHAHAVGPFSVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILRQTEEGSSRQENAQKALGAVSKIIERCSAEVGRMKQTEELIRLTQRLRFHKVKALPLVSWSRRLEFQGELTELGCRRGGVLFASRPRFTPLCLLLFSDLLLITQPKSGQRLQVLDYAHRSLVQAQQVPDPSGPPTFRLSLLSNHQGRPTHRLLQASSLSDMQRWLGAFPTPGPLPCSPDTIYEDCDCSQELCSESSAPAKTEGRSLESRAAPKHLHKTPEGWLKGLPGAFPAQLVCEVTGEHERRRHLRQNQRLLEAVGSSSGTPNAPPP
| null | null |
negative regulation of synapse maturation [GO:2000297]; positive regulation of stress fiber assembly [GO:0051496]; regulation of catalytic activity [GO:0050790]; regulation of postsynapse assembly [GO:0150052]; regulation of small GTPase mediated signal transduction [GO:0051056]; retina vasculature morphogenesis in camera-type eye [GO:0061299]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; postsynapse [GO:0098794]
|
GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF00621;
|
1.20.900.10;2.30.29.30;
| null |
PTM: Phosphorylated on tyrosine residues upon EFNA1 stimulation. EPHB2-dependent phosphorylation at Tyr-353 triggers UBE3A-mediated ubiquitination (By similarity). {ECO:0000250}.; PTM: Ubiquitinated; UBE3A-mediated ubiquitination and degradation by the proteasome promotes EFNB1-dependent synapse formation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000250}. Note=Expressed exclusively in dendrites of the developing hippocampus. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Specific GEF for RhoA activation. Does not activate RAC1 or CDC42. Regulates vascular smooth muscle contractility. Negatively regulates excitatory synapse development by suppressing the synapse-promoting activity of EPHB2. {ECO:0000269|PubMed:12775584}.
|
Homo sapiens (Human)
|
O94991
|
SLIK5_HUMAN
|
MHTCCPPVTLEQDLHRKMHSWMLQTLAFAVTSLVLSCAETIDYYGEICDNACPCEEKDGILTVSCENRGIISLSEISPPRFPIYHLLLSGNLLNRLYPNEFVNYTGASILHLGSNVIQDIETGAFHGLRGLRRLHLNNNKLELLRDDTFLGLENLEYLQVDYNYISVIEPNAFGKLHLLQVLILNDNLLSSLPNNLFRFVPLTHLDLRGNRLKLLPYVGLLQHMDKVVELQLEENPWNCSCELISLKDWLDSISYSALVGDVVCETPFRLHGRDLDEVSKQELCPRRLISDYEMRPQTPLSTTGYLHTTPASVNSVATSSSAVYKPPLKPPKGTRQPNKPRVRPTSRQPSKDLGYSNYGPSIAYQTKSPVPLECPTACSCNLQISDLGLNVNCQERKIESIAELQPKPYNPKKMYLTENYIAVVRRTDFLEATGLDLLHLGNNRISMIQDRAFGDLTNLRRLYLNGNRIERLSPELFYGLQSLQYLFLQYNLIREIQSGTFDPVPNLQLLFLNNNLLQAMPSGVFSGLTLLRLNLRSNHFTSLPVSGVLDQLKSLIQIDLHDNPWDCTCDIVGMKLWVEQLKVGVLVDEVICKAPKKFAETDMRSIKSELLCPDYSDVVVSTPTPSSIQVPARTSAVTPAVRLNSTGAPASLGAGGGASSVPLSVLILSLLLVFIMSVFVAAGLFVLVMKRRKKNQSDHTSTNNSDVSSFNMQYSVYGGGGGTGGHPHAHVHHRGPALPKVKTPAGHVYEYIPHPLGHMCKNPIYRSREGNSVEDYKDLHELKVTYSSNHHLQQQQQPPPPPQQPQQQPPPQLQLQPGEEERRESHHLRSPAYSVSTIEPREDLLSPVQDADRFYRGILEPDKHCSTTPAGNSLPEYPKFPCSPAAYTFSPNYDLRRPHQYLHPGAGDSRLREPVLYSPPSAVFVEPNRNEYLELKAKLNVEPDYLEVLEKQTTFSQF
| null | null |
adult behavior [GO:0030534]; axonogenesis [GO:0007409]; chemical synaptic transmission [GO:0007268]; circulatory system development [GO:0072359]; dendrite morphogenesis [GO:0048813]; grooming behavior [GO:0007625]; positive regulation of synapse assembly [GO:0051965]; regulation of presynapse assembly [GO:1905606]; response to xenobiotic stimulus [GO:0009410]; skin development [GO:0043588]; striatum development [GO:0021756]
|
plasma membrane [GO:0005886]; receptor complex [GO:0043235]; synapse [GO:0045202]
| null |
PF13855;
|
3.80.10.10;
|
SLITRK family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Suppresses neurite outgrowth. {ECO:0000250}.
|
Homo sapiens (Human)
|
O94992
|
HEXI1_HUMAN
|
MAEPFLSEYQHQPQTSNCTGAAAVQEELNPERPPGAEERVPEEDSRWQSRAFPQLGGRPGPEGEGSLESQPPPLQTQACPESSCLREGEKGQNGDDSSAGGDFPPPAEVEPTPEAELLAQPCHDSEASKLGAPAAGGEEEWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRIRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYSKRAAAKSDDTSDDDFMEEGGEEDGGSDGMGGDGSEFLQRDFSETYERYHTESLQNMSKQELIKEYLELEKCLSRMEDENNRLRLESKRLGGDDARVRELELELDRLRAENLQLLTENELHRQQERAPLSKFGD
| null | null |
activation of innate immune response [GO:0002218]; heart development [GO:0007507]; innate immune response [GO:0045087]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; negative regulation of viral transcription [GO:0032897]; positive regulation of signal transduction by p53 class mediator [GO:1901798]
|
7SK snRNP [GO:0120259]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
7SK snRNA binding [GO:0097322]; cyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; identical protein binding [GO:0042802]; P-TEFb complex binding [GO:0106140]; protein kinase inhibitor activity [GO:0004860]; snRNA binding [GO:0017069]
|
PF15313;
|
6.10.250.2910;
|
HEXIM family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12581153, ECO:0000269|PubMed:12832472, ECO:0000269|PubMed:12941847, ECO:0000269|PubMed:16362050, ECO:0000269|PubMed:17395637}. Cytoplasm {ECO:0000269|PubMed:12581153, ECO:0000269|PubMed:17395637}. Note=Binds alpha-importin and is mostly nuclear (PubMed:16362050).
| null | null | null | null | null |
FUNCTION: Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor (PubMed:14580347, PubMed:15201869, PubMed:15713661). Core component of the 7SK RNP complex: in cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (PubMed:12832472, PubMed:14580347, PubMed:15201869, PubMed:15713661). May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity (PubMed:15940264, PubMed:15941832, PubMed:17088550). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). {ECO:0000269|PubMed:12581153, ECO:0000269|PubMed:12832472, ECO:0000269|PubMed:14580347, ECO:0000269|PubMed:15201869, ECO:0000269|PubMed:15713661, ECO:0000269|PubMed:15940264, ECO:0000269|PubMed:15941832, ECO:0000269|PubMed:17088550, ECO:0000269|PubMed:28712728}.
|
Homo sapiens (Human)
|
O94993
|
SOX30_HUMAN
|
MERARPEPPPQPRPLRPAPPPLPVEGTSFWAAAMEPPPSSPTLSAAASATLASSCGEAVASGLQPAVRRLLQVKPEQVLLLPQPQAQNEEAAASSAQARLLQFRPDLRLLQPPTASDGATSRPELHPVQPLALHVKAKKQKLGPSLDQSVGPRGAVETGPRASRVVKLEGPGPALGYFRGDEKGKLEAEEVMRDSMQGGAGKSPAAIREGVIKTEEPERLLEDCRLGAEPASNGLVHGSAEVILAPTSGAFGPHQQDLRIPLTLHTVPPGARIQFQGAPPSELIRLTKVPLTPVPTKMQSLLEPSVKIETKDVPLTVLPSDAGIPDTPFSKDRNGHVKRPMNAFMVWARIHRPALAKANPAANNAEISVQLGLEWNKLSEEQKKPYYDEAQKIKEKHREEFPGWVYQPRPGKRKRFPLSVSNVFSGTTQNIISTNPTTVYPYRSPTYSVVIPSLQNPITHPVGETSPAIQLPTPAVQSPSPVTLFQPSVSSAAQVAVQDPSLPVYPALPPQRFTGPSQTDTHQLHSEATHTVKQPTPVSLESANRISSSASTAHARFATSTIQPPREYSSVSPCPRSAPIPQASPIPHPHVYQPPPLGHPATLFGTPPRFSFHHPYFLPGPHYFPSSTCPYSRPPFGYGNFPSSMPECLSYYEDRYPKHEGIFSTLNRDYSFRDYSSECTHSENSRSCENMNGTSYYNSHSHSGEENLNPVPQLDIGTLENVFTAPTSTPSSIQQVNVTDSDEEEEEKVLRDL
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proacrosomal vesicle fusion [GO:0120211]; regulation of transcription by RNA polymerase II [GO:0006357]; response to corticosteroid [GO:0031960]; spermatid development [GO:0007286]
|
chromatin [GO:0000785]; chromocenter [GO:0010369]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
beta-catenin binding [GO:0008013]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00505;
|
1.10.30.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10359848, ECO:0000269|PubMed:29739711}. Cytoplasm {ECO:0000269|PubMed:29739711}. Note=Enriched at the chromocenter. {ECO:0000250|UniProtKB:Q8CGW4}.
| null | null | null | null | null |
FUNCTION: Acts both as a transcriptional activator and a repressor (PubMed:10359848, PubMed:29739711). Binds to the DNA sequence 5'-ACAAT-3' and shows a preference for guanine residues surrounding this core motif (PubMed:10359848). Binds to its own promoter and activates its own transcription (By similarity). Required to activate the expression of postmeiotic genes involved in spermiogenesis (By similarity). Binds to the promoter region of CTNNB1 and represses its transcription which leads to inhibition of Wnt signaling (PubMed:29739711). Also inhibits Wnt signaling by binding to the CTNNB1 protein, preventing interaction of CTNNB1 with TCF7L2/TCF4 (PubMed:29739711). {ECO:0000250|UniProtKB:Q8CGW4, ECO:0000269|PubMed:10359848, ECO:0000269|PubMed:29739711}.
|
Homo sapiens (Human)
|
O95045
|
UPP2_HUMAN
|
MASVIPASNRSMRSDRNTYVGKRFVHVKNPYLDLMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFALFMHKELGFEEAEEDIKDICAGTDRYCMYKTGPVLAISHGMGIPSISIMLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVILDNIVTRSTELDKELSEELFNCSKEIPNFPTLVGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAFKAGVRNIEMESTVFAAMCGLCGLKAAVVCVTLLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRRRLGLCD
|
2.4.2.3
| null |
dCMP catabolic process [GO:0006249]; nucleoside metabolic process [GO:0009116]; UMP salvage [GO:0044206]; uridine catabolic process [GO:0006218]; uridine metabolic process [GO:0046108]
|
cytosol [GO:0005829]; type III intermediate filament [GO:0045098]
|
deoxyuridine phosphorylase activity [GO:0047847]; identical protein binding [GO:0042802]; uridine phosphorylase activity [GO:0004850]
|
PF01048;
|
3.40.50.1580;
|
PNP/UDP phosphorylase family
| null | null |
CATALYTIC ACTIVITY: Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3; Evidence={ECO:0000269|PubMed:12849978, ECO:0000269|PubMed:21855639}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24389; Evidence={ECO:0000305|PubMed:12849978}; CATALYTIC ACTIVITY: Reaction=2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + uracil; Xref=Rhea:RHEA:22824, ChEBI:CHEBI:16450, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; Evidence={ECO:0000269|PubMed:12849978}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22825; Evidence={ECO:0000305|PubMed:12849978};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=76 uM for uridine {ECO:0000269|PubMed:12849978}; KM=300 uM for deoxyuridine {ECO:0000269|PubMed:12849978}; KM=73 uM for thymidine {ECO:0000269|PubMed:12849978}; KM=24 uM for 5-fluorouridine {ECO:0000269|PubMed:12849978}; KM=427 uM for 5-fluoro-2(')-deoxyuridine {ECO:0000269|PubMed:12849978}; Vmax=4 nmol/min/ug enzyme toward uridine {ECO:0000269|PubMed:12849978}; Vmax=1.2 nmol/min/ug enzyme toward deoxyuridine {ECO:0000269|PubMed:12849978}; Vmax=0.18 nmol/min/ug enzyme toward thymidine {ECO:0000269|PubMed:12849978}; Vmax=1.6 nmol/min/ug enzyme toward 5-fluorouridine {ECO:0000269|PubMed:12849978}; Vmax=0.8 nmol/min/ug enzyme toward 5-fluoro-2(')-deoxyuridine {ECO:0000269|PubMed:12849978};
|
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from uridine (phosphorylase route): step 1/1. {ECO:0000269|PubMed:12849978}.
| null | null |
FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate which can then be utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (PubMed:12849978, PubMed:21855639). Shows broad substrate specificity and can also accept deoxyuridine and other analogous compounds (PubMed:12849978). {ECO:0000269|PubMed:12849978, ECO:0000269|PubMed:21855639}.
|
Homo sapiens (Human)
|
O95047
|
OR2A4_HUMAN
|
MGDNITSIREFLLLGFPVGPRIQMLLFGLFSLFYVFTLLGNGTILGLISLDSRLHAPMYFFLSHLAVVDIAYACNTVPRMLVNLLHPAKPISFAGRMMQTFLFSTFAVTECLLLVVMSYDLYVAICHPLRYLAIMTWRVCITLAVTSWTTGVLLSLIHLVLLLPLPFCRPQKIYHFFCEILAVLKLACADTHINENMVLAGAISGLVGPLSTIVVSYMCILCAILQIQSREVQRKAFRTCFSHLCVIGLVYGTAIIMYVGPRYGNPKEQKKYLLLFHSLFNPMLNPLICSLRNSEVKNTLKRVLGVERAL
| null | null |
detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; positive regulation of cytokinesis [GO:0032467]; regulation of actin cytoskeleton organization [GO:0032956]
|
cleavage furrow [GO:0032154]; Flemming body [GO:0090543]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole [GO:0097431]; recycling endosome [GO:0055037]
|
G protein-coupled receptor activity [GO:0004930]; odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984]
|
PF13853;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Odorant receptor. {ECO:0000305}.
|
Homo sapiens (Human)
|
O95049
|
ZO3_HUMAN
|
MEELTIWEQHTATLSKDPRRGFGIAISGGRDRPGGSMVVSDVVPGGPAEGRLQTGDHIVMVNGVSMENATSAFAIQILKTCTKMANITVKRPRRIHLPATKASPSSPGRQDSDEDDGPQRVEEVDQGRGYDGDSSSGSGRSWDERSRRPRPGRRGRAGSHGRRSPGGGSEANGLALVSGFKRLPRQDVQMKPVKSVLVKRRDSEEFGVKLGSQIFIKHITDSGLAARHRGLQEGDLILQINGVSSQNLSLNDTRRLIEKSEGKLSLLVLRDRGQFLVNIPPAVSDSDSSPLEDISDLASELSQAPPSHIPPPPRHAQRSPEASQTDSPVESPRLRRESSVDSRTISEPDEQRSELPRESSYDIYRVPSSQSMEDRGYSPDTRVVRFLKGKSIGLRLAGGNDVGIFVSGVQAGSPADGQGIQEGDQILQVNDVPFQNLTREEAVQFLLGLPPGEEMELVTQRKQDIFWKMVQSRVGDSFYIRTHFELEPSPPSGLGFTRGDVFHVLDTLHPGPGQSHARGGHWLAVRMGRDLREQERGIIPNQSRAEQLASLEAAQRAVGVGPGSSAGSNARAEFWRLRGLRRGAKKTTQRSREDLSALTRQGRYPPYERVVLREASFKRPVVILGPVADIAMQKLTAEMPDQFEIAETVSRTDSPSKIIKLDTVRVIAEKDKHALLDVTPSAIERLNYVQYYPIVVFFIPESRPALKALRQWLAPASRRSTRRLYAQAQKLRKHSSHLFTATIPLNGTSDTWYQELKAIIREQQTRPIWTAEDQLDGSLEDNLDLPHHGLADSSADLSCDSRVNSDYETDGEGGAYTDGEGYTDGEGGPYTDVDDEPPAPALARSSEPVQADESQSPRDRGRISAHQGAQVDSRHPQGQWRQDSMRTYEREALKKKFMRVHDAESSDEDGYDWGPATDL
| null | null |
cell-cell adhesion [GO:0098609]; cell-cell junction organization [GO:0045216]; establishment of endothelial intestinal barrier [GO:0090557]; maintenance of blood-brain barrier [GO:0035633]; positive regulation of blood-brain barrier permeability [GO:1905605]; protein localization to cell-cell junction [GO:0150105]
|
bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
cell adhesion molecule binding [GO:0050839]
|
PF00625;PF00595;PF07653;
|
2.30.42.10;3.40.50.300;2.30.30.40;
|
MAGUK family
|
PTM: Phosphorylated (By similarity). {ECO:0000250|UniProtKB:O62683}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21411630}; Peripheral membrane protein {ECO:0000269|PubMed:21411630}; Cytoplasmic side {ECO:0000269|PubMed:21411630}. Cell junction, tight junction {ECO:0000269|PubMed:21411630, ECO:0000269|PubMed:23608536}. Nucleus {ECO:0000269|PubMed:23608536}. Note=Exhibits predominant nuclear expression in proliferating cells but is exclusively junctionally expressed after confluence is reached (PubMed:23608536). Shows an epithelial-specific tight junction localization in a TJP1/TJP2-dependent fashion (By similarity). {ECO:0000250|UniProtKB:Q9QXY1, ECO:0000269|PubMed:23608536}.
| null | null | null | null | null |
FUNCTION: TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:16129888). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions (PubMed:16129888). Promotes cell-cycle progression through the sequestration of cyclin D1 (CCND1) at tight junctions during mitosis which prevents CCND1 degradation during M-phase and enables S-phase transition (PubMed:21411630). With TJP1 and TJP2, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). Contrary to TJP2, TJP3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment (By similarity). {ECO:0000250|UniProtKB:O62683, ECO:0000250|UniProtKB:Q9QXY1, ECO:0000269|PubMed:16129888, ECO:0000269|PubMed:21411630}.
|
Homo sapiens (Human)
|
O95050
|
INMT_HUMAN
|
MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLIDIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGNSGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAALCNLASLLKPGGHLVTTVTLRLPSYMVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQSYSVTNAANNGVCFIVARKKPGP
|
2.1.1.49; 2.1.1.96
| null |
amine metabolic process [GO:0009308]; methylation [GO:0032259]; response to toxic substance [GO:0009636]
|
cytosol [GO:0005829]
|
amine N-methyltransferase activity [GO:0030748]; N-methyltransferase activity [GO:0008170]; S-adenosyl-L-methionine:beta-alanine N-methyltransferase activity [GO:0102707]; thioether S-methyltransferase activity [GO:0004790]
|
PF01234;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, NNMT/PNMT/TEMT family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a tertiary amine + S-adenosyl-L-methionine = a methylated tertiary amine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53928, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:137982, ChEBI:CHEBI:137983; EC=2.1.1.49; Evidence={ECO:0000269|PubMed:10552930}; CATALYTIC ACTIVITY: Reaction=a secondary amine + S-adenosyl-L-methionine = a methylated secondary amine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53924, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:137419, ChEBI:CHEBI:137984; EC=2.1.1.49; Evidence={ECO:0000269|PubMed:10552930}; CATALYTIC ACTIVITY: Reaction=a primary amine + S-adenosyl-L-methionine = a methylated primary amine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65296, ChEBI:CHEBI:131823; EC=2.1.1.49; Evidence={ECO:0000269|PubMed:10552930}; CATALYTIC ACTIVITY: Reaction=dimethyl sulfide + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + trimethylsulfonium; Xref=Rhea:RHEA:19613, ChEBI:CHEBI:17434, ChEBI:CHEBI:17437, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.96; Evidence={ECO:0000269|PubMed:10552930};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.9 mM for tryptamine {ECO:0000269|PubMed:10552930};
| null | null | null |
FUNCTION: Functions as a thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds (By similarity). Catalyzes the N-methylation of tryptamine and structurally related compounds. {ECO:0000250, ECO:0000269|PubMed:10552930}.
|
Homo sapiens (Human)
|
O95057
|
DIRA1_HUMAN
|
MPEQSNDYRVVVFGAGGVGKSSLVLRFVKGTFRDTYIPTIEDTYRQVISCDKSVCTLQITDTTGSHQFPAMQRLSISKGHAFILVFSVTSKQSLEELGPIYKLIVQIKGSVEDIPVMLVGNKCDETQREVDTREAQAVAQEWKCAFMETSAKMNYNVKELFQELLTLETRRNMSLNIDGKRSGKQKRTDRVKGKCTLM
| null | null |
signal transduction [GO:0007165]
|
plasma membrane [GO:0005886]
|
GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Di-Ras family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Displays low GTPase activity and exists predominantly in the GTP-bound form. {ECO:0000269|PubMed:12194967}.
|
Homo sapiens (Human)
|
O95059
|
RPP14_HUMAN
|
MPAPAATYERVVYKNPSEYHYMKVCLEFQDCGVGLNAAQFKQLLISAVKDLFGEVDAALPLDILTYEEKTLSAILRICSSGLVKLWSSLTLLGSYKGKKCAFRVIQVSPFLLALSGNSRELVLD
| null | null |
tRNA 5'-leader removal [GO:0001682]
|
multimeric ribonuclease P complex [GO:0030681]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]
|
ribonuclease P activity [GO:0004526]; ribonuclease P RNA binding [GO:0033204]
|
PF01900;
|
3.30.70.3250;
|
Eukaryotic/archaeal RNase P protein component 2 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10444065, ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000269|PubMed:10024167, ECO:0000269|PubMed:30454648}.
|
Homo sapiens (Human)
|
O95067
|
CCNB2_HUMAN
|
MALLRRPTVSSDLENIDTGVNSKVKSHVTIRRTVLEEIGNRVTTRAAQVAKKAQNTKVPVQPTKTTNVNKQLKPTASVKPVQMEKLAPKGPSPTPEDVSMKEENLCQAFSDALLCKIEDIDNEDWENPQLCSDYVKDIYQYLRQLEVLQSINPHFLDGRDINGRMRAILVDWLVQVHSKFRLLQETLYMCVGIMDRFLQVQPVSRKKLQLVGITALLLASKYEEMFSPNIEDFVYITDNAYTSSQIREMETLILKELKFELGRPLPLHFLRRASKAGEVDVEQHTLAKYLMELTLIDYDMVHYHPSKVAAAASCLSQKVLGQGKWNLKQQYYTGYTENEVLEVMQHMAKNVVKVNENLTKFIAIKNKYASSKLLKISMIPQLNSKAVKDLASPLIGRS
| null | null |
cell division [GO:0051301]; G2/MI transition of meiotic cell cycle [GO:0008315]; in utero embryonic development [GO:0001701]; mitotic cell cycle phase transition [GO:0044772]; regulation of growth [GO:0040008]; spindle assembly involved in female meiosis I [GO:0007057]; T cell homeostasis [GO:0043029]; thymus development [GO:0048538]
|
centrosome [GO:0005813]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]
|
cadherin binding [GO:0045296]; cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]
|
PF02984;PF00134;
|
1.10.472.10;
|
Cyclin family, Cyclin AB subfamily
| null | null | null | null | null | null | null |
FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition.
|
Homo sapiens (Human)
|
O95069
|
KCNK2_HUMAN
|
MLPSASRERPGYRAGVAAPDLLDPKSAAQNSKPRLSFSTKPTVLASRVESDTTINVMKWKTVSTIFLVVVLYLIIGATVFKALEQPHEISQRTTIVIQKQTFISQHSCVNSTELDELIQQIVAAINAGIIPLGNTSNQISHWDLGSSFFFAGTVITTIGFGNISPRTEGGKIFCIIYALLGIPLFGFLLAGVGDQLGTIFGKGIAKVEDTFIKWNVSQTKIRIISTIIFILFGCVLFVALPAIIFKHIEGWSALDAIYFVVITLTTIGFGDYVAGGSDIEYLDFYKPVVWFWILVGLAYFAAVLSMIGDWLRVISKKTKEEVGEFRAHAAEWTANVTAEFKETRRRLSVEIYDKFQRATSIKRKLSAELAGNHNQELTPCRRTLSVNHLTSERDVLPPLLKTESIYLNGLTPHCAGEEIAVIENIK
| null | null |
cardiac ventricle development [GO:0003231]; cellular response to hypoxia [GO:0071456]; cochlea development [GO:0090102]; G protein-coupled receptor signaling pathway [GO:0007186]; memory [GO:0007613]; negative regulation of cardiac muscle cell proliferation [GO:0060044]; negative regulation of DNA biosynthetic process [GO:2000279]; positive regulation of cellular response to hypoxia [GO:1900039]; potassium ion transmembrane transport [GO:0071805]; response to axon injury [GO:0048678]; response to mechanical stimulus [GO:0009612]; stabilization of membrane potential [GO:0030322]
|
apical plasma membrane [GO:0016324]; astrocyte projection [GO:0097449]; calyx of Held [GO:0044305]; cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]
|
outward rectifier potassium channel activity [GO:0015271]; potassium channel inhibitor activity [GO:0019870]; potassium ion leak channel activity [GO:0022841]
|
PF07885;
|
1.10.287.70;
|
Two pore domain potassium channel (TC 1.A.1.8) family
|
PTM: Phosphorylation at Ser-348 controls the reversible conversion from a leak channel to a voltage-dependent channel. {ECO:0000269|PubMed:11319556}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:23169818}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:10784345}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Ion channel that contributes to passive transmembrane potassium transport (PubMed:23169818). Reversibly converts between a voltage-insensitive potassium leak channel and a voltage-dependent outward rectifying potassium channel in a phosphorylation-dependent manner (PubMed:11319556). In astrocytes, forms mostly heterodimeric potassium channels with KCNK1, with only a minor proportion of functional channels containing homodimeric KCNK2. In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (By similarity). {ECO:0000250|UniProtKB:P97438, ECO:0000269|PubMed:10784345, ECO:0000269|PubMed:11319556, ECO:0000269|PubMed:23169818}.; FUNCTION: [Isoform 4]: Does not display channel activity but reduces the channel activity of isoform 1 and isoform 2 and reduces cell surface expression of isoform 2. {ECO:0000250}.
|
Homo sapiens (Human)
|
O95070
|
YIF1A_HUMAN
|
MAYHSGYGAHGSKHRARAAPDPPPLFDDTSGGYSSQPGGYPATGADVAFSVNHLLGDPMANVAMAYGSSIASHGKDMVHKELHRFVSVSKLKYFFAVDTAYVAKKLGLLVFPYTHQNWEVQYSRDAPLPPRQDLNAPDLYIPTMAFITYVLLAGMALGIQKRFSPEVLGLCASTALVWVVMEVLALLLGLYLATVRSDLSTFHLLAYSGYKYVGMILSVLTGLLFGSDGYYVALAWTSSALMYFIVRSLRTAALGPDSMGGPVPRQRLQLYLTLGAAAFQPLIIYWLTFHLVR
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; protein transport [GO:0015031]
|
COPII-coated ER to Golgi transport vesicle [GO:0030134]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]
| null |
PF03878;
| null |
YIF1 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:15308636, ECO:0000269|PubMed:15990086, ECO:0000269|PubMed:26077767}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:26077767}; Multi-pass membrane protein {ECO:0000255}. Note=Cycles between the endoplasmic reticulum and the endoplasmic reticulum-Golgi intermediate compartment. {ECO:0000269|PubMed:15308636}.
| null | null | null | null | null |
FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000269|PubMed:15990086}.
|
Homo sapiens (Human)
|
O95071
|
UBR5_HUMAN
|
MTSIHFVVHPLPGTEDQLNDRLREVSEKLNKYNLNSHPPLNVLEQATIKQCVVGPNHAAFLLEDGRVCRIGFSVQPDRLELGKPDNNDGSKLNSNSGAGRTSRPGRTSDSPWFLSGSETLGRLAGNTLGSRWSSGVGGSGGGSSGRSSAGARDSRRQTRVIRTGRDRGSGLLGSQPQPVIPASVIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDEDGDDGDDTASESYLPGEDLMSLLDADIHSAHPSVIIDADAMFSEDISYFGYPSFRRSSLSRLGSSRVLLLPLERDSELLRERESVLRLRERRWLDGASFDNERGSTSKEGEPNLDKKNTPVQSPVSLGEDLQWWPDKDGTKFICIGALYSELLAVSSKGELYQWKWSESEPYRNAQNPSLHHPRATFLGLTNEKIVLLSANSIRATVATENNKVATWVDETLSSVASKLEHTAQTYSELQGERIVSLHCCALYTCAQLENSLYWWGVVPFSQRKKMLEKARAKNKKPKSSAGISSMPNITVGTQVCLRNNPLYHAGAVAFSISAGIPKVGVLMESVWNMNDSCRFQLRSPESLKNMEKASKTTEAKPESKQEPVKTEMGPPPSPASTCSDASSIASSASMPYKRRRSTPAPKEEEKVNEEQWSLREVVFVEDVKNVPVGKVLKVDGAYVAVKFPGTSSNTNCQNSSGPDADPSSLLQDCRLLRIDELQVVKTGGTPKVPDCFQRTPKKLCIPEKTEILAVNVDSKGVHAVLKTGNWVRYCIFDLATGKAEQENNFPTSSIAFLGQNERNVAIFTAGQESPIILRDGNGTIYPMAKDCMGGIRDPDWLDLPPISSLGMGVHSLINLPANSTIKKKAAVIIMAVEKQTLMQHILRCDYEACRQYLMNLEQAVVLEQNLQMLQTFISHRCDGNRNILHACVSVCFPTSNKETKEEEEAERSERNTFAERLSAVEAIANAISVVSSNGPGNRAGSSSSRSLRLREMMRRSLRAAGLGRHEAGASSSDHQDPVSPPIAPPSWVPDPPAMDPDGDIDFILAPAVGSLTTAATGTGQGPSTSTIPGPSTEPSVVESKDRKANAHFILKLLCDSVVLQPYLRELLSAKDARGMTPFMSAVSGRAYPAAITILETAQKIAKAEISSSEKEEDVFMGMVCPSGTNPDDSPLYVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAGQKSARLDLLYRLLTATNLVTLPNSRGEHLLLFLVQTVARQTVEHCQYRPPRIREDRNRKTASPEDSDMPDHDLEPPRFAQLALERVLQDWNALKSMIMFGSQENKDPLSASSRIGHLLPEEQVYLNQQSGTIRLDCFTHCLIVKCTADILLLDTLLGTLVKELQNKYTPGRREEAIAVTMRFLRSVARVFVILSVEMASSKKKNNFIPQPIGKCKRVFQALLPYAVEELCNVAESLIVPVRMGIARPTAPFTLASTSIDAMQGSEELFSVEPLPPRPSSDQSSSSSQSQSSYIIRNPQQRRISQSQPVRGRDEEQDDIVSADVEEVEVVEGVAGEEDHHDEQEEHGEENAEAEGQHDEHDEDGSDMELDLLAAAETESDSESNHSNQDNASGRRSVVTAATAGSEAGASSVPAFFSEDDSQSNDSSDSDSSSSQSDDIEQETFMLDEPLERTTNSSHANGAAQAPRSMQWAVRNTQHQRAASTAPSSTSTPAASSAGLIYIDPSNLRRSGTISTSAAAAAAALEASNASSYLTSASSLARAYSIVIRQISDLMGLIPKYNHLVYSQIPAAVKLTYQDAVNLQNYVEEKLIPTWNWMVSIMDSTEAQLRYGSALASAGDPGHPNHPLHASQNSARRERMTAREEASLRTLEGRRRATLLSARQGMMSARGDFLNYALSLMRSHNDEHSDVLPVLDVCSLKHVAYVFQALIYWIKAMNQQTTLDTPQLERKRTRELLELGIDNEDSEHENDDDTNQSATLNDKDDDSLPAETGQNHPFFRRSDSMTFLGCIPPNPFEVPLAEAIPLADQPHLLQPNARKEDLFGRPSQGLYSSSASSGKCLMEVTVDRNCLEVLPTKMSYAANLKNVMNMQNRQKKEGEEQPVLPEETESSKPGPSAHDLAAQLKSSLLAEIGLTESEGPPLTSFRPQCSFMGMVISHDMLLGRWRLSLELFGRVFMEDVGAEPGSILTELGGFEVKESKFRREMEKLRNQQSRDLSLEVDRDRDLLIQQTMRQLNNHFGRRCATTPMAVHRVKVTFKDEPGEGSGVARSFYTAIAQAFLSNEKLPNLECIQNANKGTHTSLMQRLRNRGERDREREREREMRRSSGLRAGSRRDRDRDFRRQLSIDTRPFRPASEGNPSDDPEPLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELIIAHGRENGADSILDLGLVDSSEKVQQENRKRHGSSRSVVDMDLDDTDDGDDNAPLFYQPGKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLILASQSSDADAVFSAMDLAFAIDLCKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAEKLLQFKRWFWSIVEKMSMTERQDLVYFWTSSPSLPASEEGFQPMPSITIRPPDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIKTKNFGFV
|
2.3.2.26
| null |
DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; heterochromatin boundary formation [GO:0033696]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of gene expression [GO:0010628]; positive regulation of protein import into nucleus [GO:0042307]; progesterone receptor signaling pathway [GO:0050847]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]
|
RNA binding [GO:0003723]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-ubiquitin ligase activity [GO:0034450]; zinc ion binding [GO:0008270]
|
PF11547;PF00632;PF00658;
|
1.10.1900.10;1.10.8.10;3.30.2160.10;3.30.2410.10;3.90.1750.10;2.130.10.30;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26;
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). Involved in maturation and/or transcriptional regulation of mRNA by activating CDK9 by polyubiquitination. May play a role in control of cell cycle progression. May have tumor suppressor function. Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response. Plays an essential role in extraembryonic development. Ubiquitinates acetylated PCK1. Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. {ECO:0000250, ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:21726808, ECO:0000269|PubMed:22884692}.
|
Homo sapiens (Human)
|
O95072
|
REC8_HUMAN
|
MFYYPNVLQRHTGCFATIWLAATRGSRLVKREYLRVNVVKTCEEILNYVLVRVQPPQPGLPRPRFSLYLSAQLQIGVIRVYSQQCQYLVEDIQHILERLHRAQLQIRIDMETELPSLLLPNHLAMMETLEDAPDPFFGMMSVDPRLPSPFDIPQIRHLLEAAIPERVEEIPPEVPTEPREPERIPVTVLPPEAITILEAEPIRMLEIEGERELPEVSRRELDLLIAEEEEAILLEIPRLPPPAPAEVEGIGEALGPEELRLTGWEPGALLMEVTPPEELRLPAPPSPERRPPVPPPPRRRRRRRLLFWDKETQISPEKFQEQLQTRAHCWECPMVQPPERTIRGPAELFRTPTLSGWLPPELLGLWTHCAQPPPKALRRELPEEAAAEEERRKIEVPSEIEVPREALEPSVPLMVSLEISLEAAEEEKSRISLIPPEERWAWPEVEAPEAPALPVVPELPEVPMEMPLVLPPELELLSLEAVHRAVALELQANREPDFSSLVSPLSPRRMAARVFYLLLVLSAQQILHVKQEKPYGRLLIQPGPRFH
| null | null |
double-strand break repair [GO:0006302]; fertilization [GO:0009566]; male meiosis I [GO:0007141]; meiotic cell cycle [GO:0051321]; meiotic sister chromatid cohesion [GO:0051177]; oocyte maturation [GO:0001556]; reciprocal meiotic recombination [GO:0007131]; replication-born double-strand break repair via sister chromatid exchange [GO:1990414]; seminiferous tubule development [GO:0072520]; sister chromatid cohesion [GO:0007062]; spermatid development [GO:0007286]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130]
|
cohesin complex [GO:0008278]; kinetochore [GO:0000776]; lateral element [GO:0000800]; male germ cell nucleus [GO:0001673]; meiotic cohesin complex [GO:0030893]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]
|
PF04824;PF04825;
|
1.10.10.580;
|
Rad21 family
|
PTM: Phosphorylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6AYJ4}. Chromosome {ECO:0000250|UniProtKB:Q6AYJ4}. Chromosome, centromere {ECO:0000250|UniProtKB:Q6AYJ4}. Note=In meiotic chromosomes, localized along axial elements in prophase from the leptotene to diplotene stages. At later prophase stages, diakinesis and metaphase I, localized along interstitial axes of chromosomes including both centromere and arm regions. No longer detected in arm regions in anaphase I but persists on centromere regions until metaphase II. Localized to centromeres and spindle poles in endopolyploid tumor cells. {ECO:0000250|UniProtKB:Q6AYJ4}.
| null | null | null | null | null |
FUNCTION: Required during meiosis for separation of sister chromatids and homologous chromosomes. Proteolytic cleavage of REC8 on chromosome arms by separin during anaphase I allows for homologous chromosome separation in meiosis I and cleavage of REC8 on centromeres during anaphase II allows for sister chromatid separation in meiosis II (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O95073
|
FSBP_HUMAN
|
MVGKARSSNFTLSEKLDLLKLVKPYVKILEEHTNKHSVIVEKNRCWDIIAVNYNAIGVDRPPRTAQGLRTLYKRLKEYAKQELLQQKETQSDFKSNISEPTKKVMEMIPQISSFCLVRDRNHIQSANLDEEAQAGTSSLQVMLDHHPVAITVEVKQEEDIKPPPPLVLNSQQSDTLEQREEHELVHVMERSLSPSLSSVDMRMTSSPSSIPRRDDFFRHESGEHFRSLLGYDPQILQMLKEEHQIILENQKNFGLYVQEKRDGLKRRQQLEEELLRAKIEVEKLKAIRLRHDLPEYNSL
| null | null | null |
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]
|
PF13873;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20531236}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor that down-regulates the expression of the fibrinogen gamma chain. Represses transcription of GSK3B gene promoter via its interaction with APBA1. {ECO:0000269|PubMed:20531236}.
|
Homo sapiens (Human)
|
O95096
|
NKX22_HUMAN
|
MSLTNTKTGFSVKDILDLPDTNDEEGSVAEGPEEENEGPEPAKRAGPLGQGALDAVQSLPLKNPFYDSSDNPYTRWLASTEGLQYSLHGLAAGAPPQDSSSKSPEPSADESPDNDKETPGGGGDAGKKRKRRVLFSKAQTYELERRFRQQRYLSAPEREHLASLIRLTPTQVKIWFQNHRYKMKRARAEKGMEVTPLPSPRRVAVPVLVRDGKPCHALKAQDLAAATFQAGIPFSAYSAQSLQHMQYNAQYSSASTPQYPTAHPLVQAQQWTW
| null | null |
astrocyte differentiation [GO:0048708]; brain development [GO:0007420]; cell differentiation [GO:0030154]; digestive tract development [GO:0048565]; negative regulation of neuron differentiation [GO:0045665]; neuroendocrine cell differentiation [GO:0061101]; neuron fate specification [GO:0048665]; oligodendrocyte development [GO:0014003]; optic nerve development [GO:0021554]; pancreatic A cell fate commitment [GO:0003326]; pancreatic PP cell fate commitment [GO:0003329]; positive regulation of epithelial cell differentiation [GO:0030858]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of oligodendrocyte differentiation [GO:0048714]; regulation of transcription by RNA polymerase II [GO:0006357]; response to glucose [GO:0009749]; response to progesterone [GO:0032570]; smoothened signaling pathway [GO:0007224]; spinal cord motor neuron differentiation [GO:0021522]; spinal cord oligodendrocyte cell fate specification [GO:0021530]; type B pancreatic cell development [GO:0003323]; type B pancreatic cell fate commitment [GO:0003327]; ventral spinal cord interneuron fate determination [GO:0060580]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00046;
|
1.10.10.60;
|
NK-2 homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator involved in the development of insulin-producting beta cells in the endocrine pancreas (By similarity). May also be involved in specifying diencephalic neuromeric boundaries, and in controlling the expression of genes that play a role in axonal guidance. Binds to elements within the NEUROD1 promoter (By similarity). {ECO:0000250|UniProtKB:P42586}.
|
Homo sapiens (Human)
|
O95104
|
SCAF4_HUMAN
|
MDAVNAFNQELFSLMDMKPPISRAKMILITKAAIKAIKLYKHVVQIVEKFIKKCKPEYKVPGLYVIDSIVRQSRHQFGTDKDVFGPRFSKNITATFQYLYLCPSEDKSKIVRVLNLWQKNGVFKIEIIQPLLDMAAGTSNAAPVAENVTNNEGSPPPPVKVSSEPPTQATPNSVPAVPQLPSSDAFAAVAQLFQTTQGQQLQQILQTFQQPPKPQSPALDNAVMAQVQAITAQLKTTPTQPSEQKAAFPPPEQKTAFDKKLLDRFDYDDEPEAVEESKKEDTTAVTTTAPAAAVPPAPTATVPAAAAPAAASPPPPQAPFGFPGDGMQQPAYTQHQNMDQFQPRMMGIQQDPMHHQVPLPPNGQMPGFGLLPTPPFPPMAQPVIPPTPPVQQPFQASFQAQNEPLTQKPHQQEMEVEQPCIQEVKRHMSDNRKSRSRSASRSPKRRRSRSGSRSRRSRHRRSRSRSRDRRRHSPRSRSQERRDREKERERRQKGLPQVKPETASVCSTTLWVGQLDKRTTQQDVASLLEEFGPIESINMIPPRGCAYIVMVHRQDAYRALQKLSRGNYKVNQKSIKIAWALNKGIKADYKQYWDVELGVTYIPWDKVKPEELESFCEGGMLDSDTLNPDWKGIPKKPENEVAQNGGAETSHTEPVSPIPKPLPVPVPPIPVPAPITVPPPQVPPHQPGPPVVGALQPPAFTPPLGIPPPGFGPGVPPPPPPPPFLRPGFNPMHLPPGFLPPGPPPPITPPVSIPPPHTPPISIPNSTIAGINEDTTKDLSIGNPIPTVVSGARGNAESGDSVKMYGSAVPPAAPTNLPTPPVTQPVSLLGTQGVAPGPVIGLQAPSTGLLGARPGLIPLQRPPGMPPPHLQRFPLMPPRPMPPHMMHRGPPPGPGGFAMPPPHGMKGPFPPHGPFVRPGGMPGLGGPGPGPGGPEDRDGRQQPPQQPQQQPQPQAPQQPQQQQQQQPPPSQQPPPTQQQPQQFRNDNRQQFNSGRDQERFGRRSFGNRVENDRERYGNRNDDRDNSNRDRREWGRRSPDRDRHRDLEERNRRSSGHRDRERDSRDRESRREKEEARGKEKPEVTDRAGGNKTVEPPISQVGNVDTASELEKGVSEAAVLKPSEELPAEATSSVEPEKDSGSAAEAPR
| null | null |
negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled [GO:2000805]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
RNA binding [GO:0003723]; RNA polymerase II C-terminal domain phosphoserine binding [GO:1990269]
|
PF04818;PF00076;
|
1.25.40.90;3.30.70.330;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31104839}.
| null | null | null | null | null |
FUNCTION: Anti-terminator protein required to prevent early mRNA termination during transcription (PubMed:31104839). Together with SCAF8, acts by suppressing the use of early, alternative poly(A) sites, thereby preventing the accumulation of non-functional truncated proteins (PubMed:31104839). Mechanistically, associates with the phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit (POLR2A), and subsequently binds nascent RNA upstream of early polyadenylation sites to prevent premature mRNA transcript cleavage and polyadenylation (PubMed:31104839). Independently of SCAF8, also acts as a suppressor of transcriptional readthrough (PubMed:31104839). {ECO:0000269|PubMed:31104839}.
|
Homo sapiens (Human)
|
O95125
|
ZN202_HUMAN
|
MATAVEPEDQDLWEEEGILMVKLEDDFTCRPESVLQRDDPVLETSHQNFRRFRYQEAASPREALIRLRELCHQWLRPERRTKEQILELLVLEQFLTVLPGELQSWVRGQRPESGEEAVTLVEGLQKQPRRPRRWVTVHVHGQEVLSEETVHLGVEPESPNELQDPVQSSTPEQSPEETTQSPDLGAPAEQRPHQEEELQTLQESEVPVPEDPDLPAERSSGDSEMVALLTALSQGLVTFKDVAVCFSQDQWSDLDPTQKEFYGEYVLEEDCGIVVSLSFPIPRPDEISQVREEEPWVPDIQEPQETQEPEILSFTYTGDRSKDEEECLEQEDLSLEDIHRPVLGEPEIHQTPDWEIVFEDNPGRLNERRFGTNISQVNSFVNLRETTPVHPLLGRHHDCSVCGKSFTCNSHLVRHLRTHTGEKPYKCMECGKSYTRSSHLARHQKVHKMNAPYKYPLNRKNLEETSPVTQAERTPSVEKPYRCDDCGKHFRWTSDLVRHQRTHTGEKPFFCTICGKSFSQKSVLTTHQRIHLGGKPYLCGECGEDFSEHRRYLAHRKTHAAEELYLCSECGRCFTHSAAFAKHLRGHASVRPCRCNECGKSFSRRDHLVRHQRTHTGEKPFTCPTCGKSFSRGYHLIRHQRTHSEKTS
| null | null |
lipid metabolic process [GO:0006629]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromosome [GO:0005694]; nuclear body [GO:0016604]; nucleolus [GO:0005730]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF01352;PF02023;PF00096;
|
6.10.140.140;3.30.160.60;1.10.4020.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor that binds to elements found predominantly in genes that participate in lipid metabolism. Among its targets are structural components of lipoprotein particles (apolipoproteins AIV, CIII, and E), enzymes involved in lipid processing (lipoprotein lipase, lecithin cholesteryl ester transferase), transporters involved in lipid homeostasis (ABCA1, ABCG1), and several genes involved in processes related to energy metabolism and vascular disease.
|
Homo sapiens (Human)
|
O95136
|
S1PR2_HUMAN
|
MGSLYSEYLNPNKVQEHYNYTKETLETQETTSRQVASAFIVILCCAIVVENLLVLIAVARNSKFHSAMYLFLGNLAASDLLAGVAFVANTLLSGSVTLRLTPVQWFAREGSAFITLSASVFSLLAIAIERHVAIAKVKLYGSDKSCRMLLLIGASWLISLVLGGLPILGWNCLGHLEACSTVLPLYAKHYVLCVVTIFSIILLAIVALYVRIYCVVRSSHADMAAPQTLALLKTVTIVLGVFIVCWLPAFSILLLDYACPVHSCPILYKAHYFFAVSTLNSLLNPVIYTWRSRDLRREVLRPLQCWRPGVGVQGRRRGGTPGHHLLPLRSSSSLERGMHMPTSPTFLEGNTVV
| null | null |
actin cytoskeleton organization [GO:0030036]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; excitatory postsynaptic potential [GO:0060079]; filopodium assembly [GO:0046847]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of excitatory postsynaptic potential [GO:0090394]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of establishment of endothelial barrier [GO:1903142]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; regulation of metabolic process [GO:0019222]; sphingosine-1-phosphate receptor signaling pathway [GO:0003376]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]
|
G protein-coupled peptide receptor activity [GO:0008528]; G protein-coupled receptor activity [GO:0004930]; G protein-coupled receptor binding [GO:0001664]; integrin binding [GO:0005178]; lipid binding [GO:0008289]; sphingosine-1-phosphate receptor activity [GO:0038036]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P) (PubMed:10617617). S1P is a bioactive lysophospholipid that elicits diverse physiological effects on most types of cells and tissues (PubMed:10617617). When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis (PubMed:10617617). Receptor for the chemokine-like protein FAM19A5 (PubMed:29453251). Mediates the inhibitory effect of FAM19A5 on vascular smooth muscle cell proliferation and migration (By similarity). {ECO:0000250|UniProtKB:P47752, ECO:0000269|PubMed:10617617, ECO:0000269|PubMed:29453251}.
|
Homo sapiens (Human)
|
O95139
|
NDUB6_HUMAN
|
MTGYTPDEKLRLQQLRELRRRWLKDQELSPREPVLPPQKMGPMEKFWNKFLENKSPWRKMVHGVYKKSIFVFTHVLVPVWIIHYYMKYHVSEKPYGIVEKKSRIFPGDTILETGEVIPPMKEFPDQHH
| null | null |
aerobic respiration [GO:0009060]; mitochondrial ATP synthesis coupled electron transport [GO:0042775]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF09782;
| null |
Complex I NDUFB6 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
|
Homo sapiens (Human)
|
O95140
|
MFN2_HUMAN
|
MSLLFSRCNSIVTVKKNKRHMAEVNASPLKHFVTAKKKINGIFEQLGAYIQESATFLEDTYRNAELDPVTTEEQVLDVKGYLSKVRGISEVLARRHMKVAFFGRTSNGKSTVINAMLWDKVLPSGIGHTTNCFLRVEGTDGHEAFLLTEGSEEKRSAKTVNQLAHALHQDKQLHAGSLVSVMWPNSKCPLLKDDLVLMDSPGIDVTTELDSWIDKFCLDADVFVLVANSESTLMQTEKHFFHKVSERLSRPNIFILNNRWDASASEPEYMEEVRRQHMERCTSFLVDELGVVDRSQAGDRIFFVSAKEVLNARIQKAQGMPEGGGALAEGFQVRMFEFQNFERRFEECISQSAVKTKFEQHTVRAKQIAEAVRLIMDSLHMAAREQQVYCEEMREERQDRLKFIDKQLELLAQDYKLRIKQITEEVERQVSTAMAEEIRRLSVLVDDYQMDFHPSPVVLKVYKNELHRHIEEGLGRNMSDRCSTAITNSLQTMQQDMIDGLKPLLPVSVRSQIDMLVPRQCFSLNYDLNCDKLCADFQEDIEFHFSLGWTMLVNRFLGPKNSRRALMGYNDQVQRPIPLTPANPSMPPLPQGSLTQEEFMVSMVTGLASLTSRTSMGILVVGGVVWKAVGWRLIALSFGLYGLLYVYERLTWTTKAKERAFKRQFVEHASEKLQLVISYTGSNCSHQVQQELSGTFAHLCQQVDVTRENLEQEIAAMNKKIEVLDSLQSKAKLLRNKAGWLDSELNMFTHQYLQPSR
|
3.6.5.-
| null |
aerobic respiration [GO:0009060]; apoptotic process [GO:0006915]; blastocyst formation [GO:0001825]; camera-type eye morphogenesis [GO:0048593]; mitochondrial fusion [GO:0008053]; mitochondrial membrane organization [GO:0007006]; mitochondrion localization [GO:0051646]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of smooth muscle cell proliferation [GO:0048662]; parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization [GO:0061734]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of vascular associated smooth muscle cell apoptotic process [GO:1905461]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; protein localization to phagophore assembly site [GO:0034497]; protein targeting to mitochondrion [GO:0006626]; response to unfolded protein [GO:0006986]
|
cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; ubiquitin protein ligase binding [GO:0031625]
|
PF00350;PF04799;
|
1.20.5.110;3.40.50.300;
|
TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family, Mitofusin subfamily
|
PTM: Phosphorylated by PINK1. {ECO:0000269|PubMed:23620051}.; PTM: Ubiquitinated by non-degradative ubiquitin by PRKN, promoting mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial fusion (PubMed:23620051). Ubiquitinated by HUWE1 when dietary stearate (C18:0) levels are low; ubiquitination inhibits mitochondrial fusion (PubMed:26214738, PubMed:30217973). {ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:30217973}.
|
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12499352, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:26214738}; Multi-pass membrane protein {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12499352, ECO:0000269|PubMed:23620051}. Note=Colocalizes with BAX during apoptosis. {ECO:0000269|PubMed:12499352}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:28114303}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:28114303};
| null | null | null | null |
FUNCTION: Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:11181170, PubMed:11950885, PubMed:19889647, PubMed:26214738, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:28114303). Overexpression induces the formation of mitochondrial networks (PubMed:28114303). Membrane clustering requires GTPase activity and may involve a major rearrangement of the coiled coil domains (Probable). Plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes (By similarity). Plays an important role in the regulation of vascular smooth muscle cell proliferation (By similarity). Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) (PubMed:23620051). Is required for PRKN recruitment to dysfunctional mitochondria (PubMed:23620051). Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress (By similarity). Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions (By similarity). {ECO:0000250|UniProtKB:Q80U63, ECO:0000250|UniProtKB:Q8R500, ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:19889647, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:26085578, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:28114303, ECO:0000305}.
|
Homo sapiens (Human)
|
O95147
|
DUS14_HUMAN
|
MSSRGHSTLPRTLMAPRMISEGDIGGIAQITSSLFLGRGSVASNRHLLQARGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPIGLYFDTVADKIHSVSRKHGATLVHCAAGVSRSATLCIAYLMKFHNVCLLEAYNWVKARRPVIRPNVGFWRQLIDYERQLFGKSTVKMVQTPYGIVPDVYEKESRHLMPYWGI
|
3.1.3.16; 3.1.3.48
| null |
dephosphorylation [GO:0016311]
|
cytoplasm [GO:0005737]
|
MAP kinase tyrosine/serine/threonine phosphatase activity [GO:0017017]; myosin phosphatase activity [GO:0017018]; protein tyrosine phosphatase activity [GO:0004725]; RNA binding [GO:0003723]
|
PF00782;
|
3.90.190.10;
|
Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:24403530}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases. Plays a negative role in TCR signaling by dephosphorylating MAP3K7 adapter TAB1 leading to its inactivation (PubMed:24403530). {ECO:0000269|PubMed:24403530}.
|
Homo sapiens (Human)
|
O95149
|
SPN1_HUMAN
|
MEELSQALASSFSVSQDLNSTAAPHPRLSQYKSKYSSLEQSERRRRLLELQKSKRLDYVNHARRLAEDDWTGMESEEENKKDDEEMDIDTVKKLPKHYANQLMLSEWLIDVPSDLGQEWIVVVCPVGKRALIVASRGSTSAYTKSGYCVNRFSSLLPGGNRRNSTAKDYTILDCIYNEVNQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKLNPFKFVGLKNFPCTPESLCDVLSMDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPYMVSDVLGVAVPAGPLTTKPDYAGHQLQQIMEHKKSQKEGMKEKLTHKASENGHYELEHLSTPKLKGSSHSPDHPGCLMEN
| null | null |
protein import into nucleus [GO:0006606]; RNA import into nucleus [GO:0006404]; snRNA import into nucleus [GO:0061015]
|
cytosol [GO:0005829]; NLS-dependent protein nuclear import complex [GO:0042564]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
nuclear import signal receptor activity [GO:0061608]; RNA cap binding [GO:0000339]
|
PF11538;
|
3.30.470.30;
|
Snurportin family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:15920472}. Cytoplasm {ECO:0000269|PubMed:12095920, ECO:0000269|PubMed:9670026, ECO:0000305|PubMed:10209022}. Note=Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor importin beta (PubMed:10209022, PubMed:12095920). It is re-exported to the cytoplasm by the XPO1-dependent nuclear export receptor pathway (PubMed:10209022). {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:12095920}.
| null | null | null | null | null |
FUNCTION: Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs. {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:15920472, ECO:0000269|PubMed:16030253, ECO:0000269|PubMed:9670026}.
|
Homo sapiens (Human)
|
O95150
|
TNF15_HUMAN
|
MAEDLGLSFGETASVEMLPEHGSCRPKARSSSARWALTCCLVLLPFLAGLTTYLLVSQLRAQGEACVQFQALKGQEFAPSHQQVYAPLRADGDKPRAHLTVVRQTPTQHFKNQFPALHWEHELGLAFTKNRMNYTNKFLLIPESGDYFIYSQVTFRGMTSECSEIRQAGRPNKPDSITVVITKVTDSYPEPTQLLMGTKSVCEVGSNWFQPIYLGAMFSLQEGDKLMVNVSDISLVDYTKEDKTFFGAFLL
| null | null |
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of NF-kappaB-inducing kinase activity [GO:0007250]; immune response [GO:0006955]; signal transduction [GO:0007165]
|
extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; signaling receptor binding [GO:0005102]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:11911831, ECO:0000305|PubMed:11923219}; Single-pass type II membrane protein {ECO:0000305|PubMed:11911831, ECO:0000305|PubMed:11923219}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 15, secreted form]: Secreted.
| null | null | null | null | null |
FUNCTION: Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis. {ECO:0000269|PubMed:10597252, ECO:0000269|PubMed:11911831, ECO:0000269|PubMed:11923219, ECO:0000269|PubMed:9872942}.
|
Homo sapiens (Human)
|
O95153
|
RIMB1_HUMAN
|
MEQLTTLPRPGDPGAMEPWALPTWHSWTPGRGGEPSSAAPSIADTPPAALQLQELRSEESSKPKGDGSSRPVGGTDPEGAEACLPSLGQQASSSGPACQRPEDEEVEAFLKAKLNMSFGDRPNLELLRALGELRQRCAILKEENQMLRKSSFPETEEKVRRLKRKNAELAVIAKRLEERARKLQETNLRVVSAPLPRPGTSLELCRKALARQRARDLSETASALLAKDKQIAALQRECRELQARLTLVGKEGPQWLHVRDFDRLLRESQREVLRLQRQIALRNQRETLPLPPSWPPGPALQARAGAPAPGAPGEATPQEDADNLPVILGEPEKEQRVQQLESELSKKRKKCESLEQEARKKQRRCEELELQLRQAQNENARLVEENSRLSGRATEKEQVEWENAELRGQLLGVTQERDSALRKSQGLQSKLESLEQVLKHMREVAQRRQQLEVEHEQARLSLREKQEEVRRLQQAQAEAQREHEGAVQLLESTLDSMQARVRELEEQCRSQTEQFSLLAQELQAFRLHPGPLDLLTSALDCGSLGDCPPPPCCCSIPQPCRGSGPKDLDLPPGSPGRCTPKSSEPAPATLTGVPRRTAKKAESLSNSSHSESIHNSPKSCPTPEVDTASEVEELEADSVSLLPAAPEGSRGGARIQVFLARYSYNPFEGPNENPEAELPLTAGEYIYIYGNMDEDGFFEGELMDGRRGLVPSNFVERVSDDDLLTSLPPELADLSHSSGPELSFLSVGGGGSSSGGQSSVGRSQPRPEEEDAGDELSLSPSPEGLGEPPAVPYPRRLVVLKQLAHSVVLAWEPPPEQVELHGFHICVNGELRQALGPGAPPKAVLENLDLWAGPLHISVQALTSRGSSDPLRCCLAVGARAGVVPSQLRVHRLTATSAEITWVPGNSNLAHAIYLNGEECPPASPSTYWATFCHLRPGTPYQAQVEAQLPPQGPWEPGWERLEQRAATLQFTTLPAGPPDAPLDVQIEPGPSPGILIISWLPVTIDAAGTSNGVRVTGYAIYADGQKIMEVASPTAGSVLVELSQLQLLQVCREVVVRTMSPHGESADSIPAPITPALAPASLPARVSCPSPHPSPEARAPLASASPGPGDPSSPLQHPAPLGTQEPPGAPPASPSREMAKGSHEDPPAPCSQEEAGAAVLGTSEERTASTSTLGEKDPGPAAPSLAKQEAEWTAGEACPASSSTQGARAQQAPNTEMCQGGDPGSGLRPRAEKEDTAELGVHLVNSLVDHGRNSDLSDIQEEEEEEEEEEEEELGSRTCSFQKQVAGNSIRENGAKSQPDPFCETDSDEEILEQILELPLQQFCSKKLFSIPEEEEEEEEDEEEEKSGAGCSSRDPGPPEPALLGLGCDSGQPRRPGQCPLSPESSRAGDCLEDMPGLVGGSSRRRGGGSPEKPPSRRRPPDPREHCSRLLSNNGPQASGRLGPTRERGGLPVIEGPRTGLEASGRGRLGPSRRCSRGRALEPGLASCLSPKCLEISIEYDSEDEQEAGSGGISITSSCYPGDGEAWGTATVGRPRGPPKANSGPKPYPRLPAWEKGEPERRGRSATGRAKEPLSRATETGEARGQDGSGRRGPQKRGVRVLRPSTAELVPARSPSETLAYQHLPVRIFVALFDYDPVSMSPNPDAGEEELPFREGQILKVFGDKDADGFYQGEGGGRTGYIPCNMVAEVAVDSPAGRQQLLQRGYLSPDILLEGSGNGPFVYSTAHTTGPPPKPRRSKKAESEGPAQPCPGPPKLVPSADLKAPHSMVAAFDYNPQESSPNMDVEAELPFRAGDVITVFGGMDDDGFYYGELNGQRGLVPSNFLEGPGPEAGGLDREPRTPQAESQRTRRRRVQC
| null | null |
regulation of neurotransmitter secretion [GO:0046928]
|
calyx of Held [GO:0044305]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]
|
benzodiazepine receptor binding [GO:0030156]; voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels [GO:0099626]
|
PF07653;PF14604;
|
2.60.40.10;2.30.30.40;
|
RIMBP family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9915832}. Mitochondrion {ECO:0000269|PubMed:9915832}. Note=Preferentially expressed in the mitochondria in the presence of TSPO.
| null | null | null | null | null |
FUNCTION: Required for synaptic transmission regulation (PubMed:33539324). It probably controls the recruitement of voltage-gated calcium channels to the presynaptic membrane, and modulates neurotransmitter release. {ECO:0000269|PubMed:33539324}.
|
Homo sapiens (Human)
|
O95154
|
ARK73_HUMAN
|
MSRQLSRARPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKAIPLFGNSLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRFFGNTWAEMYRNRYWKEHHFEGIALVEKALQAAYGASAPSMTSATLRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAAAEEGPLEPAVVDAFNQAWHLVTHECPNYFR
|
1.-.-.-
| null |
cellular aldehyde metabolic process [GO:0006081]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]
|
aldo-keto reductase (NADP) activity [GO:0004033]; electron transfer activity [GO:0009055]; identical protein binding [GO:0042802]
|
PF00248;
|
3.20.20.100;
|
Aldo/keto reductase family, Aldo/keto reductase 2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen. {ECO:0000269|PubMed:18416522}.
|
Homo sapiens (Human)
|
O95155
|
UBE4B_HUMAN
|
MEELSADEIRRRRLARLAGGQTSQPTTPLTSPQRENPPGPPIAASAPGPSQSLGLNVHNMTPATSPIGASGVAHRSQSSEGVSSLSSSPSNSLETQSQSLSRSQSMDIDGVSCEKSMSQVDVDSGIENMEVDENDRREKRSLSDKEPSSGPEVSEEQALQLVCKIFRVSWKDRDRDVIFLSSLSAQFKQNPKEVFSDFKDLIGQILMEVLMMSTQTRDENPFASLTATSQPIAAAARSPDRNLLLNTGSNPGTSPMFCSVASFGASSLSSLYESSPAPTPSFWSSVPVMGPSLASPSRAASQLAVPSTPLSPHSAASGTAAGSQPSSPRYRPYTVTHPWASSGVSILSSSPSPPALASSPQAVPASSSRQRPSSTGPPLPPASPSATSRRPSSLRISPSLGASGGASNWDSYSDHFTIETCKETDMLNYLIECFDRVGIEEKKAPKMCSQPAVSQLLSNIRSQCISHTALVLQGSLTQPRSLQQPSFLVPYMLCRNLPYGFIQELVRTTHQDEEVFKQIFIPILQGLALAAKECSLDSDYFKYPLMALGELCETKFGKTHPVCNLVASLRLWLPKSLSPGCGRELQRLSYLGAFFSFSVFAEDDVKVVEKYFSGPAITLENTRVVSQSLQHYLELGRQELFKILHSILLNGETREAALSYMAAVVNANMKKAQMQTDDRLVSTDGFMLNFLWVLQQLSTKIKLETVDPTYIFHPRCRITLPNDETRVNATMEDVNDWLTELYGDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTVEDLKNNESQWKDSPLATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLLLRILDPAYPDITLPLNSDVPKVFAALPEFYVEDVAEFLFFIVQYSPQALYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPAVQPRTQKFFEMIENHPLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQFVRYINMLINDTTFLLDESLESLKRIHEVQEEMKNKEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHILTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQLDCARFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAWMREKQNSDH
|
2.3.2.27
| null |
ERAD pathway [GO:0036503]; granzyme-mediated apoptotic signaling pathway [GO:0008626]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; response to UV [GO:0009411]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
|
enzyme binding [GO:0019899]; ubiquitin-ubiquitin ligase activity [GO:0034450]
|
PF04564;PF10408;
|
3.30.40.10;
|
Ubiquitin conjugation factor E4 family
|
PTM: Proteolytically cleaved by caspases during apoptosis. Cleaved efficiently at Asp-123 by caspase-6 and granzyme B. Cleaved with approximately 10-fold less efficiency at Asp-109 by caspase-3 and caspase-7. {ECO:0000269|PubMed:11802788}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17369820}. Nucleus {ECO:0000250|UniProtKB:Q9ES00}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9ES00};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9ES00}.
| null | null |
FUNCTION: Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases (By similarity). May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00, ECO:0000269|PubMed:17369820}.
|
Homo sapiens (Human)
|
O95159
|
ZFPL1_HUMAN
|
MGLCKCPKRKVTNLFCFEHRVNVCEHCLVANHAKCIVQSYLQWLQDSDYNPNCRLCNIPLASRETTRLVCYDLFHWACLNERAAQLPRNTAPAGYQCPSCNGPIFPPTNLAGPVASALREKLATVNWARAGLGLPLIDEVVSPEPEPLNTSDFSDWSSFNASSTPGPEEVDSASAAPAFYSQAPRPPASPGRPEQHTVIHMGNPEPLTHAPRKVYDTRDDDRTPGLHGDCDDDKYRRRPALGWLARLLRSRAGSRKRPLTLLQRAGLLLLLGLLGFLALLALMSRLGRAAADSDPNLDPLMNPHIRVGPS
| null | null |
regulation of DNA-templated transcription [GO:0006355]; vesicle-mediated transport [GO:0016192]
|
Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; zinc ion binding [GO:0008270]
| null |
3.30.40.10;
|
ZFPL1 family
|
PTM: Phosphorylated. {ECO:0000269|PubMed:18323775}.
|
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:18323775}; Single-pass membrane protein {ECO:0000269|PubMed:18323775}.
| null | null | null | null | null |
FUNCTION: Required for cis-Golgi integrity and efficient ER to Golgi transport. Involved in the maintenance of the integrity of the cis-Golgi, possibly via its interaction with GOLGA2/GM130. {ECO:0000269|PubMed:18323775}.
|
Homo sapiens (Human)
|
O95163
|
ELP1_HUMAN
|
MRNLKLFRTLEFRDIQGPGNPQCFSLRTEQGTVLIGSEHGLIEVDPVSREVKNEVSLVAEGFLPEDGSGRIVGVQDLLDQESVCVATASGDVILCSLSTQQLECVGSVASGISVMSWSPDQELVLLATGQQTLIMMTKDFEPILEQQIHQDDFGESKFITVGWGRKETQFHGSEGRQAAFQMQMHESALPWDDHRPQVTWRGDGQFFAVSVVCPETGARKVRVWNREFALQSTSEPVAGLGPALAWKPSGSLIASTQDKPNQQDIVFFEKNGLLHGHFTLPFLKDEVKVNDLLWNADSSVLAVWLEDLQREESSIPKTCVQLWTVGNYHWYLKQSLSFSTCGKSKIVSLMWDPVTPYRLHVLCQGWHYLAYDWHWTTDRSVGDNSSDLSNVAVIDGNRVLVTVFRQTVVPPPMCTYQLLFPHPVNQVTFLAHPQKSNDLAVLDASNQISVYKCGDCPSADPTVKLGAVGGSGFKVCLRTPHLEKRYKIQFENNEDQDVNPLKLGLLTWIEEDVFLAVSHSEFSPRSVIHHLTAASSEMDEEHGQLNVSSSAAVDGVIISLCCNSKTKSVVLQLADGQIFKYLWESPSLAIKPWKNSGGFPVRFPYPCTQTELAMIGEEECVLGLTDRCRFFINDIEVASNITSFAVYDEFLLLTTHSHTCQCFCLRDASFKTLQAGLSSNHVSHGEVLRKVERGSRIVTVVPQDTKLVLQMPRGNLEVVHHRALVLAQIRKWLDKLMFKEAFECMRKLRINLNLIYDHNPKVFLGNVETFIKQIDSVNHINLFFTELKEEDVTKTMYPAPVTSSVYLSRDPDGNKIDLVCDAMRAVMESINPHKYCLSILTSHVKKTTPELEIVLQKVHELQGNAPSDPDAVSAEEALKYLLHLVDVNELYDHSLGTYDFDLVLMVAEKSQKDPKEYLPFLNTLKKMETNYQRFTIDKYLKRYEKAIGHLSKCGPEYFPECLNLIKDKNLYNEALKLYSPSSQQYQDISIAYGEHLMQEHMYEPAGLMFARCGAHEKALSAFLTCGNWKQALCVAAQLNFTKDQLVGLGRTLAGKLVEQRKHIDAAMVLEECAQDYEEAVLLLLEGAAWEEALRLVYKYNRLDIIETNVKPSILEAQKNYMAFLDSQTATFSRHKKRLLVVRELKEQAQQAGLDDEVPHGQESDLFSETSSVVSGSEMSGKYSHSNSRISARSSKNRRKAERKKHSLKEGSPLEDLALLEALSEVVQNTENLKDEVYHILKVLFLFEFDEQGRELQKAFEDTLQLMERSLPEIWTLTYQQNSATPVLGPNSTANSIMASYQQQKTSVPVLDAELFIPPKINRRTQWKLSLLD
| null | null |
regulation of translation [GO:0006417]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble uridine modification [GO:0002098]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; elongator holoenzyme complex [GO:0033588]; nucleus [GO:0005634]
|
protein self-association [GO:0043621]; tRNA binding [GO:0000049]
|
PF04762;
|
2.130.10.10;
|
ELP1/IKA1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576, ECO:0000269|PubMed:22854966}. Nucleus {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576}.
| null | null |
PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000303|PubMed:29332244}.
| null | null |
FUNCTION: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:29332244). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (By similarity). ELP1 binds to tRNA, mediating interaction of the elongator complex with tRNA (By similarity). May act as a scaffold protein that assembles active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK) (PubMed:9751059). {ECO:0000250|UniProtKB:Q06706, ECO:0000250|UniProtKB:Q7TT37, ECO:0000269|PubMed:9751059, ECO:0000303|PubMed:29332244}.
|
Homo sapiens (Human)
|
O95166
|
GBRAP_HUMAN
|
MKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYGL
| null | null |
autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; cellular response to nitrogen starvation [GO:0006995]; chemical synaptic transmission [GO:0007268]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; microtubule cytoskeleton organization [GO:0000226]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein K48-linked ubiquitination [GO:1902524]; protein targeting [GO:0006605]; protein transport [GO:0015031]; regulation of Rac protein signal transduction [GO:0035020]
|
actin cytoskeleton [GO:0015629]; autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; axoneme [GO:0005930]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum [GO:0005790]; sperm midpiece [GO:0097225]; synapse [GO:0045202]
|
beta-tubulin binding [GO:0048487]; GABA receptor binding [GO:0050811]; microtubule binding [GO:0008017]; phosphatidylethanolamine binding [GO:0008429]; ubiquitin protein ligase binding [GO:0031625]
|
PF02991;
| null |
ATG8 family
|
PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) to expose the glycine at the C-terminus and form the cytosolic form, GABARAP-I (PubMed:15169837, PubMed:20818167, PubMed:30661429). The processed form is then activated by APG7L/ATG7, transferred to ATG3 and conjugated to phosphatidylethanolamine (PE) phospholipid to form the membrane-bound form, GABARAP-II (PubMed:15169837). During non-canonical autophagy, the processed form is conjugated to phosphatidylserine (PS) phospholipid (PubMed:33909989). ATG4 proteins also mediate the delipidation of PE-conjugated forms (PubMed:33909989). In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (PubMed:33909989). ATG4B constitutes the major protein for proteolytic activation (PubMed:30661429). ATG4D is the main enzyme for delipidation activity (By similarity). {ECO:0000250|UniProtKB:Q9DCD6, ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:20818167, ECO:0000269|PubMed:30661429, ECO:0000269|PubMed:33909989}.; PTM: (Microbial infection) The Legionella effector RavZ is a deconjugating enzyme that hydrolyzes the amide bond between the C-terminal glycine residue and an adjacent aromatic residue in ATG8 proteins conjugated to phosphatidylethanolamine (PE), producing an ATG8 protein that is resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine (PubMed:31722778). RavZ is also able to mediate delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989). {ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33909989}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19056683}. Endomembrane system {ECO:0000250|UniProtKB:P60517}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60517}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P60517}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P60517}. Note=Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae. Colocalizes with microtubules (By similarity). Localizes also to discrete punctae along the ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:P60517, ECO:0000250|UniProtKB:Q9DCD6}.
| null | null | null | null | null |
FUNCTION: Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton (PubMed:9892355). Involved in autophagy: while LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:15169837, PubMed:20562859, PubMed:22948227). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006538). Also required for the local activation of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, regulating ubiquitination and degradation of TIAM1, a guanyl-nucleotide exchange factor (GEF) that activates RAC1 and downstream signal transduction (PubMed:25684205). Thereby, regulates different biological processes including the organization of the cytoskeleton, cell migration and proliferation (PubMed:25684205). Involved in apoptosis (PubMed:15977068). {ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:20562859, ECO:0000269|PubMed:22948227, ECO:0000269|PubMed:25684205, ECO:0000269|PubMed:31006538, ECO:0000269|PubMed:9892355}.
|
Homo sapiens (Human)
|
O95167
|
NDUA3_HUMAN
|
MAARVGAFLKNAWDKEPVLVVSFVVGGLAVILPPLSPYFKYSVMINKATPYNYPVPVRDDGNMPDVPSHPQDPQGPSLEWLKKL
| null | null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF14987;
| null |
Complex I NDUFA3 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
|
Homo sapiens (Human)
|
O95168
|
NDUB4_HUMAN
|
MSFPKYKPSSLRTLPETLDPAEYNISPETRRAQAERLAIRAQLKREYLLQYNDPNRRGLIENPALLRWAYARTINVYPNFRPTPKNSLMGALCGFGPLIFIYYIIKTERDRKEKLIQEGKLDRTFHLSY
| null | null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to oxidative stress [GO:0006979]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF07225;
| null |
Complex I NDUFB4 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
|
Homo sapiens (Human)
|
O95169
|
NDUB8_HUMAN
|
MAVARAGVLGVQWLQRASRNVMPLGARTASHMTKDMFPGPYPRTPEERAAAAKKYNMRVEDYEPYPDDGMGYGDYPKLPDRSQHERDPWYSWDQPGLRLNWGEPMHWHLDMYNRNRVDTSPTPVSWHVMCMQLFGFLAFMIFMCWVGDVYPVYQPVGPKQYPYNNLYLERGGDPSKEPERVVHYEI
| null | null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
endoplasmic reticulum [GO:0005783]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF05821;
| null |
Complex I NDUFB8 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
|
Homo sapiens (Human)
|
O95171
|
SCEL_HUMAN
|
MSNVTLRKMSPTGNEMKSTTQGTTRKQQDFHEVNKRRTFLQDNSWIKKRPEEEKDENYGRVVLNRHNSHDALDRKVNERDVPKATISRYSSDDTLDRISDRNDAAKTYKANTLDNQLTNRSMSMFRSLEVTKLQPGGSLNANTSNTIASTSATTPVKKKRQSWFPPPPPGYNASSSTGTRRREPGVHPPIPPKPSSPVSSPNQLRQDNRQIHPPKPGVYTETNRSAERNIRSQDLDNIVKVATSLQRSDKGEELDNLIKMNKSLNRNQGLDSLFRANPKVEEREKRAKSLESLIYMSTRTDKDGKGIQSLGSPIKVNQRTDKNEKGRQNLESVAKVNARMNKTSRRSEDLDNATEVNPKGHENTTGKKDLDGLIKVDPETNKNITRGQSLDNLIKVTPEVKRSNQGSKDLNNFIKVYPGTEKSTEGGQSLDSLIKVTPERNRTNQGNQDLENLIKVIPSANKSSEQGLDEHINVSPKAVKNTDGKQDLDKLIKVNPEIFTNNQRNQDLANLIKVNPAVIRNNQSQDLDNLIKVKPSALRNTNRDQNLENLIEVNSHVSENKNGSSNTGAKQAGPQDTVVYTRTYVENSKSPKDGYQENISGKYIQTVYSTSDRSVIERDMCTYCRKPLGVETKMILDELQICCHSTCFKCEICKQPLENLQAGDSIWIYRQTIHCEPCYSKIMAKWIP
| null | null |
embryo development ending in birth or egg hatching [GO:0009792]; epidermis development [GO:0008544]; keratinocyte differentiation [GO:0030216]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; response to mechanical stimulus [GO:0009612]
|
cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; perinuclear region of cytoplasm [GO:0048471]
|
metal ion binding [GO:0046872]
| null |
2.10.110.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=May become cross-linked to membrane proteins by transglutaminase.
| null | null | null | null | null |
FUNCTION: May function in the assembly or regulation of proteins in the cornified envelope. The LIM domain may be involved in homotypic or heterotypic associations and may function to localize sciellin to the cornified envelope.
|
Homo sapiens (Human)
|
O95180
|
CAC1H_HUMAN
|
MTEGARAADEVRVPLGAPPPGPAALVGASPESPGAPGREAERGSELGVSPSESPAAERGAELGADEEQRVPYPALAATVFFCLGQTTRPRSWCLRLVCNPWFEHVSMLVIMLNCVTLGMFRPCEDVECGSERCNILEAFDAFIFAFFAVEMVIKMVALGLFGQKCYLGDTWNRLDFFIVVAGMMEYSLDGHNVSLSAIRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLDSAFVRNNNLTFLRPYYQTEEGEENPFICSSRRDNGMQKCSHIPGRRELRMPCTLGWEAYTQPQAEGVGAARNACINWNQYYNVCRSGDSNPHNGAINFDNIGYAWIAIFQVITLEGWVDIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRARHLSNDSTLASFSEPGSCYEELLKYVGHIFRKVKRRSLRLYARWQSRWRKKVDPSAVQGQGPGHRQRRAGRHTASVHHLVYHHHHHHHHHYHFSHGSPRRPGPEPGACDTRLVRAGAPPSPPSPGRGPPDAESVHSIYHADCHIEGPQERARVAHAAATAAASLRLATGLGTMNYPTILPSGVGSGKGSTSPGPKGKWAGGPPGTGGHGPLSLNSPDPYEKIPHVVGEHGLGQAPGHLSGLSVPCPLPSPPAGTLTCELKSCPYCTRALEDPEGELSGSESGDSDGRGVYEFTQDVRHGDRWDPTRPPRATDTPGPGPGSPQRRAQQRAAPGEPGWMGRLWVTFSGKLRRIVDSKYFSRGIMMAILVNTLSMGVEYHEQPEELTNALEISNIVFTSMFALEMLLKLLACGPLGYIRNPYNIFDGIIVVISVWEIVGQADGGLSVLRTFRLLRVLKLVRFLPALRRQLVVLVKTMDNVATFCTLLMLFIFIFSILGMHLFGCKFSLKTDTGDTVPDRKNFDSLLWAIVTVFQILTQEDWNVVLYNGMASTSSWAALYFVALMTFGNYVLFNLLVAILVEGFQAEGDANRSDTDEDKTSVHFEEDFHKLRELQTTELKMCSLAVTPNGHLEGRGSLSPPLIMCTAATPMPTPKSSPFLDAAPSLPDSRRGSSSSGDPPLGDQKPPASLRSSPCAPWGPSGAWSSRRSSWSSLGRAPSLKRRGQCGERESLLSGEGKGSTDDEAEDGRAAPGPRATPLRRAESLDPRPLRPAALPPTKCRDRDGQVVALPSDFFLRIDSHREDAAELDDDSEDSCCLRLHKVLEPYKPQWCRSREAWALYLFSPQNRFRVSCQKVITHKMFDHVVLVFIFLNCVTIALERPDIDPGSTERVFLSVSNYIFTAIFVAEMMVKVVALGLLSGEHAYLQSSWNLLDGLLVLVSLVDIVVAMASAGGAKILGVLRVLRLLRTLRPLRVISRAPGLKLVVETLISSLRPIGNIVLICCAFFIIFGILGVQLFKGKFYYCEGPDTRNISTKAQCRAAHYRWVRRKYNFDNLGQALMSLFVLSSKDGWVNIMYDGLDAVGVDQQPVQNHNPWMLLYFISFLLIVSFFVLNMFVGVVVENFHKCRQHQEAEEARRREEKRLRRLERRRRSTFPSPEAQRRPYYADYSPTRRSIHSLCTSHYLDLFITFIICVNVITMSMEHYNQPKSLDEALKYCNYVFTIVFVFEAALKLVAFGFRRFFKDRWNQLDLAIVLLSLMGITLEEIEMSAALPINPTIIRIMRVLRIARVLKLLKMATGMRALLDTVVQALPQVGNLGLLFMLLFFIYAALGVELFGRLECSEDNPCEGLSRHATFSNFGMAFLTLFRVSTGDNWNGIMKDTLRECSREDKHCLSYLPALSPVYFVTFVLVAQFVLVNVVVAVLMKHLEESNKEAREDAELDAEIELEMAQGPGSARRVDADRPPLPQESPGARDAPNLVARKVSVSRMLSLPNDSYMFRPVVPASAPHPRPLQEVEMETYGAGTPLGSVASVHSPPAESCASLQIPLAVSSPARSGEPLHALSPRGTARSPSLSRLLCRQEAVHTDSLEGKIDSPRDTLDPAEPGEKTPVRPVTQGGSLQSPPRSPRPASVRTRKHTFGQRCVSSRPAAPGGEEAEASDPADEEVSHITSSACPWQPTAEPHGPEASPVAGGERDLRRLYSVDAQGFLDKPGRADEQWRPSAELGSGEPGEAKAWGPEAEPALGARRKKKMSPPCISVEPPAEDEGSARPSAAEGGSTTLRRRTPSCEATPHRDSLEPTEGSGAGGDPAAKGERWGQASCRAEHLTVPSFAFEPLDLGVPSGDPFLDGSHSVTPESRASSSGAIVPLEPPESEPPMPVGDPPEKRRGLYLTVPQCPLEKPGSPSATPAPGGGADDPV
| null | null |
aldosterone biosynthetic process [GO:0032342]; calcium ion import [GO:0070509]; calcium ion import across plasma membrane [GO:0098703]; cellular response to hormone stimulus [GO:0032870]; cellular response to potassium ion [GO:0035865]; cortisol biosynthetic process [GO:0034651]; inorganic cation transmembrane transport [GO:0098662]; membrane depolarization during action potential [GO:0086010]; muscle contraction [GO:0006936]; muscle organ development [GO:0007517]; myoblast fusion [GO:0007520]; positive regulation of acrosome reaction [GO:2000344]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; regulation of heart contraction [GO:0008016]; regulation of membrane potential [GO:0042391]
|
membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; voltage-gated calcium channel complex [GO:0005891]; voltage-gated sodium channel complex [GO:0001518]
|
high voltage-gated calcium channel activity [GO:0008331]; low voltage-gated calcium channel activity [GO:0008332]; metal ion binding [GO:0046872]; scaffold protein binding [GO:0097110]; voltage-gated monoatomic ion channel activity [GO:0005244]; voltage-gated sodium channel activity [GO:0005248]
|
PF00520;
|
1.10.287.70;1.20.120.350;
|
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1H subfamily
|
PTM: In response to raising of intracellular calcium, the T-type channels are activated by CaM-kinase II.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25907736, ECO:0000269|PubMed:27149520, ECO:0000269|PubMed:27729216, ECO:0000269|PubMed:9670923, ECO:0000269|PubMed:9930755}; Multi-pass membrane protein {ECO:0000305}. Note=Interaction with STAC increases expression at the cell membrane. {ECO:0000269|PubMed:27149520}.
| null | null | null | null | null |
FUNCTION: Voltage-sensitive calcium channel that gives rise to T-type calcium currents. T-type calcium channels belong to the 'low-voltage activated (LVA)' group. A particularity of this type of channel is an opening at quite negative potentials, and a voltage-dependent inactivation (PubMed:27149520, PubMed:9670923, PubMed:9930755). T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle (Probable). They may also be involved in the modulation of firing patterns of neurons (PubMed:15048902). In the adrenal zona glomerulosa, participates in the signaling pathway leading to aldosterone production in response to either AGT/angiotensin II, or hyperkalemia (PubMed:25907736, PubMed:27729216). {ECO:0000269|PubMed:24277868, ECO:0000269|PubMed:25907736, ECO:0000269|PubMed:27149520, ECO:0000269|PubMed:27729216, ECO:0000269|PubMed:9670923, ECO:0000269|PubMed:9930755, ECO:0000305, ECO:0000305|PubMed:15048902}.
|
Homo sapiens (Human)
|
O95182
|
NDUA7_HUMAN
|
MASATRLIQRLRNWASGHDLQGKLQLRYQEISKRTQPPPKLPVGPSHKLSNNYYCTRDGRRESVPPSIIMSSQKALVSGKPAESSAVAATEKKAVTPAPPIKRWELSSDQPYL
| null | null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial translation [GO:0032543]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrial ribosome [GO:0005761]; mitochondrion [GO:0005739]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]; structural constituent of ribosome [GO:0003735]
|
PF07347;
| null |
Complex I NDUFA7 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
|
Homo sapiens (Human)
|
O95183
|
VAMP5_HUMAN
|
MAGIELERCQQQANEVTEIMRNNFGKVLERGVKLAELQQRSDQLLDMSSTFNKTTQNLAQKKCWENIRYRICVGLVVVGVLLIILIVLLVVFLPQSSDSSSAPRTQDAGIASGPGN
| null | null |
cell differentiation [GO:0030154]; Golgi to plasma membrane protein transport [GO:0043001]; muscle organ development [GO:0007517]; skeletal muscle tissue development [GO:0007519]
|
cell surface [GO:0009986]; cytoplasmic vesicle membrane [GO:0030659]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intercalated disc [GO:0014704]; late endosome [GO:0005770]; organelle membrane [GO:0031090]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
| null |
PF00957;
|
1.20.5.110;
|
Synaptobrevin family
|
PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which hydrolyzes the 40-Arg-|-Ser-41 bond and probably inhibits neurotransmitter release (PubMed:28770820). It remains unknown whether BoNT/X is ever produced, or what organisms it targets. {ECO:0000269|PubMed:28770820}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Associated with the plasma membrane as well as intracellular perinuclear and peripheral vesicular structures of myotubes. Associated with the trans-Golgi, but not with the cis-Golgi apparatus (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May participate in trafficking events that are associated with myogenesis, such as myoblast fusion and/or GLUT4 trafficking.
|
Homo sapiens (Human)
|
O95185
|
UNC5C_HUMAN
|
MRKGLRATAARCGLGLGYLLQMLVLPALALLSASGTGSAAQDDDFFHELPETFPSDPPEPLPHFLIEPEEAYIVKNKPVNLYCKASPATQIYFKCNSEWVHQKDHIVDERVDETSGLIVREVSIEISRQQVEELFGPEDYWCQCVAWSSAGTTKSRKAYVRIAYLRKTFEQEPLGKEVSLEQEVLLQCRPPEGIPVAEVEWLKNEDIIDPVEDRNFYITIDHNLIIKQARLSDTANYTCVAKNIVAKRKSTTATVIVYVNGGWSTWTEWSVCNSRCGRGYQKRTRTCTNPAPLNGGAFCEGQSVQKIACTTLCPVDGRWTPWSKWSTCGTECTHWRRRECTAPAPKNGGKDCDGLVLQSKNCTDGLCMQTAPDSDDVALYVGIVIAVIVCLAISVVVALFVYRKNHRDFESDIIDSSALNGGFQPVNIKAARQDLLAVPPDLTSAAAMYRGPVYALHDVSDKIPMTNSPILDPLPNLKIKVYNTSGAVTPQDDLSEFTSKLSPQMTQSLLENEALSLKNQSLARQTDPSCTAFGSFNSLGGHLIVPNSGVSLLIPAGAIPQGRVYEMYVTVHRKETMRPPMDDSQTLLTPVVSCGPPGALLTRPVVLTMHHCADPNTEDWKILLKNQAAQGQWEDVVVVGEENFTTPCYIQLDAEACHILTENLSTYALVGHSTTKAAAKRLKLAIFGPLCCSSLEYSIRVYCLDDTQDALKEILHLERQMGGQLLEEPKALHFKGSTHNLRLSIHDIAHSLWKSKLLAKYQEIPFYHVWSGSQRNLHCTFTLERFSLNTVELVCKLCVRQVEGEGQIFQLNCTVSEEPTGIDLPLLDPANTITTVTGPSAFSIPLPIRQKLCSSLDAPQTRGHDWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEAQNFPDGNLSMLAAVLEEMGRHETVVSLAAEGQY
| null | null |
anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; brain development [GO:0007420]; chemorepulsion of axon [GO:0061643]; dorsal root ganglion development [GO:1990791]; ectopic germ cell programmed cell death [GO:0035234]; positive regulation of apoptotic process [GO:0043065]; positive regulation of developmental process [GO:0051094]; positive regulation of reproductive process [GO:2000243]; regulation of neuron migration [GO:2001222]
|
cell surface [GO:0009986]; dendrite [GO:0030425]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
netrin receptor activity [GO:0005042]; netrin receptor activity involved in chemorepulsion [GO:0005043]; protein kinase binding [GO:0019901]; tubulin binding [GO:0015631]
|
PF00531;PF07679;PF00090;PF17217;PF00791;
|
2.60.220.30;1.10.533.10;2.60.40.10;2.20.100.10;
|
Unc-5 family
|
PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis. {ECO:0000250|UniProtKB:Q761X5}.; PTM: Phosphorylated on different cytoplasmic tyrosine residues. Phosphorylation of Tyr-568 leads to an interaction with PTPN11 phosphatase, suggesting that its activity is regulated by phosphorylation/dephosphorylation. Tyrosine phosphorylation is netrin-dependent. {ECO:0000250|UniProtKB:O08747}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25419706}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000269|PubMed:25419706}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q761X5}. Cell projection, axon {ECO:0000250|UniProtKB:O08747}. Cell projection, dendrite {ECO:0000250|UniProtKB:O08747}. Cell projection, growth cone {ECO:0000250|UniProtKB:O08747}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O08747}. Cell projection, filopodium {ECO:0000250|UniProtKB:O08747}.
| null | null | null | null | null |
FUNCTION: Receptor for netrin required for axon guidance (By similarity). Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (By similarity). NTN1/Netrin-1 binding might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Axon repulsion in growth cones may also be caused by its association with DCC that may trigger signaling for repulsion (By similarity). Might also collaborate with DSCAM in NTN1-mediated axon repulsion independently of DCC (By similarity). Also involved in corticospinal tract axon guidance independently of DCC (By similarity). Involved in dorsal root ganglion axon projection towards the spinal cord (PubMed:28483977). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). {ECO:0000250|UniProtKB:O08747, ECO:0000250|UniProtKB:Q761X5, ECO:0000269|PubMed:28483977}.
|
Homo sapiens (Human)
|
O95196
|
CSPG5_HUMAN
|
MGRAGGGGPGRGPPPLLLFLGAALVLASGAVPAREAGSAVEAEELVKGSPAWEPPANDTREEAGPPAAGEDEASWTAPGGELAGPEEVLQESAAVTGTAWLEADSPGLGGVTAEAGSGDAQALPATLQAPHEVLGQSIMPPAIPEATEASGPPSPTPGDKLSPASELPKESPLEVWLNLGGSTPDPQGPELTYPFQGTLEPQPASDIIDIDYFEGLDGEGRGADLGSFPGSPGTSENHPDTEGETPSWSLLDLYDDFTPFDESDFYPTTSFYDDLDEEEEEEEDDKDAVGGGDLEDENELLVPTGKPGLGPGTGQPTSRWHAVPPQHTLGSVPGSSIALRPRPGEPGRDLASSENGTECRSGFVRHNGSCRSVCDLFPSYCHNGGQCYLVENIGAFCRCNTQDYIWHKGMRCESIITDFQVMCVAVGSAALVLLLLFMMTVFFAKKLYLLKTENTKLRRTNKFRTPSELHNDNFSLSTIAEGSHPNVRKLCNTPRTSSPHARALAHYDNVICQDDPSAPHKIQEVLKSCLKEEESFNIQNSMSPKLEGGKGDQADLDVNCLQNNLT
| null | null |
axon regeneration [GO:0031103]; cell projection morphogenesis [GO:0048858]; cytoskeleton organization [GO:0007010]; glial cell projection elongation [GO:0106091]; intracellular transport [GO:0046907]; nervous system development [GO:0007399]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; regulation of synaptic vesicle exocytosis [GO:2000300]
|
cell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; Golgi-associated vesicle membrane [GO:0030660]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]
|
growth factor activity [GO:0008083]
|
PF06566;PF06567;
| null | null |
PTM: N-glycosylated. {ECO:0000250}.; PTM: O-glycosylated; contains chondroitin sulfate glycans (PubMed:25326458). Part-time proteoglycan, expressed in part as a proteoglycan exhibiting chondroitin sulfate glycans and in part as a non-proteoglycan form (By similarity). The relative amount of both forms depends on tissues and tissue maturation (By similarity). {ECO:0000250|UniProtKB:Q71M36, ECO:0000269|PubMed:25326458}.; PTM: Phosphorylated; in intracellular and extracellular parts. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ERQ6}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9ERQ6}. Synaptic cell membrane {ECO:0000250|UniProtKB:Q71M36}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q71M36}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q71M36}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q71M36}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q71M36}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q71M36}. Cell surface {ECO:0000250|UniProtKB:Q71M36}. Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:37453717}. Note=In neurons, localizes to synaptic junctions. Also detected in the endoplasmic reticulum and the Golgi. Partially enriched in lipid rafts. {ECO:0000250|UniProtKB:Q71M36, ECO:0000250|UniProtKB:Q9ERQ6}.
| null | null | null | null | null |
FUNCTION: May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation. {ECO:0000269|PubMed:15358134}.
|
Homo sapiens (Human)
|
O95197
|
RTN3_HUMAN
|
MAEPSAATQSHSISSSSFGAEPSAPGGGGSPGACPALGTKSCSSSCADSFVSSSSSQPVSLFSTSQEGLSSLCSDEPSSEIMTSSFLSSSEIHNTGLTILHGEKSHVLGSQPILAKEGKDHLDLLDMKKMEKPQGTSNNVSDSSVSLAAGVHCDRPSIPASFPEHPAFLSKKIGQVEEQIDKETKNPNGVSSREAKTALDADDRFTLLTAQKPPTEYSKVEGIYTYSLSPSKVSGDDVIEKDSPESPFEVIIDKAAFDKEFKDSYKESTDDFGSWSVHTDKESSEDISETNDKLFPLRNKEAGRYPMSALLSRQFSHTNAALEEVSRCVNDMHNFTNEILTWDLVPQVKQQTDKSSDCITKTTGLDMSEYNSEIPVVNLKTSTHQKTPVCSIDGSTPITKSTGDWAEASLQQENAITGKPVPDSLNSTKEFSIKGVQGNMQKQDDTLAELPGSPPEKCDSLGSGVATVKVVLPDDHLKDEMDWQSSALGEITEADSSGESDDTVIEDITADTSFENNKIQAEKPVSIPSAVVKTGEREIKEIPSCEREEKTSKNFEELVSDSELHQDQPDILGRSPASEAACSKVPDTNVSLEDVSEVAPEKPITTENPKLPSTVSPNVFNETEFSLNVTTSAYLESLHGKNVKHIDDSSPEDLIAAFTETRDKGIVDSERNAFKAISEKMTDFKTTPPVEVLHENESGGSEIKDIGSKYSEQSKETNGSEPLGVFPTQGTPVASLDLEQEQLTIKALKELGERQVEKSTSAQRDAELPSEEVLKQTFTFAPESWPQRSYDILERNVKNGSDLGISQKPITIRETTRVDAVSSLSKTELVKKHVLARLLTDFSVHDLIFWRDVKKTGFVFGTTLIMLLSLAAFSVISVVSYLILALLSVTISFRIYKSVIQAVQKSEEGHPFKAYLDVDITLSSEAFHNYMNAAMVHINRALKLIIRLFLVEDLVDSLKLAVFMWLMTYVGAVFNGITLLILAELLIFSVPIVYEKYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE
| null | null |
apoptotic process [GO:0006915]; brain development [GO:0007420]; endoplasmic reticulum tubular network formation [GO:0071787]; endoplasmic reticulum tubular network organization [GO:0071786]; negative regulation of amyloid-beta formation [GO:1902430]; neuron differentiation [GO:0030182]; vesicle-mediated transport [GO:0016192]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
| null |
PF02453;
|
1.20.5.2480;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12811824, ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:16979658, ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17182608, ECO:0000269|PubMed:17191123, ECO:0000269|PubMed:24262037, ECO:0000269|PubMed:29117567, ECO:0000269|PubMed:34313226}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:16979658, ECO:0000269|PubMed:29117567}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. Induces the formation of endoplasmic reticulum tubules (PubMed:25612671). Also acts as an inflammation-resolving regulator by interacting with both TRIM25 and RIGI, subsequently impairing RIGI 'Lys-63'-linked polyubiquitination leading to IRF3 and NF-kappa-B inhibition. {ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17191123, ECO:0000269|PubMed:25612671}.; FUNCTION: (Microbial infection) Plays a positive role in viral replication and pathogenesis of enteroviruses. {ECO:0000269|PubMed:17182608}.
|
Homo sapiens (Human)
|
O95198
|
KLHL2_HUMAN
|
METPPLPPACTKQGHQKPLDSKDDNTEKHCPVTVNPWHMKKAFKVMNELRSQNLLCDVTIVAEDMEISAHRVVLAACSPYFHAMFTGEMSESRAKRVRIKEVDGWTLRMLIDYVYTAEIQVTEENVQVLLPAAGLLQLQDVKKTCCEFLESQLHPVNCLGIRAFADMHACTDLLNKANTYAEQHFADVVLSEEFLNLGIEQVCSLISSDKLTISSEEKVFEAVIAWVNHDKDVRQEFMARLMEHVRLPLLPREYLVQRVEEEALVKNSSACKDYLIEAMKYHLLPTEQRILMKSVRTRLRTPMNLPKLMVVVGGQAPKAIRSVECYDFKEERWHQVAELPSRRCRAGMVYMAGLVFAVGGFNGSLRVRTVDSYDPVKDQWTSVANMRDRRSTLGAAVLNGLLYAVGGFDGSTGLSSVEAYNIKSNEWFHVAPMNTRRSSVGVGVVGGLLYAVGGYDGASRQCLSTVECYNATTNEWTYIAEMSTRRSGAGVGVLNNLLYAVGGHDGPLVRKSVEVYDPTTNAWRQVADMNMCRRNAGVCAVNGLLYVVGGDDGSCNLASVEYYNPTTDKWTVVSSCMSTGRSYAGVTVIDKPL
| null | null |
protein ubiquitination [GO:0016567]
|
actin cytoskeleton [GO:0015629]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; ruffle [GO:0001726]
|
actin binding [GO:0003779]; identical protein binding [GO:0042802]; ubiquitin ligase-substrate adaptor activity [GO:1990756]
|
PF07707;PF00651;PF01344;
|
1.25.40.420;2.120.10.80;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10397770, ECO:0000269|PubMed:15715669}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q8JZP3}. Cell projection {ECO:0000269|PubMed:15715669}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:F1LZF0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8JZP3}. Note=A proportion colocalizes with the actin cytoskeleton (PubMed:10397770). When over-expressed, colocalizes with NPTXR in perinuclear aggresomes (By similarity). {ECO:0000250|UniProtKB:Q8JZP3, ECO:0000269|PubMed:10397770}.
| null | null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23838290}.
| null | null |
FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, WNK1, WNK3 and WNK4, leading most often to their proteasomal degradation (PubMed:23838290). The BCR(KLHL2) complex catalyzes ubiquitination and degradation of NPTXR (By similarity). Responsible for degradative ubiquitination of the WNK kinases WNK1, WNK3 and WNK4 (PubMed:23838290). Plays a role in the reorganization of the actin cytoskeleton (PubMed:10397770). Promotes growth of cell projections in oligodendrocyte precursors (PubMed:15715669). {ECO:0000250|UniProtKB:Q8JZP3, ECO:0000269|PubMed:10397770, ECO:0000269|PubMed:15715669, ECO:0000269|PubMed:23838290}.
|
Homo sapiens (Human)
|
O95201
|
RHIT_HUMAN
|
MSADGGGIQDTQDKETPPEVPDRGHPHQEMPSKLGEAVPSGDTQESLHIKMEPEEPHSEGASQEDGAQGAWGWAPLSHGSKEKALFLPGGALPSPRIPVLSREGRTRDRQMAAALLTAWSQMPVTFEDVALYLSREEWGRLDHTQQNFYRDVLQKKNGLSLGFPFSRPFWAPQAHGKGEASGSSRQAGDEKEWRGACTGAVEVGQRVQTSSVAALGNVKPFRTRAGRVQWGVPQCAQEAACGRSSGPAKDSGQPAEPDRTPDAAPPDPSPTEPQEYRVPEKPNEEEKGAPESGEEGLAPDSEVGRKSYRCEQCGKGFSWHSHLVTHRRTHTGEKPYACTDCGKRFGRSSHLIQHQIIHTGEKPYTCPACRKSFSHHSTLIQHQRIHTGEKPYVCDRCAKRFTRRSDLVTHQGTHTGAKPHKCPICAKCFTQSSALVTHQRTHTGVKPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFSHSSHLTAHQRTHRGVRPYACPLCGKSFSRRSNLHRHEKIHTTGPKALAMLMLGAAAAGALATPPPAPT
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of hydrogen peroxide biosynthetic process [GO:0010729]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
|
PF01352;PF00096;
|
6.10.140.140;3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor involved in regulating MPV17L expression (PubMed:22306510). By regulating MPV17L expression, contributes to the regulation of genes involved in H(2)O(2) metabolism and the mitochondrial apoptotic cascade (PubMed:22306510). {ECO:0000269|PubMed:22306510}.
|
Homo sapiens (Human)
|
O95202
|
LETM1_HUMAN
|
MASILLRSCRGRAPARLPPPPRYTVPRGSPGDPAHLSCASTLGLRNCLNVPFGCCTPIHPVYTSSRGDHLGCWALRPECLRIVSRAPWTSTSVGFVAVGPQCLPVRGWHSSRPVRDDSVVEKSLKSLKDKNKKLEEGGPVYSPPAEVVVKKSLGQRVLDELKHYYHGFRLLWIDTKIAARMLWRILNGHSLTRRERRQFLRICADLFRLVPFLVFVVVPFMEFLLPVAVKLFPNMLPSTFETQSLKEERLKKELRVKLELAKFLQDTIEEMALKNKAAKGSATKDFSVFFQKIRETGERPSNEEIMRFSKLFEDELTLDNLTRPQLVALCKLLELQSIGTNNFLRFQLTMRLRSIKADDKLIAEEGVDSLNVKELQAACRARGMRALGVTEDRLRGQLKQWLDLHLHQEIPTSLLILSRAMYLPDTLSPADQLKSTLQTLPEIVAKEAQVKVAEVEGEQVDNKAKLEATLQEEAAIQQEHREKELQKRSEVAKDFEPERVVAAPQRPGTEPQPEMPDTVLQSETLKDTAPVLEGLKEEEITKEEIDILSDACSKLQEQKKSLTKEKEELELLKEDVQDYSEDLQEIKKELSKTGEEKYVEESKASKRLTKRVQQMIGQIDGLISQLEMDQQAGKLAPANGMPTGENVISVAELINAMKQVKHIPESKLTSLAAALDENKDGKVNIDDLVKVIELVDKEDVHISTSQVAEIVATLEKEEKVEEKEKAKEKAEKEVAEVKS
| null | null |
calcium export from the mitochondrion [GO:0099093]; calcium ion transport [GO:0006816]; cristae formation [GO:0042407]; inner mitochondrial membrane organization [GO:0007007]; mitochondrial calcium ion homeostasis [GO:0051560]; mitochondrial calcium ion transmembrane transport [GO:0006851]; mitochondrial potassium ion transmembrane transport [GO:0140141]; negative regulation of mitochondrial calcium ion concentration [GO:0051562]; protein hexamerization [GO:0034214]; protein homooligomerization [GO:0051260]; regulation of cellular hyperosmotic salinity response [GO:1900069]
|
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
|
calcium ion binding [GO:0005509]; calcium:proton antiporter activity [GO:0015369]; ribosome binding [GO:0043022]
|
PF07766;
|
1.10.238.10;
|
LETM1 family
|
PTM: PINK1-mediated phosphorylation at Thr-192, positively regulates its mitochondrial calcium transport activity. {ECO:0000269|PubMed:29123128}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:14706454, ECO:0000269|PubMed:15138253, ECO:0000269|PubMed:18628306, ECO:0000269|PubMed:19797662, ECO:0000269|PubMed:32139798}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) + 2 H(+)(out) = Ca(2+)(out) + 2 H(+)(in); Xref=Rhea:RHEA:72199, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:19797662, ECO:0000269|PubMed:24344246, ECO:0000269|PubMed:29123128}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:24898248, ECO:0000269|PubMed:36055214, ECO:0000269|PubMed:36321428};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=27 uM for calcium transport {ECO:0000269|PubMed:24344246}; Vmax=21 pmol/sec/ug enzyme for calcium transport {ECO:0000269|PubMed:24344246};
| null | null | null |
FUNCTION: Plays an important role in maintenance of mitochondrial morphology and in mediating either calcium or potassium/proton antiport (PubMed:18628306, PubMed:19797662, PubMed:24344246, PubMed:24898248, PubMed:29123128, PubMed:32139798, PubMed:36055214, PubMed:36321428). Mediates proton-dependent calcium efflux from mitochondrion (PubMed:19797662, PubMed:24344246, PubMed:29123128). Functions also as an electroneutral mitochondrial proton/potassium exchanger (PubMed:24898248, PubMed:36055214, PubMed:36321428). Crucial for the maintenance of mitochondrial tubular networks and for the assembly of the supercomplexes of the respiratory chain (PubMed:18628306, PubMed:36055214). Required for the maintenance of the tubular shape and cristae organization (PubMed:18628306, PubMed:32139798). {ECO:0000269|PubMed:18628306, ECO:0000269|PubMed:19797662, ECO:0000269|PubMed:24344246, ECO:0000269|PubMed:24898248, ECO:0000269|PubMed:29123128, ECO:0000269|PubMed:32139798, ECO:0000269|PubMed:36055214, ECO:0000269|PubMed:36321428}.
|
Homo sapiens (Human)
|
O95206
|
PCDH8_HUMAN
|
MSPVRRWGSPCLFPLQLFSLCWVLSVAQSKTVRYSTFEEDAPGTVIGTLAEDLHMKVSGDTSFRLMKQFNSSLLRVREGDGQLTVGDAGLDRERLCGQAPQCVLAFDVVSFSQEQFRLVHVEVEVRDVNDHAPRFPRAQIPVEVSEGAAVGTRIPLEVPVDEDVGANGLQTVRLAEPHSPFRVELQTRADGAQCADLVLLQELDRESQAAYSLELVAQDGGRPPRSATAALSVRVLDANDHSPAFPQGAVAEVELAEDAPVGSLLLDLDAADPDEGPNGDVVFAFGARTPPEARRLFRLDPRSGRLTLAGPVDYERQDTYELDVRAQDRGPGPRAATCKVIVRIRDVNDNAPDIAITPLAAPGAPATSPFAAAAAAAALGGADASSPAGAGTPEAGATSLVPEGAARESLVALVSTSDRDSGANGQVRCALYGHEHFRLQPAYAGSYLVVTAASLDRERIAEYNLTLVAEDRGAPPLRTVRPYTVRVGDENDNAPLFTRPVYEVSVRENNPPGAYLATVAARDRDLGRNGQVTYRLLEAEVGRAGGAVSTYVSVDPATGAIYALRSFDYETLRQLDVRIQASDGGSPQLSSSALVQVRVLDQNDHAPVLVHPAPANGSLEVAVPGRTAKDTVVARVQARDADEGANGELAFELQQQEPREAFAIGRRTGEILLTGDLSQEPPGRVFRALLVISDGGRPPLTTTATVSFVVTAGGGRGPAAPASAGSPERSRPPGSRLGVSGSVLQWDTPLIVIIVLAGSCTLLLAAIIAIATTCNRRKKEVRKGGALREERPGAAGGGASAPGSPEEAARGAGPRPNMFDVLTFPGTGKAPFGSPAADAPPPAVAAAEVPGSEGGSATGESACHFEGQQRLRGAHAEPYGASPGFGKEPAPPVAVWKGHSFNTISGREAEKFSGKDSGKGDSDFNDSDSDISGDALKKDLINHMQSGLWACTAECKILGHSDRCWSPSCSGPNAHPSPHPPAQMSTFCKSTSLPRDPLRRDNYYQAQLPKTVGLQSVYEKVLHRDYDRTVTLLSPPRPGRLPDLQEIGVPLYQSPPGRYLSPKKGANENV
| null | null |
cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; chemical synaptic transmission [GO:0007268]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; modulation of chemical synaptic transmission [GO:0050804]; morphogenesis of embryonic epithelium [GO:0016331]; regulation of synaptic membrane adhesion [GO:0099179]; somitogenesis [GO:0001756]
|
dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]
|
calcium ion binding [GO:0005509]
|
PF00028;PF08266;
|
2.60.40.60;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Presynaptic cell membrane. Postsynaptic cell membrane. Note=Also expressed in neuronal cell bodies. Localized to excitatory, but not with inhibitory, synapses. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Calcium-dependent cell-adhesion protein (By similarity). May play a role in activity-induced synaptic reorganization underlying long term memory (By similarity). Could be involved in CDH2 internalization through TAOK2/p38 MAPK pathway. In hippocampal neurons, may play a role in the down-regulation of dendritic spines, maybe through its action on CDH2 endocytosis (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O95208
|
EPN2_HUMAN
|
MTTSSIRRQMKNIVNNYSEAEIKVREATSNDPWGPSSSLMTEIADLTYNVVAFSEIMSMVWKRLNDHGKNWRHVYKALTLLDYLIKTGSERVAQQCRENIFAIQTLKDFQYIDRDGKDQGINVREKSKQLVALLKDEERLKAERAQALKTKERMAQVATGMGSNQITFGRGSSQPNLSTSHSEQEYGKAGGSPASYHGSPEASLCPQHRTGAPLGQSEELQPLSQRHPFLPHLGLASRPNGDWSQPCLTCDRAARATSPRVSSELEQARPQTSGEEELQLQLALAMSREVAEQEERLRRGDDLRLQMALEESRRDTVKIPKKKEHGSLPQQTTLLDLMDALPSSGPAAQKAEPWGPSASTNQTNPWGGPAAPASTSDPWPSFGTKPAASIDPWGVPTGATVQSVPKNSDPWAASQQPASSAGKRASDAWGAVSTTKPVSVSGSFELFSNLNGTIKDDFSEFDNLRTSKKTAESVTSLPSQNNGTTSPDPFESQPLTVASSKPSSARKTPESFLGPNAALVNLDSLVTRPAPPAQSLNPFLAPGAPATSAPVNPFQVNQPQPLTLNQLRGSPVLGTSTSFGPGPGVESMAVASMTSAAPQPALGATGSSLTPLGPAMMNMVGSVGIPPSAAQATGTTNPFLL
| null | null |
endocytosis [GO:0006897]; negative regulation of sprouting angiogenesis [GO:1903671]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; positive regulation of Notch signaling pathway [GO:0045747]
|
clathrin vesicle coat [GO:0030125]; cytosol [GO:0005829]; endosome [GO:0005768]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]
|
cadherin binding [GO:0045296]; clathrin binding [GO:0030276]; phospholipid binding [GO:0005543]
|
PF01417;
|
1.25.40.90;
|
Epsin family
|
PTM: Ubiquitinated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10567358}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:10567358}. Note=In punctate structures throughout the cell, associated with clathrin-coated vesicles, and particularly concentrated in the region of the Golgi complex.
| null | null | null | null | null |
FUNCTION: Plays a role in the formation of clathrin-coated invaginations and endocytosis. {ECO:0000269|PubMed:10567358}.
|
Homo sapiens (Human)
|
O95210
|
STBD1_HUMAN
|
MGAVWSALLVGGGLAGALFVWLLRGGPGDTGKDGDAEQEKDAPLGGAAIPGGHQSGSSGLSPGPSGQELVTKPEHLQESNGHLISKTKDLGKLQAASWRLQNPSREVCDNSREHVPSGQFPDTEAPATSETSNSRSYSEVSRNESLESPMGEWGFQKGQEISAKAATCFAEKLPSSNLLKNRAKEEMSLSDLNSQDRVDHEEWEMVPRHSSWGDVGVGGSLKAPVLNLNQGMDNGRSTLVEARGQQVHGKMERVAVMPAGSQQVSVRFQVHYVTSTDVQFIAVTGDHECLGRWNTYIPLHYNKDGFWSHSIFLPADTVVEWKFVLVENGGVTRWEECSNRFLETGHEDKVVHAWWGIH
| null | null |
glycogen catabolic process [GO:0005980]; glycophagy [GO:0061723]; intracellular transport [GO:0046907]; substrate localization to autophagosome [GO:0061753]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; ficolin-1-rich granule membrane [GO:0101003]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; phagophore assembly site membrane [GO:0034045]; plasma membrane [GO:0005886]; T-tubule [GO:0030315]; tertiary granule membrane [GO:0070821]
|
cargo receptor activity [GO:0038024]; enzyme binding [GO:0019899]; glycogen binding [GO:2001069]; polysaccharide binding [GO:0030247]; starch binding [GO:2001070]
|
PF00686;
|
2.60.40.10;
| null |
PTM: Ubiquitinated, which leads to proteasomal degradation. {ECO:0000269|PubMed:24837458}.
|
SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:20810658, ECO:0000305|PubMed:21893048}; Single-pass type III membrane protein {ECO:0000305|PubMed:9794794}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24837458}; Single-pass type III membrane protein {ECO:0000305|PubMed:9794794}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:9794794}. Note=Also detected near the junctional sarcoplasmic reticulum (PubMed:9794794). Concentrates at perinuclear structures (PubMed:21893048). {ECO:0000269|PubMed:21893048, ECO:0000269|PubMed:9794794}.
| null | null | null | null | null |
FUNCTION: Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes. {ECO:0000269|PubMed:20810658, ECO:0000269|PubMed:21893048, ECO:0000269|PubMed:24837458}.
|
Homo sapiens (Human)
|
O95214
|
LERL1_HUMAN
|
MAGIKALISLSFGGAIGLMFLMLGCALPIYNKYWPLFVLFFYILSPIPYCIARRLVDDTDAMSNACKELAIFLTTGIVVSAFGLPIVFARAHLIEWGACALVLTGNTVIFATILGFFLVFGSNDDFSWQQW
| null | null |
late endosome to vacuole transport via multivesicular body sorting pathway [GO:0032511]; negative regulation of growth hormone receptor signaling pathway [GO:0060400]
|
endosome [GO:0005768]; membrane [GO:0016020]
|
identical protein binding [GO:0042802]
|
PF04133;
| null |
OB-RGRP/VPS55 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability. {ECO:0000269|PubMed:19907080}.
|
Homo sapiens (Human)
|
O95218
|
ZRAB2_HUMAN
|
MSTKNFRVSDGDWICPDKKCGNVNFARRTSCNRCGREKTTEAKMMKAGGTEIGKTLAEKSRGLFSANDWQCKTCSNVNWARRSECNMCNTPKYAKLEERTGYGGGFNERENVEYIEREESDGEYDEFGRKKKKYRGKAVGPASILKEVEDKESEGEEEDEDEDLSKYKLDEDEDEDDADLSKYNLDASEEEDSNKKKSNRRSRSKSRSSHSRSSSRSSSPSSSRSRSRSRSRSSSSSQSRSRSSSRERSRSRGSKSRSSSRSHRGSSSPRKRSYSSSSSSPERNRKRSRSRSSSSGDRKKRRTRSRSPERRHRSSSGSSHSGSRSSSKKK
| null | null |
mRNA processing [GO:0006397]; RNA splicing [GO:0008380]
|
nucleoplasm [GO:0005654]
|
lipopolysaccharide binding [GO:0001530]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]
|
PF00641;
|
4.10.1060.10;
|
ZRANB2 family
|
PTM: Isoform 2 is phosphorylated on Ser-310 upon DNA damage, probably by ATM or ATR.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11448987}.
| null | null | null | null | null |
FUNCTION: Splice factor required for alternative splicing of TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-splice site selection. {ECO:0000269|PubMed:11448987}.
|
Homo sapiens (Human)
|
O95219
|
SNX4_HUMAN
|
MEQAPPDPERQLQPAPLEPLGSPDAGLGAAVGKEAEGAGEESSGVDTMTHNNFWLKKIEISVSEAEKRTGRNAMNMQETYTAYLIETRSVEHTDGQSVLTDSLWRRYSEFELLRSYLLVYYPHIVVPPLPEKRAEFVWHKLSADNMDPDFVERRRIGLENFLLRIASHPILCRDKIFYLFLTQEGNWKETVNETGFQLKADSRLKALNATFRVKNPDKRFTDLKHYSDELQSVISHLLRVRARVADRLYGVYKVHGNYGRVFSEWSAIEKEMGDGLQSAGHHMDVYASSIDDILEDEEHYADQLKEYLFYAEALRAVCRKHELMQYDLEMAAQDLASKKQQCEELVTGTVRTFSLKGMTTKLFGQETPEQREARIKVLEEQINEGEQQLKSKNLEGREFVKNAWADIERFKEQKNRDLKEALISYAVMQISMCKKGIQVWTNAKECFSKM
| null | null |
endocytic recycling [GO:0032456]; positive regulation of autophagosome assembly [GO:2000786]; positive regulation of histamine secretion by mast cell [GO:1903595]; protein transport [GO:0015031]
|
cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; membrane [GO:0016020]; plasma membrane [GO:0005886]; presynaptic endosome [GO:0098830]; protein-containing complex [GO:0032991]; SNARE complex [GO:0031201]
|
epidermal growth factor receptor binding [GO:0005154]; insulin receptor binding [GO:0005158]; leptin receptor binding [GO:1990460]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3-phosphate binding [GO:0032266]; transferrin receptor binding [GO:1990459]
|
PF00787;
|
1.20.1270.60;3.30.1520.10;
|
Sorting nexin family
| null |
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:17994011, ECO:0000269|PubMed:32513819, ECO:0000269|PubMed:33468622}; Peripheral membrane protein {ECO:0000269|PubMed:17994011}; Cytoplasmic side {ECO:0000269|PubMed:17994011}. Note=Also detected on a juxtanuclear endocytic recycling compartment (ERC). {ECO:0000269|PubMed:17994011}.
| null | null | null | null | null |
FUNCTION: Involved in the regulation of endocytosis and in several stages of intracellular trafficking (PubMed:12668730, PubMed:17994011, PubMed:32513819, PubMed:33468622). Plays a role in recycling endocytosed transferrin receptor and prevent its degradation (PubMed:17994011). Involved in autophagosome assembly by regulating trafficking and recycling of phospholipid scramblase ATG9A (PubMed:32513819, PubMed:33468622). {ECO:0000269|PubMed:12668730, ECO:0000269|PubMed:17994011, ECO:0000269|PubMed:32513819, ECO:0000269|PubMed:33468622}.
|
Homo sapiens (Human)
|
O95229
|
ZWINT_HUMAN
|
MEAAETEAEAAALEVLAEVAGILEPVGLQEEAELPAKILVEFVVDSQKKDKLLCSQLQVADFLQNILAQEDTAKGLDPLASEDTSRQKAIAAKEQWKELKATYREHVEAIKIGLTKALTQMEEAQRKRTQLREAFEQLQAKKQMAMEKRRAVQNQWQLQQEKHLQHLAEVSAEVRERKTGTQQELDRVFQKLGNLKQQAEQERDKLQRYQTFLQLLYTLQGKLLFPEAEAEAENLPDDKPQQPTRPQEQSTGDTMGRDPGVSFKAVGLQPAGDVNLP
| null | null |
cell division [GO:0051301]; establishment of localization in cell [GO:0051649]; homologous chromosome orientation in meiotic metaphase I [GO:0031619]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint signaling [GO:0007094]; regulation of meiosis I spindle assembly checkpoint [GO:1905325]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; kinetochore [GO:0000776]; Knl1/Spc105 complex [GO:0180019]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]
| null |
PF15556;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Localizes to kinetochores from late prophase to anaphase.
| null | null | null | null | null |
FUNCTION: Part of the MIS12 complex, which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase. {ECO:0000269|PubMed:15094189, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131, ECO:0000269|PubMed:16732327}.
|
Homo sapiens (Human)
|
O95231
|
VENTX_HUMAN
|
MRLSSSPPRGPQQLSSFGSVDWLSQSSCSGPTHTPRPADFSLGSLPGPGQTSGAREPPQAVSIKEAAGSSNLPAPERTMAGLSKEPNTLRAPRVRTAFTMEQVRTLEGVFQHHQYLSPLERKRLAREMQLSEVQIKTWFQNRRMKHKRQMQDPQLHSPFSGSLHAPPAFYSTSSGLANGLQLLCPWAPLSGPQALMLPPGSFWGLCQVAQEALASAGASCCGQPLASHPPTPGRPSLGPALSTGPRGLCAMPQTGDAF
| null | null |
positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May be involved in ventralization.
|
Homo sapiens (Human)
|
O95232
|
LC7L3_HUMAN
|
MISAAQLLDELMGRDRNLAPDEKRSNVRWDHESVCKYYLCGFCPAELFTNTRSDLGPCEKIHDENLRKQYEKSSRFMKVGYERDFLRYLQSLLAEVERRIRRGHARLALSQNQQSSGAAGPTGKNEEKIQVLTDKIDVLLQQIEELGSEGKVEEAQGMMKLVEQLKEERELLRSTTSTIESFAAQEKQMEVCEVCGAFLIVGDAQSRVDDHLMGKQHMGYAKIKATVEELKEKLRKRTEEPDRDERLKKEKQEREEREKEREREREERERKRRREEEEREKERARDRERRKRSRSRSRHSSRTSDRRCSRSRDHKRSRSRERRRSRSRDRRRSRSHDRSERKHRSRSRDRRRSKSRDRKSYKHRSKSRDREQDRKSKEKEKRGSDDKKSSVKSGSREKQSEDTNTESKESDTKNEVNGTSEDIKSEGDTQSN
| null | null |
mRNA splice site recognition [GO:0006376]; RNA splicing [GO:0008380]
|
nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U1 snRNP [GO:0005685]; U2-type prespliceosome [GO:0071004]
|
DNA binding [GO:0003677]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]
|
PF03194;
| null |
Luc7 family
|
PTM: Phosphorylated in vitro by SRPK1, SRPK2 and CLK1. {ECO:0000269|PubMed:12565863}.
|
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:10631324, ECO:0000269|PubMed:12565863}. Note=The subnuclear localization is affected by cisplatin.
| null | null | null | null | null |
FUNCTION: Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing. {ECO:0000269|PubMed:16462885}.
|
Homo sapiens (Human)
|
O95235
|
KI20A_HUMAN
|
MSQGILSPPAGLLSDDDVVVSPMFESTAADLGSVVRKNLLSDCSVVSTSLEDKQQVPSEDSMEKVKVYLRVRPLLPSELERQEDQGCVRIENVETLVLQAPKDSFALKSNERGIGQATHRFTFSQIFGPEVGQASFFNLTVKEMVKDVLKGQNWLIYTYGVTNSGKTHTIQGTIKDGGILPRSLALIFNSLQGQLHPTPDLKPLLSNEVIWLDSKQIRQEEMKKLSLLNGGLQEEELSTSLKRSVYIESRIGTSTSFDSGIAGLSSISQCTSSSQLDETSHRWAQPDTAPLPVPANIRFSIWISFFEIYNELLYDLLEPPSQQRKRQTLRLCEDQNGNPYVKDLNWIHVQDAEEAWKLLKVGRKNQSFASTHLNQNSSRSHSIFSIRILHLQGEGDIVPKISELSLCDLAGSERCKDQKSGERLKEAGNINTSLHTLGRCIAALRQNQQNRSKQNLVPFRDSKLTRVFQGFFTGRGRSCMIVNVNPCASTYDETLHVAKFSAIASQLVHAPPMQLGFPSLHSFIKEHSLQVSPSLEKGAKADTGLDDDIENEADISMYGKEELLQVVEAMKTLLLKERQEKLQLEMHLRDEICNEMVEQMQQREQWCSEHLDTQKELLEEMYEEKLNILKESLTSFYQEEIQERDEKIEELEALLQEARQQSVAHQQSGSELALRRSQRLAASASTQQLQEVKAKLQQCKAELNSTTEELHKYQKMLEPPPSAKPFTIDVDKKLEEGQKNIRLLRTELQKLGESLQSAERACCHSTGAGKLRQALTTCDDILIKQDQTLAELQNNMVLVKLDLRKKAACIAEQYHTVLKLQGQVSAKKRLGTNQENQQPNQQPPGKKPFLRNLLPRTPTCQSSTDCSPYARILRSRRSPLLKSGPFGKKY
| null | null |
microtubule bundle formation [GO:0001578]; microtubule-based movement [GO:0007018]; midbody abscission [GO:0061952]; mitotic cytokinesis [GO:0000281]; protein transport [GO:0015031]; regulation of cytokinesis [GO:0032465]
|
Golgi apparatus [GO:0005794]; intercellular bridge [GO:0045171]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; protein kinase binding [GO:0019901]
|
PF00225;
|
3.40.850.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family
|
PTM: Phosphorylated by PLK1 at Ser-528 during mitosis, creating a docking site for PLK1 and recruiting PLK1 at central spindle. {ECO:0000269|PubMed:12939256}.
|
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12939256, ECO:0000269|PubMed:29357359}. Note=Localizes to the spindle midzone during anaphase and telophase. {ECO:0000269|PubMed:29357359}.
| null | null | null | null | null |
FUNCTION: Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. {ECO:0000269|PubMed:12939256}.
|
Homo sapiens (Human)
|
O95236
|
APOL3_HUMAN
|
MGLGQGWGWEASCFACLIRSCCQVVTFTFPFGFQGISQSLENVSGYYADARLEVGSTQLRTAGSCSHSFKRSFLEKKRFTEEATKYFRERVSPVHLQILLTNNEAWKRFVTAAELPRDEADALYEALKKLRTYAAIEDEYVQQKDEQFREWFLKEFPQVKRKIQESIEKLRALANGIEEVHRGCTISNVVSSSTGAASGIMSLAGLVLAPFTAGTSLALTAAGVGLGAASAVTGITTSIVEHSYTSSAEAEASRLTATSIDRLKVFKEVMRDITPNLLSLLNNYYEATQTIGSEIRAIRQARARARLPVTTWRISAGSGGQAERTIAGTTRAVSRGARILSATTSGIFLALDVVNLVYESKHLHEGAKSASAEELRRQAQELEENLMELTQIYQRLNPCHTH
| null | null |
inflammatory response [GO:0006954]; lipoprotein metabolic process [GO:0042157]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; membrane [GO:0016020]
|
lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]
|
PF05461;
| null |
Apolipoprotein L family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles.
|
Homo sapiens (Human)
|
O95237
|
LRAT_HUMAN
|
MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTHYGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGANILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDKFCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
|
2.3.1.135
| null |
cellular response to leukemia inhibitory factor [GO:1990830]; positive regulation of lipid transport [GO:0032370]; response to bacterium [GO:0009617]; response to retinoic acid [GO:0032526]; response to vitamin A [GO:0033189]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]; visual perception [GO:0007601]; vitamin A metabolic process [GO:0006776]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; multivesicular body [GO:0005771]; perinuclear region of cytoplasm [GO:0048471]; rough endoplasmic reticulum [GO:0005791]
|
acyltransferase activity [GO:0016746]; lecithin:11-cis retinol acyltransferase activity [GO:0102279]; O-palmitoyltransferase activity [GO:0016416]; phosphatidylcholine-retinol O-acyltransferase activity [GO:0047173]; retinoic acid binding [GO:0001972]; retinol binding [GO:0019841]
|
PF04970;
|
3.90.1720.10;
|
H-rev107 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Rough endoplasmic reticulum {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = a 2-acyl-sn-glycero-3-phosphocholine + an all-trans-retinyl ester + apo--[retinol-binding protein]; Xref=Rhea:RHEA:17469, Rhea:RHEA-COMP:14426, Rhea:RHEA-COMP:14428, ChEBI:CHEBI:17336, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875, ChEBI:CHEBI:63410, ChEBI:CHEBI:83228; EC=2.3.1.135; Evidence={ECO:0000305|PubMed:10819989}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17470; Evidence={ECO:0000305|PubMed:10819989}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + all-trans-retinol = 2-hexadecanoyl-sn-glycero-3-phosphocholine + all-trans-retinyl hexadecanoate; Xref=Rhea:RHEA:43904, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078; Evidence={ECO:0000269|PubMed:10819989}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43905; Evidence={ECO:0000305|PubMed:10819989}; CATALYTIC ACTIVITY: Reaction=1,2-diheptanoyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = 2-heptanoyl-sn-glycero-3-phosphocholine + all-trans-retinyl heptanoate + apo--[retinol-binding protein]; Xref=Rhea:RHEA:55320, Rhea:RHEA-COMP:14426, Rhea:RHEA-COMP:14428, ChEBI:CHEBI:17336, ChEBI:CHEBI:83228, ChEBI:CHEBI:138195, ChEBI:CHEBI:138266, ChEBI:CHEBI:138724; Evidence={ECO:0000250|UniProtKB:Q9JI60}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55321; Evidence={ECO:0000250|UniProtKB:Q9JI60}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = 2-octanoyl-sn-glycero-3-phosphocholine + all-trans-retinyl octanoate + apo--[retinol-binding protein]; Xref=Rhea:RHEA:56240, Rhea:RHEA-COMP:14426, Rhea:RHEA-COMP:14428, ChEBI:CHEBI:17336, ChEBI:CHEBI:78228, ChEBI:CHEBI:83228, ChEBI:CHEBI:140082, ChEBI:CHEBI:140084; Evidence={ECO:0000250|UniProtKB:Q9JI60}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56241; Evidence={ECO:0000250|UniProtKB:Q9JI60}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = 2-hexadecanoyl-sn-glycero-3-phosphocholine + all-trans-retinyl hexadecanoate + apo--[retinol-binding protein]; Xref=Rhea:RHEA:56244, Rhea:RHEA-COMP:14426, Rhea:RHEA-COMP:14428, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078, ChEBI:CHEBI:83228; Evidence={ECO:0000250|UniProtKB:Q9JI60}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56245; Evidence={ECO:0000250|UniProtKB:Q9JI60}; CATALYTIC ACTIVITY: Reaction=1,2-didodecanoyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = 2-dodecanoyl-sn-glycero-3-phosphocholine + all-trans-retinyl dodecanoate + apo--[retinol-binding protein]; Xref=Rhea:RHEA:56248, Rhea:RHEA-COMP:14426, Rhea:RHEA-COMP:14428, ChEBI:CHEBI:17336, ChEBI:CHEBI:65211, ChEBI:CHEBI:83228, ChEBI:CHEBI:140088, ChEBI:CHEBI:140089; Evidence={ECO:0000250|UniProtKB:Q9JI60}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56249; Evidence={ECO:0000250|UniProtKB:Q9JI60};
| null |
PATHWAY: Cofactor metabolism; retinol metabolism.
| null | null |
FUNCTION: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters (PubMed:9920938). Retinyl esters are storage forms of vitamin A (Probable). LRAT plays a critical role in vision (Probable). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (Probable). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (By similarity). {ECO:0000250|UniProtKB:Q9JI60, ECO:0000269|PubMed:9920938, ECO:0000305|PubMed:9920938}.
|
Homo sapiens (Human)
|
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