| IED ID | IndEnz0002011258 |
| Enzyme Type ID | protease011258 |
| Protein Name |
E3 ubiquitin-protein ligase synoviolin EC 2.3.2.27 RING-type E3 ubiquitin transferase synoviolin Synovial apoptosis inhibitor 1 |
| Gene Name | SYVN1 HRD1 KIAA1810 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MFRTAVMMAASLALTGAVVAHAYYLKHQFYPTVVYLTKSSPSMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTETCLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVDFMERSPNISWLFHCRIVSLMFLLGILDFLFVSHAYHSILTRGASVQLVFGFEYAILMTMVLTIFIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPLFAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRASLPAQSPPPPEPADQGPPPAPHPPPLLPQPPNFPQGLLPPFPPGMFPLWPPMGPFPPVPPPPSSGEAVAPPSTSAAALSRPSGAATTTAAGTSATAASATASGPGSGSAPEAGPAPGFPFPPPWMGMPLPPPFAFPPMPVPPAGFAGLTPEELRALEGHERQHLEARLQSLRNIHTLLDAAMLQINQYLTVLASLGPPRPATSVNSTEETATTVVAAASSTSIPSSEATTPTPGASPPAPEMERPPAPESVGTEEMPEDGEPDAAELRRRRLQKLESPVAH |
| Enzyme Length | 617 |
| Uniprot Accession Number | Q86TM6 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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:12646171, ECO:0000269|PubMed:12975321, ECO:0000269|PubMed:14593114, ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:17141218, ECO:0000269|PubMed:17170702}; |
| DNA Binding | |
| EC Number | 2.3.2.27 |
| Enzyme Function | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation (PubMed:12459480, PubMed:12646171, PubMed:12975321, PubMed:14593114, PubMed:16289116, PubMed:16847254, PubMed:17059562, PubMed:17141218, PubMed:17170702, PubMed:22607976, PubMed:26471130, PubMed:28827405). Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:12459480, PubMed:12646171, PubMed:12975321, PubMed:14593114, PubMed:16289116, PubMed:16847254, PubMed:17059562, PubMed:17141218, PubMed:17170702, PubMed:22607976, PubMed:26471130, PubMed:28842558). Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation (PubMed:17141218). Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis (PubMed:17170702). Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (By similarity). During the early stage of B cell development, required for degradation of the pre-B cell receptor (pre-BCR) complex, hence supporting further differentiation into mature B cells (By similarity). {ECO:0000250|UniProtKB:Q9DBY1, ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:12975321, ECO:0000269|PubMed:14593114, ECO:0000269|PubMed:16289116, ECO:0000269|PubMed:16847254, ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:17141218, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:22607976, ECO:0000269|PubMed:26471130, ECO:0000269|PubMed:28827405, ECO:0000269|PubMed:28842558}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:16289116, ECO:0000269|PubMed:16847254, ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:22607976, ECO:0000269|PubMed:26471130}. |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (2); Chain (1); Compositional bias (5); Erroneous initiation (1); Helix (2); Metal binding (8); Modified residue (1); Mutagenesis (3); Region (7); Sequence conflict (3); Topological domain (7); Transmembrane (6); Turn (4); Zinc finger (1) |
| Keywords | 3D-structure;Alternative splicing;Endoplasmic reticulum;Membrane;Metal-binding;Phosphoprotein;Reference proteome;Stress response;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | O75477; O94905; O75460; O75460-1; Q9UBU6; Q9UBV2; P04637; Q9Y385; Q9Y4E8 |
| Induction | INDUCTION: By endoplasmic reticulum stress-inducing agents such as thapsigargin, tunicamycin or brefeldin A, but not by heat shock. {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:14593114}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:14593114, ECO:0000269|PubMed:16186510, ECO:0000269|PubMed:26471130}; Multi-pass membrane protein {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:14593114, ECO:0000269|PubMed:16186510}. |
| Modified Residue | MOD_RES 613; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | PTM: Not N-glycosylated.; PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:12975321}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 6A3Z; |
| Mapped Pubmed ID | 16713569; 16786162; 16802346; 17582219; 17967421; 18235538; 18314878; 18344614; 18369366; 18417469; 18664523; 18711132; 19002207; 19084021; 19116932; 19443960; 19690564; 19828134; 19835843; 19864457; 20237263; 20414249; 20519503; 20606367; 20711500; 21149444; 21343306; 21357747; 21454652; 22280354; 23129766; 23232094; 23363602; 23867461; 23929775; 24100225; 24366871; 24478453; 24565866; 24584735; 24636985; 25385046; 26107514; 26536657; 26740554; 26945068; 27417417; 27756846; 27827840; 28121484; 28260078; 28334804; 28411238; 28423597; 29039504; 29233968; 29743537; 29863080; 29958993; 30106139; 30306455; 31932479; 32182217; 32308114; 33207079; 33243462; 33530981; 33588886; 34196494; 34272738; |
| Motif | |
| Gene Encoded By | |
| Mass | 67,685 |
| Kinetics | |
| Metal Binding | METAL 291; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:30345569, ECO:0007744|PDB:6A3Z"; METAL 294; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:30345569, ECO:0007744|PDB:6A3Z"; METAL 307; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:30345569, ECO:0007744|PDB:6A3Z"; METAL 309; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:30345569, ECO:0007744|PDB:6A3Z"; METAL 312; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:30345569, ECO:0007744|PDB:6A3Z"; METAL 315; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:30345569, ECO:0007744|PDB:6A3Z"; METAL 326; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:30345569, ECO:0007744|PDB:6A3Z"; METAL 329; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:30345569, ECO:0007744|PDB:6A3Z" |
| Rhea ID | |
| Cross Reference Brenda |