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Details on Person UniProt:Q86TM6-2 SYVN1
| Class:Id | ReferenceIsoform:250156 |
|---|---|
| _chainChangeLog | signal peptide:1-22 added on Fri February 6 2015;chain:23-617 added on Fri February 6 2015;signal peptide:1-22 for 250156 removed on Wed August 26 2020;chain:23-617 for 250156 removed on Wed August 26 2020;chain:1-617 for 250156 added on Wed August 26 2020 |
| _displayName | UniProt:Q86TM6-2 SYVN1 |
| _timestamp | 2025-08-15 22:12:20 |
| chain | chain:1-617 |
| checksum | B8A6BACBAF9673C1 |
| comment | 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:27827840, 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).CATALYTIC ACTIVITY 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.PATHWAY Protein modification; protein ubiquitination.SUBUNIT Homodimer (PubMed:16289116). Interacts with p53/TP53 (PubMed:17170702). Interacts with HTT (PubMed:17141218). Component of the HRD1 complex, which comprises at least SYNV1/HRD1, DERL1/2, FAM8A1, HERPUD1/HERP, OS9, SEL1L and UBE2J1 (PubMed:16186509, PubMed:16289116, PubMed:18264092, PubMed:26471130, PubMed:28827405, PubMed:37943610). FAM8A1 is stabilized by interaction with SYNV1, which prevents its proteasomal degradation. OS9 and UBE2J1 recruitment to the complex may be mediated by SEL1L (PubMed:28827405). SYNV1 assembles with SEL1L and FAM8A1 through its transmembrane domains, but interaction with its cytoplasmic domain is required to confer stability to FAM8A1 and enhance recruitment of HERPUD1 (PubMed:28827405). The HRD1 complex also associates with VIMP and may transfer misfolded proteins from the endoplasmic reticulum to VCP (PubMed:16289116). May form a complex with ERLEC1, HSPA5, OS9 and SEL1L (PubMed:18264092, PubMed:18502753). Interacts with VCP (PubMed:16186510, PubMed:16289116). Interacts with UBXN6 (PubMed:18656546). Interacts with BAG6 (PubMed:21636303). Interacts with NFE2L1 (By similarity). Interacts (via N-terminus) with components of the pre-B cell receptor, including IGLL1 and VPREB1 (By similarity). Interacts with CREB3L3; this interaction leads to CREB3L3 ubiquitination and proteasomal degradation (By similarity).INTERACTION Ubiquitously expressed, with highest levels in liver and kidney (at protein level). Up-regulated in synovial tissues from patients with rheumatoid arthritis (at protein level).INDUCTION By endoplasmic reticulum stress-inducing agents such as thapsigargin, tunicamycin or brefeldin A, but not by heat shock.DOMAIN The RING-type zinc finger is required for E3 ligase activity.PTM Not N-glycosylated.PTM Auto-ubiquitinated. Deubiquitinated by USP19 (PubMed:27827840).DISEASE In certain aggressive cases of activated B cell-like diffuse large B-cell lymphoma (ABC-DLBCL), plays a role in the degradation of misfolded N-terminal mutated PRDM1 proteins.SIMILARITY Belongs to the HRD1 family.SEQUENCE CAUTION Extended N-terminus. |
| created | [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 |
| description | recommendedName: E3 ubiquitin-protein ligase synoviolin ecNumber evidence="6 7 8 13 14 15"2.3.2.27 alternativeName: fullName evidence="29"RING-type E3 ubiquitin transferase synoviolin alternativeName: Synovial apoptosis inhibitor 1 |
| geneName | SYVN1 HRD1 KIAA1810 |
| identifier | Q86TM6 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing Endoplasmic reticulum Membrane Metal-binding Phosphoprotein Proteomics identification Reference proteome Stress response Transferase Transmembrane Transmembrane helix Ubl conjugation Ubl conjugation pathway Zinc Zinc-finger |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | SYVN1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:5642217] ENSEMBL:ENSG00000162298 SYVN1 [Homo sapiens] |
| secondaryIdentifier | SYVN1_HUMAN Q8N3K3 Q8N6E8 Q96JL5 Q96PK3 |
| sequenceLength | 617 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | Q86TM6-2 |
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No pathways have been reviewed or authored by UniProt:Q86TM6-2 SYVN1 (250156)
