Q86TM6 · SYVN1_HUMAN
- ProteinE3 ubiquitin-protein ligase synoviolin
- GeneSYVN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids617 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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
Pathway
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 291 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 294 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 307 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 309 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 312 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 315 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 326 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 329 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase synoviolin
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ86TM6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-4 | Cytoplasmic | ||||
Sequence: MFRT | ||||||
Transmembrane | 5-25 | Helical | ||||
Sequence: AVMMAASLALTGAVVAHAYYL | ||||||
Topological domain | 26-41 | Lumenal | ||||
Sequence: KHQFYPTVVYLTKSSP | ||||||
Transmembrane | 42-62 | Helical | ||||
Sequence: SMAVLYIQAFVLVFLLGKVMG | ||||||
Topological domain | 63-98 | Cytoplasmic | ||||
Sequence: KVFFGQLRAAEMEHLLERSWYAVTETCLAFTVFRDD | ||||||
Transmembrane | 99-119 | Helical | ||||
Sequence: FSPRFVALFTLLLFLKCFHWL | ||||||
Topological domain | 120-140 | Lumenal | ||||
Sequence: AEDRVDFMERSPNISWLFHCR | ||||||
Transmembrane | 141-161 | Helical | ||||
Sequence: IVSLMFLLGILDFLFVSHAYH | ||||||
Topological domain | 162-169 | Cytoplasmic | ||||
Sequence: SILTRGAS | ||||||
Transmembrane | 170-190 | Helical | ||||
Sequence: VQLVFGFEYAILMTMVLTIFI | ||||||
Topological domain | 191-224 | Lumenal | ||||
Sequence: KYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKV | ||||||
Transmembrane | 225-245 | Helical | ||||
Sequence: LLYMAFMTIMIKVHTFPLFAI | ||||||
Topological domain | 246-617 | Cytoplasmic | ||||
Sequence: RPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRASLPAQSPPPPEPADQGPPPAPHPPPLLPQPPNFPQGLLPPFPPGMFPLWPPMGPFPPVPPPPSSGEAVAPPSTSAAALSRPSGAATTTAAGTSATAASATASGPGSGSAPEAGPAPGFPFPPPWMGMPLPPPFAFPPMPVPPAGFAGLTPEELRALEGHERQHLEARLQSLRNIHTLLDAAMLQINQYLTVLASLGPPRPATSVNSTEETATTVVAAASSTSIPSSEATTPTPGASPPAPEMERPPAPESVGTEEMPEDGEPDAAELRRRRLQKLESPVAH |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 294 | No effect on interaction with FAM8A1, HERPUD1, OS9, SEL1L and UBE2J1. | ||||
Sequence: C → A | ||||||
Mutagenesis | 329 | Abolishes E3 ligase activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 503 | Loss of interaction with FAM8A1, HERPUD1, OS9 and UBE2J1, impaired degradation of immature core-glycosylated basigin/CD147. | ||||
Sequence: R → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 628 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000280548 | 1-617 | UniProt | E3 ubiquitin-protein ligase synoviolin | |||
Sequence: MFRTAVMMAASLALTGAVVAHAYYLKHQFYPTVVYLTKSSPSMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTETCLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVDFMERSPNISWLFHCRIVSLMFLLGILDFLFVSHAYHSILTRGASVQLVFGFEYAILMTMVLTIFIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPLFAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRASLPAQSPPPPEPADQGPPPAPHPPPLLPQPPNFPQGLLPPFPPGMFPLWPPMGPFPPVPPPPSSGEAVAPPSTSAAALSRPSGAATTTAAGTSATAASATASGPGSGSAPEAGPAPGFPFPPPWMGMPLPPPFAFPPMPVPPAGFAGLTPEELRALEGHERQHLEARLQSLRNIHTLLDAAMLQINQYLTVLASLGPPRPATSVNSTEETATTVVAAASSTSIPSSEATTPTPGASPPAPEMERPPAPESVGTEEMPEDGEPDAAELRRRRLQKLESPVAH | |||||||
Modified residue | 613 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 613 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
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).
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).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q86TM6 | ERLIN1 O75477 | 2 | EBI-947849, EBI-359299 | |
BINARY | Q86TM6 | ERLIN2 O94905 | 2 | EBI-947849, EBI-4400770 | |
BINARY | Q86TM6 | ERN1 O75460 | 2 | EBI-947849, EBI-371750 | |
BINARY | Q86TM6 | ERN1 O75460-1 | 3 | EBI-947849, EBI-15600828 | |
BINARY | Q86TM6 | FAM8A1 Q9UBU6 | 22 | EBI-947849, EBI-6309101 | |
BINARY | Q86TM6 | SEL1L Q9UBV2 | 21 | EBI-947849, EBI-358766 | |
BINARY | Q86TM6 | TP53 P04637 | 5 | EBI-947849, EBI-366083 | |
BINARY | Q86TM6 | UBE2J1 Q9Y385 | 15 | EBI-947849, EBI-988826 | |
BINARY | Q86TM6 | USP15 Q9Y4E8 | 8 | EBI-947849, EBI-1043104 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-84 | Necessary and sufficient for SEL1L interaction | ||||
Sequence: MFRTAVMMAASLALTGAVVAHAYYLKHQFYPTVVYLTKSSPSMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYA | ||||||
Region | 1-251 | Involved in FAM8A1 interaction | ||||
Sequence: MFRTAVMMAASLALTGAVVAHAYYLKHQFYPTVVYLTKSSPSMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTETCLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVDFMERSPNISWLFHCRIVSLMFLLGILDFLFVSHAYHSILTRGASVQLVFGFEYAILMTMVLTIFIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPLFAIRPMYLA | ||||||
Region | 236-270 | Interaction with p53/TP53 | ||||
Sequence: KVHTFPLFAIRPMYLAMRQFKKAVTDAIMSRRAIR | ||||||
Zinc finger | 291-330 | RING-type; atypical | ||||
Sequence: CIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCR | ||||||
Region | 337-375 | Disordered | ||||
Sequence: SLPAQSPPPPEPADQGPPPAPHPPPLLPQPPNFPQGLLP | ||||||
Compositional bias | 339-375 | Pro residues | ||||
Sequence: PAQSPPPPEPADQGPPPAPHPPPLLPQPPNFPQGLLP | ||||||
Region | 393-453 | Disordered | ||||
Sequence: PVPPPPSSGEAVAPPSTSAAALSRPSGAATTTAAGTSATAASATASGPGSGSAPEAGPAPG | ||||||
Compositional bias | 411-441 | Polar residues | ||||
Sequence: AAALSRPSGAATTTAAGTSATAASATASGPG | ||||||
Region | 480-535 | HAF-H domain; necessary to form higher-order Hrd1 complexes | ||||
Sequence: GFAGLTPEELRALEGHERQHLEARLQSLRNIHTLLDAAMLQINQYLTVLASLGPPR | ||||||
Compositional bias | 535-566 | Polar residues | ||||
Sequence: RPATSVNSTEETATTVVAAASSTSIPSSEATT | ||||||
Region | 535-617 | Disordered | ||||
Sequence: RPATSVNSTEETATTVVAAASSTSIPSSEATTPTPGASPPAPEMERPPAPESVGTEEMPEDGEPDAAELRRRRLQKLESPVAH | ||||||
Compositional bias | 567-581 | Pro residues | ||||
Sequence: PTPGASPPAPEMERP | ||||||
Compositional bias | 598-617 | Basic and acidic residues | ||||
Sequence: PDAAELRRRRLQKLESPVAH |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q86TM6-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Synonymsb, long
- Length617
- Mass (Da)67,685
- Last updated2007-03-20 v2
- ChecksumB8A6BACBAF9673C1
Q86TM6-2
- Name2
Q86TM6-3
- Name3
- Synonymsa, short
- Differences from canonical
- 411-411: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_023777 | 127-177 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 145 | in Ref. 1; BAC24801 and 4; AAL26903 | ||||
Sequence: M → I | ||||||
Compositional bias | 339-375 | Pro residues | ||||
Sequence: PAQSPPPPEPADQGPPPAPHPPPLLPQPPNFPQGLLP | ||||||
Alternative sequence | VSP_023778 | 411 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 411-441 | Polar residues | ||||
Sequence: AAALSRPSGAATTTAAGTSATAASATASGPG | ||||||
Compositional bias | 535-566 | Polar residues | ||||
Sequence: RPATSVNSTEETATTVVAAASSTSIPSSEATT | ||||||
Sequence conflict | 545 | in Ref. 3; BAC57449 | ||||
Sequence: E → G | ||||||
Compositional bias | 567-581 | Pro residues | ||||
Sequence: PTPGASPPAPEMERP | ||||||
Compositional bias | 598-617 | Basic and acidic residues | ||||
Sequence: PDAAELRRRRLQKLESPVAH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB085847 EMBL· GenBank· DDBJ | BAC24801.1 EMBL· GenBank· DDBJ | mRNA | ||
AB024690 EMBL· GenBank· DDBJ | BAC57449.1 EMBL· GenBank· DDBJ | mRNA | ||
AF317634 EMBL· GenBank· DDBJ | AAL26903.1 EMBL· GenBank· DDBJ | mRNA | ||
AB058713 EMBL· GenBank· DDBJ | BAB47439.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL834262 EMBL· GenBank· DDBJ | CAD38937.1 EMBL· GenBank· DDBJ | mRNA | ||
BC030530 EMBL· GenBank· DDBJ | AAH30530.1 EMBL· GenBank· DDBJ | mRNA |