Q8CF97 · VCIP1_RAT
- ProteinDeubiquitinating protein VCPIP1
- GeneVcpip1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1221 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Deubiquitinating enzyme involved in DNA repair and reassembly of the Golgi apparatus and the endoplasmic reticulum following mitosis (PubMed:12473691, PubMed:15037600).
Necessary for VCP-mediated reassembly of Golgi stacks after mitosis (PubMed:12473691, PubMed:15037600).
Plays a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (PubMed:12473691, PubMed:15037600).
Mediates dissociation of the ternary complex containing STX5A, NSFL1C and VCP (PubMed:12473691, PubMed:15037600).
Also involved in DNA repair following phosphorylation by ATM or ATR: acts by catalyzing deubiquitination of SPRTN, thereby promoting SPRTN recruitment to chromatin and subsequent proteolytic cleavage of covalent DNA-protein cross-links (DPCs) (By similarity).
Hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains (By similarity).
Necessary for VCP-mediated reassembly of Golgi stacks after mitosis (PubMed:12473691, PubMed:15037600).
Plays a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (PubMed:12473691, PubMed:15037600).
Mediates dissociation of the ternary complex containing STX5A, NSFL1C and VCP (PubMed:12473691, PubMed:15037600).
Also involved in DNA repair following phosphorylation by ATM or ATR: acts by catalyzing deubiquitination of SPRTN, thereby promoting SPRTN recruitment to chromatin and subsequent proteolytic cleavage of covalent DNA-protein cross-links (DPCs) (By similarity).
Hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains (By similarity).
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 215 | |||||
Sequence: D | ||||||
Active site | 218 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 353 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | Golgi stack | |
Cellular Component | nucleus | |
Cellular Component | synapse | |
Molecular Function | cysteine-type deubiquitinase activity | |
Biological Process | DNA damage response | |
Biological Process | endoplasmic reticulum membrane fusion | |
Biological Process | Golgi organization | |
Biological Process | Golgi reassembly | |
Biological Process | protein deubiquitination | |
Biological Process | protein K11-linked deubiquitination | |
Biological Process | protein K48-linked deubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | protein-DNA covalent cross-linking repair | |
Biological Process | proteolysis | |
Biological Process | regulation of protein localization to chromatin |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDeubiquitinating protein VCPIP1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ8CF97
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with Golgi stacks and endoplasmic reticulum (PubMed:12473691).
Displays cytoplasmic to nuclear translocation in response to DNA-protein cross-links (DPCs)-inducing agents (By similarity).
Displays cytoplasmic to nuclear translocation in response to DNA-protein cross-links (DPCs)-inducing agents (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 218 | Loss of deubiquitinating activity and ability to promote VCP-mediated Golgi membrane fusion. | ||||
Sequence: C → A or S |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000065771 | 1-1221 | Deubiquitinating protein VCPIP1 | |||
Sequence: MSQPPPPPPLPPPPPPPEAPQTSSSLAAAATPGGLSKRRDRRILSGSCPDPKCQARLFFPASGSVSIECTECGQRHEQQQLLGVEEVTDPDVVLHNLLRNALLGVTGAPKKNTELVKVMGLSNYHCKLLSPILARYGMDKQTGRAKLLRDMNQGELFDCALLGDRAFLIEPEHVNTVGYGKDRSGSLLYLHDTLEDIKRANKSQECLIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLKQHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFLPGLIPAEKCTGRDGHLNKPICIAWSSSGRNHYIPLVGIKGAALPKLPMNLLPKAWGVPQDLIKKYIKLEEDGGCVIGGDRSLQDKYLLRLVAAMEEVFMDKHGIHPSLVADVHQYFYRRTGVIGVQPEEVTAAAKKAVMDNRLHKCLLCGALSELHVPPEWLAPGGKLYNLAKSTHGQLRPDKNYSFPLNNLVCSYDPVKDVLLPDYGLSNLTACNWCHGTSVRRVRGDGSIVYLDGDRTNSRSTGGKCGCGFKHFWEGKEYDNLPEAFPITLEWGGRVVRETVYWFQYESDPSLNSNVYDVAMKLVTKHFPGEFGSEILVQKVVHTILHQTAKKNPDDYTPVNIDGAHAQRIGDVQGQELESQLPTKIILTGQKTKTLHKEELNMSKTERTIQQNITEQASVMQKRKTEKLKQEQKGQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEKKIRITTNDGRQSMVTLKSSTTFFELQESIAREFNIPPYLQCIRYGFPPKELMPPQAGMEKEPVPLQHGDRITIEILKGKAEGGPSTAAHSAHTVRQEEIAVTGKLSSKELQEQADKEMYSLCLLATLMGEDVWSYAKGLPHMFQQGGVFYNIMKKTMGMADGKHCTFPHLPGKTFVYNASEDRLELCVDAAGHFPIGPDVEDLVKEAVSQVRAEATTRSRESSPSHGLLKLGSGGVVKKKSEQLHNVTAFQGKGHSLGTASSNPHMDPRARETLAVRKHNTGTDFSNSSIKTEPPVFTAASSNSELIRIAPGVVTMRDGRQIDPDVVEAQRKKLQEMVSSIQASMDKHLRDQSTEQTPSDLSQRKVEAVSSSVRPGNLQTGLPESFSLTGGTENLNTETTDSRVADVLGAAFATRSKAQKENSMEEPEEMDSQDAETTNTTEPMDHS | ||||||
Modified residue | 407 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 746 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 756 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 762 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 767 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 993 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 997 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1076 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1197 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1206 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated at Ser-1206 by ATM or ATR following induction of covalent DNA-protein cross-links (DPCs).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binds VCP and the ternary complex containing STX5A, NSFL1C and VCP.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Pro residues | ||||
Sequence: MSQPPPPPPLPPPPPPPEAPQ | ||||||
Region | 1-40 | Disordered | ||||
Sequence: MSQPPPPPPLPPPPPPPEAPQTSSSLAAAATPGGLSKRRD | ||||||
Domain | 207-360 | OTU | ||||
Sequence: LIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLKQHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFLPGLIPAEKCTGRDGHLNKPICIAWSSSGRNHYIPLVGI | ||||||
Region | 724-778 | Disordered | ||||
Sequence: SVMQKRKTEKLKQEQKGQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEKKIRI | ||||||
Compositional bias | 740-774 | Polar residues | ||||
Sequence: GQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEK | ||||||
Region | 988-1009 | Disordered | ||||
Sequence: EATTRSRESSPSHGLLKLGSGG | ||||||
Region | 1117-1177 | Disordered | ||||
Sequence: ASMDKHLRDQSTEQTPSDLSQRKVEAVSSSVRPGNLQTGLPESFSLTGGTENLNTETTDSR | ||||||
Compositional bias | 1129-1177 | Polar residues | ||||
Sequence: EQTPSDLSQRKVEAVSSSVRPGNLQTGLPESFSLTGGTENLNTETTDSR | ||||||
Region | 1189-1221 | Disordered | ||||
Sequence: RSKAQKENSMEEPEEMDSQDAETTNTTEPMDHS |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,221
- Mass (Da)134,566
- Last updated2004-11-23 v2
- Checksum23487E853AD9FD4B
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Pro residues | ||||
Sequence: MSQPPPPPPLPPPPPPPEAPQ | ||||||
Sequence conflict | 7 | in Ref. 3; AAQ14350 | ||||
Sequence: P → L | ||||||
Sequence conflict | 158 | in Ref. 3; AAQ14350 | ||||
Sequence: D → N | ||||||
Sequence conflict | 603 | in Ref. 3; AAQ14350 | ||||
Sequence: R → K | ||||||
Sequence conflict | 652 | in Ref. 3; AAQ14350 | ||||
Sequence: H → L | ||||||
Sequence conflict | 675 | in Ref. 3; AAQ14350 | ||||
Sequence: I → V | ||||||
Compositional bias | 740-774 | Polar residues | ||||
Sequence: GQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEK | ||||||
Compositional bias | 1129-1177 | Polar residues | ||||
Sequence: EQTPSDLSQRKVEAVSSSVRPGNLQTGLPESFSLTGGTENLNTETTDSR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB045378 EMBL· GenBank· DDBJ | BAC44841.2 EMBL· GenBank· DDBJ | mRNA | ||
AF289091 EMBL· GenBank· DDBJ | AAQ14350.1 EMBL· GenBank· DDBJ | mRNA |