Q96JH7 · VCIP1_HUMAN
- ProteinDeubiquitinating protein VCPIP1
- GeneVCPIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1222 (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:32649882).
Necessary for VCP-mediated reassembly of Golgi stacks after mitosis (By similarity).
Plays a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity).
Mediates dissociation of the ternary complex containing STX5A, NSFL1C and VCP (By similarity).
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) (PubMed:32649882).
Hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains (PubMed:23827681).
Necessary for VCP-mediated reassembly of Golgi stacks after mitosis (By similarity).
Plays a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity).
Mediates dissociation of the ternary complex containing STX5A, NSFL1C and VCP (By similarity).
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) (PubMed:32649882).
Hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains (PubMed:23827681).
(Microbial infection) Regulates the duration of C.botulinum neurotoxin type A (BoNT/A) intoxication by catalyzing deubiquitination of Botulinum neurotoxin A light chain (LC), thereby preventing LC degradation by the proteasome, and accelerating botulinum neurotoxin intoxication in patients.
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 216 | |||||
Sequence: D | ||||||
Active site | 219 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 354 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | Golgi stack | |
Cellular Component | nucleus | |
Molecular Function | cysteine-type deubiquitinase activity | |
Biological Process | DNA damage response | |
Biological Process | endoplasmic reticulum membrane fusion | |
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 > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96JH7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with Golgi stacks and endoplasmic reticulum (By similarity).
Displays cytoplasmic to nuclear translocation in response to DNA-protein cross-links (DPCs)-inducing agents (PubMed:32649882).
Displays cytoplasmic to nuclear translocation in response to DNA-protein cross-links (DPCs)-inducing agents (PubMed:32649882).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 219 | Loss of deubiquitinating activity and ability to deubiquitinate SPRTN. | ||||
Sequence: C → A | ||||||
Mutagenesis | 1207 | Abolished phosphorylation in response to covalent DNA-protein cross-links (DPCs). | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,005 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000065769 | 1-1222 | UniProt | Deubiquitinating protein VCPIP1 | |||
Sequence: MSQPPPPPPPLPPPPPPPEAPQTPSSLASAAASGGLLKRRDRRILSGSCPDPKCQARLFFPASGSVSIECTECGQRHEQQQLLGVEEVTDPDVVLHNLLRNALLGVTGAPKKNTELVKVMGLSNYHCKLLSPILARYGMDKQTGRAKLLRDMNQGELFDCALLGDRAFLIEPEHVNTVGYGKDRSGSLLYLHDTLEDIKRANKSQECLIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLKQHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFLPGLIPAEKCTGKDGHLNKPICIAWSSSGRNHYIPLVGIKGAALPKLPMNLLPKAWGVPQDLIKKYIKLEEDGGCVIGGDRSLQDKYLLRLVAAMEEVFMDKHGIHPSLVADVHQYFYRRTGVIGVQPEEVTAAAKKAVMDNRLHKCLLCGALSELHVPPEWLAPGGKLYNLAKSTHGQLRTDKNYSFPLNNLVCSYDSVKDVLVPDYGMSNLTACNWCHGTSVRKVRGDGSIVYLDGDRTNSRSTGGKCGCGFKHFWDGKEYDNLPEAFPITLEWGGRVVRETVYWFQYESDSSLNSNVYDVAMKLVTKHFPGEFGSEILVQKVVHTILHQTAKKNPDDYTPVNIDGAHAQRVGDVQGQESESQLPTKIILTGQKTKTLHKEELNMSKTERTIQQNITEQASVMQKRKTEKLKQEQKGQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEKKIRITTNDGRQSMVTLKSSTTFFELQESIAREFNIPPYLQCIRYGFPPKELMPPQAGMEKEPVPLQHGDRITIEILKSKAEGGQSAAAHSAHTVKQEDIAVTGKLSSKELQEQAEKEMYSLCLLATLMGEDVWSYAKGLPHMFQQGGVFYSIMKKTMGMADGKHCTFPHLPGKTFVYNASEDRLELCVDAAGHFPIGPDVEDLVKEAVSQVRAEATTRSRESSPSHGLLKLGSGGVVKKKSEQLHNVTAFQGKGHSLGTASGNPHLDPRARETSVVRKHNTGTDFSNSSTKTEPSVFTASSSNSELIRIAPGVVTMRDGRQLDPDLVEAQRKKLQEMVSSIQASMDRHLRDQSTEQSPSDLPQRKTEVVSSSAKSGSLQTGLPESFPLTGGTENLNTETTDGCVADALGAAFATRSKAQRGNSVEELEEMDSQDAEMTNTTEPMDHS | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 131 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 185 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 408 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 747 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 747 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 749 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 756 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 757 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 757 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 761 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 763 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 763 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 767 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 768 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 768 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 994 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 994 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 997 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 998 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 998 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1000 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1064 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1077 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1128 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1198 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1198 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1207 | UniProt | Phosphoserine; by ATM | ||||
Sequence: S |
Post-translational modification
Phosphorylated at Ser-1207 by ATM or ATR following induction of covalent DNA-protein cross-links (DPCs).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Binds VCP and the ternary complex containing STX5A, NSFL1C and VCP.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96JH7 | PLAAT5 Q96KN8 | 3 | EBI-1995920, EBI-10753637 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Pro residues | ||||
Sequence: MSQPPPPPPPLPPPPPPPEAPQT | ||||||
Region | 1-36 | Disordered | ||||
Sequence: MSQPPPPPPPLPPPPPPPEAPQTPSSLASAAASGGL | ||||||
Domain | 208-361 | OTU | ||||
Sequence: LIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLKQHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFLPGLIPAEKCTGKDGHLNKPICIAWSSSGRNHYIPLVGI | ||||||
Region | 725-776 | Disordered | ||||
Sequence: SVMQKRKTEKLKQEQKGQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEKK | ||||||
Compositional bias | 741-775 | Polar residues | ||||
Sequence: GQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEK | ||||||
Region | 989-1009 | Disordered | ||||
Sequence: EATTRSRESSPSHGLLKLGSG | ||||||
Region | 1024-1074 | Disordered | ||||
Sequence: AFQGKGHSLGTASGNPHLDPRARETSVVRKHNTGTDFSNSSTKTEPSVFTA | ||||||
Compositional bias | 1054-1074 | Polar residues | ||||
Sequence: HNTGTDFSNSSTKTEPSVFTA | ||||||
Region | 1113-1175 | Disordered | ||||
Sequence: VSSIQASMDRHLRDQSTEQSPSDLPQRKTEVVSSSAKSGSLQTGLPESFPLTGGTENLNTETT | ||||||
Compositional bias | 1130-1175 | Polar residues | ||||
Sequence: EQSPSDLPQRKTEVVSSSAKSGSLQTGLPESFPLTGGTENLNTETT | ||||||
Region | 1188-1222 | Disordered | ||||
Sequence: ATRSKAQRGNSVEELEEMDSQDAEMTNTTEPMDHS |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,222
- Mass (Da)134,321
- Last updated2004-02-16 v2
- Checksum5CE99D723386782D
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Pro residues | ||||
Sequence: MSQPPPPPPPLPPPPPPPEAPQT | ||||||
Sequence conflict | 169 | in Ref. 2; CAD89944 | ||||
Sequence: L → P | ||||||
Sequence conflict | 437 | in Ref. 2; CAD89944 | ||||
Sequence: Q → R | ||||||
Compositional bias | 741-775 | Polar residues | ||||
Sequence: GQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEK | ||||||
Sequence conflict | 811 | in Ref. 3; AAH49379 | ||||
Sequence: P → F | ||||||
Sequence conflict | 927 | in Ref. 3 | ||||
Sequence: Missing | ||||||
Sequence conflict | 988 | in Ref. 3; AAH49379 | ||||
Sequence: A → S | ||||||
Compositional bias | 1054-1074 | Polar residues | ||||
Sequence: HNTGTDFSNSSTKTEPSVFTA | ||||||
Compositional bias | 1130-1175 | Polar residues | ||||
Sequence: EQSPSDLPQRKTEVVSSSAKSGSLQTGLPESFPLTGGTENLNTETT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB058753 EMBL· GenBank· DDBJ | BAB47479.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL834476 EMBL· GenBank· DDBJ | CAD39135.1 EMBL· GenBank· DDBJ | mRNA | ||
AL832606 EMBL· GenBank· DDBJ | CAD89944.1 EMBL· GenBank· DDBJ | mRNA | ||
BC049379 EMBL· GenBank· DDBJ | AAH49379.1 EMBL· GenBank· DDBJ | mRNA | ||
BC094799 EMBL· GenBank· DDBJ | AAH94799.1 EMBL· GenBank· DDBJ | mRNA | ||
AK026785 EMBL· GenBank· DDBJ | BAB15552.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |