| IED ID | IndEnz0002009830 |
| Enzyme Type ID | protease009830 |
| Protein Name |
Deubiquitinating protein VCPIP1 EC 3.4.19.12 Valosin-containing protein p97/p47 complex-interacting protein 1 Valosin-containing protein p97/p47 complex-interacting protein p135 VCP/p47 complex-interacting 135-kDa protein |
| Gene Name | Vcpip1 Vcip135 |
| Organism | Rattus norvegicus (Rat) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MSQPPPPPPLPPPPPPPEAPQTSSSLAAAATPGGLSKRRDRRILSGSCPDPKCQARLFFPASGSVSIECTECGQRHEQQQLLGVEEVTDPDVVLHNLLRNALLGVTGAPKKNTELVKVMGLSNYHCKLLSPILARYGMDKQTGRAKLLRDMNQGELFDCALLGDRAFLIEPEHVNTVGYGKDRSGSLLYLHDTLEDIKRANKSQECLIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLKQHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFLPGLIPAEKCTGRDGHLNKPICIAWSSSGRNHYIPLVGIKGAALPKLPMNLLPKAWGVPQDLIKKYIKLEEDGGCVIGGDRSLQDKYLLRLVAAMEEVFMDKHGIHPSLVADVHQYFYRRTGVIGVQPEEVTAAAKKAVMDNRLHKCLLCGALSELHVPPEWLAPGGKLYNLAKSTHGQLRPDKNYSFPLNNLVCSYDPVKDVLLPDYGLSNLTACNWCHGTSVRRVRGDGSIVYLDGDRTNSRSTGGKCGCGFKHFWEGKEYDNLPEAFPITLEWGGRVVRETVYWFQYESDPSLNSNVYDVAMKLVTKHFPGEFGSEILVQKVVHTILHQTAKKNPDDYTPVNIDGAHAQRIGDVQGQELESQLPTKIILTGQKTKTLHKEELNMSKTERTIQQNITEQASVMQKRKTEKLKQEQKGQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEKKIRITTNDGRQSMVTLKSSTTFFELQESIAREFNIPPYLQCIRYGFPPKELMPPQAGMEKEPVPLQHGDRITIEILKGKAEGGPSTAAHSAHTVRQEEIAVTGKLSSKELQEQADKEMYSLCLLATLMGEDVWSYAKGLPHMFQQGGVFYNIMKKTMGMADGKHCTFPHLPGKTFVYNASEDRLELCVDAAGHFPIGPDVEDLVKEAVSQVRAEATTRSRESSPSHGLLKLGSGGVVKKKSEQLHNVTAFQGKGHSLGTASSNPHMDPRARETLAVRKHNTGTDFSNSSIKTEPPVFTAASSNSELIRIAPGVVTMRDGRQIDPDVVEAQRKKLQEMVSSIQASMDKHLRDQSTEQTPSDLSQRKVEAVSSSVRPGNLQTGLPESFSLTGGTENLNTETTDSRVADVLGAAFATRSKAQKENSMEEPEEMDSQDAETTNTTEPMDHS |
| Enzyme Length | 1221 |
| Uniprot Accession Number | Q8CF97 |
| Absorption | |
| Active Site | ACT_SITE 215; /evidence=ECO:0000250|UniProtKB:Q96FW1; ACT_SITE 218; /note=Nucleophile; /evidence=ECO:0000305|PubMed:15037600; ACT_SITE 353; /evidence=ECO:0000250|UniProtKB:Q96FW1 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:15037600}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme 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). {ECO:0000250|UniProtKB:Q96JH7, ECO:0000269|PubMed:12473691, ECO:0000269|PubMed:15037600}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (2); Chain (1); Compositional bias (3); Domain (1); Helix (1); Modified residue (10); Mutagenesis (1); Region (5); Sequence conflict (5); Turn (3) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;DNA damage;DNA repair;Direct protein sequencing;Endoplasmic reticulum;Golgi apparatus;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96JH7}. Cytoplasm {ECO:0000250|UniProtKB:Q96JH7}. Endoplasmic reticulum {ECO:0000269|PubMed:12473691}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:12473691}. 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). {ECO:0000250|UniProtKB:Q96JH7, ECO:0000269|PubMed:12473691}. |
| Modified Residue | MOD_RES 407; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q96JH7; MOD_RES 746; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 756; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96JH7; MOD_RES 762; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q96JH7; MOD_RES 767; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96JH7; MOD_RES 993; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96JH7; MOD_RES 997; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96JH7; MOD_RES 1076; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96JH7; MOD_RES 1197; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 1206; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96JH7 |
| Post Translational Modification | PTM: Phosphorylated at Ser-1206 by ATM or ATR following induction of covalent DNA-protein cross-links (DPCs). {ECO:0000250|UniProtKB:Q96JH7}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 2MX2; |
| Mapped Pubmed ID | 25904330; |
| Motif | |
| Gene Encoded By | |
| Mass | 134,566 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |