Protein detail
VCIP1
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)
Entry name VCIP1 | UniProt ID | EVMP confidence score 0.28 |
Supporting publications (n) 4 | Transmembrane count | Protein classification EnzymesPlasma proteinsPredicted intracellular proteins |
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.70High >= 0.60Medium >= 0.40Low >= 0.30Basic Information
Protein Names
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)
Protein Class (3)
EnzymesPlasma proteinsPredicted intracellular proteins
Protein Function (3)
- Enzymes
- Predicted intracellular proteins
- ENZYME proteins:Hydrolases
Ensembl
Entrez Gene Symbol
Gene Synonym (4)
DUBA3FLJ23132KIAA1850VCIP135
Gene Description
Valosin containing protein interacting protein 1
Chromosome
8
Position
66628487-66667231
Supporting publications (n)
4
EVMP confidence score
0.28
Fluorescence & Localization
Tissue SpecificlungCell SpecificAlveolar cells type 1Single-Nuclei Brain Specificcerebellar inhibitory
Function & Pathway
Protein Function (3)
- Enzymes
- Predicted intracellular proteins
- ENZYME proteins:Hydrolases
Cellular Component (4)
Molecular Function (2)
Biological Process (3)
Reactome (3)
Mediation Categories
Metabolism mediation
Relations & Evidence13
Enzyme-Mediated Modification (3)
3 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| VCPIP1 | CDK1 | P06493 | S | 768 | phosphorylation | Sparser_ProtMapperSIGNORProtMapperRLIMS-P_ProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapper | ProtMapper:23500464SIGNOR:23500464 |
| VCPIP1 | CDK1 | P06493 | T | 761 | phosphorylation | Sparser_ProtMapperSIGNORProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapper | ProtMapper:23500464SIGNOR:23500464 |
| VCPIP1 | CDK1 | P06493 | S | 131 | phosphorylation | RLIMS-P_ProtMapperReactome_ProtMapperREACH_ProtMapperProtMapper | ProtMapper:25904330 |
Ligand-Receptor Signaling (5)
5 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | LOCATE | |||||
| intracellular | intracellular | ComPPI | |||||
| intracellular | intracellular | GO_Intercell | |||||
| intracellular | intracellular | UniProt_location | |||||
| intracellular | intracellular | OmniPath |
Regulatory Interaction Network (2)
2 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| CDK1 | P06493 | VCIP1 | Q96JH7 | Yes | Yes | Sparser_ProtMapperPhosphoSite_norefSIGNORiPTMnetProtMapperRLIMS-P_ProtMapperReactome_ProtMapperSIGNOR_ProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapper | SIGNOR:23500464ProtMapper:23500464ProtMapper:25904330PhosphoSite:23500464 | |
| VCIP1 | Q96JH7 | TERA | P55072 | Yes | Yes | HPRDHINTSIGNORBioGRID | HINT:21811234HPRD:12473691HINT:35271311BioGRID:24163436HINT:19615732HINT:12473691SIGNOR:23500464HINT:23500464 |
Protein Complex Composition (2)
2 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| VCP-VCPIP1 AAA ATPase complex | VCPVCPIP1 | P55072Q96JH7 | 6:3 | ComplexPortalPDB | PDB:8ykaintact:EBI-46425257PDB:9mq6PDB:9dil | 24163436198187072881900936825201147552922173386 |
| ARHGAP39CNKSR3SAMD10SAMD12VCPIP1 | Q6P9H4Q8N8I0Q96JH7Q9BYL1Q9C0H5 | 0:0:0:0:0 | hu.MAP2 |
Sequence, Structure & Domains
Sequences
Length
1,222
Mass
134,321
Sequence
MSQPPPPPPPLPPPPPPPEAPQTPSSLASAAASGGLLKRRDRRILSGSCPDPKCQARLFFPASGSVSIECTECGQRHEQQQLLGVEEVTDPDVVLHNLLRNALLGVTGAPKKNTELVKVMGLSNYHCKLLSPILARYGMDKQTGRAKLLRDMNQGELFDCALLGDRAFLIEPEHVNTVGYGKDRSGSLLYLHDTLEDIKRANKSQECLIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLKQHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFLPGLIPAEKCTGKDGHLNKPICIAWSSSGRNHYIPLVGIKGAALPKLPMNLLPKAWGVPQDLIKKYIKLEEDGGCVIGGDRSLQDKYLLRLVAAMEEVFMDKHGIHPSLVADVHQYFYRRTGVIGVQPEEVTAAAKKAVMDNRLHKCLLCGALSELHVPPEWLAPGGKLYNLAKSTHGQLRTDKNYSFPLNNLVCSYDSVKDVLVPDYGMSNLTACNWCHGTSVRKVRGDGSIVYLDGDRTNSRSTGGKCGCGFKHFWDGKEYDNLPEAFPITLEWGGRVVRETVYWFQYESDSSLNSNVYDVAMKLVTKHFPGEFGSEILVQKVVHTILHQTAKKNPDDYTPVNIDGAHAQRVGDVQGQESESQLPTKIILTGQKTKTLHKEELNMSKTERTIQQNITEQASVMQKRKTEKLKQEQKGQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEKKIRITTNDGRQSMVTLKSSTTFFELQESIAREFNIPPYLQCIRYGFPPKELMPPQAGMEKEPVPLQHGDRITIEILKSKAEGGQSAAAHSAHTVKQEDIAVTGKLSSKELQEQAEKEMYSLCLLATLMGEDVWSYAKGLPHMFQQGGVFYSIMKKTMGMADGKHCTFPHLPGKTFVYNASEDRLELCVDAAGHFPIGPDVEDLVKEAVSQVRAEATTRSRESSPSHGLLKLGSGGVVKKKSEQLHNVTAFQGKGHSLGTASGNPHLDPRARETSVVRKHNTGTDFSNSSTKTEPSVFTASSSNSELIRIAPGVVTMRDGRQLDPDLVEAQRKKLQEMVSSIQASMDRHLRDQSTEQSPSDLPQRKTEVVSSSAKSGSLQTGLPESFPLTGGTENLNTETTDGCVADALGAAFATRSKAQRGNSVEELEEMDSQDAEMTNTTEPMDHS
3D Structural Models
Turn
114..116; 149..153; 155..158; 178..180; 258..260; 371..373; 511..513; 521..524; 530..532; 669..671
Helix
124..128; 131..134; 160..165; 172..174; 187..190; 192..201; 219..228; 235..248; 250..257; 263..272; 290..298; 309..313; 329..332; 384..388; 407..425; 429..438; 441..443; 450..462; 482..484; 490..499; 616..618; 622..633; 640..655
Beta Strand
137..139; 141..143; 146..148; 175..177; 209..211; 303..306; 337..339; 343..347; 355..361; 377..380; 466..472; 475..477; 516..520; 525..528; 539..541; 546..549; 562..566; 576..580; 583..587; 590..598; 601..609
3D Structure
Electron microscopy (3)
Domain & Motif Annotations
Compositional Bias
1..21; Pro residues; 25..36; Low complexity; 755..771; Low complexity; 1041..1050; Basic and acidic residues; 1057..1074; Polar residues; 1143..1157; Polar residues; 1163..1175; Low complexity; 1200..1209; Acidic residues; 1210..1222; Polar residues
Domain (FT)
208..361; OTU
Region
1..36; Disordered; 725..776; Disordered; 989..1009; Disordered; 1024..1074; Disordered; 1113..1175; Disordered; 1188..1222; Disordered
Clinical Relevance
Antibody
Interaction Protein (2)
ENSG00000165280ENSG00000167671
Interaction Count
2
Interaction Dataset (2)
biogrid_opencellbiogrid_bioplex
Supporting Publications4
| PMID | Title | Related sentences |
|---|---|---|
| 29148239 | Metabolic Signature of Microvesicles from Umbilical Cord Mesenchymal Stem Cells of Preterm and Term Infants. | No related sentences available |
| 32089743 | Human umbilical cord mesenchymal stromal cells-derived extracellular vesicles exert potent bone protective effects by CLEC11A-mediated regulation of bone metabolism. | No related sentences available |
| 34817906 | Proteomic dissection of large extracellular vesicle surfaceome unravels interactive surface platform. | No related sentences available |
| 38321535 | Identification of specific markers for human pluripotent stem cell-derived small extracellular vesicles. | No related sentences available |