VAV1
Proto-oncogene vav
Also known as: VAV, VAV_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P15498
- Gene
- VAV1
- Ensembl
- ENSG00000141968
- Chromosome
- 19
- Canonical length
- 845 aa
- Protein class
- Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Cytosol
OverviewNCBI Gene
This gene is a member of the VAV gene family. The VAV proteins are guanine nucleotide exchange factors (GEFs) for Rho family GTPases that activate pathways leading to actin cytoskeletal rearrangements and transcriptional alterations. The encoded protein is important in hematopoiesis, playing a role in T-cell and B-cell development and activation. The encoded protein has been identified as the specific binding partner of Nef proteins from HIV-1. Coexpression and binding of these partners initiates profound morphological changes, cytoskeletal rearrangements and the JNK/SAPK signaling cascade, leading to increased levels of viral transcription and replication. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Apr 2012]
Canonical amino-acid sequenceUniProt
845 residues, UniProt reviewed canonical sequence.
>P15498|VAV1
1 MELWRQCTHW LIQCRVLPPS HRVTWDGAQV CELAQALRDG VLLCQLLNNL LPHAINLREV
61 NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF DVQDFGKVIY TLSALSWTPI
121 AQNRGIMPFP TEEESVGDED IYSGLSDQID DTVEEDEDLY DCVENEEAEG DEIYEDLMRS
181 EPVSMPPKMT EYDKRCCCLR EIQQTEEKYT DTLGSIQQHF LKPLQRFLKP QDIEIIFINI
241 EDLLRVHTHF LKEMKEALGT PGAANLYQVF IKYKERFLVY GRYCSQVESA SKHLDRVAAA
301 REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQEA MEKENLRLAL
361 DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLAHY GRPKIDGELK ITSVERRSKM
421 DRYAFLLDKA LLICKRRGDS YDLKDFVNLH SFQVRDDSSG DRDNKKWSHM FLLIEDQGAQ
481 GYELFFKTRE LKKKWMEQFE MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF
541 YQGYRCHRCR ASAHKECLGR VPPCGRHGQD FPGTMKKDKL HRRAQDKKRN ELGLPKMEVF
601 QEYYGLPPPP GAIGPFLRLN PGDIVELTKA EAEQNWWEGR NTSTNEIGWF PCNRVKPYVH
661 GPPQDLSVHL WYAGPMERAG AESILANRSD GTFLVRQRVK DAAEFAISIK YNVEVKHIKI
721 MTAEGLYRIT EKKAFRGLTE LVEFYQQNSL KDCFKSLDTT LQFPFKEPEK RTISRPAVGS
781 TKYFGTAKAR YDFCARDRSE LSLKEGDIIK ILNKKGQQGW WRGEIYGRVG WFPANYVEED
841 YSEYCLocalizationUniProt · AlphaFold · HPA
Whether an antibody against VAV1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.29
- Highest tissue expression
- 51 nTPM
Expression across tissuesHPA
Tissue
- bone marrow: 51 nTPM
- lymph node: 44 nTPM
- thymus: 43 nTPM
- spleen: 41 nTPM
- tonsil: 37 nTPM
- appendix: 34 nTPM
Single-cell type
- neutrophils: 913 nCPM
- neutrophil progenitors: 284 nCPM
- tuft cells: 242 nCPM
- monocytes: 178 nCPM
- microglia: 168 nCPM
- mast cells: 132 nCPM
Immune cell
- neutrophil: 41 nTPM
- non-classical monocyte: 40 nTPM
- intermediate monocyte: 30 nTPM
- gdT-cell: 22 nTPM
- eosinophil: 20 nTPM
- memory CD8 T-cell: 19 nTPM
Brain region
- white matter: 13 nTPM
- medulla oblongata: 11 nTPM
- thalamus: 9.9 nTPM
- pons: 9.5 nTPM
- spinal cord: 8.2 nTPM
- cerebral cortex: 7.5 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.23
- gnomAD pLI
- 1
- gnomAD missense Z
- 3.86
- DepMap mean gene effect
- -0.05
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- B cell proliferation
- cell migration
- cellular response to xenobiotic stimulus
- Fc-epsilon receptor signaling pathway
- Fc-gamma receptor signaling pathway involved in phagocytosis
- G protein-coupled receptor signaling pathway
- immune response-regulating cell surface receptor signaling pathway
- integrin-mediated signaling pathway
- natural killer cell activation
- natural killer cell mediated cytotoxicity
- neutrophil chemotaxis
- platelet activation
- positive regulation of natural killer cell mediated cytotoxicity
- positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
- reactive oxygen species metabolic process
- regulation of cell size
- regulation of small GTPase mediated signal transduction
- small GTPase-mediated signal transduction
- T cell costimulation
- T cell differentiation
- vascular endothelial growth factor receptor signaling pathway
Molecular functions
- guanyl-nucleotide exchange factor activity
- phosphorylation-dependent protein binding
- phosphotyrosine residue binding
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Dbl homology domain
- SH2 domain
- Guanine-nucleotide dissociation stimulator, CDC24, conserved site
- SH3 domain
- Calponin homology domain
- Pleckstrin homology domain
- Protein kinase C-like, phorbol ester/diacylglycerol-binding domain
- Smooth muscle protein/calponin
- PH-like domain superfamily
- CASAMP, second calponin-homology domain
- Dbl homology (DH) domain superfamily
- SH3-like domain superfamily
- SH2 domain superfamily
- CH domain superfamily
- Vav, PH domain
- SH2 domain
- SH3 domain
- Phorbol esters/diacylglycerol binding domain (C1 domain)
- PH domain
- RhoGEF domain
- CAMSAP CH domain
- VAV1 protein, second SH3 domain
- VAV1 protein, first SH3 domain
- VAV1, SH2 domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of VAV1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads VAV1 as an antibody target. Whether an autoantibody or antibody against VAV1 could matter depends on whether native VAV1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
VAV1 is annotated at the cell surface, where native VAV1 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label VAV1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
Loading the interactive Seroatlas protein explorer...