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Protein

Proto-oncogene vav

Gene

Vav1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri515 – 564Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST50

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • Rac guanyl-nucleotide exchange factor activity Source: MGI
  • Rho guanyl-nucleotide exchange factor activity Source: MGI

GO - Biological processi

  • G-protein coupled receptor signaling pathway Source: MGI
  • immune response Source: MGI
  • integrin-mediated signaling pathway Source: MGI
  • intracellular signal transduction Source: MGI
  • neutrophil chemotaxis Source: MGI
  • phagocytosis Source: MGI
  • platelet activation Source: Reactome
  • positive regulation of cell adhesion Source: MGI
  • positive regulation of GTPase activity Source: MGI
  • positive regulation of natural killer cell mediated cytotoxicity Source: MGI
  • reactive oxygen species metabolic process Source: MGI
  • regulation of cell size Source: Ensembl
  • regulation of GTPase activity Source: MGI
  • regulation of Rho protein signal transduction Source: InterPro
  • small GTPase mediated signal transduction Source: InterPro
  • T cell activation Source: MGI
  • T cell differentiation Source: MGI
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-2871809. FCERI mediated Ca+2 mobilization.
R-MMU-389359. CD28 dependent Vav1 pathway.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-5218920. VEGFR2 mediated vascular permeability.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-912631. Regulation of signaling by CBL.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene vav
Alternative name(s):
p95vav
Gene namesi
Name:Vav1
Synonyms:Vav
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:98923. Vav1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: MGI
  • cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi529C → S: Abolishes transforming activity. 1 Publication1
Mutagenesisi532C → S: Abolishes transforming activity. 1 Publication1
Mutagenesisi554H → D: Abolishes transforming activity. 1 Publication1

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000809811 – 845Proto-oncogene vavAdd BLAST845

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei826PhosphotyrosineBy similarity1
Modified residuei844PhosphotyrosineCombined sources1

Post-translational modificationi

Phosphorylated by FYN (By similarity). Phosphorylated on tyrosine residues by HCK in response to IFNG and bacterial lipopolysaccharide (LPS).By similarity3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP27870.
PaxDbiP27870.
PeptideAtlasiP27870.
PRIDEiP27870.

PTM databases

iPTMnetiP27870.
PhosphoSitePlusiP27870.

Expressioni

Tissue specificityi

Widely expressed in hematopoietic cells but not in other cell types. Found in the spleen and lung.1 Publication

Gene expression databases

BgeeiENSMUSG00000034116.
CleanExiMM_VAV1.
ExpressionAtlasiP27870. baseline and differential.
GenevisibleiP27870. MM.

Interactioni

Subunit structurei

Interacts with SHB (By similarity). Interacts with APS, DOCK2, GRB2, GRB3, DOCK2, SLA, TEC and ZNF655/VIK. Interacts with SIAH2; without leading to its degradation. Associates with BLNK, PLCG1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB; which inhibits tyrosine phosphorylation and down-regulates activity (PubMed:10646609, PubMed:10646608). May interact with CCPG1 (PubMed:17000758). Interacts with CLNK (PubMed:11463797). Interacts with THEMIS2 (PubMed:20644716). Interacts with NEK3 and this interaction is prolactin-dependent. Interacts with ITK. Interacts with PTK2B/PYK2 (By similarity). Interacts with HCK. Interacts with PTK2B/PYK2. Interacts (via SH2 domain) with SYK (By similarity). Interacts with ANKRD54 (PubMed:19064729). Interacts with CD6 (PubMed:24584089).By similarity9 Publications

Protein-protein interaction databases

BioGridi204500. 7 interactors.
DIPiDIP-31010N.
IntActiP27870. 7 interactors.
MINTiMINT-85069.
STRINGi10090.ENSMUSP00000005889.

Structurei

Secondary structure

1845
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi170 – 177Combined sources8
Turni178 – 180Combined sources3
Helixi191 – 219Combined sources29
Helixi221 – 224Combined sources4
Turni225 – 227Combined sources3
Helixi230 – 237Combined sources8
Helixi240 – 259Combined sources20
Helixi261 – 263Combined sources3
Helixi266 – 273Combined sources8
Helixi276 – 278Combined sources3
Helixi279 – 300Combined sources22
Helixi302 – 316Combined sources15
Helixi322 – 325Combined sources4
Helixi328 – 333Combined sources6
Helixi336 – 346Combined sources11
Helixi350 – 389Combined sources40
Beta strandi390 – 392Combined sources3
Helixi397 – 400Combined sources4
Beta strandi402 – 412Combined sources11
Beta strandi420 – 437Combined sources18
Beta strandi440 – 448Combined sources9
Turni449 – 451Combined sources3
Beta strandi452 – 455Combined sources4
Beta strandi469 – 475Combined sources7
Beta strandi481 – 488Combined sources8
Helixi489 – 506Combined sources18
Turni509 – 512Combined sources4
Helixi513 – 515Combined sources3
Beta strandi518 – 521Combined sources4
Turni530 – 532Combined sources3
Beta strandi538 – 541Combined sources4
Beta strandi543 – 546Combined sources4
Turni547 – 549Combined sources3
Helixi555 – 560Combined sources6
Turni585 – 587Combined sources3
Beta strandi596 – 599Combined sources4
Beta strandi603 – 607Combined sources5
Helixi610 – 612Combined sources3
Beta strandi624 – 629Combined sources6
Beta strandi635 – 641Combined sources7
Turni642 – 644Combined sources3
Beta strandi647 – 651Combined sources5
Helixi652 – 654Combined sources3
Beta strandi655 – 657Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F5XNMR-A170-375[»]
1GCPX-ray2.10A/B/C/D595-660[»]
1GCQX-ray1.68C595-660[»]
1K1ZNMR-A583-660[»]
2KBTNMR-A784-844[»]
2VRWX-ray1.85B170-575[»]
ProteinModelPortaliP27870.
SMRiP27870.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27870.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 119CHPROSITE-ProRule annotationAdd BLAST119
Domaini194 – 373DHPROSITE-ProRule annotationAdd BLAST180
Domaini402 – 504PHPROSITE-ProRule annotationAdd BLAST103
Domaini617 – 660SH3 1PROSITE-ProRule annotationAdd BLAST44
Domaini671 – 765SH2PROSITE-ProRule annotationAdd BLAST95
Domaini782 – 842SH3 2PROSITE-ProRule annotationAdd BLAST61

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi33 – 99Leu-richAdd BLAST67

Domaini

The DH domain is involved in interaction with CCPG1.

Sequence similaritiesi

Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 2 SH3 domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri515 – 564Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST50

Keywords - Domaini

Repeat, SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiKOG2996. Eukaryota.
ENOG410XPH6. LUCA.
GeneTreeiENSGT00800000124085.
HOGENOMiHOG000234364.
HOVERGENiHBG018066.
InParanoidiP27870.
KOiK05730.
OMAiEKDNKKW.
OrthoDBiEOG091G01O3.
PhylomeDBiP27870.
TreeFamiTF316171.

Family and domain databases

CDDicd00029. C1. 1 hit.
Gene3Di1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR022613. CAMSAP_CH.
IPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR003096. SM22_calponin.
IPR028530. Vav.
[Graphical view]
PANTHERiPTHR22826:SF97. PTHR22826:SF97. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00888. SM22CALPONIN.
SMARTiSM00109. C1. 1 hit.
SM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27870-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELWRQCTHW LIQCRVLPPS HRVTWEGAQV CELAQALRDG VLLCQLLNNL
60 70 80 90 100
LPQAINLREV NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF
110 120 130 140 150
DVQDFGKVIY TLSALSWTPI AQNKGIMPFP TEDSALNDED IYSGLSDQID
160 170 180 190 200
DTAEEDEDLY DCVENEEAEG DEIYEDLMRL ESVPTPPKMT EYDKRCCCLR
210 220 230 240 250
EIQQTEEKYT DTLGSIQQHF MKPLQRFLKP QDMETIFVNI EELFSVHTHF
260 270 280 290 300
LKELKDALAG PGATTLYQVF IKYKERFLVY GRYCSQVESA SKHLDQVATA
310 320 330 340 350
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQDA
360 370 380 390 400
TEKENLRLAL DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLANY
410 420 430 440 450
GRPKIDGELK ITSVERRSKT DRYAFLLDKA LLICKRRGDS YDLKASVNLH
460 470 480 490 500
SFQVRDDSSG ERDNKKWSHM FLLIEDQGAQ GYELFFKTRE LKKKWMEQFE
510 520 530 540 550
MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF YQGYRCYRCR
560 570 580 590 600
APAHKECLGR VPPCGRHGQD FAGTMKKDKL HRRAQDKKRN ELGLPKMEVF
610 620 630 640 650
QEYYGIPPPP GAFGPFLRLN PGDIVELTKA EAEHNWWEGR NTATNEVGWF
660 670 680 690 700
PCNRVHPYVH GPPQDLSVHL WYAGPMERAG AEGILTNRSD GTYLVRQRVK
710 720 730 740 750
DTAEFAISIK YNVEVKHIKI MTSEGLYRIT EKKAFRGLLE LVEFYQQNSL
760 770 780 790 800
KDCFKSLDTT LQFPYKEPER RAISKPPAGS TKYFGTAKAR YDFCARDRSE
810 820 830 840
LSLKEGDIIK ILNKKGQQGW WRGEIYGRIG WFPSNYVEED YSEYC
Length:845
Mass (Da):98,137
Last modified:August 1, 1992 - v1
Checksum:i3666DCCD1C5229DA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29Q → E in AAA63402 (PubMed:2005887).Curated1
Sequence conflicti226R → L in BAC40436 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64361 mRNA. Translation: CAA45713.1.
AK088586 mRNA. Translation: BAC40436.1.
M59833 mRNA. Translation: AAA63402.1.
CCDSiCCDS28931.1.
PIRiA61187. TVMSVV.
RefSeqiNP_035821.3. NM_011691.4.
UniGeneiMm.248172.

Genome annotation databases

EnsembliENSMUST00000005889; ENSMUSP00000005889; ENSMUSG00000034116.
GeneIDi22324.
KEGGimmu:22324.
UCSCiuc008dep.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64361 mRNA. Translation: CAA45713.1.
AK088586 mRNA. Translation: BAC40436.1.
M59833 mRNA. Translation: AAA63402.1.
CCDSiCCDS28931.1.
PIRiA61187. TVMSVV.
RefSeqiNP_035821.3. NM_011691.4.
UniGeneiMm.248172.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F5XNMR-A170-375[»]
1GCPX-ray2.10A/B/C/D595-660[»]
1GCQX-ray1.68C595-660[»]
1K1ZNMR-A583-660[»]
2KBTNMR-A784-844[»]
2VRWX-ray1.85B170-575[»]
ProteinModelPortaliP27870.
SMRiP27870.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204500. 7 interactors.
DIPiDIP-31010N.
IntActiP27870. 7 interactors.
MINTiMINT-85069.
STRINGi10090.ENSMUSP00000005889.

PTM databases

iPTMnetiP27870.
PhosphoSitePlusiP27870.

Proteomic databases

EPDiP27870.
PaxDbiP27870.
PeptideAtlasiP27870.
PRIDEiP27870.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005889; ENSMUSP00000005889; ENSMUSG00000034116.
GeneIDi22324.
KEGGimmu:22324.
UCSCiuc008dep.2. mouse.

Organism-specific databases

CTDi7409.
MGIiMGI:98923. Vav1.

Phylogenomic databases

eggNOGiKOG2996. Eukaryota.
ENOG410XPH6. LUCA.
GeneTreeiENSGT00800000124085.
HOGENOMiHOG000234364.
HOVERGENiHBG018066.
InParanoidiP27870.
KOiK05730.
OMAiEKDNKKW.
OrthoDBiEOG091G01O3.
PhylomeDBiP27870.
TreeFamiTF316171.

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-2871809. FCERI mediated Ca+2 mobilization.
R-MMU-389359. CD28 dependent Vav1 pathway.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-5218920. VEGFR2 mediated vascular permeability.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-912631. Regulation of signaling by CBL.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP27870.
PROiP27870.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000034116.
CleanExiMM_VAV1.
ExpressionAtlasiP27870. baseline and differential.
GenevisibleiP27870. MM.

Family and domain databases

CDDicd00029. C1. 1 hit.
Gene3Di1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR022613. CAMSAP_CH.
IPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR003096. SM22_calponin.
IPR028530. Vav.
[Graphical view]
PANTHERiPTHR22826:SF97. PTHR22826:SF97. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00888. SM22CALPONIN.
SMARTiSM00109. C1. 1 hit.
SM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVAV_MOUSE
AccessioniPrimary (citable) accession number: P27870
Secondary accession number(s): Q8BTV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 30, 2016
This is version 181 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.