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P27870 (VAV_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proto-oncogene vav
Alternative name(s):
p95vav
Gene names
Name:Vav1
Synonyms:Vav
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length845 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. May interact with CCPG1. Interacts with CLNK. Interacts with THEMIS2. 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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14

Tissue specificity

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

Domain

The DH domain is involved in interaction with CCPG1.

Post-translational modification

Phosphorylated by FYN By similarity. Phosphorylated on tyrosine residues by HCK in response to IFNG and bacterial lipopolysaccharide (LPS). Ref.6 Ref.8 Ref.9

Sequence similarities

Contains 1 CH (calponin-homology) domain.

Contains 1 DH (DBL-homology) domain.

Contains 1 PH domain.

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Ontologies

Keywords
   DiseaseProto-oncogene
   DomainRepeat
SH2 domain
SH3 domain
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionGuanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from genetic interaction PubMed 21178006. Source: MGI

T cell activation

Inferred from mutant phenotype PubMed 11070165. Source: MGI

T cell differentiation

Inferred from genetic interaction PubMed 21178006. Source: MGI

immune response

Inferred from mutant phenotype PubMed 11070165. Source: MGI

integrin-mediated signaling pathway

Inferred from genetic interaction PubMed 15249579. Source: MGI

intracellular signal transduction

Inferred from mutant phenotype PubMed 11070165. Source: MGI

neutrophil chemotaxis

Inferred from genetic interaction PubMed 21178006. Source: MGI

phagocytosis

Inferred from genetic interaction PubMed 15249579. Source: MGI

positive regulation of Rac GTPase activity

Inferred from genetic interaction PubMed 21178006. Source: MGI

positive regulation of cell adhesion

Inferred from genetic interaction PubMed 15249579PubMed 21178006. Source: MGI

reactive oxygen species metabolic process

Inferred from genetic interaction PubMed 21178006. Source: MGI

regulation of GTPase activity

Inferred from genetic interaction PubMed 15249579. Source: MGI

regulation of Rac GTPase activity

Inferred from genetic interaction PubMed 15249579. Source: GOC

   Cellular_componentcell-cell junction

Inferred from direct assay PubMed 23793062. Source: MGI

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionRac guanyl-nucleotide exchange factor activity

Inferred from genetic interaction PubMed 15249579. Source: MGI

Rho guanyl-nucleotide exchange factor activity

Inferred from genetic interaction PubMed 15249579. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.13PubMed 22732588PubMed 8632004. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 845845Proto-oncogene vav
PRO_0000080981

Regions

Domain1 – 119119CH
Domain194 – 373180DH
Domain402 – 504103PH
Domain617 – 66044SH3 1
Domain671 – 76595SH2
Domain782 – 84261SH3 2
Zinc finger515 – 56450Phorbol-ester/DAG-type
Compositional bias33 – 9967Leu-rich

Amino acid modifications

Modified residue8261Phosphotyrosine By similarity
Modified residue8441Phosphotyrosine Ref.12

Experimental info

Mutagenesis5291C → S: Abolishes transforming activity. Ref.1
Mutagenesis5321C → S: Abolishes transforming activity. Ref.1
Mutagenesis5541H → D: Abolishes transforming activity. Ref.1
Sequence conflict291Q → E in AAA63402. Ref.4
Sequence conflict2261R → L in BAC40436. Ref.3

Secondary structure

......................................................................................... 845
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27870 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 3666DCCD1C5229DA

FASTA84598,137
        10         20         30         40         50         60 
MELWRQCTHW LIQCRVLPPS HRVTWEGAQV CELAQALRDG VLLCQLLNNL LPQAINLREV 

        70         80         90        100        110        120 
NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF DVQDFGKVIY TLSALSWTPI 

       130        140        150        160        170        180 
AQNKGIMPFP TEDSALNDED IYSGLSDQID DTAEEDEDLY DCVENEEAEG DEIYEDLMRL 

       190        200        210        220        230        240 
ESVPTPPKMT EYDKRCCCLR EIQQTEEKYT DTLGSIQQHF MKPLQRFLKP QDMETIFVNI 

       250        260        270        280        290        300 
EELFSVHTHF LKELKDALAG PGATTLYQVF IKYKERFLVY GRYCSQVESA SKHLDQVATA 

       310        320        330        340        350        360 
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQDA TEKENLRLAL 

       370        380        390        400        410        420 
DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLANY GRPKIDGELK ITSVERRSKT 

       430        440        450        460        470        480 
DRYAFLLDKA LLICKRRGDS YDLKASVNLH SFQVRDDSSG ERDNKKWSHM FLLIEDQGAQ 

       490        500        510        520        530        540 
GYELFFKTRE LKKKWMEQFE MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF 

       550        560        570        580        590        600 
YQGYRCYRCR APAHKECLGR VPPCGRHGQD FAGTMKKDKL HRRAQDKKRN ELGLPKMEVF 

       610        620        630        640        650        660 
QEYYGIPPPP GAFGPFLRLN PGDIVELTKA EAEHNWWEGR NTATNEVGWF PCNRVHPYVH 

       670        680        690        700        710        720 
GPPQDLSVHL WYAGPMERAG AEGILTNRSD GTYLVRQRVK DTAEFAISIK YNVEVKHIKI 

       730        740        750        760        770        780 
MTSEGLYRIT EKKAFRGLLE LVEFYQQNSL KDCFKSLDTT LQFPYKEPER RAISKPPAGS 

       790        800        810        820        830        840 
TKYFGTAKAR YDFCARDRSE LSLKEGDIIK ILNKKGQQGW WRGEIYGRIG WFPSNYVEED 


YSEYC 

« Hide

References

« Hide 'large scale' references
[1]"Mechanism of activation of the vav protooncogene."
Coppola J., Bryant S., Koda T., Conway D., Barbacid M.
Cell Growth Differ. 2:95-105(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, MUTAGENESIS OF CYS-529; CYS-532 AND HIS-554.
[2]"The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization."
Adams J.M., Houston H., Allen J., Lints T., Harvey R.
Oncogene 7:611-618(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: Thymus.
[4]"Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential."
Katzav S., Cleveland J.L., Heslop H.E., Pulido D.
Mol. Cell. Biol. 11:1912-1920(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-93.
[5]"Tec protein tyrosine kinase is involved in the signaling mechanism of granulocyte colony-stimulating factor receptor."
Miyazato A., Yamashita Y., Hatake K., Miura Y., Ozawa K., Mano H.
Cell Growth Differ. 7:1135-1139(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TEC.
[6]"Bacterial LPS and IFN-gamma trigger the tyrosine phosphorylation of vav in macrophages: evidence for involvement of the hck tyrosine kinase."
English B.K., Orlicek S.L., Mei Z., Meals E.A.
J. Leukoc. Biol. 62:859-864(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCK, PHOSPHORYLATION.
[7]"Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor signaling."
Sosinowski T., Pandey A., Dixit V.M., Weiss A.
J. Exp. Med. 191:463-474(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLA.
[8]"Cbl-b regulates the CD28 dependence of T-cell activation."
Chiang Y.J., Kole H.K., Brown K., Naramura M., Fukuhara S., Hu R.-J., Jang I.K., Gutkind J.S., Shevach E., Gu H.
Nature 403:216-220(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH CBLB.
[9]"Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b."
Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T., Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M.
Nature 403:211-216(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH CBLB.
[10]"MIST functions through distinct domains in immunoreceptor signaling in the presence and absence of LAT."
Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.
J. Biol. Chem. 276:36043-36050(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLNK.
[11]"Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs."
Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.
Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INTERACTION WITH CCPG1.
[12]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-844, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[13]"Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation."
Samuels A.L., Klinken S.P., Ingley E.
Blood 113:3845-3856(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANKRD54.
[14]"Themis2/ICB1 is a signaling scaffold that selectively regulates macrophage Toll-like receptor signaling and cytokine production."
Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S., Lanfrancotti A., Notley C., Hussell T., Cope A.P., Wait R.
PLoS ONE 5:E11465-E11465(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THEMIS2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64361 mRNA. Translation: CAA45713.1.
AK088586 mRNA. Translation: BAC40436.1.
M59833 mRNA. Translation: AAA63402.1.
CCDSCCDS28931.1.
PIRTVMSVV. A61187.
RefSeqNP_035821.3. NM_011691.4.
UniGeneMm.248172.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP27870.
SMRP27870. Positions 2-565, 596-779, 784-844.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204500. 8 interactions.
DIPDIP-31010N.
IntActP27870. 7 interactions.
MINTMINT-85069.

PTM databases

PhosphoSiteP27870.

Proteomic databases

MaxQBP27870.
PaxDbP27870.
PRIDEP27870.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005889; ENSMUSP00000005889; ENSMUSG00000034116.
GeneID22324.
KEGGmmu:22324.
UCSCuc008dep.2. mouse.

Organism-specific databases

CTD7409.
MGIMGI:98923. Vav1.

Phylogenomic databases

eggNOGNOG326494.
HOGENOMHOG000234364.
HOVERGENHBG018066.
InParanoidP27870.
KOK05730.
OMASHRVTWD.
PhylomeDBP27870.
TreeFamTF316171.

Enzyme and pathway databases

ReactomeREACT_224553. Hemostasis.

Gene expression databases

ArrayExpressP27870.
BgeeP27870.
CleanExMM_VAV1.
GenevestigatorP27870.

Family and domain databases

Gene3D1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR022613. CAMSAP_CH.
IPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003096. SM22_calponin.
IPR028530. Vav.
[Graphical view]
PANTHERPTHR22826:SF112. PTHR22826:SF112. 1 hit.
PfamPF00130. C1_1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00888. SM22CALPONIN.
SMARTSM00109. 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]
SUPFAMSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50021. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP27870.
NextBio302549.
PROP27870.
SOURCESearch...

Entry information

Entry nameVAV_MOUSE
AccessionPrimary (citable) accession number: P27870
Secondary accession number(s): Q8BTV7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot