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P15498 (VAV_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proto-oncogene vav
Gene names
Name:VAV1
Synonyms:VAV
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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

May interact with CCPG1 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. Interacts with SHB and CLNK By similarity. Interacts with THEMIS2. Interacts with HCK By similarity. Interacts with NEK3 and this interaction is prolactin-dependent. Interacts with ITK. Interacts with PTK2B/PYK2. Interacts (via SH2 domain) with SYK. Interacts with ANKRD54 By similarity. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22

Tissue specificity

Widely expressed in hematopoietic cells but not in other cell types.

Domain

The DH domain is involved in interaction with CCPG1 By similarity.

Post-translational modification

Phosphorylated on tyrosine residues by HCK in response to IFNG and bacterial lipopolysaccharide (LPS) By similarity. Phosphorylated by FYN. Ref.14

Miscellaneous

'Vav' stands for the sixth letter of the Hebrew alphabet.

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.

Sequence caution

The sequence BAG62721.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA34383.1 differs from that shown. Reason: Frameshift at positions 322 and 355.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   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_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

T cell activation

Inferred from electronic annotation. Source: Ensembl

T cell costimulation

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Traceable author statement Ref.6. Source: GOC

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionRac guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: Ensembl

guanyl-nucleotide exchange factor activity

Inferred from experiment. Source: Reactome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.6. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15498-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P15498-2)

The sequence of this isoform differs from the canonical sequence as follows:
     187-218: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 845845Proto-oncogene vav
PRO_0000080980

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 Ref.20
Modified residue8441Phosphotyrosine By similarity

Natural variations

Alternative sequence187 – 21832Missing in isoform 2.
VSP_047563
Natural variant7391T → M.
Corresponds to variant rs36097961 [ dbSNP | Ensembl ].
VAR_051997

Experimental info

Mutagenesis5291C → R: Abolishes transforming activity. Ref.1
Mutagenesis6961R → L: Loss of interaction with SYK. Ref.10
Sequence conflict2641A → P in CAA34383. Ref.6
Sequence conflict3681Q → R in BAG62721. Ref.5
Sequence conflict7181I → TV Ref.6

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 21, 2001. Version 4.
Checksum: AC3BC9736FD2F138

FASTA84598,314
        10         20         30         40         50         60 
MELWRQCTHW LIQCRVLPPS HRVTWDGAQV CELAQALRDG VLLCQLLNNL LPHAINLREV 

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

       130        140        150        160        170        180 
AQNRGIMPFP TEEESVGDED IYSGLSDQID DTVEEDEDLY DCVENEEAEG DEIYEDLMRS 

       190        200        210        220        230        240 
EPVSMPPKMT EYDKRCCCLR EIQQTEEKYT DTLGSIQQHF LKPLQRFLKP QDIEIIFINI 

       250        260        270        280        290        300 
EDLLRVHTHF LKEMKEALGT PGAANLYQVF IKYKERFLVY GRYCSQVESA SKHLDRVAAA 

       310        320        330        340        350        360 
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQEA MEKENLRLAL 

       370        380        390        400        410        420 
DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLAHY GRPKIDGELK ITSVERRSKM 

       430        440        450        460        470        480 
DRYAFLLDKA LLICKRRGDS YDLKDFVNLH SFQVRDDSSG DRDNKKWSHM FLLIEDQGAQ 

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

       550        560        570        580        590        600 
YQGYRCHRCR ASAHKECLGR VPPCGRHGQD FPGTMKKDKL HRRAQDKKRN ELGLPKMEVF 

       610        620        630        640        650        660 
QEYYGLPPPP GAIGPFLRLN PGDIVELTKA EAEQNWWEGR NTSTNEIGWF PCNRVKPYVH 

       670        680        690        700        710        720 
GPPQDLSVHL WYAGPMERAG AESILANRSD GTFLVRQRVK DAAEFAISIK YNVEVKHIKI 

       730        740        750        760        770        780 
MTAEGLYRIT EKKAFRGLTE LVEFYQQNSL KDCFKSLDTT LQFPFKEPEK RTISRPAVGS 

       790        800        810        820        830        840 
TKYFGTAKAR YDFCARDRSE LSLKEGDIIK ILNKKGQQGW WRGEIYGRVG WFPANYVEED 


YSEYC 

« Hide

Isoform 2 [UniParc].

Checksum: 2DD711DA5E0A8403
Show »

FASTA81394,493

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] (ISOFORM 1), MUTAGENESIS OF CYS-529.
[2]"Genomic organization and regulation of the vav proto-oncogene."
Denkinger D.J., Borges C.R., Butler C.L., Cushman A.M., Kawahara R.S.
Biochim. Biophys. Acta 1491:253-262(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 [GENOMIC DNA] OF 1-61.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-813 (ISOFORM 2).
Tissue: Spleen.
[6]"vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells."
Katzav S., Martin-Zanca D., Barbacid M.
EMBO J. 8:2283-2290(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-845 (ISOFORM 1).
[7]Romero F.
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 299-837 (ISOFORM 1).
[8]"The proline-rich region of Vav binds to Grb2 and Grb3-3."
Ramos-Morales F., Romero F., Schweighoffer F., Bismuth G., Camonis J., Tortolero M., Fischer S.
Oncogene 11:1665-1669(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 299-334 (ISOFORM 1).
[9]"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: SIMILARITY TO CDC24 FAMILY.
[10]"Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product."
Deckert M., Tartare-Deckert S., Couture C., Mustelin T., Altman A.
Immunity 5:591-604(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYK, MUTAGENESIS OF ARG-696.
[11]"Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation."
Bustelo X.R., Crespo P., Lopez-Barahona M., Gutkind J.S., Barbacid M.
Oncogene 15:2511-2520(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBLB.
[12]"BLNK: a central linker protein in B cell activation."
Fu C., Turck C.W., Kurosaki T., Chan A.C.
Immunity 9:93-103(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BLNK; PLCG1; GRB2 AND NCK1.
[13]"hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways."
Germani A., Romero F., Houlard M., Camonis J., Gisselbrecht S., Fischer S., Varin-Blank N.
Mol. Cell. Biol. 19:3798-3807(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH2.
[14]"T-cell receptor antagonists induce Vav phosphorylation by selective activation of Fyn kinase."
Huang J., Tilly D., Altman A., Sugie K., Grey H.M.
Proc. Natl. Acad. Sci. U.S.A. 97:10923-10929(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY FYN.
[15]"DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines."
Nishihara H., Maeda M., Oda A., Tsuda M., Sawa H., Nagashima K., Tanaka S.
Blood 100:3968-3974(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DOCK2.
[16]"Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."
Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.
Eur. J. Biochem. 269:3279-3288(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHB.
[17]"Adaptor protein APS binds the NH2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity."
Yabana N., Shibuya M.
Oncogene 21:7720-7729(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APS.
[18]"Kinase-independent functions for Itk in TCR-induced regulation of Vav and the actin cytoskeleton."
Dombroski D., Houghtling R.A., Labno C.M., Precht P., Takesono A., Caplen N.J., Billadeau D.D., Wange R.L., Burkhardt J.K., Schwartzberg P.L.
J. Immunol. 174:1385-1392(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITK.
[19]"Novel association of Vav2 and Nek3 modulates signaling through the human prolactin receptor."
Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.
Mol. Endocrinol. 19:939-949(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEK3.
[20]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-826, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Characterization of VIK-1: a new Vav-interacting Kruppel-like protein."
Houlard M., Romero-Portillo F., Germani A., Depaux A., Regnier-Ricard F., Gisselbrecht S., Varin-Blank N.
Oncogene 24:28-38(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF655/VIK.
[22]"A Pyk2-Vav1 complex is recruited to beta3-adhesion sites to initiate Rho activation."
Gao C., Blystone S.D.
Biochem. J. 420:49-56(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2B/PYK2.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Solution structure of the SH2 domain of human proto-oncogene protein VAV1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 661-775.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF030227 expand/collapse EMBL AC list , AF030201, AF030202, AF030203, AF030204, AF030205, AF030206, AF030207, AF030208, AF030209, AF030210, AF030211, AF030212, AF030213, AF030214, AF030215, AF030216, AF030217, AF030218, AF030219, AF030220, AF030221, AF030222, AF030223, AF030224, AF030225, AF030226 Genomic DNA. Translation: AAC25011.1.
AC010647 Genomic DNA. No translation available.
AC020895 Genomic DNA. No translation available.
AC020954 Genomic DNA. No translation available.
AC022156 Genomic DNA. No translation available.
M59834 Genomic DNA. Translation: AAA63267.1.
AK301128 mRNA. Translation: BAG62721.1. Different initiation.
X16316 mRNA. Translation: CAA34383.1. Frameshift.
X83931 mRNA. Translation: CAA58783.1.
PIRTVHUVV. B39576.
RefSeqNP_001245136.1. NM_001258207.1.
NP_005419.2. NM_005428.3.
UniGeneHs.116237.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CRHNMR-A629-775[»]
2LCTNMR-A664-767[»]
2MC1NMR-A664-767[»]
2RORNMR-A629-775[»]
3BJIX-ray2.60A/B189-565[»]
3KY9X-ray2.73A/B2-584[»]
ProteinModelPortalP15498.
SMRP15498. Positions 2-565, 583-780, 784-844.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113252. 68 interactions.
DIPDIP-1061N.
IntActP15498. 24 interactions.
MINTMINT-1211643.
STRING9606.ENSP00000302269.

PTM databases

PhosphoSiteP15498.

Polymorphism databases

DMDM13124807.

Proteomic databases

PaxDbP15498.
PeptideAtlasP15498.
PRIDEP15498.

Protocols and materials databases

DNASU7409.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000596764; ENSP00000469450; ENSG00000141968. [P15498-2]
ENST00000602142; ENSP00000472929; ENSG00000141968. [P15498-1]
GeneID7409.
KEGGhsa:7409.
UCSCuc002mfu.2. human. [P15498-1]

Organism-specific databases

CTD7409.
GeneCardsGC19P006772.
H-InvDBHIX0202828.
HGNCHGNC:12657. VAV1.
HPAHPA001864.
MIM164875. gene.
neXtProtNX_P15498.
PharmGKBPA37280.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326494.
HOGENOMHOG000234364.
HOVERGENHBG018066.
InParanoidP15498.
KOK05730.
OMASHRVTWD.
OrthoDBEOG73FQKZ.
PhylomeDBP15498.
TreeFamTF316171.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
REACT_85674. Hemostasis.
SignaLinkP15498.

Gene expression databases

ArrayExpressP15498.
BgeeP15498.
CleanExHS_VAV1.
GenevestigatorP15498.

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.
InterProIPR001715. 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.
IPR001452. SH3_domain.
IPR003096. SM22_calponin.
IPR028530. Vav.
[Graphical view]
PANTHERPTHR22826:SF53. PTHR22826:SF53. 1 hit.
PfamPF00130. C1_1. 1 hit.
PF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[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

EvolutionaryTraceP15498.
GenomeRNAi7409.
NextBio29008.
PMAP-CutDBP15498.
PROP15498.
SOURCESearch...

Entry information

Entry nameVAV_HUMAN
AccessionPrimary (citable) accession number: P15498
Secondary accession number(s): B4DVK9, M0QXX6, Q15860
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 21, 2001
Last modified: April 16, 2014
This is version 172 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM