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P52735 (VAV2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide exchange factor VAV2

Short name=VAV-2
Gene names
Name:VAV2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length878 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly By similarity.

Subunit structure

Interacts (via SH2 domains) with the phosphorylated form of EPHA2. Interacts with SSX2IP By similarity. Interacts with NEK3 and PRLR and this interaction is prolactin-dependent. Ref.9

Tissue specificity

Widely expressed.

Post-translational modification

Phosphorylated on tyrosine residues in response to FGR activation. Ref.7 Ref.8

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
   Biological processAngiogenesis
   Coding sequence diversityAlternative splicing
Polymorphism
   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

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic signaling pathway

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell migration

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

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 phosphatidylinositol 3-kinase activity

Inferred from electronic annotation. Source: Ensembl

regulation of GTPase activity

Inferred from experiment. Source: GOC

regulation of blood coagulation

Inferred from mutant phenotype PubMed 21810271. Source: UniProt

regulation of gene expression

Inferred from mutant phenotype PubMed 21810271. Source: UniProt

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement Ref.1. Source: ProtInc

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

guanyl-nucleotide exchange factor activity

Inferred from experiment. Source: Reactome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 11390470PubMed 15345594Ref.9PubMed 16273093PubMed 18654987PubMed 20598684PubMed 24728074. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P52735-1)

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: P52735-2)

The sequence of this isoform differs from the canonical sequence as follows:
     185-189: Missing.
     470-474: Missing.
Isoform 3 (identifier: P52735-3)

The sequence of this isoform differs from the canonical sequence as follows:
     185-189: Missing.
     470-474: Missing.
     783-811: Missing.
Note: Contains a phosphoserine at position 769.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 878878Guanine nucleotide exchange factor VAV2
PRO_0000080984

Regions

Domain1 – 119119CH
Domain198 – 376179DH
Domain405 – 512108PH
Domain586 – 65267SH3 1
Domain673 – 76795SH2
Domain816 – 87762SH3 2
Zinc finger523 – 57250Phorbol-ester/DAG-type

Amino acid modifications

Modified residue1421Phosphotyrosine; by EGFR Ref.7
Modified residue1591Phosphotyrosine; by EGFR Ref.7
Modified residue1721Phosphotyrosine; by EGFR Ref.7
Modified residue5761Phosphoserine Ref.14
Modified residue6261Phosphoserine Ref.11

Natural variations

Alternative sequence185 – 1895Missing in isoform 2 and isoform 3.
VSP_034900
Alternative sequence470 – 4745Missing in isoform 2 and isoform 3.
VSP_034901
Alternative sequence783 – 81129Missing in isoform 3.
VSP_034902
Natural variant5941M → V. Ref.1 Ref.4
Corresponds to variant rs602990 [ dbSNP | Ensembl ].
VAR_045690

Experimental info

Sequence conflict2411F → L in CAE45861. Ref.5
Sequence conflict2541F → L in CAE45861. Ref.5
Sequence conflict8771I → T in CAE45861. Ref.5

Secondary structure

.................................... 878
Helix Strand Turn

Details...

Sequences

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

Last modified July 22, 2008. Version 2.
Checksum: C186911605FD5B73

FASTA878101,289
        10         20         30         40         50         60 
MEQWRQCGRW LIDCKVLPPN HRVVWPSAVV FDLAQALRDG VLLCQLLHNL SPGSIDLKDI 

        70         80         90        100        110        120 
NFRPQMSQFL CLKNIRTFLK VCHDKFGLRN SELFDPFDLF DVRDFGKVIS AVSRLSLHSI 

       130        140        150        160        170        180 
AQNKGIRPFP SEETTENDDD VYRSLEELAD EHDLGEDIYD CVPCEDGGDD IYEDIIKVEV 

       190        200        210        220        230        240 
QQPMIRYMQK MGMTEDDKRN CCLLEIQETE AKYYRTLEDI EKNYMSPLRL VLSPADMAAV 

       250        260        270        280        290        300 
FINLEDLIKV HHSFLRAIDV SVMVGGSTLA KVFLDFKERL LIYGEYCSHM EHAQNTLNQL 

       310        320        330        340        350        360 
LASREDFRQK VEECTLKVQD GKFKLQDLLV VPMQRVLKYH LLLKELLSHS AERPERQQLK 

       370        380        390        400        410        420 
EALEAMQDLA MYINEVKRDK ETLRKISEFQ SSIENLQVKL EEFGRPKIDG ELKVRSIVNH 

       430        440        450        460        470        480 
TKQDRYLFLF DKVVIVCKRK GYSYELKEII ELLFHKMTDD PMNNKDVKKS HGKMWSYGFY 

       490        500        510        520        530        540 
LIHLQGKQGF QFFCKTEDMK RKWMEQFEMA MSNIKPDKAN ANHHSFQMYT FDKTTNCKAC 

       550        560        570        580        590        600 
KMFLRGTFYQ GYMCTKCGVG AHKECLEVIP PCKFTSPADL DASGAGPGPK MVAMQNYHGN 

       610        620        630        640        650        660 
PAPPGKPVLT FQTGDVLELL RGDPESPWWE GRLVQTRKSG YFPSSSVKPC PVDGRPPISR 

       670        680        690        700        710        720 
PPSREIDYTA YPWFAGNMER QQTDNLLKSH ASGTYLIRER PAEAERFAIS IKFNDEVKHI 

       730        740        750        760        770        780 
KVVEKDNWIH ITEAKKFDSL LELVEYYQCH SLKESFKQLD TTLKYPYKSR ERSASRASSR 

       790        800        810        820        830        840 
SPASCASYNF SFLSPQGLSF ASQGPSAPFW SVFTPRVIGT AVARYNFAAR DMRELSLREG 

       850        860        870 
DVVRIYSRIG GDQGWWKGET NGRIGWFPST YVEEEGIQ 

« Hide

Isoform 2 [UniParc].

Checksum: 6C67C472825D2DFD
Show »

FASTA868100,057
Isoform 3 [UniParc].

Checksum: 21910D516F4A211D
Show »

FASTA83997,032

References

« Hide 'large scale' references
[1]"Identification of VAV2 on 9q34 and its exclusion as the tuberous sclerosis gene TSC1."
Henske E.P., Short M.P., Jozwiak S., Bovey C.M., Ramlakhan S., Haines J.L., Kwiatkowski D.J.
Ann. Hum. Genet. 59:25-37(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
Tissue: Brain.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT VAL-594.
Tissue: Kidney.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-878 (ISOFORM 3).
Tissue: Rectum tumor.
[6]"Transcript variant of VAV2 gene in tumoral cell lines (FaDu, HEp2, HeLa and SiHa)."
Mancini U.M., Tajara E.H.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 453-506 (ISOFORMS 2/3).
[7]"Mechanism of epidermal growth factor regulation of Vav2, a guanine nucleotide exchange factor for Rac."
Tamas P., Solti Z., Bauer P., Illes A., Sipeki S., Bauer A., Farago A., Downward J., Buday L.
J. Biol. Chem. 278:5163-5171(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-142; TYR-159 AND TYR-172 BY EGFR.
[8]"The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization."
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G.
Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[9]"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 AND PRLR.
[10]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"Solution structure of the SH2 domain and of the second SH3 domain of human protein VAV-2."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 663-878.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S76992 mRNA. Translation: AAB34377.1.
AL590710, AL357934, AL445931 Genomic DNA. Translation: CAI12279.1.
AL445931, AL357934, AL590710 Genomic DNA. Translation: CAI13722.1.
AL357934, AL445931, AL590710 Genomic DNA. Translation: CAI15783.1.
AL590710, AL357934, AL445931 Genomic DNA. Translation: CAI12278.1.
AL445931, AL357934, AL590710 Genomic DNA. Translation: CAI13723.1.
AL357934, AL445931, AL590710 Genomic DNA. Translation: CAI15781.1.
AL590710, AL357934, AL445931 Genomic DNA. Translation: CAI12280.1.
AL445931, AL357934, AL590710 Genomic DNA. Translation: CAI13724.1.
AL357934, AL445931, AL590710 Genomic DNA. Translation: CAI15782.1.
CH471090 Genomic DNA. Translation: EAW88108.1.
BC033187 mRNA. Translation: AAH33187.1.
BC132965 mRNA. Translation: AAI32966.1.
BC132967 mRNA. Translation: AAI32968.1.
BX640754 mRNA. Translation: CAE45861.1.
AY563001 mRNA. Translation: AAS75591.1.
CCDSCCDS48053.1. [P52735-1]
CCDS6979.1. [P52735-3]
PIRI51940.
RefSeqNP_001127870.1. NM_001134398.1. [P52735-1]
NP_003362.2. NM_003371.3. [P52735-3]
XP_005272270.1. XM_005272213.1. [P52735-2]
UniGeneHs.369921.
Hs.689325.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DLZNMR-A663-767[»]
2DM1NMR-A819-878[»]
2LNWNMR-A659-771[»]
2LNXNMR-A659-771[»]
ProteinModelPortalP52735.
SMRP52735. Positions 1-572, 589-878.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113253. 61 interactions.
DIPDIP-33088N.
IntActP52735. 59 interactions.
MINTMINT-1494337.

PTM databases

PhosphoSiteP52735.

Polymorphism databases

DMDM212287930.

Proteomic databases

MaxQBP52735.
PaxDbP52735.
PRIDEP52735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371850; ENSP00000360916; ENSG00000160293. [P52735-1]
ENST00000371851; ENSP00000360917; ENSG00000160293. [P52735-2]
ENST00000406606; ENSP00000385362; ENSG00000160293. [P52735-3]
GeneID7410.
KEGGhsa:7410.
UCSCuc004cer.3. human. [P52735-3]
uc004ces.3. human. [P52735-1]

Organism-specific databases

CTD7410.
GeneCardsGC09M136627.
HGNCHGNC:12658. VAV2.
HPAHPA003224.
MIM600428. gene.
neXtProtNX_P52735.
PharmGKBPA37281.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326494.
HOVERGENHBG018066.
InParanoidP52735.
KOK05730.
OMAWFAGNME.
OrthoDBEOG73FQKZ.
PhylomeDBP52735.
TreeFamTF316171.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP52735.

Gene expression databases

BgeeP52735.
GenevestigatorP52735.

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.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR028530. Vav.
[Graphical view]
PANTHERPTHR22826:SF95. PTHR22826:SF95. 1 hit.
PfamPF00130. C1_1. 1 hit.
PF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF07653. SH3_2. 2 hits.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
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. 2 hits.
SSF55550. SSF55550. 2 hits.
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

ChiTaRSVAV2. human.
EvolutionaryTraceP52735.
GeneWikiVAV2.
GenomeRNAi7410.
NextBio29012.
PROP52735.
SOURCESearch...

Entry information

Entry nameVAV2_HUMAN
AccessionPrimary (citable) accession number: P52735
Secondary accession number(s): A2RUM4 expand/collapse secondary AC list , A8MQ12, B6ZDF5, Q5SYV3, Q5SYV4, Q5SYV5, Q6N012, Q6PIJ9, Q6Q317
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 150 of the entry and version 2 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 9

Human chromosome 9: entries, gene names and cross-references to MIM