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Database: UniProt
Entry: P52735
LinkDB: P52735
Original site: P52735 
ID   VAV2_HUMAN              Reviewed;         878 AA.
AC   P52735; A2RUM4; A8MQ12; B6ZDF5; Q5SYV3; Q5SYV4; Q5SYV5; Q6N012;
AC   Q6PIJ9; Q6Q317;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   09-JUL-2014, entry version 150.
DE   RecName: Full=Guanine nucleotide exchange factor VAV2;
DE            Short=VAV-2;
GN   Name=VAV2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-594.
RC   TISSUE=Brain;
RX   PubMed=7762982; DOI=10.1111/j.1469-1809.1995.tb01603.x;
RA   Henske E.P., Short M.P., Jozwiak S., Bovey C.M., Ramlakhan S.,
RA   Haines J.L., Kwiatkowski D.J.;
RT   "Identification of VAV2 on 9q34 and its exclusion as the tuberous
RT   sclerosis gene TSC1.";
RL   Ann. Hum. Genet. 59:25-37(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP   VAL-594.
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-878 (ISOFORM 3).
RC   TISSUE=Rectum tumor;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 453-506 (ISOFORMS 2/3).
RA   Mancini U.M., Tajara E.H.;
RT   "Transcript variant of VAV2 gene in tumoral cell lines (FaDu, HEp2,
RT   HeLa and SiHa).";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PHOSPHORYLATION AT TYR-142; TYR-159 AND TYR-172 BY EGFR.
RX   PubMed=12454019; DOI=10.1074/jbc.M207555200;
RA   Tamas P., Solti Z., Bauer P., Illes A., Sipeki S., Bauer A.,
RA   Farago A., Downward J., Buday L.;
RT   "Mechanism of epidermal growth factor regulation of Vav2, a guanine
RT   nucleotide exchange factor for Rac.";
RL   J. Biol. Chem. 278:5163-5171(2003).
RN   [8]
RP   PHOSPHORYLATION.
RX   PubMed=15561106; DOI=10.1016/j.yexcr.2004.09.005;
RA   Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,
RA   Lowell C.A., Berton G.;
RT   "The proto-oncogene Fgr regulates cell migration and this requires its
RT   plasma membrane localization.";
RL   Exp. Cell Res. 302:253-269(2005).
RN   [9]
RP   INTERACTION WITH NEK3 AND PRLR.
RX   PubMed=15618286; DOI=10.1210/me.2004-0443;
RA   Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.;
RT   "Novel association of Vav2 and Nek3 modulates signaling through the
RT   human prolactin receptor.";
RL   Mol. Endocrinol. 19:939-949(2005).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769 (ISOFORM 3), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [16]
RP   STRUCTURE BY NMR OF 663-878.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SH2 domain and of the second SH3 domain of
RT   human protein VAV-2.";
RL   Submitted (APR-2007) to the PDB data bank.
CC   -!- FUNCTION: Guanine nucleotide exchange factor for the Rho family of
CC       Ras-related GTPases. Plays an important role in angiogenesis. Its
CC       recruitment by phosphorylated EPHA2 is critical for EFNA1-induced
CC       RAC1 GTPase activation and vascular endothelial cell migration and
CC       assembly (By similarity).
CC   -!- SUBUNIT: Interacts (via SH2 domains) with the phosphorylated form
CC       of EPHA2. Interacts with SSX2IP (By similarity). Interacts with
CC       NEK3 and PRLR and this interaction is prolactin-dependent.
CC   -!- INTERACTION:
CC       Q8IZP0:ABI1; NbExp=2; IntAct=EBI-297549, EBI-375446;
CC       P04626:ERBB2; NbExp=3; IntAct=EBI-297549, EBI-641062;
CC       Q13480:GAB1; NbExp=2; IntAct=EBI-297549, EBI-517684;
CC       P51956:NEK3; NbExp=3; IntAct=EBI-297549, EBI-476041;
CC       P78314:SH3BP2; NbExp=4; IntAct=EBI-297549, EBI-727062;
CC       O75674:TOM1L1; NbExp=2; IntAct=EBI-297549, EBI-712991;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P52735-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P52735-2; Sequence=VSP_034900, VSP_034901;
CC       Name=3;
CC         IsoId=P52735-3; Sequence=VSP_034900, VSP_034901, VSP_034902;
CC         Note=Contains a phosphoserine at position 769;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- PTM: Phosphorylated on tyrosine residues in response to FGR
CC       activation.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
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DR   EMBL; S76992; AAB34377.1; -; mRNA.
DR   EMBL; AL590710; CAI12279.1; -; Genomic_DNA.
DR   EMBL; AL357934; CAI12279.1; JOINED; Genomic_DNA.
DR   EMBL; AL445931; CAI12279.1; JOINED; Genomic_DNA.
DR   EMBL; AL445931; CAI13722.1; -; Genomic_DNA.
DR   EMBL; AL357934; CAI13722.1; JOINED; Genomic_DNA.
DR   EMBL; AL590710; CAI13722.1; JOINED; Genomic_DNA.
DR   EMBL; AL357934; CAI15783.1; -; Genomic_DNA.
DR   EMBL; AL445931; CAI15783.1; JOINED; Genomic_DNA.
DR   EMBL; AL590710; CAI15783.1; JOINED; Genomic_DNA.
DR   EMBL; AL590710; CAI12278.1; -; Genomic_DNA.
DR   EMBL; AL357934; CAI12278.1; JOINED; Genomic_DNA.
DR   EMBL; AL445931; CAI12278.1; JOINED; Genomic_DNA.
DR   EMBL; AL445931; CAI13723.1; -; Genomic_DNA.
DR   EMBL; AL357934; CAI13723.1; JOINED; Genomic_DNA.
DR   EMBL; AL590710; CAI13723.1; JOINED; Genomic_DNA.
DR   EMBL; AL357934; CAI15781.1; -; Genomic_DNA.
DR   EMBL; AL445931; CAI15781.1; JOINED; Genomic_DNA.
DR   EMBL; AL590710; CAI15781.1; JOINED; Genomic_DNA.
DR   EMBL; AL590710; CAI12280.1; -; Genomic_DNA.
DR   EMBL; AL357934; CAI12280.1; JOINED; Genomic_DNA.
DR   EMBL; AL445931; CAI12280.1; JOINED; Genomic_DNA.
DR   EMBL; AL445931; CAI13724.1; -; Genomic_DNA.
DR   EMBL; AL357934; CAI13724.1; JOINED; Genomic_DNA.
DR   EMBL; AL590710; CAI13724.1; JOINED; Genomic_DNA.
DR   EMBL; AL357934; CAI15782.1; -; Genomic_DNA.
DR   EMBL; AL445931; CAI15782.1; JOINED; Genomic_DNA.
DR   EMBL; AL590710; CAI15782.1; JOINED; Genomic_DNA.
DR   EMBL; CH471090; EAW88108.1; -; Genomic_DNA.
DR   EMBL; BC033187; AAH33187.1; -; mRNA.
DR   EMBL; BC132965; AAI32966.1; -; mRNA.
DR   EMBL; BC132967; AAI32968.1; -; mRNA.
DR   EMBL; BX640754; CAE45861.1; -; mRNA.
DR   EMBL; AY563001; AAS75591.1; -; mRNA.
DR   CCDS; CCDS48053.1; -. [P52735-1]
DR   CCDS; CCDS6979.1; -. [P52735-3]
DR   PIR; I51940; I51940.
DR   RefSeq; NP_001127870.1; NM_001134398.1. [P52735-1]
DR   RefSeq; NP_003362.2; NM_003371.3. [P52735-3]
DR   RefSeq; XP_005272270.1; XM_005272213.1. [P52735-2]
DR   UniGene; Hs.369921; -.
DR   UniGene; Hs.689325; -.
DR   PDB; 2DLZ; NMR; -; A=663-767.
DR   PDB; 2DM1; NMR; -; A=819-878.
DR   PDB; 2LNW; NMR; -; A=659-771.
DR   PDB; 2LNX; NMR; -; A=659-771.
DR   PDBsum; 2DLZ; -.
DR   PDBsum; 2DM1; -.
DR   PDBsum; 2LNW; -.
DR   PDBsum; 2LNX; -.
DR   ProteinModelPortal; P52735; -.
DR   SMR; P52735; 1-572, 589-878.
DR   BioGrid; 113253; 61.
DR   DIP; DIP-33088N; -.
DR   IntAct; P52735; 59.
DR   MINT; MINT-1494337; -.
DR   PhosphoSite; P52735; -.
DR   DMDM; 212287930; -.
DR   MaxQB; P52735; -.
DR   PaxDb; P52735; -.
DR   PRIDE; P52735; -.
DR   Ensembl; ENST00000371850; ENSP00000360916; ENSG00000160293. [P52735-1]
DR   Ensembl; ENST00000371851; ENSP00000360917; ENSG00000160293. [P52735-2]
DR   Ensembl; ENST00000406606; ENSP00000385362; ENSG00000160293. [P52735-3]
DR   GeneID; 7410; -.
DR   KEGG; hsa:7410; -.
DR   UCSC; uc004cer.3; human. [P52735-3]
DR   UCSC; uc004ces.3; human. [P52735-1]
DR   CTD; 7410; -.
DR   GeneCards; GC09M136627; -.
DR   HGNC; HGNC:12658; VAV2.
DR   HPA; HPA003224; -.
DR   MIM; 600428; gene.
DR   neXtProt; NX_P52735; -.
DR   PharmGKB; PA37281; -.
DR   eggNOG; NOG326494; -.
DR   HOVERGEN; HBG018066; -.
DR   InParanoid; P52735; -.
DR   KO; K05730; -.
DR   OMA; WFAGNME; -.
DR   OrthoDB; EOG73FQKZ; -.
DR   PhylomeDB; P52735; -.
DR   TreeFam; TF316171; -.
DR   Reactome; REACT_111045; Developmental Biology.
DR   Reactome; REACT_111102; Signal Transduction.
DR   Reactome; REACT_604; Hemostasis.
DR   Reactome; REACT_6900; Immune System.
DR   SignaLink; P52735; -.
DR   ChiTaRS; VAV2; human.
DR   EvolutionaryTrace; P52735; -.
DR   GeneWiki; VAV2; -.
DR   GenomeRNAi; 7410; -.
DR   NextBio; 29012; -.
DR   PRO; PR:P52735; -.
DR   Bgee; P52735; -.
DR   Genevestigator; P52735; -.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR   GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR   GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
DR   GO; GO:0030193; P:regulation of blood coagulation; IMP:UniProt.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:UniProt.
DR   GO; GO:0043087; P:regulation of GTPase activity; EXP:GOC.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR   Gene3D; 1.10.418.10; -; 1.
DR   Gene3D; 1.20.900.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR028530; Vav.
DR   PANTHER; PTHR22826:SF95; PTHR22826:SF95; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF07653; SH3_2; 2.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   SUPFAM; SSF48065; SSF48065; 1.
DR   SUPFAM; SSF50044; SSF50044; 2.
DR   SUPFAM; SSF55550; SSF55550; 2.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 2.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Angiogenesis; Complete proteome;
KW   Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; SH2 domain; SH3 domain;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    878       Guanine nucleotide exchange factor VAV2.
FT                                /FTId=PRO_0000080984.
FT   DOMAIN        1    119       CH.
FT   DOMAIN      198    376       DH.
FT   DOMAIN      405    512       PH.
FT   DOMAIN      586    652       SH3 1.
FT   DOMAIN      673    767       SH2.
FT   DOMAIN      816    877       SH3 2.
FT   ZN_FING     523    572       Phorbol-ester/DAG-type.
FT   MOD_RES     142    142       Phosphotyrosine; by EGFR.
FT   MOD_RES     159    159       Phosphotyrosine; by EGFR.
FT   MOD_RES     172    172       Phosphotyrosine; by EGFR.
FT   MOD_RES     576    576       Phosphoserine.
FT   MOD_RES     626    626       Phosphoserine.
FT   VAR_SEQ     185    189       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_034900.
FT   VAR_SEQ     470    474       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_034901.
FT   VAR_SEQ     783    811       Missing (in isoform 3).
FT                                /FTId=VSP_034902.
FT   VARIANT     594    594       M -> V (in dbSNP:rs602990).
FT                                /FTId=VAR_045690.
FT   CONFLICT    241    241       F -> L (in Ref. 5; CAE45861).
FT   CONFLICT    254    254       F -> L (in Ref. 5; CAE45861).
FT   CONFLICT    877    877       I -> T (in Ref. 5; CAE45861).
FT   STRAND      661    664
FT   HELIX       668    670
FT   STRAND      674    677
FT   HELIX       680    689
FT   STRAND      694    698
FT   STRAND      707    712
FT   STRAND      714    725
FT   STRAND      728    731
FT   STRAND      737    739
FT   HELIX       740    747
FT   TURN        752    755
FT   STRAND      767    769
FT   STRAND      819    825
FT   STRAND      842    844
FT   STRAND      847    854
FT   STRAND      856    860
FT   STRAND      863    867
FT   STRAND      869    874
SQ   SEQUENCE   878 AA;  101289 MW;  C186911605FD5B73 CRC64;
     MEQWRQCGRW LIDCKVLPPN HRVVWPSAVV FDLAQALRDG VLLCQLLHNL SPGSIDLKDI
     NFRPQMSQFL CLKNIRTFLK VCHDKFGLRN SELFDPFDLF DVRDFGKVIS AVSRLSLHSI
     AQNKGIRPFP SEETTENDDD VYRSLEELAD EHDLGEDIYD CVPCEDGGDD IYEDIIKVEV
     QQPMIRYMQK MGMTEDDKRN CCLLEIQETE AKYYRTLEDI EKNYMSPLRL VLSPADMAAV
     FINLEDLIKV HHSFLRAIDV SVMVGGSTLA KVFLDFKERL LIYGEYCSHM EHAQNTLNQL
     LASREDFRQK VEECTLKVQD GKFKLQDLLV VPMQRVLKYH LLLKELLSHS AERPERQQLK
     EALEAMQDLA MYINEVKRDK ETLRKISEFQ SSIENLQVKL EEFGRPKIDG ELKVRSIVNH
     TKQDRYLFLF DKVVIVCKRK GYSYELKEII ELLFHKMTDD PMNNKDVKKS HGKMWSYGFY
     LIHLQGKQGF QFFCKTEDMK RKWMEQFEMA MSNIKPDKAN ANHHSFQMYT FDKTTNCKAC
     KMFLRGTFYQ GYMCTKCGVG AHKECLEVIP PCKFTSPADL DASGAGPGPK MVAMQNYHGN
     PAPPGKPVLT FQTGDVLELL RGDPESPWWE GRLVQTRKSG YFPSSSVKPC PVDGRPPISR
     PPSREIDYTA YPWFAGNMER QQTDNLLKSH ASGTYLIRER PAEAERFAIS IKFNDEVKHI
     KVVEKDNWIH ITEAKKFDSL LELVEYYQCH SLKESFKQLD TTLKYPYKSR ERSASRASSR
     SPASCASYNF SFLSPQGLSF ASQGPSAPFW SVFTPRVIGT AVARYNFAAR DMRELSLREG
     DVVRIYSRIG GDQGWWKGET NGRIGWFPST YVEEEGIQ
//
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