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Guanine nucleotide exchange factor VAV2 (VAV-2)

 VAV2_HUMAN              Reviewed;         878 AA.
P52735; A2RUM4; A8MQ12; B6ZDF5; Q5SYV3; Q5SYV4; Q5SYV5; Q6N012;
Q6PIJ9; Q6Q317;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
27-SEP-2017, entry version 181.
RecName: Full=Guanine nucleotide exchange factor VAV2;
Short=VAV-2;
Name=VAV2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-594.
TISSUE=Brain;
PubMed=7762982; DOI=10.1111/j.1469-1809.1995.tb01603.x;
Henske E.P., Short M.P., Jozwiak S., Bovey C.M., Ramlakhan S.,
Haines J.L., Kwiatkowski D.J.;
"Identification of VAV2 on 9q34 and its exclusion as the tuberous
sclerosis gene TSC1.";
Ann. Hum. Genet. 59:25-37(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
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., 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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
VAL-594.
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-878 (ISOFORM 3).
TISSUE=Rectum tumor;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 453-506 (ISOFORMS 2/3).
Mancini U.M., Tajara E.H.;
"Transcript variant of VAV2 gene in tumoral cell lines (FaDu, HEp2,
HeLa and SiHa).";
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[7]
PHOSPHORYLATION AT TYR-142; TYR-159 AND TYR-172 BY EGFR.
PubMed=12454019; DOI=10.1074/jbc.M207555200;
Tamas P., Solti Z., Bauer P., Illes A., Sipeki S., Bauer A.,
Farago A., Downward J., Buday L.;
"Mechanism of epidermal growth factor regulation of Vav2, a guanine
nucleotide exchange factor for Rac.";
J. Biol. Chem. 278:5163-5171(2003).
[8]
PHOSPHORYLATION.
PubMed=15561106; DOI=10.1016/j.yexcr.2004.09.005;
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,
Lowell C.A., Berton G.;
"The proto-oncogene Fgr regulates cell migration and this requires its
plasma membrane localization.";
Exp. Cell Res. 302:253-269(2005).
[9]
INTERACTION WITH NEK3 AND PRLR.
PubMed=15618286; DOI=10.1210/me.2004-0443;
Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.;
"Novel association of Vav2 and Nek3 modulates signaling through the
human prolactin receptor.";
Mol. Endocrinol. 19:939-949(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-771 (ISOFORM 3), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
STRUCTURE BY NMR OF 663-878.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH2 domain and of the second SH3 domain of
human protein VAV-2.";
Submitted (APR-2007) to the PDB data bank.
-!- 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). {ECO:0000250}.
-!- SUBUNIT: 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.
{ECO:0000250, ECO:0000269|PubMed:15618286}.
-!- INTERACTION:
Q8IZP0:ABI1; NbExp=2; IntAct=EBI-297549, EBI-375446;
P04626:ERBB2; NbExp=3; IntAct=EBI-297549, EBI-641062;
Q13480:GAB1; NbExp=2; IntAct=EBI-297549, EBI-517684;
P51956:NEK3; NbExp=3; IntAct=EBI-297549, EBI-476041;
P78314:SH3BP2; NbExp=4; IntAct=EBI-297549, EBI-727062;
O75674:TOM1L1; NbExp=2; IntAct=EBI-297549, EBI-712991;
Q9H3M7:TXNIP; NbExp=2; IntAct=EBI-297549, EBI-1369170;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P52735-1; Sequence=Displayed;
Name=2;
IsoId=P52735-2; Sequence=VSP_034900, VSP_034901;
Name=3;
IsoId=P52735-3; Sequence=VSP_034900, VSP_034901, VSP_034902;
Note=Contains a phosphoserine at position 769. Contains a
phosphoserine at position 771. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569};
-!- TISSUE SPECIFICITY: Widely expressed.
-!- PTM: Phosphorylated on tyrosine residues in response to FGR
activation. {ECO:0000269|PubMed:12454019,
ECO:0000269|PubMed:15561106}.
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EMBL; S76992; AAB34377.1; -; mRNA.
EMBL; AL590710; CAI12279.1; -; Genomic_DNA.
EMBL; AL357934; CAI12279.1; JOINED; Genomic_DNA.
EMBL; AL445931; CAI12279.1; JOINED; Genomic_DNA.
EMBL; AL445931; CAI13722.1; -; Genomic_DNA.
EMBL; AL357934; CAI13722.1; JOINED; Genomic_DNA.
EMBL; AL590710; CAI13722.1; JOINED; Genomic_DNA.
EMBL; AL357934; CAI15783.1; -; Genomic_DNA.
EMBL; AL445931; CAI15783.1; JOINED; Genomic_DNA.
EMBL; AL590710; CAI15783.1; JOINED; Genomic_DNA.
EMBL; AL590710; CAI12278.1; -; Genomic_DNA.
EMBL; AL357934; CAI12278.1; JOINED; Genomic_DNA.
EMBL; AL445931; CAI12278.1; JOINED; Genomic_DNA.
EMBL; AL445931; CAI13723.1; -; Genomic_DNA.
EMBL; AL357934; CAI13723.1; JOINED; Genomic_DNA.
EMBL; AL590710; CAI13723.1; JOINED; Genomic_DNA.
EMBL; AL357934; CAI15781.1; -; Genomic_DNA.
EMBL; AL445931; CAI15781.1; JOINED; Genomic_DNA.
EMBL; AL590710; CAI15781.1; JOINED; Genomic_DNA.
EMBL; AL590710; CAI12280.1; -; Genomic_DNA.
EMBL; AL357934; CAI12280.1; JOINED; Genomic_DNA.
EMBL; AL445931; CAI12280.1; JOINED; Genomic_DNA.
EMBL; AL445931; CAI13724.1; -; Genomic_DNA.
EMBL; AL357934; CAI13724.1; JOINED; Genomic_DNA.
EMBL; AL590710; CAI13724.1; JOINED; Genomic_DNA.
EMBL; AL357934; CAI15782.1; -; Genomic_DNA.
EMBL; AL445931; CAI15782.1; JOINED; Genomic_DNA.
EMBL; AL590710; CAI15782.1; JOINED; Genomic_DNA.
EMBL; CH471090; EAW88108.1; -; Genomic_DNA.
EMBL; BC033187; AAH33187.1; -; mRNA.
EMBL; BC132965; AAI32966.1; -; mRNA.
EMBL; BC132967; AAI32968.1; -; mRNA.
EMBL; BX640754; CAE45861.1; -; mRNA.
EMBL; AY563001; AAS75591.1; -; mRNA.
CCDS; CCDS48053.1; -. [P52735-1]
CCDS; CCDS6979.1; -. [P52735-3]
PIR; I51940; I51940.
RefSeq; NP_001127870.1; NM_001134398.1. [P52735-1]
RefSeq; NP_003362.2; NM_003371.3. [P52735-3]
RefSeq; XP_005272270.1; XM_005272213.1. [P52735-2]
UniGene; Hs.369921; -.
UniGene; Hs.689325; -.
PDB; 2DLZ; NMR; -; A=663-767.
PDB; 2DM1; NMR; -; A=819-878.
PDB; 2LNW; NMR; -; A=659-771.
PDB; 2LNX; NMR; -; A=659-771.
PDB; 4ROJ; X-ray; 1.95 A; A/B/C=667-782.
PDBsum; 2DLZ; -.
PDBsum; 2DM1; -.
PDBsum; 2LNW; -.
PDBsum; 2LNX; -.
PDBsum; 4ROJ; -.
ProteinModelPortal; P52735; -.
SMR; P52735; -.
BioGrid; 113253; 69.
DIP; DIP-33088N; -.
IntAct; P52735; 67.
MINT; MINT-1494337; -.
STRING; 9606.ENSP00000360916; -.
iPTMnet; P52735; -.
PhosphoSitePlus; P52735; -.
BioMuta; VAV2; -.
DMDM; 212287930; -.
EPD; P52735; -.
MaxQB; P52735; -.
PaxDb; P52735; -.
PeptideAtlas; P52735; -.
PRIDE; P52735; -.
TopDownProteomics; P52735-3; -. [P52735-3]
Ensembl; ENST00000371850; ENSP00000360916; ENSG00000160293. [P52735-1]
Ensembl; ENST00000371851; ENSP00000360917; ENSG00000160293. [P52735-2]
Ensembl; ENST00000406606; ENSP00000385362; ENSG00000160293. [P52735-3]
GeneID; 7410; -.
KEGG; hsa:7410; -.
UCSC; uc004cer.4; human. [P52735-1]
CTD; 7410; -.
DisGeNET; 7410; -.
EuPathDB; HostDB:ENSG00000160293.16; -.
GeneCards; VAV2; -.
HGNC; HGNC:12658; VAV2.
HPA; HPA003224; -.
MIM; 600428; gene.
neXtProt; NX_P52735; -.
OpenTargets; ENSG00000160293; -.
PharmGKB; PA37281; -.
eggNOG; KOG2996; Eukaryota.
eggNOG; ENOG410XPH6; LUCA.
GeneTree; ENSGT00880000137925; -.
HOVERGEN; HBG018066; -.
InParanoid; P52735; -.
KO; K05730; -.
OMA; RFAISIK; -.
OrthoDB; EOG091G01O3; -.
PhylomeDB; P52735; -.
TreeFam; TF316171; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
SignaLink; P52735; -.
SIGNOR; P52735; -.
ChiTaRS; VAV2; human.
EvolutionaryTrace; P52735; -.
GeneWiki; VAV2; -.
GenomeRNAi; 7410; -.
PRO; PR:P52735; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000160293; -.
Genevisible; P52735; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
GO; GO:0030193; P:regulation of blood coagulation; IMP:UniProtKB.
GO; GO:0008361; P:regulation of cell size; IGI:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IGI:UniProtKB.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd00029; C1; 1.
CDD; cd00014; CH; 1.
Gene3D; 1.10.418.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR022613; CAMSAP_CH.
InterPro; IPR001715; CH-domain.
InterPro; IPR000219; DH-domain.
InterPro; IPR001331; GDS_CDC24_CS.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR000980; SH2.
InterPro; IPR011511; SH3_2.
InterPro; IPR001452; SH3_domain.
Pfam; PF00130; C1_1; 1.
Pfam; PF11971; CAMSAP_CH; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00621; RhoGEF; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF07653; SH3_2; 2.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00109; C1; 1.
SMART; SM00033; CH; 1.
SMART; SM00233; PH; 1.
SMART; SM00325; RhoGEF; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 2.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF50044; SSF50044; 2.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF55550; SSF55550; 2.
PROSITE; PS50021; CH; 1.
PROSITE; PS00741; DH_1; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 2.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; Complete proteome;
Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; SH2 domain; SH3 domain;
Zinc; Zinc-finger.
CHAIN 1 878 Guanine nucleotide exchange factor VAV2.
/FTId=PRO_0000080984.
DOMAIN 1 119 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 198 376 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 405 512 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 586 652 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 673 767 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 816 877 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
ZN_FING 523 572 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
MOD_RES 142 142 Phosphotyrosine; by EGFR.
{ECO:0000269|PubMed:12454019}.
MOD_RES 159 159 Phosphotyrosine; by EGFR.
{ECO:0000269|PubMed:12454019}.
MOD_RES 172 172 Phosphotyrosine; by EGFR.
{ECO:0000269|PubMed:12454019}.
MOD_RES 576 576 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 583 583 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
VAR_SEQ 185 189 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_034900.
VAR_SEQ 470 474 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_034901.
VAR_SEQ 783 811 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_034902.
VARIANT 594 594 M -> V (in dbSNP:rs602990).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7762982}.
/FTId=VAR_045690.
CONFLICT 241 241 F -> L (in Ref. 5; CAE45861).
{ECO:0000305}.
CONFLICT 254 254 F -> L (in Ref. 5; CAE45861).
{ECO:0000305}.
CONFLICT 877 877 I -> T (in Ref. 5; CAE45861).
{ECO:0000305}.
STRAND 661 664 {ECO:0000244|PDB:2LNX}.
HELIX 668 670 {ECO:0000244|PDB:2DLZ}.
STRAND 674 677 {ECO:0000244|PDB:2DLZ}.
HELIX 680 687 {ECO:0000244|PDB:4ROJ}.
STRAND 694 699 {ECO:0000244|PDB:4ROJ}.
STRAND 703 705 {ECO:0000244|PDB:4ROJ}.
STRAND 707 713 {ECO:0000244|PDB:4ROJ}.
STRAND 716 725 {ECO:0000244|PDB:4ROJ}.
STRAND 728 732 {ECO:0000244|PDB:4ROJ}.
STRAND 735 739 {ECO:0000244|PDB:4ROJ}.
HELIX 740 749 {ECO:0000244|PDB:4ROJ}.
HELIX 752 754 {ECO:0000244|PDB:4ROJ}.
STRAND 767 769 {ECO:0000244|PDB:2LNW}.
STRAND 819 825 {ECO:0000244|PDB:2DM1}.
STRAND 842 844 {ECO:0000244|PDB:2DM1}.
STRAND 847 854 {ECO:0000244|PDB:2DM1}.
STRAND 856 860 {ECO:0000244|PDB:2DM1}.
STRAND 863 867 {ECO:0000244|PDB:2DM1}.
STRAND 869 874 {ECO:0000244|PDB:2DM1}.
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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