VAV2_HUMAN
ID VAV2_HUMAN Reviewed; 878 AA.
AC P52735; A2RUM4; A8MQ12; B6ZDF5; Q5SYV3; Q5SYV4; Q5SYV5; Q6N012; Q6PIJ9;
AC Q6Q317;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 212.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Haines J.L.,
RA Kwiatkowski D.J.;
RT "Identification of VAV2 on 9q34 and its exclusion as the tuberous sclerosis
RT 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., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., 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., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., 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., Rogers J.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 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 project:
RT 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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, HeLa
RT 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., Farago A.,
RA 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 human
RT 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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND IDENTIFICATION BY
RP 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 the
RT 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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION BY
RP 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-771 (ISOFORM 3), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
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 human
RT protein VAV-2.";
RL Submitted (APR-2007) to the PDB data bank.
CC -!- FUNCTION: Guanine nucleotide exchange factor for the Rho family of Ras-
CC related GTPases. Plays an important role in angiogenesis. Its
CC recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1
CC GTPase activation and vascular endothelial cell migration and assembly
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via SH2 domains) with the phosphorylated form of
CC EPHA2. Interacts with SSX2IP (By similarity). Interacts with NEK3 and
CC PRLR and this interaction is prolactin-dependent. {ECO:0000250,
CC ECO:0000269|PubMed:15618286}.
CC -!- INTERACTION:
CC P52735; Q8IZP0: ABI1; NbExp=2; IntAct=EBI-297549, EBI-375446;
CC P52735; Q03135: CAV1; NbExp=2; IntAct=EBI-297549, EBI-603614;
CC P52735; P04626: ERBB2; NbExp=3; IntAct=EBI-297549, EBI-641062;
CC P52735; Q13480: GAB1; NbExp=2; IntAct=EBI-297549, EBI-517684;
CC P52735; P51956: NEK3; NbExp=3; IntAct=EBI-297549, EBI-476041;
CC P52735; P78314: SH3BP2; NbExp=4; IntAct=EBI-297549, EBI-727062;
CC P52735; O75674: TOM1L1; NbExp=2; IntAct=EBI-297549, EBI-712991;
CC P52735; Q9H3M7: TXNIP; NbExp=2; IntAct=EBI-297549, EBI-1369170;
CC P52735-1; Q03135: CAV1; NbExp=3; IntAct=EBI-15875004, EBI-603614;
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 -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- PTM: Phosphorylated on tyrosine residues in response to FGR activation.
CC {ECO:0000269|PubMed:12454019, ECO:0000269|PubMed:15561106}.
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DR EMBL; S76992; AAB34377.1; -; mRNA.
DR EMBL; AL590710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357934; -; NOT_ANNOTATED_CDS; 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 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 PDB; 4ROJ; X-ray; 1.95 A; A/B/C=667-782.
DR PDB; 7RNV; X-ray; 2.15 A; A=665-774.
DR PDBsum; 2DLZ; -.
DR PDBsum; 2DM1; -.
DR PDBsum; 2LNW; -.
DR PDBsum; 2LNX; -.
DR PDBsum; 4ROJ; -.
DR PDBsum; 7RNV; -.
DR AlphaFoldDB; P52735; -.
DR BMRB; P52735; -.
DR SMR; P52735; -.
DR BioGRID; 113253; 88.
DR DIP; DIP-33088N; -.
DR IntAct; P52735; 72.
DR MINT; P52735; -.
DR STRING; 9606.ENSP00000360916; -.
DR MoonDB; P52735; Predicted.
DR GlyGen; P52735; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P52735; -.
DR PhosphoSitePlus; P52735; -.
DR BioMuta; VAV2; -.
DR DMDM; 212287930; -.
DR EPD; P52735; -.
DR jPOST; P52735; -.
DR MassIVE; P52735; -.
DR MaxQB; P52735; -.
DR PaxDb; P52735; -.
DR PeptideAtlas; P52735; -.
DR PRIDE; P52735; -.
DR ProteomicsDB; 56505; -. [P52735-1]
DR ProteomicsDB; 56506; -. [P52735-2]
DR ProteomicsDB; 56507; -. [P52735-3]
DR TopDownProteomics; P52735-3; -. [P52735-3]
DR Antibodypedia; 1190; 348 antibodies from 40 providers.
DR DNASU; 7410; -.
DR Ensembl; ENST00000371850.8; ENSP00000360916.3; ENSG00000160293.17. [P52735-1]
DR Ensembl; ENST00000371851.1; ENSP00000360917.1; ENSG00000160293.17. [P52735-2]
DR Ensembl; ENST00000406606.7; ENSP00000385362.3; ENSG00000160293.17. [P52735-3]
DR GeneID; 7410; -.
DR KEGG; hsa:7410; -.
DR MANE-Select; ENST00000371850.8; ENSP00000360916.3; NM_001134398.2; NP_001127870.1.
DR UCSC; uc004cer.4; human. [P52735-1]
DR CTD; 7410; -.
DR DisGeNET; 7410; -.
DR GeneCards; VAV2; -.
DR HGNC; HGNC:12658; VAV2.
DR HPA; ENSG00000160293; Low tissue specificity.
DR MIM; 600428; gene.
DR neXtProt; NX_P52735; -.
DR OpenTargets; ENSG00000160293; -.
DR PharmGKB; PA37281; -.
DR VEuPathDB; HostDB:ENSG00000160293; -.
DR eggNOG; KOG2996; Eukaryota.
DR GeneTree; ENSGT00940000159718; -.
DR HOGENOM; CLU_013787_0_0_1; -.
DR InParanoid; P52735; -.
DR OMA; MYTFDRT; -.
DR OrthoDB; 710582at2759; -.
DR PhylomeDB; P52735; -.
DR TreeFam; TF316171; -.
DR PathwayCommons; P52735; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-2424491; DAP12 signaling.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-445144; Signal transduction by L1.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-9748787; Azathioprine ADME.
DR SignaLink; P52735; -.
DR SIGNOR; P52735; -.
DR BioGRID-ORCS; 7410; 14 hits in 1070 CRISPR screens.
DR ChiTaRS; VAV2; human.
DR EvolutionaryTrace; P52735; -.
DR GeneWiki; VAV2; -.
DR GenomeRNAi; 7410; -.
DR Pharos; P52735; Tbio.
DR PRO; PR:P52735; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P52735; protein.
DR Bgee; ENSG00000160293; Expressed in parotid gland and 163 other tissues.
DR Genevisible; P52735; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; 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:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; TAS:Reactome.
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:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
DR GO; GO:0008361; P:regulation of cell size; IGI:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IGI:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR CDD; cd00029; C1; 1.
DR CDD; cd00014; CH; 1.
DR CDD; cd01223; PH_Vav; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd10406; SH2_Vav2; 1.
DR CDD; cd11980; SH3_VAV2_1; 1.
DR CDD; cd11977; SH3_VAV2_2; 1.
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; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037832; PH_Vav.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035880; VAV2_SH2.
DR InterPro; IPR035733; VAV2_SH3_1.
DR InterPro; IPR035732; VAV2_SH3_2.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF11971; CAMSAP_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; 1.
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;
KW Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH2 domain; SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..878
FT /note="Guanine nucleotide exchange factor VAV2"
FT /id="PRO_0000080984"
FT DOMAIN 1..120
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 198..376
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 405..512
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 586..652
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 673..767
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 816..877
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 523..572
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT MOD_RES 142
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000269|PubMed:12454019"
FT MOD_RES 159
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000269|PubMed:12454019"
FT MOD_RES 172
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000269|PubMed:12454019"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 185..189
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_034900"
FT VAR_SEQ 470..474
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_034901"
FT VAR_SEQ 783..811
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_034902"
FT VARIANT 594
FT /note="M -> V (in dbSNP:rs602990)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7762982"
FT /id="VAR_045690"
FT CONFLICT 241
FT /note="F -> L (in Ref. 5; CAE45861)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="F -> L (in Ref. 5; CAE45861)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="I -> T (in Ref. 5; CAE45861)"
FT /evidence="ECO:0000305"
FT STRAND 661..664
FT /evidence="ECO:0007829|PDB:2LNX"
FT HELIX 668..670
FT /evidence="ECO:0007829|PDB:7RNV"
FT STRAND 674..677
FT /evidence="ECO:0007829|PDB:7RNV"
FT HELIX 680..687
FT /evidence="ECO:0007829|PDB:4ROJ"
FT STRAND 694..699
FT /evidence="ECO:0007829|PDB:4ROJ"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:4ROJ"
FT STRAND 707..713
FT /evidence="ECO:0007829|PDB:4ROJ"
FT STRAND 716..725
FT /evidence="ECO:0007829|PDB:4ROJ"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:4ROJ"
FT STRAND 735..739
FT /evidence="ECO:0007829|PDB:4ROJ"
FT HELIX 740..749
FT /evidence="ECO:0007829|PDB:4ROJ"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:4ROJ"
FT STRAND 765..767
FT /evidence="ECO:0007829|PDB:7RNV"
FT STRAND 819..825
FT /evidence="ECO:0007829|PDB:2DM1"
FT STRAND 842..844
FT /evidence="ECO:0007829|PDB:2DM1"
FT STRAND 847..854
FT /evidence="ECO:0007829|PDB:2DM1"
FT STRAND 856..860
FT /evidence="ECO:0007829|PDB:2DM1"
FT STRAND 863..867
FT /evidence="ECO:0007829|PDB:2DM1"
FT STRAND 869..874
FT /evidence="ECO:0007829|PDB:2DM1"
FT MOD_RES P52735-3:769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES P52735-3:771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
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
