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Guanine nucleotide exchange factor VAV2 (VAV-2)

 VAV2_MOUSE              Reviewed;         868 AA.
Q60992; A2AH49;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
12-SEP-2018, entry version 160.
RecName: Full=Guanine nucleotide exchange factor VAV2;
Short=VAV-2;
Name=Vav2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=8710375;
Schuebel K.E., Bustelo X.R., Nielsen D.A., Song B.J., Barbacid M.,
Goldman D., Lee I.J.;
"Isolation and characterization of murine vav2, a member of the vav
family of proto-oncogenes.";
Oncogene 13:363-371(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
FUNCTION, AND INTERACTION WITH EPHA2.
PubMed=16782872; DOI=10.1128/MCB.02215-05;
Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W.,
Chen J.;
"Essential role of Vav family guanine nucleotide exchange factors in
EphA receptor-mediated angiogenesis.";
Mol. Cell. Biol. 26:4830-4842(2006).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
INTERACTION WITH SSX2IP.
PubMed=22027834; DOI=10.1074/jbc.M111.308858;
Fukumoto Y., Kurita S., Takai Y., Ogita H.;
"Role of scaffold protein afadin dilute domain-interacting protein
(ADIP) in platelet-derived growth factor-induced cell movement by
activating Rac protein through Vav2 protein.";
J. Biol. Chem. 286:43537-43548(2011).
-!- 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. {ECO:0000269|PubMed:16782872}.
-!- SUBUNIT: Interacts (via SH2 domains) with the phosphorylated form
of EPHA2. Interacts with NEK3 and PRLR and this interaction is
prolactin-dependent (By similarity). Interacts with SSX2IP.
{ECO:0000250, ECO:0000269|PubMed:16782872,
ECO:0000269|PubMed:22027834}.
-!- PTM: Phosphorylated on tyrosine residues in response to FGR
activation. {ECO:0000250}.
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EMBL; U37017; AAC52761.1; -; mRNA.
EMBL; AL731552; CAM13732.1; -; Genomic_DNA.
EMBL; AL772282; CAM13732.1; JOINED; Genomic_DNA.
EMBL; AL772282; CAM21000.1; -; Genomic_DNA.
EMBL; AL731552; CAM21000.1; JOINED; Genomic_DNA.
CCDS; CCDS15827.1; -.
RefSeq; NP_033526.1; NM_009500.2.
UniGene; Mm.179011; -.
ProteinModelPortal; Q60992; -.
SMR; Q60992; -.
IntAct; Q60992; 4.
STRING; 10090.ENSMUSP00000062782; -.
iPTMnet; Q60992; -.
PhosphoSitePlus; Q60992; -.
MaxQB; Q60992; -.
PaxDb; Q60992; -.
PeptideAtlas; Q60992; -.
PRIDE; Q60992; -.
DNASU; 22325; -.
Ensembl; ENSMUST00000056176; ENSMUSP00000062782; ENSMUSG00000009621.
GeneID; 22325; -.
KEGG; mmu:22325; -.
UCSC; uc008ixh.1; mouse.
CTD; 7410; -.
MGI; MGI:102718; Vav2.
eggNOG; KOG2996; Eukaryota.
eggNOG; ENOG410XPH6; LUCA.
GeneTree; ENSGT00920000148946; -.
HOGENOM; HOG000234364; -.
HOVERGEN; HBG018066; -.
InParanoid; Q60992; -.
KO; K05730; -.
OMA; PGPKMVA; -.
OrthoDB; EOG091G01O3; -.
PhylomeDB; Q60992; -.
TreeFam; TF316171; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-193648; NRAGE signals death through JNK.
Reactome; R-MMU-194840; Rho GTPase cycle.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-MMU-416482; G alpha (12/13) signalling events.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-445144; Signal transduction by L1.
Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
ChiTaRS; Vav2; mouse.
PRO; PR:Q60992; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000009621; Expressed in 219 organ(s), highest expression level in mesenteric lymph node.
CleanEx; MM_VAV2; -.
ExpressionAtlas; Q60992; baseline and differential.
Genevisible; Q60992; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:MGI.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IGI:MGI.
GO; GO:0030031; P:cell projection assembly; IGI:MGI.
GO; GO:0030032; P:lamellipodium assembly; IGI:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IGI:MGI.
GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:MGI.
CDD; cd00029; C1; 1.
CDD; cd00014; CH; 1.
CDD; cd01223; PH_Vav; 1.
CDD; cd00160; RhoGEF; 1.
CDD; cd10406; SH2_Vav2; 1.
CDD; cd11980; SH3_VAV2_1; 1.
CDD; cd11977; SH3_VAV2_2; 1.
Gene3D; 1.10.418.10; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR022613; CAMSAP_CH.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR001331; GDS_CDC24_CS.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR037832; PH_Vav.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR035880; VAV2_SH2.
InterPro; IPR035733; VAV2_SH3_1.
InterPro; IPR035732; VAV2_SH3_2.
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; 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;
Angiogenesis; Complete proteome; Guanine-nucleotide releasing factor;
Metal-binding; Phosphoprotein; Reference proteome; Repeat; SH2 domain;
SH3 domain; Zinc; Zinc-finger.
CHAIN 1 868 Guanine nucleotide exchange factor VAV2.
/FTId=PRO_0000080985.
DOMAIN 1 120 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 193 371 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 400 502 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 576 642 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 663 757 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 806 867 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
ZN_FING 513 562 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
MOD_RES 142 142 Phosphotyrosine; by EGFR.
{ECO:0000250|UniProtKB:P52735}.
MOD_RES 159 159 Phosphotyrosine; by EGFR.
{ECO:0000250|UniProtKB:P52735}.
MOD_RES 172 172 Phosphotyrosine; by EGFR.
{ECO:0000250|UniProtKB:P52735}.
MOD_RES 566 566 Phosphoserine.
{ECO:0000250|UniProtKB:P52735}.
MOD_RES 616 616 Phosphoserine.
{ECO:0000250|UniProtKB:P52735}.
SEQUENCE 868 AA; 99915 MW; D18581E7EEB2DBC2 CRC64;
MEQWRQCGRW LIDCKVLPPN HRVVWPSAVV FDLAQALRDG VLLCQLLHNL SPGSIDLKDI
NFRPQMSQFL CLKNIRTFLK VCHDKFGLRN SELFDPFDLF DVRDFGKVIS AVSRLSLHSI
AQSKGIRPFP SEETAENDDD VYRSLEELAD EHDLGEDIYD CVPCEDEGDD IYEDIIKVEV
QQPMKMGMTE DDKRSCCLLE IQETEAKYYR TLEDIEKNYM GPLRLVLSPA DMAAVFINLE
DLIKVHHSFL RAIDVSMMAG GSTLAKVFLE FKERLLIYGE YCSHMEHAQS TLNQLLASRE
DFRQKVEECT LRVQDGKFKL QDLLVVPMQR VLKYHLLLKE LLSHSADRPE RQQLKEALEA
MQDLAMYINE VKRDKETLKK ISEFQCSIEN LQVKLEEFGR PKIDGELKVR SIVNHTKQDR
YLFLFDKVVI VCKRKGYSYE LKEVIELLFH KMTDDPMHNK DIKKWSYGFY LIHLQGKQGF
QFFCKTEDMK RKWMEQFEMA MSNIKPDKAN ANHHSFQMYT FDKTTNCKAC KMFLRGTFYQ
GYLCTRCGVG AHKECLEVIP PCKMSSPADV DAPGAGPGPK MVAVQNYHGN PAPPGKPVLT
FQTGDVIELL RGDPDSPWWE GRLVQTRKSG YFPSSSVKPC PVDGRPPTGR PPSREIDYTA
YPWFAGNMER QQTDNLLKSH ASGTYLIRER PAEAERFAIS IKFNDEVKHI KVVEKDSWIH
ITEAKKFESL LELVEYYQCH SLKESFKQLD TTLKFPYKSR ERTTSRASSR SPASCASYNF
SFLSPQGLSF APQAPSAPFW SVFTPRVIGT AVARYNFAAR DMRELSLREG DVVKIYSRIG
GDQGWWKGET NGRIGWFPST YVEEEGVQ


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