VAV2_MOUSE
ID VAV2_MOUSE Reviewed; 868 AA.
AC Q60992; A2AH49;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Guanine nucleotide exchange factor VAV2;
DE Short=VAV-2;
GN Name=Vav2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=8710375;
RA Schuebel K.E., Bustelo X.R., Nielsen D.A., Song B.J., Barbacid M.,
RA Goldman D., Lee I.J.;
RT "Isolation and characterization of murine vav2, a member of the vav family
RT of proto-oncogenes.";
RL Oncogene 13:363-371(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, AND INTERACTION WITH EPHA2.
RX PubMed=16782872; DOI=10.1128/mcb.02215-05;
RA Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W.,
RA Chen J.;
RT "Essential role of Vav family guanine nucleotide exchange factors in EphA
RT receptor-mediated angiogenesis.";
RL Mol. Cell. Biol. 26:4830-4842(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH SSX2IP.
RX PubMed=22027834; DOI=10.1074/jbc.m111.308858;
RA Fukumoto Y., Kurita S., Takai Y., Ogita H.;
RT "Role of scaffold protein afadin dilute domain-interacting protein (ADIP)
RT in platelet-derived growth factor-induced cell movement by activating Rac
RT protein through Vav2 protein.";
RL J. Biol. Chem. 286:43537-43548(2011).
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 {ECO:0000269|PubMed:16782872}.
CC -!- SUBUNIT: Interacts (via SH2 domains) with the phosphorylated form of
CC EPHA2. Interacts with NEK3 and PRLR and this interaction is prolactin-
CC dependent (By similarity). Interacts with SSX2IP. {ECO:0000250,
CC ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:22027834}.
CC -!- PTM: Phosphorylated on tyrosine residues in response to FGR activation.
CC {ECO:0000250}.
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DR EMBL; U37017; AAC52761.1; -; mRNA.
DR EMBL; AL731552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL772282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15827.1; -.
DR RefSeq; NP_033526.1; NM_009500.2.
DR AlphaFoldDB; Q60992; -.
DR SMR; Q60992; -.
DR BioGRID; 204501; 31.
DR IntAct; Q60992; 28.
DR MINT; Q60992; -.
DR STRING; 10090.ENSMUSP00000062782; -.
DR iPTMnet; Q60992; -.
DR PhosphoSitePlus; Q60992; -.
DR EPD; Q60992; -.
DR MaxQB; Q60992; -.
DR PaxDb; Q60992; -.
DR PeptideAtlas; Q60992; -.
DR PRIDE; Q60992; -.
DR ProteomicsDB; 297809; -.
DR Antibodypedia; 1190; 348 antibodies from 40 providers.
DR DNASU; 22325; -.
DR Ensembl; ENSMUST00000056176; ENSMUSP00000062782; ENSMUSG00000009621.
DR GeneID; 22325; -.
DR KEGG; mmu:22325; -.
DR UCSC; uc008ixh.1; mouse.
DR CTD; 7410; -.
DR MGI; MGI:102718; Vav2.
DR VEuPathDB; HostDB:ENSMUSG00000009621; -.
DR eggNOG; KOG2996; Eukaryota.
DR GeneTree; ENSGT00940000159718; -.
DR HOGENOM; CLU_013787_0_0_1; -.
DR InParanoid; Q60992; -.
DR OMA; MYTFDRT; -.
DR OrthoDB; 710582at2759; -.
DR PhylomeDB; Q60992; -.
DR TreeFam; TF316171; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-2424491; DAP12 signaling.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9748787; Azathioprine ADME.
DR BioGRID-ORCS; 22325; 2 hits in 61 CRISPR screens.
DR ChiTaRS; Vav2; mouse.
DR PRO; PR:Q60992; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q60992; protein.
DR Bgee; ENSMUSG00000009621; Expressed in habenula and 196 other tissues.
DR ExpressionAtlas; Q60992; baseline and differential.
DR Genevisible; Q60992; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0030031; P:cell projection assembly; IGI:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; IGI:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IGI:MGI.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:MGI.
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 Angiogenesis; Guanine-nucleotide releasing factor; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain; Zinc;
KW Zinc-finger.
FT CHAIN 1..868
FT /note="Guanine nucleotide exchange factor VAV2"
FT /id="PRO_0000080985"
FT DOMAIN 1..120
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 193..371
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 400..502
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 576..642
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 663..757
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 806..867
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 513..562
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:0000250|UniProtKB:P52735"
FT MOD_RES 159
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000250|UniProtKB:P52735"
FT MOD_RES 172
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000250|UniProtKB:P52735"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52735"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52735"
SQ 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
