ID VAV_HUMAN Reviewed; 845 AA.
AC P15498; B4DVK9; M0QXX6; Q15860;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 4.
DT 27-MAR-2024, entry version 249.
DE RecName: Full=Proto-oncogene vav;
GN Name=VAV1; Synonyms=VAV;
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] (ISOFORM 1), AND MUTAGENESIS OF CYS-529.
RX PubMed=2069873;
RA Coppola J., Bryant S., Koda T., Conway D., Barbacid M.;
RT "Mechanism of activation of the vav protooncogene.";
RL Cell Growth Differ. 2:95-105(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10760587; DOI=10.1016/s0167-4781(00)00008-7;
RA Denkinger D.J., Borges C.R., Butler C.L., Cushman A.M., Kawahara R.S.;
RT "Genomic organization and regulation of the vav proto-oncogene.";
RL Biochim. Biophys. Acta 1491:253-262(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
RX PubMed=2005887; DOI=10.1128/mcb.11.4.1912-1920.1991;
RA Katzav S., Cleveland J.L., Heslop H.E., Pulido D.;
RT "Loss of the amino-terminal helix-loop-helix domain of the vav proto-
RT oncogene activates its transforming potential.";
RL Mol. Cell. Biol. 11:1912-1920(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-813 (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 68-845 (ISOFORM 1).
RX PubMed=2477241; DOI=10.1002/j.1460-2075.1989.tb08354.x;
RA Katzav S., Martin-Zanca D., Barbacid M.;
RT "vav, a novel human oncogene derived from a locus ubiquitously expressed in
RT hematopoietic cells.";
RL EMBO J. 8:2283-2290(1989).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 299-837 (ISOFORM 1).
RA Romero F.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 299-334 (ISOFORM 1).
RX PubMed=7478592;
RA Ramos-Morales F., Romero F., Schweighoffer F., Bismuth G., Camonis J.,
RA Tortolero M., Fischer S.;
RT "The proline-rich region of Vav binds to Grb2 and Grb3-3.";
RL Oncogene 11:1665-1669(1995).
RN [9]
RP SIMILARITY TO CDC24 FAMILY.
RX PubMed=1565462;
RA Adams J.M., Houston H., Allen J., Lints T., Harvey R.;
RT "The hematopoietically expressed vav proto-oncogene shares homology with
RT the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24)
RT involved in cytoskeletal organization.";
RL Oncogene 7:611-618(1992).
RN [10]
RP INTERACTION WITH SYK, AND MUTAGENESIS OF ARG-696.
RX PubMed=8986718; DOI=10.1016/s1074-7613(00)80273-3;
RA Deckert M., Tartare-Deckert S., Couture C., Mustelin T., Altman A.;
RT "Functional and physical interactions of Syk family kinases with the Vav
RT proto-oncogene product.";
RL Immunity 5:591-604(1996).
RN [11]
RP INTERACTION WITH CBLB.
RX PubMed=9399639; DOI=10.1038/sj.onc.1201430;
RA Bustelo X.R., Crespo P., Lopez-Barahona M., Gutkind J.S., Barbacid M.;
RT "Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated
RT c-Jun N-terminal kinase activation.";
RL Oncogene 15:2511-2520(1997).
RN [12]
RP INTERACTION WITH BLNK; PLCG1; GRB2 AND NCK1.
RX PubMed=9697839; DOI=10.1016/s1074-7613(00)80591-9;
RA Fu C., Turck C.W., Kurosaki T., Chan A.C.;
RT "BLNK: a central linker protein in B cell activation.";
RL Immunity 9:93-103(1998).
RN [13]
RP INTERACTION WITH SIAH2.
RX PubMed=10207103; DOI=10.1128/mcb.19.5.3798;
RA Germani A., Romero F., Houlard M., Camonis J., Gisselbrecht S., Fischer S.,
RA Varin-Blank N.;
RT "hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling
RT pathways.";
RL Mol. Cell. Biol. 19:3798-3807(1999).
RN [14]
RP PHOSPHORYLATION BY FYN.
RX PubMed=11005864; DOI=10.1073/pnas.97.20.10923;
RA Huang J., Tilly D., Altman A., Sugie K., Grey H.M.;
RT "T-cell receptor antagonists induce Vav phosphorylation by selective
RT activation of Fyn kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10923-10929(2000).
RN [15]
RP INTERACTION WITH DOCK2.
RX PubMed=12393632; DOI=10.1182/blood-2001-11-0032;
RA Nishihara H., Maeda M., Oda A., Tsuda M., Sawa H., Nagashima K., Tanaka S.;
RT "DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell
RT lines.";
RL Blood 100:3968-3974(2002).
RN [16]
RP INTERACTION WITH SHB.
RX PubMed=12084069; DOI=10.1046/j.1432-1033.2002.03008.x;
RA Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.;
RT "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells.";
RL Eur. J. Biochem. 269:3279-3288(2002).
RN [17]
RP INTERACTION WITH SH2B2.
RX PubMed=12400014; DOI=10.1038/sj.onc.1205927;
RA Yabana N., Shibuya M.;
RT "Adaptor protein APS binds the NH2-terminal autoinhibitory domain of
RT guanine nucleotide exchange factor Vav3 and augments its activity.";
RL Oncogene 21:7720-7729(2002).
RN [18]
RP INTERACTION WITH ITK.
RX PubMed=15661896; DOI=10.4049/jimmunol.174.3.1385;
RA Dombroski D., Houghtling R.A., Labno C.M., Precht P., Takesono A.,
RA Caplen N.J., Billadeau D.D., Wange R.L., Burkhardt J.K., Schwartzberg P.L.;
RT "Kinase-independent functions for Itk in TCR-induced regulation of Vav and
RT the actin cytoskeleton.";
RL J. Immunol. 174:1385-1392(2005).
RN [19]
RP INTERACTION WITH NEK3.
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-826, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [21]
RP INTERACTION WITH ZNF655/VIK.
RX PubMed=15558030; DOI=10.1038/sj.onc.1208043;
RA Houlard M., Romero-Portillo F., Germani A., Depaux A., Regnier-Ricard F.,
RA Gisselbrecht S., Varin-Blank N.;
RT "Characterization of VIK-1: a new Vav-interacting Kruppel-like protein.";
RL Oncogene 24:28-38(2005).
RN [22]
RP INTERACTION WITH PTK2B/PYK2.
RX PubMed=19207108; DOI=10.1042/bj20090037;
RA Gao C., Blystone S.D.;
RT "A Pyk2-Vav1 complex is recruited to beta3-adhesion sites to initiate Rho
RT activation.";
RL Biochem. J. 420:49-56(2009).
RN [23]
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 [24]
RP INTERACTION WITH CRACR2A.
RX PubMed=27016526; DOI=10.1126/scisignal.aac9171;
RA Srikanth S., Kim K.D., Gao Y., Woo J.S., Ghosh S., Calmettes G., Paz A.,
RA Abramson J., Jiang M., Gwack Y.;
RT "A large Rab GTPase encoded by CRACR2A is a component of subsynaptic
RT vesicles that transmit T cell activation signals.";
RL Sci. Signal. 9:ra31-ra31(2016).
RN [25]
RP STRUCTURE BY NMR OF 661-775.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH2 domain of human proto-oncogene protein
RT VAV1.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Couples tyrosine kinase signals with the activation of the
CC Rho/Rac GTPases, thus leading to cell differentiation and/or
CC proliferation.
CC -!- SUBUNIT: Interacts with SHB (PubMed:12084069). Interacts with SH2B2,
CC GRB2, GRB3, DOCK2, SLA, TEC and ZNF655/VIK (PubMed:12393632,
CC PubMed:12400014, PubMed:15558030). Interacts with SIAH2; without
CC leading to its degradation (PubMed:10207103). Associates with BLNK,
CC PLCG1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion
CC (PubMed:9697839). Interacts with CBLB; which inhibits tyrosine
CC phosphorylation and down-regulates activity (PubMed:9399639). May
CC interact with CCPG1. Interacts with CLNK. Interacts with THEMIS2 (By
CC similarity). Interacts with NEK3 and this interaction is prolactin-
CC dependent (PubMed:15618286). Interacts with ITK (PubMed:15661896).
CC Interacts with PTK2B/PYK2 (By similarity). Interacts with HCK.
CC Interacts with PTK2B/PYK2 (PubMed:19207108). Interacts (via SH2 domain)
CC with SYK (PubMed:8986718). Interacts with ANKRD54. Interacts with CD6
CC (By similarity). Interacts with isoform 2 of CRACR2A (PubMed:27016526).
CC {ECO:0000250|UniProtKB:P27870, ECO:0000269|PubMed:10207103,
CC ECO:0000269|PubMed:12084069, ECO:0000269|PubMed:12393632,
CC ECO:0000269|PubMed:12400014, ECO:0000269|PubMed:15558030,
CC ECO:0000269|PubMed:15618286, ECO:0000269|PubMed:15661896,
CC ECO:0000269|PubMed:19207108, ECO:0000269|PubMed:27016526,
CC ECO:0000269|PubMed:8986718, ECO:0000269|PubMed:9399639,
CC ECO:0000269|PubMed:9697839}.
CC -!- INTERACTION:
CC P15498; Q8IZP0: ABI1; NbExp=2; IntAct=EBI-625518, EBI-375446;
CC P15498; P00519: ABL1; NbExp=5; IntAct=EBI-625518, EBI-375543;
CC P15498; Q13480: GAB1; NbExp=2; IntAct=EBI-625518, EBI-517684;
CC P15498; P62993: GRB2; NbExp=3; IntAct=EBI-625518, EBI-401755;
CC P15498; Q07666: KHDRBS1; NbExp=3; IntAct=EBI-625518, EBI-1364;
CC P15498; Q13094: LCP2; NbExp=9; IntAct=EBI-625518, EBI-346946;
CC P15498; P63000: RAC1; NbExp=2; IntAct=EBI-625518, EBI-413628;
CC P15498; P78314: SH3BP2; NbExp=8; IntAct=EBI-625518, EBI-727062;
CC P15498; Q8N720: ZNF655; NbExp=5; IntAct=EBI-625518, EBI-625509;
CC P15498; P08487: PLCG1; Xeno; NbExp=4; IntAct=EBI-625518, EBI-8013886;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P15498-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15498-2; Sequence=VSP_047563;
CC -!- TISSUE SPECIFICITY: Widely expressed in hematopoietic cells but not in
CC other cell types.
CC -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues by HCK in response to IFNG and
CC bacterial lipopolysaccharide (LPS) (By similarity). Phosphorylated by
CC FYN. {ECO:0000250, ECO:0000269|PubMed:11005864}.
CC -!- MISCELLANEOUS: 'Vav' stands for the sixth letter of the Hebrew
CC alphabet.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG62721.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA34383.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/195/VAV1";
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DR EMBL; AF030227; AAC25011.1; -; Genomic_DNA.
DR EMBL; AF030201; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030202; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030203; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030204; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030205; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030206; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030207; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030208; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030209; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030210; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030211; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030212; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030213; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030214; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030215; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030216; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030217; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030218; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030219; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030220; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030221; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030222; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030223; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030224; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030225; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AF030226; AAC25011.1; JOINED; Genomic_DNA.
DR EMBL; AC010647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M59834; AAA63267.1; -; Genomic_DNA.
DR EMBL; AK301128; BAG62721.1; ALT_INIT; mRNA.
DR EMBL; X16316; CAA34383.1; ALT_FRAME; mRNA.
DR EMBL; X83931; CAA58783.1; -; mRNA.
DR CCDS; CCDS12174.1; -. [P15498-1]
DR CCDS; CCDS59342.1; -. [P15498-2]
DR PIR; B39576; TVHUVV.
DR RefSeq; NP_001245136.1; NM_001258207.1. [P15498-2]
DR RefSeq; NP_005419.2; NM_005428.3. [P15498-1]
DR PDB; 2CRH; NMR; -; A=629-775.
DR PDB; 2LCT; NMR; -; A=664-767.
DR PDB; 2MC1; NMR; -; A=664-767.
DR PDB; 2ROR; NMR; -; A=629-775.
DR PDB; 3BJI; X-ray; 2.60 A; A/B=189-565.
DR PDB; 3KY9; X-ray; 2.73 A; A/B=2-584.
DR PDB; 6NEW; X-ray; 2.50 A; A=170-575.
DR PDB; 6NF1; X-ray; 2.60 A; A=2-575.
DR PDB; 6NFA; X-ray; 2.70 A; A=170-575.
DR PDBsum; 2CRH; -.
DR PDBsum; 2LCT; -.
DR PDBsum; 2MC1; -.
DR PDBsum; 2ROR; -.
DR PDBsum; 3BJI; -.
DR PDBsum; 3KY9; -.
DR PDBsum; 6NEW; -.
DR PDBsum; 6NF1; -.
DR PDBsum; 6NFA; -.
DR AlphaFoldDB; P15498; -.
DR BMRB; P15498; -.
DR SMR; P15498; -.
DR BioGRID; 113252; 190.
DR CORUM; P15498; -.
DR DIP; DIP-1061N; -.
DR IntAct; P15498; 140.
DR MINT; P15498; -.
DR STRING; 9606.ENSP00000472929; -.
DR BindingDB; P15498; -.
DR ChEMBL; CHEMBL3259472; -.
DR iPTMnet; P15498; -.
DR PhosphoSitePlus; P15498; -.
DR BioMuta; VAV1; -.
DR DMDM; 13124807; -.
DR CPTAC; CPTAC-1226; -.
DR CPTAC; CPTAC-1227; -.
DR EPD; P15498; -.
DR jPOST; P15498; -.
DR MassIVE; P15498; -.
DR MaxQB; P15498; -.
DR PaxDb; 9606-ENSP00000472929; -.
DR PeptideAtlas; P15498; -.
DR ProteomicsDB; 53143; -. [P15498-1]
DR Pumba; P15498; -.
DR Antibodypedia; 665; 829 antibodies from 42 providers.
DR DNASU; 7409; -.
DR Ensembl; ENST00000596764.5; ENSP00000469450.1; ENSG00000141968.8. [P15498-2]
DR Ensembl; ENST00000602142.6; ENSP00000472929.1; ENSG00000141968.8. [P15498-1]
DR GeneID; 7409; -.
DR KEGG; hsa:7409; -.
DR MANE-Select; ENST00000602142.6; ENSP00000472929.1; NM_005428.4; NP_005419.2.
DR UCSC; uc002mfu.3; human. [P15498-1]
DR AGR; HGNC:12657; -.
DR CTD; 7409; -.
DR DisGeNET; 7409; -.
DR GeneCards; VAV1; -.
DR HGNC; HGNC:12657; VAV1.
DR HPA; ENSG00000141968; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 164875; gene.
DR neXtProt; NX_P15498; -.
DR OpenTargets; ENSG00000141968; -.
DR PharmGKB; PA37280; -.
DR VEuPathDB; HostDB:ENSG00000141968; -.
DR eggNOG; KOG2996; Eukaryota.
DR GeneTree; ENSGT00940000159125; -.
DR InParanoid; P15498; -.
DR OMA; PYISRPT; -.
DR OrthoDB; 2911406at2759; -.
DR PhylomeDB; P15498; -.
DR TreeFam; TF316171; -.
DR PathwayCommons; P15498; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-1433557; Signaling by SCF-KIT.
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-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8980692; RHOA 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-9027284; Erythropoietin activates RAS.
DR Reactome; R-HSA-912631; Regulation of signaling by CBL.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9748787; Azathioprine ADME.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; P15498; -.
DR SIGNOR; P15498; -.
DR BioGRID-ORCS; 7409; 21 hits in 1156 CRISPR screens.
DR ChiTaRS; VAV1; human.
DR EvolutionaryTrace; P15498; -.
DR GenomeRNAi; 7409; -.
DR Pharos; P15498; Tchem.
DR PRO; PR:P15498; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P15498; Protein.
DR Bgee; ENSG00000141968; Expressed in granulocyte and 127 other cell types or tissues.
DR ExpressionAtlas; P15498; baseline and differential.
DR Genevisible; P15498; HS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0140031; F:phosphorylation-dependent protein binding; IEA:Ensembl.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
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:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; 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:0031295; P:T cell costimulation; TAS:Reactome.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR CDD; cd20867; C1_VAV1; 1.
DR CDD; cd21262; CH_VAV1; 1.
DR CDD; cd01223; PH_Vav; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd10405; SH2_Vav1; 1.
DR CDD; cd11979; SH3_VAV1_1; 1.
DR CDD; cd11976; SH3_VAV1_2; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR IDEAL; IID00652; -.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR001715; CH_dom.
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; IPR003096; SM22_calponin.
DR InterPro; IPR035879; VAV1_SH2.
DR InterPro; IPR035730; VAV1_SH3_1.
DR InterPro; IPR035729; VAV1_SH3_2.
DR PANTHER; PTHR45818; PROTEIN VAV; 1.
DR PANTHER; PTHR45818:SF2; PROTO-ONCOGENE VAV; 1.
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; PF00018; SH3_1; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00888; SM22CALPONIN.
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; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 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; Guanine-nucleotide releasing factor;
KW Metal-binding; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
KW SH2 domain; SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..845
FT /note="Proto-oncogene vav"
FT /id="PRO_0000080980"
FT DOMAIN 1..119
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 194..373
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 402..504
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 592..660
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 671..765
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 782..842
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 515..564
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT MOD_RES 826
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 844
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P27870"
FT VAR_SEQ 187..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047563"
FT VARIANT 739
FT /note="T -> M (in dbSNP:rs36097961)"
FT /id="VAR_051997"
FT MUTAGEN 529
FT /note="C->R: Abolishes transforming activity."
FT /evidence="ECO:0000269|PubMed:2069873"
FT MUTAGEN 696
FT /note="R->L: Loss of interaction with SYK."
FT /evidence="ECO:0000269|PubMed:8986718"
FT CONFLICT 264
FT /note="A -> P (in Ref. 6; CAA34383)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="Q -> R (in Ref. 5; BAG62721)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="I -> TV (in Ref. 6)"
FT /evidence="ECO:0000305"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:6NF1"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:6NF1"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:6NF1"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 191..219
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 240..259
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 302..316
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6NF1"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 328..333
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 350..389
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 420..437
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:6NEW"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 481..488
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 489..506
FT /evidence="ECO:0007829|PDB:6NEW"
FT TURN 509..512
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:6NEW"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:6NEW"
FT STRAND 543..546
FT /evidence="ECO:0007829|PDB:6NEW"
FT TURN 547..549
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 555..560
FT /evidence="ECO:0007829|PDB:6NEW"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:2CRH"
FT STRAND 669..672
FT /evidence="ECO:0007829|PDB:2CRH"
FT HELIX 678..684
FT /evidence="ECO:0007829|PDB:2CRH"
FT TURN 685..687
FT /evidence="ECO:0007829|PDB:2CRH"
FT STRAND 692..696
FT /evidence="ECO:0007829|PDB:2CRH"
FT STRAND 700..702
FT /evidence="ECO:0007829|PDB:2LCT"
FT STRAND 706..711
FT /evidence="ECO:0007829|PDB:2CRH"
FT STRAND 714..719
FT /evidence="ECO:0007829|PDB:2CRH"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:2CRH"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:2CRH"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:2CRH"
FT HELIX 738..745
FT /evidence="ECO:0007829|PDB:2CRH"
FT HELIX 750..752
FT /evidence="ECO:0007829|PDB:2CRH"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:2LCT"
FT STRAND 763..766
FT /evidence="ECO:0007829|PDB:2CRH"
SQ SEQUENCE 845 AA; 98314 MW; AC3BC9736FD2F138 CRC64;
MELWRQCTHW LIQCRVLPPS HRVTWDGAQV CELAQALRDG VLLCQLLNNL LPHAINLREV
NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF DVQDFGKVIY TLSALSWTPI
AQNRGIMPFP TEEESVGDED IYSGLSDQID DTVEEDEDLY DCVENEEAEG DEIYEDLMRS
EPVSMPPKMT EYDKRCCCLR EIQQTEEKYT DTLGSIQQHF LKPLQRFLKP QDIEIIFINI
EDLLRVHTHF LKEMKEALGT PGAANLYQVF IKYKERFLVY GRYCSQVESA SKHLDRVAAA
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQEA MEKENLRLAL
DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLAHY GRPKIDGELK ITSVERRSKM
DRYAFLLDKA LLICKRRGDS YDLKDFVNLH SFQVRDDSSG DRDNKKWSHM FLLIEDQGAQ
GYELFFKTRE LKKKWMEQFE MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF
YQGYRCHRCR ASAHKECLGR VPPCGRHGQD FPGTMKKDKL HRRAQDKKRN ELGLPKMEVF
QEYYGLPPPP GAIGPFLRLN PGDIVELTKA EAEQNWWEGR NTSTNEIGWF PCNRVKPYVH
GPPQDLSVHL WYAGPMERAG AESILANRSD GTFLVRQRVK DAAEFAISIK YNVEVKHIKI
MTAEGLYRIT EKKAFRGLTE LVEFYQQNSL KDCFKSLDTT LQFPFKEPEK RTISRPAVGS
TKYFGTAKAR YDFCARDRSE LSLKEGDIIK ILNKKGQQGW WRGEIYGRVG WFPANYVEED
YSEYC
//
