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Proto-oncogene vav

 VAV_HUMAN               Reviewed;         845 AA.
P15498; B4DVK9; M0QXX6; Q15860;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 4.
12-SEP-2018, entry version 217.
RecName: Full=Proto-oncogene vav;
Name=VAV1; Synonyms=VAV;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF CYS-529.
PubMed=2069873;
Coppola J., Bryant S., Koda T., Conway D., Barbacid M.;
"Mechanism of activation of the vav protooncogene.";
Cell Growth Differ. 2:95-105(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10760587; DOI=10.1016/S0167-4781(00)00008-7;
Denkinger D.J., Borges C.R., Butler C.L., Cushman A.M., Kawahara R.S.;
"Genomic organization and regulation of the vav proto-oncogene.";
Biochim. Biophys. Acta 1491:253-262(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
PubMed=2005887; DOI=10.1128/MCB.11.4.1912;
Katzav S., Cleveland J.L., Heslop H.E., Pulido D.;
"Loss of the amino-terminal helix-loop-helix domain of the vav proto-
oncogene activates its transforming potential.";
Mol. Cell. Biol. 11:1912-1920(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-813 (ISOFORM 2).
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 68-845 (ISOFORM 1).
PubMed=2477241;
Katzav S., Martin-Zanca D., Barbacid M.;
"vav, a novel human oncogene derived from a locus ubiquitously
expressed in hematopoietic cells.";
EMBO J. 8:2283-2290(1989).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 299-837 (ISOFORM 1).
Romero F.;
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 299-334 (ISOFORM 1).
PubMed=7478592;
Ramos-Morales F., Romero F., Schweighoffer F., Bismuth G., Camonis J.,
Tortolero M., Fischer S.;
"The proline-rich region of Vav binds to Grb2 and Grb3-3.";
Oncogene 11:1665-1669(1995).
[9]
SIMILARITY TO CDC24 FAMILY.
PubMed=1565462;
Adams J.M., Houston H., Allen J., Lints T., Harvey R.;
"The hematopoietically expressed vav proto-oncogene shares homology
with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene
(CDC24) involved in cytoskeletal organization.";
Oncogene 7:611-618(1992).
[10]
INTERACTION WITH SYK, AND MUTAGENESIS OF ARG-696.
PubMed=8986718; DOI=10.1016/S1074-7613(00)80273-3;
Deckert M., Tartare-Deckert S., Couture C., Mustelin T., Altman A.;
"Functional and physical interactions of Syk family kinases with the
Vav proto-oncogene product.";
Immunity 5:591-604(1996).
[11]
INTERACTION WITH CBLB.
PubMed=9399639; DOI=10.1038/sj.onc.1201430;
Bustelo X.R., Crespo P., Lopez-Barahona M., Gutkind J.S., Barbacid M.;
"Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-
mediated c-Jun N-terminal kinase activation.";
Oncogene 15:2511-2520(1997).
[12]
INTERACTION WITH BLNK; PLCG1; GRB2 AND NCK1.
PubMed=9697839; DOI=10.1016/S1074-7613(00)80591-9;
Fu C., Turck C.W., Kurosaki T., Chan A.C.;
"BLNK: a central linker protein in B cell activation.";
Immunity 9:93-103(1998).
[13]
INTERACTION WITH SIAH2.
PubMed=10207103; DOI=10.1128/MCB.19.5.3798;
Germani A., Romero F., Houlard M., Camonis J., Gisselbrecht S.,
Fischer S., Varin-Blank N.;
"hSiah2 is a new Vav binding protein which inhibits Vav-mediated
signaling pathways.";
Mol. Cell. Biol. 19:3798-3807(1999).
[14]
PHOSPHORYLATION BY FYN.
PubMed=11005864; DOI=10.1073/pnas.97.20.10923;
Huang J., Tilly D., Altman A., Sugie K., Grey H.M.;
"T-cell receptor antagonists induce Vav phosphorylation by selective
activation of Fyn kinase.";
Proc. Natl. Acad. Sci. U.S.A. 97:10923-10929(2000).
[15]
INTERACTION WITH DOCK2.
PubMed=12393632; DOI=10.1182/blood-2001-11-0032;
Nishihara H., Maeda M., Oda A., Tsuda M., Sawa H., Nagashima K.,
Tanaka S.;
"DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell
lines.";
Blood 100:3968-3974(2002).
[16]
INTERACTION WITH SHB.
PubMed=12084069; DOI=10.1046/j.1432-1033.2002.03008.x;
Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.;
"Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells.";
Eur. J. Biochem. 269:3279-3288(2002).
[17]
INTERACTION WITH APS.
PubMed=12400014; DOI=10.1038/sj.onc.1205927;
Yabana N., Shibuya M.;
"Adaptor protein APS binds the NH2-terminal autoinhibitory domain of
guanine nucleotide exchange factor Vav3 and augments its activity.";
Oncogene 21:7720-7729(2002).
[18]
INTERACTION WITH ITK.
PubMed=15661896; DOI=10.4049/jimmunol.174.3.1385;
Dombroski D., Houghtling R.A., Labno C.M., Precht P., Takesono A.,
Caplen N.J., Billadeau D.D., Wange R.L., Burkhardt J.K.,
Schwartzberg P.L.;
"Kinase-independent functions for Itk in TCR-induced regulation of Vav
and the actin cytoskeleton.";
J. Immunol. 174:1385-1392(2005).
[19]
INTERACTION WITH NEK3.
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-826, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[21]
INTERACTION WITH ZNF655/VIK.
PubMed=15558030; DOI=10.1038/sj.onc.1208043;
Houlard M., Romero-Portillo F., Germani A., Depaux A.,
Regnier-Ricard F., Gisselbrecht S., Varin-Blank N.;
"Characterization of VIK-1: a new Vav-interacting Kruppel-like
protein.";
Oncogene 24:28-38(2005).
[22]
INTERACTION WITH PTK2B/PYK2.
PubMed=19207108; DOI=10.1042/BJ20090037;
Gao C., Blystone S.D.;
"A Pyk2-Vav1 complex is recruited to beta3-adhesion sites to initiate
Rho activation.";
Biochem. J. 420:49-56(2009).
[23]
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).
[24]
STRUCTURE BY NMR OF 661-775.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH2 domain of human proto-oncogene protein
VAV1.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: Couples tyrosine kinase signals with the activation of
the Rho/Rac GTPases, thus leading to cell differentiation and/or
proliferation.
-!- SUBUNIT: Interacts with SHB (PubMed:12084069). Interacts with APS,
GRB2, GRB3, DOCK2, SLA, TEC and ZNF655/VIK (PubMed:12393632,
PubMed:12400014, PubMed:15558030). Interacts with SIAH2; without
leading to its degradation (PubMed:10207103). Associates with
BLNK, PLCG1, GRB2 and NCK1 in a B-cell antigen receptor-dependent
fashion (PubMed:9697839). Interacts with CBLB; which inhibits
tyrosine phosphorylation and down-regulates activity
(PubMed:9399639). May interact with CCPG1. Interacts with CLNK.
Interacts with THEMIS2 (By similarity). Interacts with NEK3 and
this interaction is prolactin-dependent (PubMed:15618286).
Interacts with ITK (PubMed:15661896). Interacts with PTK2B/PYK2
(By similarity). Interacts with HCK. Interacts with PTK2B/PYK2
(PubMed:19207108). Interacts (via SH2 domain) with SYK
(PubMed:8986718). Interacts with ANKRD54. Interacts with CD6 (By
similarity). {ECO:0000250|UniProtKB:P27870,
ECO:0000269|PubMed:10207103, ECO:0000269|PubMed:12084069,
ECO:0000269|PubMed:12393632, ECO:0000269|PubMed:12400014,
ECO:0000269|PubMed:15558030, ECO:0000269|PubMed:15618286,
ECO:0000269|PubMed:15661896, ECO:0000269|PubMed:19207108,
ECO:0000269|PubMed:8986718, ECO:0000269|PubMed:9399639,
ECO:0000269|PubMed:9697839}.
-!- INTERACTION:
Q8IZP0:ABI1; NbExp=2; IntAct=EBI-625518, EBI-375446;
P00519:ABL1; NbExp=5; IntAct=EBI-625518, EBI-375543;
Q13480:GAB1; NbExp=2; IntAct=EBI-625518, EBI-517684;
P62993:GRB2; NbExp=2; IntAct=EBI-625518, EBI-401755;
Q07666:KHDRBS1; NbExp=3; IntAct=EBI-625518, EBI-1364;
Q13094:LCP2; NbExp=9; IntAct=EBI-625518, EBI-346946;
P08487:PLCG1 (xeno); NbExp=4; IntAct=EBI-625518, EBI-8013886;
P63000:RAC1; NbExp=2; IntAct=EBI-625518, EBI-413628;
P78314:SH3BP2; NbExp=8; IntAct=EBI-625518, EBI-727062;
Q8N720:ZNF655; NbExp=5; IntAct=EBI-625518, EBI-625509;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P15498-1; Sequence=Displayed;
Name=2;
IsoId=P15498-2; Sequence=VSP_047563;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed in hematopoietic cells but
not in other cell types.
-!- DOMAIN: The DH domain is involved in interaction with CCPG1.
{ECO:0000250}.
-!- PTM: Phosphorylated on tyrosine residues by HCK in response to
IFNG and bacterial lipopolysaccharide (LPS) (By similarity).
Phosphorylated by FYN. {ECO:0000250, ECO:0000269|PubMed:11005864}.
-!- MISCELLANEOUS: 'Vav' stands for the sixth letter of the Hebrew
alphabet.
-!- SEQUENCE CAUTION:
Sequence=BAG62721.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA34383.1; Type=Frameshift; Positions=322, 355; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/VAV1ID195ch19p13.html";
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EMBL; AF030227; AAC25011.1; -; Genomic_DNA.
EMBL; AF030201; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030202; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030203; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030204; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030205; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030206; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030207; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030208; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030209; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030210; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030211; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030212; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030213; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030214; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030215; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030216; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030217; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030218; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030219; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030220; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030221; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030222; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030223; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030224; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030225; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AF030226; AAC25011.1; JOINED; Genomic_DNA.
EMBL; AC010647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC020895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC020954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M59834; AAA63267.1; -; Genomic_DNA.
EMBL; AK301128; BAG62721.1; ALT_INIT; mRNA.
EMBL; X16316; CAA34383.1; ALT_FRAME; mRNA.
EMBL; X83931; CAA58783.1; -; mRNA.
CCDS; CCDS12174.1; -. [P15498-1]
CCDS; CCDS59342.1; -. [P15498-2]
PIR; B39576; TVHUVV.
RefSeq; NP_001245136.1; NM_001258207.1. [P15498-2]
RefSeq; NP_005419.2; NM_005428.3. [P15498-1]
UniGene; Hs.116237; -.
PDB; 2CRH; NMR; -; A=629-775.
PDB; 2LCT; NMR; -; A=664-767.
PDB; 2MC1; NMR; -; A=664-767.
PDB; 2ROR; NMR; -; A=629-775.
PDB; 3BJI; X-ray; 2.60 A; A/B=189-565.
PDB; 3KY9; X-ray; 2.73 A; A/B=2-584.
PDBsum; 2CRH; -.
PDBsum; 2LCT; -.
PDBsum; 2MC1; -.
PDBsum; 2ROR; -.
PDBsum; 3BJI; -.
PDBsum; 3KY9; -.
ProteinModelPortal; P15498; -.
SMR; P15498; -.
BioGrid; 113252; 88.
CORUM; P15498; -.
DIP; DIP-1061N; -.
IntAct; P15498; 29.
MINT; P15498; -.
STRING; 9606.ENSP00000472929; -.
BindingDB; P15498; -.
ChEMBL; CHEMBL3259472; -.
iPTMnet; P15498; -.
PhosphoSitePlus; P15498; -.
BioMuta; VAV1; -.
DMDM; 13124807; -.
EPD; P15498; -.
MaxQB; P15498; -.
PaxDb; P15498; -.
PeptideAtlas; P15498; -.
PRIDE; P15498; -.
ProteomicsDB; 53143; -.
DNASU; 7409; -.
Ensembl; ENST00000596764; ENSP00000469450; ENSG00000141968. [P15498-2]
Ensembl; ENST00000602142; ENSP00000472929; ENSG00000141968. [P15498-1]
GeneID; 7409; -.
KEGG; hsa:7409; -.
UCSC; uc002mfu.3; human. [P15498-1]
CTD; 7409; -.
DisGeNET; 7409; -.
EuPathDB; HostDB:ENSG00000141968.7; -.
GeneCards; VAV1; -.
H-InvDB; HIX0202828; -.
HGNC; HGNC:12657; VAV1.
HPA; HPA001864; -.
MIM; 164875; gene.
neXtProt; NX_P15498; -.
OpenTargets; ENSG00000141968; -.
PharmGKB; PA37280; -.
eggNOG; KOG2996; Eukaryota.
eggNOG; ENOG410XPH6; LUCA.
GeneTree; ENSGT00920000148946; -.
HOGENOM; HOG000234364; -.
HOVERGEN; HBG018066; -.
InParanoid; P15498; -.
KO; K05730; -.
OMA; DKRECCL; -.
OrthoDB; EOG091G01O3; -.
PhylomeDB; P15498; -.
TreeFam; TF316171; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
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-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; P15498; -.
SIGNOR; P15498; -.
ChiTaRS; VAV1; human.
EvolutionaryTrace; P15498; -.
GenomeRNAi; 7409; -.
PMAP-CutDB; P15498; -.
PRO; PR:P15498; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000141968; Expressed in 124 organ(s), highest expression level in blood.
CleanEx; HS_VAV1; -.
ExpressionAtlas; P15498; baseline and differential.
Genevisible; P15498; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; IEA:Ensembl.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0019221; P:cytokine-mediated 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:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0008361; P:regulation of cell size; IGI: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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd00029; C1; 1.
CDD; cd01223; PH_Vav; 1.
CDD; cd00160; RhoGEF; 1.
CDD; cd10405; SH2_Vav1; 1.
CDD; cd11979; SH3_VAV1_1; 1.
CDD; cd11976; SH3_VAV1_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; IPR003096; SM22_calponin.
InterPro; IPR028530; Vav1.
InterPro; IPR035879; VAV1_SH2.
InterPro; IPR035730; VAV1_SH3_1.
InterPro; IPR035729; VAV1_SH3_2.
PANTHER; PTHR22826:SF112; PTHR22826:SF112; 1.
Pfam; PF00130; C1_1; 1.
Pfam; PF11971; CAMSAP_CH; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00621; RhoGEF; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 2.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00888; SM22CALPONIN.
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; 1.
SUPFAM; SSF55550; SSF55550; 1.
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; Complete proteome;
Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; Repeat; SH2 domain;
SH3 domain; Zinc; Zinc-finger.
CHAIN 1 845 Proto-oncogene vav.
/FTId=PRO_0000080980.
DOMAIN 1 119 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 194 373 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 402 504 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 592 660 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 671 765 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 782 842 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
ZN_FING 515 564 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
COMPBIAS 33 99 Leu-rich.
MOD_RES 826 826 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 844 844 Phosphotyrosine.
{ECO:0000250|UniProtKB:P27870}.
VAR_SEQ 187 218 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047563.
VARIANT 739 739 T -> M (in dbSNP:rs36097961).
/FTId=VAR_051997.
MUTAGEN 529 529 C->R: Abolishes transforming activity.
{ECO:0000269|PubMed:2069873}.
MUTAGEN 696 696 R->L: Loss of interaction with SYK.
{ECO:0000269|PubMed:8986718}.
CONFLICT 264 264 A -> P (in Ref. 6; CAA34383).
{ECO:0000305}.
CONFLICT 368 368 Q -> R (in Ref. 5; BAG62721).
{ECO:0000305}.
CONFLICT 718 718 I -> TV (in Ref. 6). {ECO:0000305}.
HELIX 3 13 {ECO:0000244|PDB:3KY9}.
TURN 22 24 {ECO:0000244|PDB:3KY9}.
HELIX 30 37 {ECO:0000244|PDB:3KY9}.
HELIX 41 50 {ECO:0000244|PDB:3KY9}.
HELIX 57 59 {ECO:0000244|PDB:3KY9}.
HELIX 68 84 {ECO:0000244|PDB:3KY9}.
HELIX 96 100 {ECO:0000244|PDB:3KY9}.
HELIX 105 117 {ECO:0000244|PDB:3KY9}.
TURN 119 121 {ECO:0000244|PDB:3KY9}.
HELIX 122 124 {ECO:0000244|PDB:3KY9}.
HELIX 145 149 {ECO:0000244|PDB:3KY9}.
HELIX 159 162 {ECO:0000244|PDB:3KY9}.
HELIX 168 178 {ECO:0000244|PDB:3KY9}.
HELIX 191 218 {ECO:0000244|PDB:3BJI}.
HELIX 221 224 {ECO:0000244|PDB:3BJI}.
TURN 225 227 {ECO:0000244|PDB:3BJI}.
HELIX 230 237 {ECO:0000244|PDB:3BJI}.
HELIX 240 259 {ECO:0000244|PDB:3BJI}.
TURN 260 262 {ECO:0000244|PDB:3BJI}.
HELIX 267 273 {ECO:0000244|PDB:3BJI}.
HELIX 276 278 {ECO:0000244|PDB:3BJI}.
HELIX 279 300 {ECO:0000244|PDB:3BJI}.
HELIX 302 316 {ECO:0000244|PDB:3BJI}.
STRAND 317 319 {ECO:0000244|PDB:3KY9}.
HELIX 322 326 {ECO:0000244|PDB:3BJI}.
HELIX 328 333 {ECO:0000244|PDB:3BJI}.
HELIX 336 344 {ECO:0000244|PDB:3BJI}.
HELIX 351 388 {ECO:0000244|PDB:3BJI}.
HELIX 397 400 {ECO:0000244|PDB:3BJI}.
STRAND 403 412 {ECO:0000244|PDB:3BJI}.
STRAND 420 435 {ECO:0000244|PDB:3BJI}.
STRAND 442 448 {ECO:0000244|PDB:3BJI}.
HELIX 449 451 {ECO:0000244|PDB:3BJI}.
STRAND 452 456 {ECO:0000244|PDB:3BJI}.
STRAND 469 479 {ECO:0000244|PDB:3BJI}.
STRAND 481 488 {ECO:0000244|PDB:3BJI}.
HELIX 489 506 {ECO:0000244|PDB:3BJI}.
TURN 509 512 {ECO:0000244|PDB:3BJI}.
HELIX 513 515 {ECO:0000244|PDB:3BJI}.
STRAND 518 521 {ECO:0000244|PDB:3BJI}.
TURN 530 532 {ECO:0000244|PDB:3BJI}.
STRAND 538 540 {ECO:0000244|PDB:3BJI}.
STRAND 543 546 {ECO:0000244|PDB:3BJI}.
TURN 547 549 {ECO:0000244|PDB:3BJI}.
HELIX 555 560 {ECO:0000244|PDB:3BJI}.
HELIX 666 668 {ECO:0000244|PDB:2CRH}.
STRAND 669 672 {ECO:0000244|PDB:2CRH}.
HELIX 678 684 {ECO:0000244|PDB:2CRH}.
TURN 685 687 {ECO:0000244|PDB:2CRH}.
STRAND 692 696 {ECO:0000244|PDB:2CRH}.
STRAND 700 702 {ECO:0000244|PDB:2LCT}.
STRAND 706 711 {ECO:0000244|PDB:2CRH}.
STRAND 714 719 {ECO:0000244|PDB:2CRH}.
STRAND 721 723 {ECO:0000244|PDB:2CRH}.
STRAND 726 730 {ECO:0000244|PDB:2CRH}.
STRAND 735 737 {ECO:0000244|PDB:2CRH}.
HELIX 738 745 {ECO:0000244|PDB:2CRH}.
HELIX 750 752 {ECO:0000244|PDB:2CRH}.
STRAND 754 756 {ECO:0000244|PDB:2LCT}.
STRAND 763 766 {ECO:0000244|PDB:2CRH}.
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


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