LOCUS VAV_HUMAN 845 aa linear PRI 03-AUG-2022 DEFINITION RecName: Full=Proto-oncogene vav. ACCESSION P15498 VERSION P15498.4 DBSOURCE UniProtKB: locus VAV_HUMAN, accession P15498; class: standard. extra accessions:B4DVK9,M0QXX6,Q15860 created: Apr 1, 1990. sequence updated: Feb 21, 2001. annotation updated: Aug 3, 2022. xrefs: AF030227.1, AAC25011.1, AF030201.1, AF030202.1, AF030203.1, AF030204.1, AF030205.1, AF030206.1, AF030207.1, AF030208.1, AF030209.1, AF030210.1, AF030211.1, AF030212.1, AF030213.1, AF030214.1, AF030215.1, AF030216.1, AF030217.1, AF030218.1, AF030219.1, AF030220.1, AF030221.1, AF030222.1, AF030223.1, AF030224.1, AF030225.1, AF030226.1, AC010647.5, AC020895.8, AC020954.8, AC022156.8, M59834.1, AAA63267.1, AK301128.1, BAG62721.1, X16316.1, CAA34383.1, X83931.1, CAA58783.1, TVHUVV, NP_001245136.1, NP_005419.2, 2CRH_A, 2LCT_A, 2MC1_A, 2ROR_A, 3BJI_A, 3BJI_B, 3KY9_A, 3KY9_B, 6NEW_A, 6NF1_A, 6NFA_A xrefs (non-sequence databases): CCDS:CCDS12174.1, CCDS:CCDS59342.1, PDBsum:2CRH, PDBsum:2LCT, PDBsum:2MC1, PDBsum:2ROR, PDBsum:3BJI, PDBsum:3KY9, PDBsum:6NEW, PDBsum:6NF1, PDBsum:6NFA, AlphaFoldDB:P15498, BMRB:P15498, SMR:P15498, BioGRID:113252, CORUM:P15498, DIP:DIP-1061N, IntAct:P15498, MINT:P15498, STRING:9606.ENSP00000472929, BindingDB:P15498, ChEMBL:CHEMBL3259472, iPTMnet:P15498, PhosphoSitePlus:P15498, BioMuta:VAV1, DMDM:13124807, CPTAC:CPTAC-1226, CPTAC:CPTAC-1227, EPD:P15498, jPOST:P15498, MassIVE:P15498, MaxQB:P15498, PaxDb:P15498, PeptideAtlas:P15498, PRIDE:P15498, ProteomicsDB:53143, Antibodypedia:665, DNASU:7409, Ensembl:ENST00000596764.5, Ensembl:ENSP00000469450.1, Ensembl:ENSG00000141968.8, Ensembl:ENST00000602142.6, Ensembl:ENSP00000472929.1, GeneID:7409, KEGG:hsa:7409, MANE-Select:ENST00000602142.6, UCSC:uc002mfu.3, CTD:7409, DisGeNET:7409, GeneCards:VAV1, HGNC:12657, HPA:ENSG00000141968, MIM 164875, neXtProt:NX_P15498, OpenTargets:ENSG00000141968, PharmGKB:PA37280, VEuPathDB:HostDB:ENSG00000141968, eggNOG:KOG2996, GeneTree:ENSGT00940000159125, InParanoid:P15498, OMA:PYISRPT, PhylomeDB:P15498, TreeFam:TF316171, PathwayCommons:P15498, Reactome:R-HSA-114604, Reactome:R-HSA-1257604, Reactome:R-HSA-1433557, Reactome:R-HSA-193648, Reactome:R-HSA-2029482, Reactome:R-HSA-2219530, Reactome:R-HSA-2871796, Reactome:R-HSA-2871809, Reactome:R-HSA-389359, Reactome:R-HSA-416482, Reactome:R-HSA-4420097, Reactome:R-HSA-512988, Reactome:R-HSA-5218920, Reactome:R-HSA-6811558, Reactome:R-HSA-8980692, Reactome:R-HSA-9013149, Reactome:R-HSA-9013404, Reactome:R-HSA-9013408, Reactome:R-HSA-9027284, Reactome:R-HSA-912631, Reactome:R-HSA-9664422, Reactome:R-HSA-9748787, Reactome:R-HSA-983695, SignaLink:P15498, SIGNOR:P15498, BioGRID-ORCS:7409, ChiTaRS:VAV1, EvolutionaryTrace:P15498, GenomeRNAi:7409, Pharos:P15498, PRO:PR:P15498, Proteomes:UP000005640, RNAct:P15498, Bgee:ENSG00000141968, ExpressionAtlas:P15498, Genevisible:P15498, GO:0005911, GO:0005737, GO:0005829, GO:0005886, GO:0005085, GO:0046872, GO:0140031, GO:0001784, GO:0016477, GO:0071466, GO:0038095, GO:0038096, GO:0007186, GO:0006955, GO:0007229, GO:0030593, GO:0030168, GO:0043547, GO:0045954, GO:0072593, GO:0008361, GO:0043087, GO:0051056, GO:0007264, GO:0031295, GO:0030217, GO:0048010, CDD:cd00029, CDD:cd01223, CDD:cd00160, CDD:cd10405, CDD:cd11979, CDD:cd11976, Gene3D:1.10.418.10, Gene3D:1.20.900.10, Gene3D:2.30.29.30, Gene3D:3.30.505.10, IDEAL:IID00652, InterPro:IPR022613, InterPro:IPR001715, InterPro:IPR036872, InterPro:IPR035899, InterPro:IPR000219, InterPro:IPR001331, InterPro:IPR002219, InterPro:IPR011993, InterPro:IPR001849, InterPro:IPR037832, InterPro:IPR000980, InterPro:IPR036860, InterPro:IPR036028, InterPro:IPR001452, InterPro:IPR003096, InterPro:IPR028530, InterPro:IPR035879, InterPro:IPR035730, InterPro:IPR035729, PANTHER:PTHR45818:SF2, Pfam:PF00130, Pfam:PF11971, Pfam:PF00169, Pfam:PF00621, Pfam:PF00017, Pfam:PF00018, PRINTS:PR00401, PRINTS:PR00452, PRINTS:PR00888, SMART:SM00109, SMART:SM00033, SMART:SM00233, SMART:SM00325, SMART:SM00252, SMART:SM00326, SUPFAM:SSF47576, SUPFAM:SSF48065, SUPFAM:SSF50044, SUPFAM:SSF55550, PROSITE:PS50021, PROSITE:PS00741, PROSITE:PS50010, PROSITE:PS50003, PROSITE:PS50001, PROSITE:PS50002, PROSITE:PS00479, PROSITE:PS50081 KEYWORDS 3D-structure; Alternative splicing; Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; SH2 domain; SH3 domain; Zinc; Zinc-finger. SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 845) AUTHORS Coppola,J., Bryant,S., Koda,T., Conway,D. and Barbacid,M. TITLE Mechanism of activation of the vav protooncogene JOURNAL Cell Growth Differ 2 (2), 95-105 (1991) PUBMED 2069873 REMARK NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF CYS-529. REFERENCE 2 (residues 1 to 845) AUTHORS Denkinger,D.J., Borges,C.R., Butler,C.L., Cushman,A.M. and Kawahara,R.S. TITLE Genomic organization and regulation of the vav proto-oncogene JOURNAL Biochim Biophys Acta 1491 (1-3), 253-262 (2000) PUBMED 10760587 REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA]. REFERENCE 3 (residues 1 to 845) AUTHORS Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J., Lamerdin,J., 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., 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., 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. and Lucas,S.M. TITLE The DNA sequence and biology of human chromosome 19 JOURNAL Nature 428 (6982), 529-535 (2004) PUBMED 15057824 REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. REFERENCE 4 (residues 1 to 845) AUTHORS Katzav,S., Cleveland,J.L., Heslop,H.E. and Pulido,D. TITLE Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential JOURNAL Mol Cell Biol 11 (4), 1912-1920 (1991) PUBMED 2005887 REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61. REFERENCE 5 (residues 1 to 845) AUTHORS 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. and Sugano,S. TITLE Complete sequencing and characterization of 21,243 full-length human cDNAs JOURNAL Nat Genet 36 (1), 40-45 (2004) PUBMED 14702039 REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-813 (ISOFORM 2).; TISSUE=Spleen REFERENCE 6 (residues 1 to 845) AUTHORS Katzav,S., Martin-Zanca,D. and Barbacid,M. TITLE vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells JOURNAL EMBO J 8 (8), 2283-2290 (1989) PUBMED 2477241 REMARK NUCLEOTIDE SEQUENCE [MRNA] OF 68-845 (ISOFORM 1). REFERENCE 7 (residues 1 to 845) AUTHORS Romero,F. TITLE Direct Submission JOURNAL Submitted (??-JAN-1995) to the EMBL/GenBank/DDBJ databases REMARK NUCLEOTIDE SEQUENCE [MRNA] OF 299-837 (ISOFORM 1). REFERENCE 8 (residues 1 to 845) AUTHORS Ramos-Morales,F., Romero,F., Schweighoffer,F., Bismuth,G., Camonis,J., Tortolero,M. and Fischer,S. TITLE The proline-rich region of Vav binds to Grb2 and Grb3-3 JOURNAL Oncogene 11 (8), 1665-1669 (1995) PUBMED 7478592 REMARK NUCLEOTIDE SEQUENCE [MRNA] OF 299-334 (ISOFORM 1). REFERENCE 9 (residues 1 to 845) AUTHORS Adams,J.M., Houston,H., Allen,J., Lints,T. and Harvey,R. TITLE 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 JOURNAL Oncogene 7 (4), 611-618 (1992) PUBMED 1565462 REMARK SIMILARITY TO CDC24 FAMILY. REFERENCE 10 (residues 1 to 845) AUTHORS Deckert,M., Tartare-Deckert,S., Couture,C., Mustelin,T. and Altman,A. TITLE Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product JOURNAL Immunity 5 (6), 591-604 (1996) PUBMED 8986718 REMARK INTERACTION WITH SYK, AND MUTAGENESIS OF ARG-696. REFERENCE 11 (residues 1 to 845) AUTHORS Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and Barbacid,M. TITLE Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation JOURNAL Oncogene 15 (21), 2511-2520 (1997) PUBMED 9399639 REMARK INTERACTION WITH CBLB. REFERENCE 12 (residues 1 to 845) AUTHORS Fu,C., Turck,C.W., Kurosaki,T. and Chan,A.C. TITLE BLNK: a central linker protein in B cell activation JOURNAL Immunity 9 (1), 93-103 (1998) PUBMED 9697839 REMARK INTERACTION WITH BLNK; PLCG1; GRB2 AND NCK1. REFERENCE 13 (residues 1 to 845) AUTHORS Germani,A., Romero,F., Houlard,M., Camonis,J., Gisselbrecht,S., Fischer,S. and Varin-Blank,N. TITLE hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways JOURNAL Mol Cell Biol 19 (5), 3798-3807 (1999) PUBMED 10207103 REMARK INTERACTION WITH SIAH2. REFERENCE 14 (residues 1 to 845) AUTHORS Huang,J., Tilly,D., Altman,A., Sugie,K. and Grey,H.M. TITLE T-cell receptor antagonists induce Vav phosphorylation by selective activation of Fyn kinase JOURNAL Proc Natl Acad Sci U S A 97 (20), 10923-10929 (2000) PUBMED 11005864 REMARK PHOSPHORYLATION BY FYN. REFERENCE 15 (residues 1 to 845) AUTHORS Nishihara,H., Maeda,M., Oda,A., Tsuda,M., Sawa,H., Nagashima,K. and Tanaka,S. TITLE DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines JOURNAL Blood 100 (12), 3968-3974 (2002) PUBMED 12393632 REMARK INTERACTION WITH DOCK2. REFERENCE 16 (residues 1 to 845) AUTHORS Lindholm,C.K., Henriksson,M.L., Hallberg,B. and Welsh,M. TITLE Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells JOURNAL Eur J Biochem 269 (13), 3279-3288 (2002) PUBMED 12084069 REMARK INTERACTION WITH SHB. REFERENCE 17 (residues 1 to 845) AUTHORS Yabana,N. and Shibuya,M. TITLE Adaptor protein APS binds the NH2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity JOURNAL Oncogene 21 (50), 7720-7729 (2002) PUBMED 12400014 REMARK INTERACTION WITH SH2B2. REFERENCE 18 (residues 1 to 845) AUTHORS Dombroski,D., Houghtling,R.A., Labno,C.M., Precht,P., Takesono,A., Caplen,N.J., Billadeau,D.D., Wange,R.L., Burkhardt,J.K. and Schwartzberg,P.L. TITLE Kinase-independent functions for Itk in TCR-induced regulation of Vav and the actin cytoskeleton JOURNAL J Immunol 174 (3), 1385-1392 (2005) PUBMED 15661896 REMARK INTERACTION WITH ITK. REFERENCE 19 (residues 1 to 845) AUTHORS Miller,S.L., DeMaria,J.E., Freier,D.O., Riegel,A.M. and Clevenger,C.V. TITLE Novel association of Vav2 and Nek3 modulates signaling through the human prolactin receptor JOURNAL Mol Endocrinol 19 (4), 939-949 (2005) PUBMED 15618286 REMARK INTERACTION WITH NEK3. REFERENCE 20 (residues 1 to 845) AUTHORS Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J., Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J. TITLE Immunoaffinity profiling of tyrosine phosphorylation in cancer cells JOURNAL Nat Biotechnol 23 (1), 94-101 (2005) PUBMED 15592455 REMARK PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-826, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. REFERENCE 21 (residues 1 to 845) AUTHORS Houlard,M., Romero-Portillo,F., Germani,A., Depaux,A., Regnier-Ricard,F., Gisselbrecht,S. and Varin-Blank,N. TITLE Characterization of VIK-1: a new Vav-interacting Kruppel-like protein JOURNAL Oncogene 24 (1), 28-38 (2005) PUBMED 15558030 REMARK INTERACTION WITH ZNF655/VIK. REFERENCE 22 (residues 1 to 845) AUTHORS Gao,C. and Blystone,S.D. TITLE A Pyk2-Vav1 complex is recruited to beta3-adhesion sites to initiate Rho activation JOURNAL Biochem J 420 (1), 49-56 (2009) PUBMED 19207108 REMARK INTERACTION WITH PTK2B/PYK2. Publication Status: Online-Only REFERENCE 23 (residues 1 to 845) AUTHORS Burkard,T.R., Planyavsky,M., Kaupe,I., Breitwieser,F.P., Burckstummer,T., Bennett,K.L., Superti-Furga,G. and Colinge,J. TITLE Initial characterization of the human central proteome JOURNAL BMC Syst Biol 5, 17 (2011) PUBMED 21269460 REMARK IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Publication Status: Online-Only REFERENCE 24 (residues 1 to 845) AUTHORS Srikanth,S., Kim,K.D., Gao,Y., Woo,J.S., Ghosh,S., Calmettes,G., Paz,A., Abramson,J., Jiang,M. and Gwack,Y. TITLE A large Rab GTPase encoded by CRACR2A is a component of subsynaptic vesicles that transmit T cell activation signals JOURNAL Sci Signal 9 (420), ra31 (2016) PUBMED 27016526 REMARK INTERACTION WITH CRACR2A. Publication Status: Online-Only REFERENCE 25 (residues 1 to 845) CONSRTM RIKEN structural genomics initiative (RSGI) TITLE Direct Submission JOURNAL Submitted (??-NOV-2005) to the PDB data bank REMARK STRUCTURE BY NMR OF 661-775. COMMENT On or before Apr 6, 2005 this sequence version replaced gi:2144604, gi:586213. [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 SH2B2, 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). Interacts with isoform 2 of CRACR2A (PubMed:27016526). {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:27016526, ECO:0000269|PubMed:8986718, ECO:0000269|PubMed:9399639, ECO:0000269|PubMed:9697839}. [INTERACTION] P15498; Q8IZP0: ABI1; NbExp=2; IntAct=EBI-625518, EBI-375446; P15498; P00519: ABL1; NbExp=5; IntAct=EBI-625518, EBI-375543; P15498; Q13480: GAB1; NbExp=2; IntAct=EBI-625518, EBI-517684; P15498; P62993: GRB2; NbExp=3; IntAct=EBI-625518, EBI-401755; P15498; Q07666: KHDRBS1; NbExp=3; IntAct=EBI-625518, EBI-1364; P15498; Q13094: LCP2; NbExp=9; IntAct=EBI-625518, EBI-346946; P15498; P63000: RAC1; NbExp=2; IntAct=EBI-625518, EBI-413628; P15498; P78314: SH3BP2; NbExp=8; IntAct=EBI-625518, EBI-727062; P15498; Q8N720: ZNF655; NbExp=5; IntAct=EBI-625518, EBI-625509; P15498; P08487: PLCG1; Xeno; NbExp=4; IntAct=EBI-625518, EBI-8013886. [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P15498-1; Sequence=Displayed; Name=2; IsoId=P15498-2; Sequence=VSP_047563. [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=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=CAA34383.1; Type=Frameshift; Evidence={ECO:0000305}. [WEB RESOURCE] Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL='http://atlasgeneticsoncology.org/Genes/VAV1ID195ch19p13.html'. FEATURES Location/Qualifiers source 1..845 /organism="Homo sapiens" /db_xref="taxon:9606" gene 1..845 /gene="VAV1" /gene_synonym="VAV" Protein 1..845 /product="Proto-oncogene vav" /UniProtKB_evidence="Evidence at protein level" Region 1..845 /region_name="Mature chain" /note="Proto-oncogene vav. /id=PRO_0000080980." Region 1..119 /region_name="Domain" /note="Calponin-homology (CH). /evidence=ECO:0000255|PROSITE-ProRule:PRU00044." Region 2..121 /region_name="CH_VAV1" /note="calponin homology (CH) domain found in VAV1 protein; cd21262" /db_xref="CDD:409111" Site order(3,7,70,72..73,76..77,79,90..98,104,106..107, 109..110,113..114,117) /site_type="other" /note="putative actin binding site [polypeptide binding]" /db_xref="CDD:409111" Region 3..13 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 22..24 /region_name="Hydrogen bonded turn" /note="/evidence=ECO:0007829|PDB:6NF1." Region 30..37 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 41..50 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 57..59 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 68..84 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 90..92 /region_name="Hydrogen bonded turn" /note="/evidence=ECO:0007829|PDB:6NF1." Region 96..100 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 105..116 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 119..122 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 123..125 /region_name="Hydrogen bonded turn" /note="/evidence=ECO:0007829|PDB:6NF1." Region 145..148 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 158..160 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 173..177 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 187..218 /region_name="Splicing variant" /note="Missing (in isoform 2). /evidence=ECO:0000303|PubMed:14702039. /id=VSP_047563." Region 191..219 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 194..373 /region_name="Domain" /note="DH. /evidence=ECO:0000255|PROSITE-ProRule:PRU00062." Region 195..371 /region_name="RhoGEF" /note="Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains; cd00160" /db_xref="CDD:238091" Site order(201,205,295,323..324,327..328,330..331,334..335, 338..339,342,367,371) /site_type="other" /note="GTPase interaction site [polypeptide binding]" /db_xref="CDD:238091" Region 221..225 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 230..236 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 240..259 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 261..263 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 264 /region_name="Conflict" /note="A -> P (in Ref. 6; CAA34383). /evidence=ECO:0000305." Region 266..273 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 276..278 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 279..285 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 287..300 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 302..316 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 317..319 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NF1." Region 322..325 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 328..333 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 336..345 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 350..389 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 368 /region_name="Conflict" /note="Q -> R (in Ref. 5; BAG62721). /evidence=ECO:0000305." Region 385..508 /region_name="PH_Vav" /note="Vav pleckstrin homology (PH) domain; cd01223" /db_xref="CDD:269930" Region 390..392 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 397..400 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 402..504 /region_name="Domain" /note="PH. /evidence=ECO:0000255|PROSITE-ProRule:PRU00145." Region 403..412 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 420..437 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 440..448 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 449..451 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 452..456 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 458..460 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 461..463 /region_name="Hydrogen bonded turn" /note="/evidence=ECO:0007829|PDB:6NEW." Region 469..475 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 481..488 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 489..506 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 509..512 /region_name="Hydrogen bonded turn" /note="/evidence=ECO:0007829|PDB:6NEW." Region 510..566 /region_name="C1_VAV1" /note="protein kinase C conserved region 1 (C1 domain) found in VAV1 protein; cd20867" /db_xref="CDD:410417" Region 513..515 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 515..564 /region_name="Zinc finger region" /note="Phorbol-ester/DAG-type. /evidence=ECO:0000255|PROSITE-ProRule:PRU00226." Site order(516,529,532,546,549,554,557,564) /site_type="other" /note="Zn binding site [ion binding]" /db_xref="CDD:410417" Region 518..521 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NEW." Site 529 /site_type="mutagenized" /note="C->R: Abolishes transforming activity. /evidence=ECO:0000269|PubMed:2069873." Region 530..532 /region_name="Hydrogen bonded turn" /note="/evidence=ECO:0007829|PDB:6NEW." Region 538..540 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 543..546 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 547..549 /region_name="Hydrogen bonded turn" /note="/evidence=ECO:0007829|PDB:6NEW." Region 555..560 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:6NEW." Region 592..660 /region_name="Domain" /note="SH3 1. /evidence=ECO:0000255|PROSITE-ProRule:PRU00192." Region 596..658 /region_name="SH3_VAV1_1" /note="First Src homology 3 domain of VAV1 protein; cd11979" /db_xref="CDD:212912" Site order(601,603,606,616,635..636,651,653..654) /site_type="other" /note="peptide ligand binding site [polypeptide binding]" /db_xref="CDD:212912" Region 665..767 /region_name="SH2_Vav1" /note="Src homology 2 (SH2) domain found in the Vav1 proteins; cd10405" /db_xref="CDD:198268" Region 666..668 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:2CRH." Region 669..672 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:2CRH." Region 671..765 /region_name="Domain" /note="SH2. /evidence=ECO:0000255|PROSITE-ProRule:PRU00191." Site order(678,696,717,719) /site_type="other" /note="phosphotyrosine binding pocket [polypeptide binding]" /db_xref="CDD:198268" Region 678..684 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:2CRH." Region 685..687 /region_name="Hydrogen bonded turn" /note="/evidence=ECO:0007829|PDB:2CRH." Region 692..696 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:2CRH." Site 696 /site_type="mutagenized" /note="R->L: Loss of interaction with SYK. /evidence=ECO:0000269|PubMed:8986718." Region 700..702 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:2LCT." Region 706..711 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:2CRH." Region 714..719 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:2CRH." Site order(718,745) /site_type="other" /note="hydrophobic binding pocket [polypeptide binding]" /db_xref="CDD:198268" Region 718 /region_name="Conflict" /note="I -> TV (in Ref. 6). /evidence=ECO:0000305." Region 721..723 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:2CRH." Region 726..730 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:2CRH." Region 735..737 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:2CRH." Region 738..745 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:2CRH." Region 739 /region_name="Variant" /note="T -> M (in dbSNP:rs36097961). /id=VAR_051997." Region 750..752 /region_name="Helical region" /note="/evidence=ECO:0007829|PDB:2CRH." Region 754..756 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:2LCT." Region 763..766 /region_name="Beta-strand region" /note="/evidence=ECO:0007829|PDB:2CRH." Region 782..842 /region_name="Domain" /note="SH3 2. /evidence=ECO:0000255|PROSITE-ProRule:PRU00192." Region 786..839 /region_name="SH3_VAV1_2" /note="C-terminal (or second) Src homology 3 domain of VAV1 protein; cd11976" /db_xref="CDD:212909" Site order(791,793,796,800,819..820,833,835..836) /site_type="other" /note="peptide ligand binding site [polypeptide binding]" /db_xref="CDD:212909" Site 826 /site_type="phosphorylation" /note="Phosphotyrosine. /evidence=ECO:0007744|PubMed:15592455." Site 844 /site_type="phosphorylation" /note="Phosphotyrosine. /evidence=ECO:0000250|UniProtKB:P27870." ORIGIN 1 melwrqcthw liqcrvlpps hrvtwdgaqv celaqalrdg vllcqllnnl lphainlrev 61 nlrpqmsqfl clknirtfls tccekfglkr selfeafdlf dvqdfgkviy tlsalswtpi 121 aqnrgimpfp teeesvgded iysglsdqid dtveededly dcveneeaeg deiyedlmrs 181 epvsmppkmt eydkrccclr eiqqteekyt dtlgsiqqhf lkplqrflkp qdieiifini 241 edllrvhthf lkemkealgt pgaanlyqvf ikykerflvy grycsqvesa skhldrvaaa 301 redvqmklee csqranngrf tlrdllmvpm qrvlkyhlll qelvkhtqea mekenlrlal 361 damrdlaqcv nevkrdnetl rqitnfqlsi enldqslahy grpkidgelk itsverrskm 421 dryaflldka llickrrgds ydlkdfvnlh sfqvrddssg drdnkkwshm flliedqgaq 481 gyelffktre lkkkwmeqfe maisniypen atanghdfqm fsfeettsck acqmllrgtf 541 yqgyrchrcr asahkeclgr vppcgrhgqd fpgtmkkdkl hrraqdkkrn elglpkmevf 601 qeyyglpppp gaigpflrln pgdiveltka eaeqnwwegr ntstneigwf pcnrvkpyvh 661 gppqdlsvhl wyagpmerag aesilanrsd gtflvrqrvk daaefaisik ynvevkhiki 721 mtaeglyrit ekkafrglte lvefyqqnsl kdcfksldtt lqfpfkepek rtisrpavgs 781 tkyfgtakar ydfcardrse lslkegdiik ilnkkgqqgw wrgeiygrvg wfpanyveed 841 yseyc //