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VAV3









VAV3


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VAV3
Protein VAV3 PDB 2d86.png







Available structures
PDB Ortholog search: PDBe RCSB



Identifiers
Aliases
VAV3, vav guanine nucleotide exchange factor 3
External IDs MGI: 1888518 HomoloGene: 38143 GeneCards: VAV3


















Gene location (Human)
Chromosome 1 (human)
Chr. Chromosome 1 (human)[1]

Chromosome 1 (human)
Genomic location for VAV3

Genomic location for VAV3

Band 1p13.3 Start 107,571,160 bp[1]
End 107,965,144 bp[1]























RNA expression pattern

PBB GE VAV3 218806 s at fs.png

PBB GE VAV3 218807 at fs.png
More reference expression data















Orthologs
Species Human Mouse
Entrez





Ensembl





UniProt





RefSeq (mRNA)


NM_001079874
NM_006113




NM_020505
NM_146139

RefSeq (protein)


NP_001073343
NP_006104




NP_065251
NP_666251

Location (UCSC) Chr 1: 107.57 – 107.97 Mb Chr 3: 109.34 – 109.69 Mb

PubMed search
[3] [4]
Wikidata



View/Edit Human View/Edit Mouse

Guanine nucleotide exchange factor VAV3 is a protein that in humans is encoded by the VAV3 gene.[5]


This gene is a member of the VAV gene family. The VAV proteins are guanine nucleotide exchange factors (GEFs) for Rho family GTPases that activate pathways leading to actin cytoskeletal rearrangements and transcriptional alterations. This gene product acts as a GEF preferentially for RhoG, RhoA, and to a lesser extent, RAC1, and it associates maximally with the nucleotide-free states of these GTPases. Alternatively spliced transcript variants encoding different isoforms have been described for this gene.[5]



Interactions[edit]


VAV3 has been shown to interact with Grb2.[6][7]



References[edit]





  1. ^ abc GRCh38: Ensembl release 89: ENSG00000134215 - Ensembl, May 2017


  2. ^ abc GRCm38: Ensembl release 89: ENSMUSG00000033721 - Ensembl, May 2017


  3. ^ "Human PubMed Reference:"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-maint{display:none;color:#33aa33;margin-left:0.3em}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}


  4. ^ "Mouse PubMed Reference:".


  5. ^ ab "Entrez Gene: VAV3 vav 3 oncogene".


  6. ^ Blagoev, Blagoy; Kratchmarova Irina; Ong Shao-En; Nielsen Mogens; Foster Leonard J; Mann Matthias (March 2003). "A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling". Nat. Biotechnol. United States. 21 (3): 315–318. doi:10.1038/nbt790. ISSN 1087-0156. PMID 12577067.


  7. ^ Zeng, L; Sachdev P; Yan L; Chan J L; Trenkle T; McClelland M; Welsh J; Wang L H (December 2000). "Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation". Mol. Cell. Biol. UNITED STATES. 20 (24): 9212–9224. doi:10.1128/MCB.20.24.9212-9224.2000. ISSN 0270-7306. PMC 102179. PMID 11094073.




Further reading[edit]


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  • Hobert O, Schilling JW, Beckerle MC, et al. (1996). "SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin". Oncogene. 12 (7): 1577–81. PMID 8622875.


  • Tamma SM, Chirmule N, Yagura H, et al. (1997). "CD4 cross-linking (CD4XL) induces RAS activation and tumor necrosis factor-alpha secretion in CD4+ T cells". Blood. 90 (4): 1588–93. PMID 9269777.


  • Trenkle T, Welsh J, Jung B, et al. (1998). "Non-stoichiometric reduced complexity probes for cDNA arrays". Nucleic Acids Res. 26 (17): 3883–3891. doi:10.1093/nar/26.17.3883. PMC 147802. PMID 9705494.


  • Movilla N, Bustelo XR (1999). "Biological and regulatory properties of Vav-3, a new member of the Vav family of oncoproteins". Mol. Cell. Biol. 19 (11): 7870–85. doi:10.1128/mcb.19.11.7870. PMC 84867. PMID 10523675.


  • Trenkle T, McClelland M, Adlkofer K, Welsh J (2000). "Major transcript variants of VAV3, a new member of the VAV family of guanine nucleotide exchange factors". Gene. 245 (1): 139–149. doi:10.1016/S0378-1119(00)00026-3. PMID 10713454.


  • Zeng L, Sachdev P, Yan L, et al. (2001). "Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation". Mol. Cell. Biol. 20 (24): 9212–9224. doi:10.1128/MCB.20.24.9212-9224.2000. PMC 102179. PMID 11094073.


  • Inabe K, Ishiai M, Scharenberg AM, et al. (2002). "Vav3 modulates B cell receptor responses by regulating phosphoinositide 3-kinase activation". J. Exp. Med. 195 (2): 189–200. doi:10.1084/jem.20011571. PMC 2193613. PMID 11805146.


  • Yabana N, Shibuya M (2002). "Adaptor protein APS binds the NH2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity". Oncogene. 21 (50): 7720–7729. doi:10.1038/sj.onc.1205927. PMID 12400014.


  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–45. doi:10.1038/ng1285. PMID 14702039.


  • Zakaria S, Gomez TS, Savoy DN, et al. (2004). "Differential regulation of TCR-mediated gene transcription by Vav family members". J. Exp. Med. 199 (3): 429–434. doi:10.1084/jem.20031228. PMC 2211790. PMID 14757747.


  • Pearce AC, Senis YA, Billadeau DD, et al. (2005). "Vav1 and vav3 have critical but redundant roles in mediating platelet activation by collagen". J. Biol. Chem. 279 (52): 53955–53962. doi:10.1074/jbc.M410355200. PMID 15456756.


  • Charvet C, Canonigo AJ, Billadeau DD, Altman A (2005). "Membrane localization and function of Vav3 in T cells depend on its association with the adapter SLP-76". J. Biol. Chem. 280 (15): 15289–15299. doi:10.1074/jbc.M500275200. PMID 15708849.


  • Lyons LS, Burnstein KL (2006). "Vav3, a Rho GTPase guanine nucleotide exchange factor, increases during progression to androgen independence in prostate cancer cells and potentiates androgen receptor transcriptional activity". Mol. Endocrinol. 20 (5): 1061–1072. doi:10.1210/me.2005-0346. PMID 16384856.


  • Dong Z, Liu Y, Lu S, et al. (2006). "Vav3 oncogene is overexpressed and regulates cell growth and androgen receptor activity in human prostate cancer". Mol. Endocrinol. 20 (10): 2315–2325. doi:10.1210/me.2006-0048. PMID 16762975.














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