YWHAG
Template:PBB 14-3-3 protein gamma is a protein that in humans is encoded by the YWHAG gene.[1][2]
This gene product belongs to the 14-3-3 protein family which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in both plants and mammals, and this protein is 100% identical to the rat ortholog. It is induced by growth factors in human vascular smooth muscle cells, and is also highly expressed in skeletal and heart muscles, suggesting an important role for this protein in muscle tissue. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.[3]
Interactions
YWHAG has been shown to interact with C-Raf,[2][4][5] EPB41L3,[4][6] KIF1C[7] and Stratifin.[8]
References
- ^ Horie M, Suzuki M, Takahashi E, Tanigami A (November 1999). "Cloning, expression, and chromosomal mapping of the human 14-3-3gamma gene (YWHAG) to 7q11.23". Genomics. 60 (2): 241–3. doi:10.1006/geno.1999.5887. PMID 10486217.
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: CS1 maint: multiple names: authors list (link) - ^ a b Autieri MV, Carbone CJ (August 1999). "14-3-3Gamma interacts with and is phosphorylated by multiple protein kinase C isoforms in PDGF-stimulated human vascular smooth muscle cells". DNA Cell Biol. 18 (7): 555–64. doi:10.1089/104454999315105. PMID 10433554.
- ^ "Entrez Gene: YWHAG tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide".
- ^ a b Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1). England: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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(help)CS1 maint: multiple names: authors list (link) - ^ Van Der Hoeven, P C; Van Der Wal J C, Ruurs P, Van Dijk M C, Van Blitterswijk J (January 2000). "14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylation". Biochem. J. 345 (2). ENGLAND: 297–306. doi:10.1042/0264-6021:3450297. ISSN 0264-6021. PMC 1220759. PMID 10620507.
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(help)CS1 maint: multiple names: authors list (link) - ^ Yu, Tingxi; Robb Victoria A; Singh Vinita; Gutmann David H; Newsham Irene F (August 2002). "The 4.1/ezrin/radixin/moesin domain of the DAL-1/Protein 4.1B tumour suppressor interacts with 14-3-3 proteins". Biochem. J. 365 (Pt 3). England: 783–9. doi:10.1042/BJ20020060. ISSN 0264-6021. PMC 1222735. PMID 11996670.
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(help) - ^ Dorner, C; Ullrich A; Häring H U; Lammers R (November 1999). "The kinesin-like motor protein KIF1C occurs in intact cells as a dimer and associates with proteins of the 14-3-3 family". J. Biol. Chem. 274 (47). UNITED STATES: 33654–60. doi:10.1074/jbc.274.47.33654. ISSN 0021-9258. PMID 10559254.
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(help)CS1 maint: unflagged free DOI (link) - ^ Benzinger, Anne; Muster Nemone; Koch Heike B; Yates John R; Hermeking Heiko (June 2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell Proteomics. 4 (6). United States: 785–95. doi:10.1074/mcp.M500021-MCP200. ISSN 1535-9476. PMID 15778465.
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