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Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma
Protein YWHAG PDB 2b05.png
PDB rendering based on 2b05.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols YWHAG ; 14-3-3GAMMA; PPP1R170
External IDs OMIM605356 MGI108109 HomoloGene22725 ChEMBL: 1293296 GeneCards: YWHAG Gene
Species Human Mouse
Entrez 7532 22628
Ensembl ENSG00000170027 ENSMUSG00000051391
UniProt P61981 P61982
RefSeq (mRNA) NM_012479 NM_018871
RefSeq (protein) NP_036611 NP_061359
Location (UCSC) Chr 7:
75.96 – 75.99 Mb
Chr 5:
135.91 – 135.93 Mb
PubMed search [1] [2]

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]


YWHAG has been shown to interact with C-Raf,[2][4][5] EPB41L3,[4][6] KIF1C[7] and Stratifin.[8]


  1. ^ 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. 
  2. ^ 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. 
  3. ^ "Entrez Gene: YWHAG tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide". 
  4. ^ 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. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. 
  5. ^ 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. (ENGLAND) 345 (2): 297–306. doi:10.1042/0264-6021:3450297. ISSN 0264-6021. PMC 1220759. PMID 10620507. 
  6. ^ 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. (England) 365 (Pt 3): 783–9. doi:10.1042/BJ20020060. ISSN 0264-6021. PMC 1222735. PMID 11996670. 
  7. ^ 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. (UNITED STATES) 274 (47): 33654–60. doi:10.1074/jbc.274.47.33654. ISSN 0021-9258. PMID 10559254. 
  8. ^ 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 (United States) 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. ISSN 1535-9476. PMID 15778465. 

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