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==References==
==References==
{{reflist}}
{{reflist|2}}


==Further reading==
==Further reading==

Revision as of 13:56, 4 September 2012


V-akt murine thymoma viral oncogene homolog 2
PDB rendering based on 1gzk.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols AKT2 ; PKBBETA; PRKBB; RAC-BETA
External IDs Template:OMIM5 Template:MGI HomoloGene48773
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

V-akt murine thymoma viral oncogene homolog 2, also known as AKT2, is a human gene.

This gene is a putative oncogene encoding a protein belonging to a subfamily of serine/threonine kinases containing SH2-like (Src homology 2-like) domains. The gene was shown to be amplified and overexpressed in 2 of 8 ovarian carcinoma cell lines and 2 of 15 primary ovarian tumors. Overexpression contributes to the malignant phenotype of a subset of human ductal pancreatic cancers. The encoded protein is a general protein kinase capable of phophorylating several known proteins.[1]. Mice lacking Akt2 have a normal body mass, but display a profound diabetic phenotype, indicating that Akt2 plaays a key role in signal transduction downstream of the insulin receptor. Mice lacking Akt2 show worse outcome in breast cancer initaited by the large T antigen as well as the neu oncogene.

References

  1. "Entrez Gene: AKT2 v-akt murine thymoma viral oncogene homolog 2".

Further reading

  • Cheng JQ, Godwin AK, Bellacosa A; et al. (1992). "AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 9267–71. PMID 1409633.
  • Jones PF, Jakubowicz T, Hemmings BA (1992). "Molecular cloning of a second form of rac protein kinase". Cell Regul. 2 (12): 1001–9. PMID 1801921.
  • Staal SP (1987). "Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma". Proc. Natl. Acad. Sci. U.S.A. 84 (14): 5034–7. PMID 3037531.
  • Cheng JQ, Ruggeri B, Klein WM; et al. (1996). "Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA". Proc. Natl. Acad. Sci. U.S.A. 93 (8): 3636–41. PMID 8622988.
  • Meier R, Alessi DR, Cron P; et al. (1997). "Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bbeta". J. Biol. Chem. 272 (48): 30491–7. PMID 9374542.
  • Borgatti P, Zauli G, Colamussi ML; et al. (1998). "Extracellular HIV-1 Tat protein activates phosphatidylinositol 3- and Akt/PKB kinases in CD4+ T lymphoblastoid Jurkat cells". Eur. J. Immunol. 27 (11): 2805–11. PMID 9394803.
  • Walker KS, Deak M, Paterson A; et al. (1998). "Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha". Biochem. J. 331 ( Pt 1): 299–308. PMID 9512493.
  • Joel PB, Smith J, Sturgill TW; et al. (1998). "pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167". Mol. Cell. Biol. 18 (4): 1978–84. PMID 9528769.
  • Delcommenne M, Tan C, Gray V; et al. (1998). "Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase". Proc. Natl. Acad. Sci. U.S.A. 95 (19): 11211–6. PMID 9736715.
  • Mitsuuchi Y, Johnson SW, Sonoda G; et al. (1999). "Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2". Oncogene. 18 (35): 4891–8. doi:10.1038/sj.onc.1203080. PMID 10490823.
  • Masure S, Haefner B, Wesselink JJ; et al. (1999). "Molecular cloning, expression and characterization of the human serine/threonine kinase Akt-3". Eur. J. Biochem. 265 (1): 353–60. PMID 10491192.
  • Meucci O, Fatatis A, Simen AA, Miller RJ (2000). "Expression of CX3CR1 chemokine receptors on neurons and their role in neuronal survival". Proc. Natl. Acad. Sci. U.S.A. 97 (14): 8075–80. doi:10.1073/pnas.090017497. PMID 10869418.
  • Laine J, Künstle G, Obata T; et al. (2000). "The protooncogene TCL1 is an Akt kinase coactivator". Mol. Cell. 6 (2): 395–407. PMID 10983986.
  • Campbell RA, Bhat-Nakshatri P, Patel NM; et al. (2001). "Phosphatidylinositol 3-kinase/AKT-mediated activation of estrogen receptor alpha: a new model for anti-estrogen resistance". J. Biol. Chem. 276 (13): 9817–24. doi:10.1074/jbc.M010840200. PMID 11139588.
  • Zauli G, Milani D, Mirandola P; et al. (2001). "HIV-1 Tat protein down-regulates CREB transcription factor expression in PC12 neuronal cells through a phosphatidylinositol 3-kinase/AKT/cyclic nucleoside phosphodiesterase pathway". FASEB J. 15 (2): 483–91. doi:10.1096/fj.00-0354com. PMID 11156964.
  • Kapasi AA, Fan S, Singhal PC (2001). "Role of 14-3-3epsilon, c-Myc/Max, and Akt phosphorylation in HIV-1 gp 120-induced mesangial cell proliferation". Am. J. Physiol. Renal Physiol. 280 (2): F333–42. PMID 11208609.
  • Matsumoto M, Ogawa W, Hino Y; et al. (2001). "Inhibition of insulin-induced activation of Akt by a kinase-deficient mutant of the epsilon isozyme of protein kinase C.". J. Biol. Chem. 276 (17): 14400–6. doi:10.1074/jbc.M011093200. PMID 11278835.
  • Brownawell AM, Kops GJ, Macara IG, Burgering BM (2001). "Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX". Mol. Cell. Biol. 21 (10): 3534–46. doi:10.1128/MCB.21.10.3534-3546.2001. PMID 11313479.
  • Clark DE, Poteet-Smith CE, Smith JA, Lannigan DA (2001). "Rsk2 allosterically activates estrogen receptor alpha by docking to the hormone-binding domain". EMBO J. 20 (13): 3484–94. doi:10.1093/emboj/20.13.3484. PMID 11432835.
  • Chen R, Kim O, Yang J; et al. (2001). "Regulation of Akt/PKB activation by tyrosine phosphorylation". J. Biol. Chem. 276 (34): 31858–62. doi:10.1074/jbc.C100271200. PMID 11445557.

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