Available structures
PDBOrtholog search: PDBe RCSB
AliasesAKT2, v-akt murine thymoma viral oncogene homolog 2, HIHGHH, PKBB, PKBBETA, PRKBB, RAC-BETA, AKT serine/threonine kinase 2
External IDsOMIM: 164731 MGI: 104874 HomoloGene: 48773 GeneCards: AKT2
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 19: 40.23 – 40.29 MbChr 7: 27.29 – 27.34 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

AKT2, also known as RAC-beta serine/threonine-protein kinase,[5] is an enzyme that in humans is encoded by the AKT2 gene.[6] It influences metabolite storage as part of the insulin signal transduction pathway.[5]


This gene is a putative oncogene encoding a protein belonging to the AKT subfamily of serine/threonine kinases that contain SH2-like (Src homology 2-like) domains. The encoded protein is a general protein kinase capable of phosphorylating several known proteins.[7]

AKT2 has important roles in controlling glycogenesis, gluconeogenesis, and glucose transport as part of the insulin signal transduction pathway.[5]

Clinical significance

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.[7]

Mice lacking Akt2 have a normal body mass, but display a profound diabetic phenotype, indicating that Akt2 plays a key role in signal transduction downstream of the insulin receptor. Mice lacking Akt2 show worse outcome in breast cancer initiated by the large T antigen as well as the neu oncogene.[8]


AKT2 has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105221 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000004056 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c Tsoukas MA, Mantzoros CS (2016-01-01), Jameson JL, De Groot LJ, de Kretser DM, Giudice LC (eds.), "Chapter 37 - Lipodystrophy Syndromes", Endocrinology: Adult and Pediatric (Seventh Edition), Philadelphia: W.B. Saunders, pp. 648–661.e5, doi:10.1016/b978-0-323-18907-1.00037-8, ISBN 978-0-323-18907-1, retrieved 2020-12-18
  6. ^ Cheng JQ, Godwin AK, Bellacosa A, Taguchi T, Franke TF, Hamilton TC, Tsichlis PN, Testa JR (November 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. Bibcode:1992PNAS...89.9267C. doi:10.1073/pnas.89.19.9267. PMC 50107. PMID 1409633.
  7. ^ a b "Entrez Gene: AKT2 v-akt murine thymoma viral oncogene homolog 2".
  8. ^ Heron-Milhavet L, Khouya N, Fernandez A, Lamb NJ (2011). "Akt1 and Akt2: differentiating the aktion". Histol. Histopathol. 26 (5): 651–62. PMID 21432781.
  9. ^ Mitsuuchi Y, Johnson SW, Sonoda G, Tanno S, Golemis EA, Testa JR (September 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.
  10. ^ Yuan ZQ, Feldman RI, Sun M, Olashaw NE, Coppola D, Sussman GE, Shelley SA, Nicosia SV, Cheng JQ (August 2002). "Inhibition of JNK by cellular stress- and tumor necrosis factor alpha-induced AKT2 through activation of the NF kappa B pathway in human epithelial Cells". J. Biol. Chem. 277 (33): 29973–82. doi:10.1074/jbc.M203636200. PMID 12048203.
  11. ^ Figueroa C, Tarras S, Taylor J, Vojtek AB (November 2003). "Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex". J. Biol. Chem. 278 (48): 47922–7. doi:10.1074/jbc.M307357200. PMID 14504284.
  12. ^ Laine J, Künstle G, Obata T, Noguchi M (February 2002). "Differential regulation of Akt kinase isoforms by the members of the TCL1 oncogene family". J. Biol. Chem. 277 (5): 3743–51. doi:10.1074/jbc.M107069200. PMID 11707444.
  13. ^ Laine J, Künstle G, Obata T, Sha M, Noguchi M (August 2000). "The protooncogene TCL1 is an Akt kinase coactivator". Mol. Cell. 6 (2): 395–407. doi:10.1016/S1097-2765(00)00039-3. PMID 10983986.

Further reading