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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''RAC-beta serine/threonine-protein kinase''' is an [[enzyme]] that in humans is encoded by the ''AKT2'' [[gene]].<ref name="pmid1409633">{{cite journal | vauthors = Cheng JQ, Godwin AK, Bellacosa A, Taguchi T, Franke TF, Hamilton TC, Tsichlis PN, Testa JR | title = AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas | journal = Proc Natl Acad Sci U S A | volume = 89 | issue = 19 | pages = 9267–71 | date = November 1992 | pmid = 1409633 | pmc = 50107 | doi = 10.1073/pnas.89.19.9267 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_AKT2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gzk.
| PDB = {{PDB2|1gzk}}, {{PDB2|1gzn}}, {{PDB2|1gzo}}, {{PDB2|1mrv}}, {{PDB2|1mry}}, {{PDB2|1o6k}}, {{PDB2|1o6l}}, {{PDB2|1p6s}}, {{PDB2|2jdo}}, {{PDB2|2jdr}}, {{PDB2|2uw9}}
| Name = V-akt murine thymoma viral oncogene homolog 2
| HGNCid = 392
| Symbol = AKT2
| AltSymbols =; PKBBETA; PRKBB; RAC-BETA
| OMIM = 164731
| ECnumber = 
| Homologene = 48773
| MGIid = 104874
| GeneAtlas_image1 = PBB_GE_AKT2_203809_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_AKT2_211453_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 208
    | Hs_Ensembl = ENSG00000105221
    | Hs_RefseqProtein = NP_001617
    | Hs_RefseqmRNA = NM_001626
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 45430084
    | Hs_GenLoc_end = 45483036
    | Hs_Uniprot = P31751
    | Mm_EntrezGene = 11652
    | Mm_Ensembl = ENSMUSG00000004056
    | Mm_RefseqmRNA = XM_001000182
    | Mm_RefseqProtein = XP_001000182
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 27300516
    | Mm_GenLoc_end = 27348213
    | Mm_Uniprot = Q3TY95
  }}
}}
'''V-akt murine thymoma viral oncogene homolog 2''', also known as '''AKT2''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene is a putative [[oncogene]] encoding a protein belonging to the [[Protein Kinase B|AKT]] subfamily of [[serine/threonine kinases]] that contain [[SH2 domain|SH2]]-like (Src homology 2-like) domains. The encoded protein is a general protein kinase capable of phosphorylating several known proteins.<ref name ="entrez"/>
{{PBB_Summary
 
| section_title =
== Clinical significance ==
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: AKT2 v-akt murine thymoma viral oncogene homolog 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=208| accessdate = }}</ref>. 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.
 
}}
The gene was shown to be amplified and overexpressed in 2 of 8 ovarian carcinoma cell lines and 2 of 15 primary [[ovarian tumor]]s. Overexpression contributes to the malignant phenotype of a subset of human ductal [[pancreatic cancer]]s.<ref name ="entrez">{{cite web | title = Entrez Gene: AKT2 v-akt murine thymoma viral oncogene homolog 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=208| accessdate = }}</ref>
 
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 [[HER2/neu|neu oncogene]].<ref name="pmid21432781">{{cite journal | vauthors = Heron-Milhavet L, Khouya N, Fernandez A, Lamb NJ | title = Akt1 and Akt2: differentiating the aktion | journal = Histol. Histopathol. | volume = 26 | issue = 5 | pages = 651–62 | year = 2011 | pmid = 21432781 | doi =  }}</ref>
 
==Interactions==
AKT2 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[APPL1]],<ref name = pmid10490823>{{cite journal | vauthors = Mitsuuchi Y, Johnson SW, Sonoda G, Tanno S, Golemis EA, Testa JR | title = Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2 | journal = Oncogene | volume = 18 | issue = 35 | pages = 4891–8 | date = September 1999 | pmid = 10490823 | doi = 10.1038/sj.onc.1203080 }}</ref>
* [[CHUK]],<ref name = pmid12048203>{{cite journal | vauthors = Yuan ZQ, Feldman RI, Sun M, Olashaw NE, Coppola D, Sussman GE, Shelley SA, Nicosia SV, Cheng JQ | title = 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 | journal = J. Biol. Chem. | volume = 277 | issue = 33 | pages = 29973–82 | date = August 2002 | pmid = 12048203 | doi = 10.1074/jbc.M203636200 }}</ref>
* [[SH3RF1]]<ref name = pmid14504284>{{cite journal | vauthors = Figueroa C, Tarras S, Taylor J, Vojtek AB | title = Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex | journal = J. Biol. Chem. | volume = 278 | issue = 48 | pages = 47922–7 | date = November 2003 | pmid = 14504284 | doi = 10.1074/jbc.M307357200 }}</ref>  and
* [[TCL1A]].<ref name = pmid11707444>{{cite journal | vauthors = Laine J, Künstle G, Obata T, Noguchi M | title = Differential regulation of Akt kinase isoforms by the members of the TCL1 oncogene family | journal = J. Biol. Chem. | volume = 277 | issue = 5 | pages = 3743–51 | date = February 2002 | pmid = 11707444 | doi = 10.1074/jbc.M107069200 }}</ref><ref name = pmid10983986>{{cite journal | vauthors = Laine J, Künstle G, Obata T, Sha M, Noguchi M | title = The protooncogene TCL1 is an Akt kinase coactivator | journal = Mol. Cell | volume = 6 | issue = 2 | pages = 395–407 | date = August 2000 | pmid = 10983986 | doi =  10.1016/S1097-2765(00)00039-3}}</ref>
{{Div col end}}


==References==
==References==
{{reflist}}
{{reflist}}
{{Clear}}


==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal | vauthors = Jones PF, Jakubowicz T, Hemmings BA | title = Molecular cloning of a second form of rac protein kinase. | journal = Cell Regul. | volume = 2 | issue = 12 | pages = 1001–9 | year = 1992 | pmid = 1801921 | pmc = 361900 | doi = 10.1091/mbc.2.12.1001 }}
| citations =
*{{cite journal | author = Staal SP | title = Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 84 | issue = 14 | pages = 5034–7 | year = 1987 | pmid = 3037531 | pmc = 305241 | doi = 10.1073/pnas.84.14.5034 }}
*{{cite journal | author=Cheng JQ, Godwin AK, Bellacosa A, ''et al.'' |title=AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 19 |pages= 9267–71 |year= 1992 |pmid= 1409633 |doi= }}
*{{cite journal | vauthors = Cheng JQ, Ruggeri B, Klein WM, Sonoda G, Altomare DA, Watson DK, Testa JR | title = Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 8 | pages = 3636–41 | year = 1996 | pmid = 8622988 | pmc = 39663 | doi = 10.1073/pnas.93.8.3636 }}
*{{cite journal | author=Jones PF, Jakubowicz T, Hemmings BA |title=Molecular cloning of a second form of rac protein kinase. |journal=Cell Regul. |volume=2 |issue= 12 |pages= 1001–9 |year= 1992 |pmid= 1801921 |doi= }}
*{{cite journal | vauthors = Meier R, Alessi DR, Cron P, Andjelković M, Hemmings BA | title = Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bbeta. | journal = J. Biol. Chem. | volume = 272 | issue = 48 | pages = 30491–7 | year = 1997 | pmid = 9374542 | doi = 10.1074/jbc.272.48.30491 }}
*{{cite journal | author=Staal SP |title=Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 14 |pages= 5034–7 |year= 1987 |pmid= 3037531 |doi= }}
*{{cite journal | vauthors = Borgatti P, Zauli G, Colamussi ML, Gibellini D, Previati M, Cantley LL, Capitani S | title = Extracellular HIV-1 Tat protein activates phosphatidylinositol 3- and Akt/PKB kinases in CD4+ T lymphoblastoid Jurkat cells. | journal = Eur. J. Immunol. | volume = 27 | issue = 11 | pages = 2805–11 | year = 1998 | pmid = 9394803 | doi = 10.1002/eji.1830271110 }}
*{{cite journal | author=Cheng JQ, Ruggeri B, Klein WM, ''et al.'' |title=Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 8 |pages= 3636–41 |year= 1996 |pmid= 8622988 |doi= }}
*{{cite journal | vauthors = Walker KS, Deak M, Paterson A, Hudson K, Cohen P, Alessi DR | title = 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. | journal = Biochem. J. | volume = ( Pt 1) | issue = | pages = 299–308 | year = 1998 | pmid = 9512493 | pmc = 1219352 | doi =  | series = 331 }}
*{{cite journal | author=Meier R, Alessi DR, Cron P, ''et al.'' |title=Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bbeta. |journal=J. Biol. Chem. |volume=272 |issue= 48 |pages= 30491–7 |year= 1997 |pmid= 9374542 |doi= }}
*{{cite journal | vauthors = Joel PB, Smith J, Sturgill TW, Fisher TL, Blenis J, Lannigan DA | title = pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167. | journal = Mol. Cell. Biol. | volume = 18 | issue = 4 | pages = 1978–84 | year = 1998 | pmid = 9528769 | pmc = 121427 | doi =  10.1128/mcb.18.4.1978}}
*{{cite journal | author=Borgatti P, Zauli G, Colamussi ML, ''et al.'' |title=Extracellular HIV-1 Tat protein activates phosphatidylinositol 3- and Akt/PKB kinases in CD4+ T lymphoblastoid Jurkat cells. |journal=Eur. J. Immunol. |volume=27 |issue= 11 |pages= 2805–11 |year= 1998 |pmid= 9394803 |doi=  }}
*{{cite journal | vauthors = Delcommenne M, Tan C, Gray V, Rue L, Woodgett J, Dedhar S | title = Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 95 | issue = 19 | pages = 11211–6 | year = 1998 | pmid = 9736715 | pmc = 21621 | doi = 10.1073/pnas.95.19.11211 }}
*{{cite journal | author=Walker KS, Deak M, Paterson A, ''et al.'' |title=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. |journal=Biochem. J. |volume=331 ( Pt 1) |issue= |pages= 299–308 |year= 1998 |pmid= 9512493 |doi=  }}
*{{cite journal | vauthors = Mitsuuchi Y, Johnson SW, Sonoda G, Tanno S, Golemis EA, Testa JR | title = Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2. | journal = Oncogene | volume = 18 | issue = 35 | pages = 4891–8 | year = 1999 | pmid = 10490823 | doi = 10.1038/sj.onc.1203080 }}
*{{cite journal | author=Joel PB, Smith J, Sturgill TW, ''et al.'' |title=pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167. |journal=Mol. Cell. Biol. |volume=18 |issue= 4 |pages= 1978–84 |year= 1998 |pmid= 9528769 |doi= }}
*{{cite journal | vauthors = Masure S, Haefner B, Wesselink JJ, Hoefnagel E, Mortier E, Verhasselt P, Tuytelaars A, Gordon R, Richardson A | title = Molecular cloning, expression and characterization of the human serine/threonine kinase Akt-3. | journal = Eur. J. Biochem. | volume = 265 | issue = 1 | pages = 353–60 | year = 1999 | pmid = 10491192 | doi = 10.1046/j.1432-1327.1999.00774.x }}
*{{cite journal | author=Delcommenne M, Tan C, Gray V, ''et al.'' |title=Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 19 |pages= 11211–6 |year= 1998 |pmid= 9736715 |doi= }}
*{{cite journal | vauthors = Meucci O, Fatatis A, Simen AA, Miller RJ | title = Expression of CX3CR1 chemokine receptors on neurons and their role in neuronal survival. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 14 | pages = 8075–80 | year = 2000 | pmid = 10869418 | pmc = 16672 | doi = 10.1073/pnas.090017497 }}
*{{cite journal | author=Mitsuuchi Y, Johnson SW, Sonoda G, ''et al.'' |title=Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2. |journal=Oncogene |volume=18 |issue= 35 |pages= 4891–8 |year= 1999 |pmid= 10490823 |doi= 10.1038/sj.onc.1203080 }}
*{{cite journal | vauthors = Laine J, Künstle G, Obata T, Sha M, Noguchi M | title = The protooncogene TCL1 is an Akt kinase coactivator. | journal = Mol. Cell | volume = 6 | issue = 2 | pages = 395–407 | year = 2000 | pmid = 10983986 | doi = 10.1016/S1097-2765(00)00039-3 }}
*{{cite journal | author=Masure S, Haefner B, Wesselink JJ, ''et al.'' |title=Molecular cloning, expression and characterization of the human serine/threonine kinase Akt-3. |journal=Eur. J. Biochem. |volume=265 |issue= 1 |pages= 353–60 |year= 1999 |pmid= 10491192 |doi= }}
*{{cite journal | vauthors = Campbell RA, Bhat-Nakshatri P, Patel NM, Constantinidou D, Ali S, Nakshatri H | title = Phosphatidylinositol 3-kinase/AKT-mediated activation of estrogen receptor alpha: a new model for anti-estrogen resistance. | journal = J. Biol. Chem. | volume = 276 | issue = 13 | pages = 9817–24 | year = 2001 | pmid = 11139588 | doi = 10.1074/jbc.M010840200 }}
*{{cite journal | author=Meucci O, Fatatis A, Simen AA, Miller RJ |title=Expression of CX3CR1 chemokine receptors on neurons and their role in neuronal survival. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 14 |pages= 8075–80 |year= 2000 |pmid= 10869418 |doi= 10.1073/pnas.090017497 }}
*{{cite journal | vauthors = Zauli G, Milani D, Mirandola P, Mazzoni M, Secchiero P, Miscia S, Capitani S | title = HIV-1 Tat protein down-regulates CREB transcription factor expression in PC12 neuronal cells through a phosphatidylinositol 3-kinase/AKT/cyclic nucleoside phosphodiesterase pathway. | journal = FASEB J. | volume = 15 | issue = 2 | pages = 483–91 | year = 2001 | pmid = 11156964 | doi = 10.1096/fj.00-0354com }}
*{{cite journal | author=Laine J, Künstle G, Obata T, ''et al.'' |title=The protooncogene TCL1 is an Akt kinase coactivator. |journal=Mol. Cell |volume=6 |issue= 2 |pages= 395–407 |year= 2000 |pmid= 10983986 |doi= }}
*{{cite journal | vauthors = Kapasi AA, Fan S, Singhal PC | title = Role of 14-3-3epsilon, c-Myc/Max, and Akt phosphorylation in HIV-1 gp 120-induced mesangial cell proliferation. | journal = Am. J. Physiol. Renal Physiol. | volume = 280 | issue = 2 | pages = F333–42 | year = 2001 | pmid = 11208609 | doi = }}
*{{cite journal | author=Campbell RA, Bhat-Nakshatri P, Patel NM, ''et al.'' |title=Phosphatidylinositol 3-kinase/AKT-mediated activation of estrogen receptor alpha: a new model for anti-estrogen resistance. |journal=J. Biol. Chem. |volume=276 |issue= 13 |pages= 9817–24 |year= 2001 |pmid= 11139588 |doi= 10.1074/jbc.M010840200 }}
*{{cite journal | vauthors = Matsumoto M, Ogawa W, Hino Y, Furukawa K, Ono Y, Takahashi M, Ohba M, Kuroki T, Kasuga M | title = Inhibition of insulin-induced activation of Akt by a kinase-deficient mutant of the epsilon isozyme of protein kinase C. | journal = J. Biol. Chem. | volume = 276 | issue = 17 | pages = 14400–6 | year = 2001 | pmid = 11278835 | doi = 10.1074/jbc.M011093200 }}
*{{cite journal | author=Zauli G, Milani D, Mirandola P, ''et al.'' |title=HIV-1 Tat protein down-regulates CREB transcription factor expression in PC12 neuronal cells through a phosphatidylinositol 3-kinase/AKT/cyclic nucleoside phosphodiesterase pathway. |journal=FASEB J. |volume=15 |issue= 2 |pages= 483–91 |year= 2001 |pmid= 11156964 |doi= 10.1096/fj.00-0354com }}
*{{cite journal | vauthors = Brownawell AM, Kops GJ, Macara IG, Burgering BM | title = Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX. | journal = Mol. Cell. Biol. | volume = 21 | issue = 10 | pages = 3534–46 | year = 2001 | pmid = 11313479 | pmc = 100275 | doi = 10.1128/MCB.21.10.3534-3546.2001 }}
*{{cite journal | author=Kapasi AA, Fan S, Singhal PC |title=Role of 14-3-3epsilon, c-Myc/Max, and Akt phosphorylation in HIV-1 gp 120-induced mesangial cell proliferation. |journal=Am. J. Physiol. Renal Physiol. |volume=280 |issue= 2 |pages= F333–42 |year= 2001 |pmid= 11208609 |doi= }}
*{{cite journal | vauthors = Clark DE, Poteet-Smith CE, Smith JA, Lannigan DA | title = Rsk2 allosterically activates estrogen receptor alpha by docking to the hormone-binding domain. | journal = EMBO J. | volume = 20 | issue = 13 | pages = 3484–94 | year = 2001 | pmid = 11432835 | pmc = 125527 | doi = 10.1093/emboj/20.13.3484 }}
*{{cite journal | author=Matsumoto M, Ogawa W, Hino Y, ''et al.'' |title=Inhibition of insulin-induced activation of Akt by a kinase-deficient mutant of the epsilon isozyme of protein kinase C. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 14400–6 |year= 2001 |pmid= 11278835 |doi= 10.1074/jbc.M011093200 }}
*{{cite journal | vauthors = Chen R, Kim O, Yang J, Sato K, Eisenmann KM, McCarthy J, Chen H, Qiu Y | title = Regulation of Akt/PKB activation by tyrosine phosphorylation. | journal = J. Biol. Chem. | volume = 276 | issue = 34 | pages = 31858–62 | year = 2001 | pmid = 11445557 | doi = 10.1074/jbc.C100271200 }}
*{{cite journal | author=Brownawell AM, Kops GJ, Macara IG, Burgering BM |title=Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX. |journal=Mol. Cell. Biol. |volume=21 |issue= 10 |pages= 3534–46 |year= 2001 |pmid= 11313479 |doi= 10.1128/MCB.21.10.3534-3546.2001 }}
*{{cite journal | author=Clark DE, Poteet-Smith CE, Smith JA, Lannigan DA |title=Rsk2 allosterically activates estrogen receptor alpha by docking to the hormone-binding domain. |journal=EMBO J. |volume=20 |issue= 13 |pages= 3484–94 |year= 2001 |pmid= 11432835 |doi= 10.1093/emboj/20.13.3484 }}
*{{cite journal  | author=Chen R, Kim O, Yang J, ''et al.'' |title=Regulation of Akt/PKB activation by tyrosine phosphorylation. |journal=J. Biol. Chem. |volume=276 |issue= 34 |pages= 31858–62 |year= 2001 |pmid= 11445557 |doi= 10.1074/jbc.C100271200 }}
}}
{{refend}}
{{refend}}


{{gene-19-stub}}
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[[Category:EC 2.7.11]]

Latest revision as of 17:56, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

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RefSeq (mRNA)

n/a

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

RAC-beta serine/threonine-protein kinase is an enzyme that in humans is encoded by the AKT2 gene.[1]

Function

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.[2]

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.[2]

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.[3]

Interactions

AKT2 has been shown to interact with:

References

  1. ↑ 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. doi:10.1073/pnas.89.19.9267. PMC 50107. PMID 1409633.
  2. ↑ 2.0 2.1 "Entrez Gene: AKT2 v-akt murine thymoma viral oncogene homolog 2".
  3. ↑ Heron-Milhavet L, Khouya N, Fernandez A, Lamb NJ (2011). "Akt1 and Akt2: differentiating the aktion". Histol. Histopathol. 26 (5): 651–62. PMID 21432781.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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

External links

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