AKT3: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''RAC-gamma serine/threonine-protein kinase''' is an [[enzyme]] that in humans is encoded by the ''AKT3'' [[gene]].<ref name="pmid10092583">{{cite journal | vauthors = Brodbeck D, Cron P, Hemmings BA | title = A human protein kinase Bgamma with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain | journal = J Biol Chem | volume = 274 | issue = 14 | pages = 9133–6 | date = Apr 1999 | pmid = 10092583 | pmc =  | doi = 10.1074/jbc.274.14.9133 }}</ref><ref name="pmid10208883">{{cite journal | vauthors = Nakatani K, Sakaue H, Thompson DA, Weigel RJ, Roth RA | title = Identification of a human Akt3 (protein kinase B gamma) which contains the regulatory serine phosphorylation site | journal = Biochem Biophys Res Commun | volume = 257 | issue = 3 | pages = 906–10 | date = Jun 1999 | pmid = 10208883 | pmc = | doi = 10.1006/bbrc.1999.0559 }}</ref>
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = V-akt murine thymoma viral oncogene homolog 3 (protein kinase B, gamma)
| HGNCid = 393
| Symbol = AKT3
| AltSymbols =; DKFZP434N0250; PKBG; PRKBG; RAC-PK-gamma; RAC-gamma; STK-2
| OMIM = 
| ECnumber = 
| Homologene = 55904
| MGIid = 1345147
| GeneAtlas_image1 = PBB_GE_AKT3_219393_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_AKT3_212607_at_tn.png
| GeneAtlas_image3 = PBB_GE_AKT3_212609_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}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10000
    | Hs_Ensembl = ENSG00000117020
    | Hs_RefseqProtein = NP_005456
    | Hs_RefseqmRNA = NM_005465
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 241718158
    | Hs_GenLoc_end = 242080053
    | Hs_Uniprot = Q9Y243
    | Mm_EntrezGene = 23797
    | Mm_Ensembl = ENSMUSG00000019699
    | Mm_RefseqmRNA = NM_011785
    | Mm_RefseqProtein = NP_035915
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 178862039
    | Mm_GenLoc_end = 178967772
    | Mm_Uniprot = Q6NXW0
  }}
}}
'''V-akt murine thymoma viral oncogene homolog 3 (protein kinase B, gamma)''', also known as '''AKT3''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a member of the [[Protein Kinase B|AKT]] subfamily of [[serine/threonine protein kinase]]s. AKT kinases are known to be regulators of cell signaling in response to [[insulin]] and [[growth factor]]s. They are involved in a wide variety of biological processes including cell proliferation, differentiation, [[apoptosis]], [[tumorigenesis]], as well as [[glycogen]] synthesis and [[glucose]] uptake. This kinase has been shown to be stimulated by [[platelet-derived growth factor]] (PDGF), insulin, and [[insulin-like growth factor 1]] (IGF1). Alternatively splice transcript variants encoding distinct isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: AKT3 v-akt murine thymoma viral oncogene homolog 3 (protein kinase B, gamma)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10000| accessdate = }}</ref> Mice lacking Akt3 have a normal glucose metabolism (no diabetes), have approximately normal body weight, but have a 25% reduction in brain mass. Incidentally, Akt3 is highly expressed in the brain.
{{PBB_Summary
 
| section_title =
== Interactions ==
| summary_text = The protein encoded by this gene is a member of the AKT, also called PKB,  serine/threonine protein kinase family. AKT kinases are known to be regulators of cell signaling in response to insulin and growth factors. They are involved in a wide variety of biological processes including cell proliferation, differentiation, apoptosis, tumorigenesis, as well as glycogen synthesis and glucose uptake. This kinase has been shown to be stimulated by platelet-derived growth factor (PDGF), insulin, and insulin-like growth factor 1 (IGF1). Alternatively splice transcript variants encoding distinct isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: AKT3 v-akt murine thymoma viral oncogene homolog 3 (protein kinase B, gamma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10000| accessdate = }}</ref> Mice lacking Akt3 have a normal glucose metabolism (no diabetes), have approximately normal body weight, but have a 25% reduction in brain mass. Incidentally, Akt3 is highly expressed in the brain.
 
}}
AKT3 has been shown to [[Protein-protein interaction|interact]] with [[Protein kinase Mζ]].<ref name="pmid12162751">{{cite journal | vauthors = Hodgkinson CP, Sale EM, Sale GJ | title = Characterization of PDK2 activity against protein kinase B gamma | journal = Biochemistry | volume = 41 | issue = 32 | pages = 10351–9 | year = 2002 | pmid = 12162751 | doi = 10.1021/bi026065r }}</ref>


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


==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal | vauthors = Li W, Zhang J, Bottaro DP, Pierce JH | title = Identification of serine 643 of protein kinase C-delta as an important autophosphorylation site for its enzymatic activity. | journal = J. Biol. Chem. | volume = 272 | issue = 39 | pages = 24550–5 | year = 1997 | pmid = 9305920 | doi = 10.1074/jbc.272.39.24550 }}
| citations =
*{{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=Li W, Zhang J, Bottaro DP, Pierce JH |title=Identification of serine 643 of protein kinase C-delta as an important autophosphorylation site for its enzymatic activity. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24550–5 |year= 1997 |pmid= 9305920 |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 = 331 ( Pt 1) | issue = Pt 1 | pages = 299–308 | year = 1998 | pmid = 9512493 | pmc = 1219352 | doi =  }}
*{{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 = Nakatani K, Thompson DA, Barthel A, Sakaue H, Liu W, Weigel RJ, Roth RA | title = Up-regulation of Akt3 in estrogen receptor-deficient breast cancers and androgen-independent prostate cancer lines | journal = J. Biol. Chem. | volume = 274 | issue = 31 | pages = 21528–32 | year = 1999 | pmid = 10419456 | doi = 10.1074/jbc.274.31.21528 }}
*{{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 = 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=Brodbeck D, Cron P, Hemmings BA |title=A human protein kinase Bgamma with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9133–6 |year= 1999 |pmid= 10092583 |doi= }}
*{{cite journal | vauthors = Murthy SS, Tosolini A, Taguchi T, Testa JR | title = Mapping of AKT3, encoding a member of the Akt/protein kinase B family, to human and rodent chromosomes by fluorescence in situ hybridization | journal = Cytogenet. Cell Genet. | volume = 88 | issue = 1–2 | pages = 38–40 | year = 2000 | pmid = 10773662 | doi = 10.1159/000015481 }}
*{{cite journal | author=Nakatani K, Sakaue H, Thompson DA, ''et al.'' |title=Identification of a human Akt3 (protein kinase B gamma) which contains the regulatory serine phosphorylation site. |journal=Biochem. Biophys. Res. Commun. |volume=257 |issue= 3 |pages= 906–10 |year= 1999 |pmid= 10208883 |doi= 10.1006/bbrc.1999.0559 }}
*{{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=Nakatani K, Thompson DA, Barthel A, ''et al.'' |title=Up-regulation of Akt3 in estrogen receptor-deficient breast cancers and androgen-independent prostate cancer lines. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21528–32 |year= 1999 |pmid= 10419456 |doi= }}
*{{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA Cloning Using In Vitro Site-Specific Recombination | journal = Genome Res. | volume = 10 | issue = 11 | pages = 1788–95 | year = 2001 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
*{{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 = 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=Murthy SS, Tosolini A, Taguchi T, Testa JR |title=Mapping of AKT3, encoding a member of the Akt/protein kinase B family, to human and rodent chromosomes by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=88 |issue= 1-2 |pages= 38–40 |year= 2000 |pmid= 10773662 |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=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 = Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A | title = Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs | journal = Genome Res. | volume = 11 | issue = 3 | pages = 422–35 | year = 2001 | pmid = 11230166 | pmc = 311072 | doi = 10.1101/gr.GR1547R }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal | vauthors = Sandirasegarane L, Kester M | title = Enhanced stimulation of Akt-3/protein kinase B-gamma in human aortic smooth muscle cells | journal = Biochem. Biophys. Res. Commun. | volume = 283 | issue = 1 | pages = 158–63 | year = 2001 | pmid = 11322783 | doi = 10.1006/bbrc.2001.4739 }}
*{{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 = Brodbeck D, Hill MM, Hemmings BA | title = Two splice variants of protein kinase B gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site serine 472 in the carboxyl-terminal hydrophobic domain | journal = J. Biol. Chem. | volume = 276 | issue = 31 | pages = 29550–8 | year = 2001 | pmid = 11387345 | doi = 10.1074/jbc.M104633200 }}
*{{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 = Mende I, Malstrom S, Tsichlis PN, Vogt PK, Aoki M | title = Oncogenic transformation induced by membrane-targeted Akt2 and Akt3 | journal = Oncogene | volume = 20 | issue = 32 | pages = 4419–23 | year = 2001 | pmid = 11466625 | doi = 10.1038/sj.onc.1204486 }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal | vauthors = Zinda MJ, Johnson MA, Paul JD, Horn C, Konicek BW, Lu ZH, Sandusky G, Thomas JE, Neubauer BL, Lai MT, Graff JR | title = AKT-1, -2, and -3 are expressed in both normal and tumor tissues of the lung, breast, prostate, and colon | journal = Clin. Cancer Res. | volume = 7 | issue = 8 | pages = 2475–9 | year = 2001 | pmid = 11489829 | doi = }}
*{{cite journal | author=Sandirasegarane L, Kester M |title=Enhanced stimulation of Akt-3/protein kinase B-gamma in human aortic smooth muscle cells. |journal=Biochem. Biophys. Res. Commun. |volume=283 |issue= 1 |pages= 158–63 |year= 2001 |pmid= 11322783 |doi= 10.1006/bbrc.2001.4739 }}
*{{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 | year = 2002 | pmid = 11707444 | doi = 10.1074/jbc.M107069200 }}
*{{cite journal | author=Brodbeck D, Hill MM, Hemmings BA |title=Two splice variants of protein kinase B gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site serine 472 in the carboxyl-terminal hydrophobic domain. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 29550–8 |year= 2001 |pmid= 11387345 |doi= 10.1074/jbc.M104633200 }}
*{{cite journal | vauthors = Deregibus MC, Cantaluppi V, Doublier S, Brizzi MF, Deambrosis I, Albini A, Camussi G | title = HIV-1-Tat protein activates phosphatidylinositol 3-kinase/ AKT-dependent survival pathways in Kaposi's sarcoma cells | journal = J. Biol. Chem. | volume = 277 | issue = 28 | pages = 25195–202 | year = 2002 | pmid = 11994280 | doi = 10.1074/jbc.M200921200 }}
*{{cite journal | author=Mende I, Malstrom S, Tsichlis PN, ''et al.'' |title=Oncogenic transformation induced by membrane-targeted Akt2 and Akt3. |journal=Oncogene |volume=20 |issue= 32 |pages= 4419–23 |year= 2001 |pmid= 11466625 |doi= 10.1038/sj.onc.1204486 }}
*{{cite journal | vauthors = Hodgkinson CP, Sale EM, Sale GJ | title = Characterization of PDK2 activity against protein kinase B gamma | journal = Biochemistry | volume = 41 | issue = 32 | pages = 10351–9 | year = 2002 | pmid = 12162751 | doi = 10.1021/bi026065r }}
*{{cite journal | author=Zinda MJ, Johnson MA, Paul JD, ''et al.'' |title=AKT-1, -2, and -3 are expressed in both normal and tumor tissues of the lung, breast, prostate, and colon. |journal=Clin. Cancer Res. |volume=7 |issue= 8 |pages= 2475–9 |year= 2001 |pmid= 11489829 |doi= }}
*{{cite journal | author=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 |year= 2002 |pmid= 11707444 |doi= 10.1074/jbc.M107069200 }}
*{{cite journal  | author=Deregibus MC, Cantaluppi V, Doublier S, ''et al.'' |title=HIV-1-Tat protein activates phosphatidylinositol 3-kinase/ AKT-dependent survival pathways in Kaposi's sarcoma cells. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25195–202 |year= 2002 |pmid= 11994280 |doi= 10.1074/jbc.M200921200 }}
*{{cite journal  | author=Hodgkinson CP, Sale EM, Sale GJ |title=Characterization of PDK2 activity against protein kinase B gamma. |journal=Biochemistry |volume=41 |issue= 32 |pages= 10351–9 |year= 2002 |pmid= 12162751 |doi=  }}
}}
{{refend}}
{{refend}}
==External links==
* {{UCSC genome browser|AKT3}}
* {{UCSC gene details|AKT3}}
{{Serine/threonine-specific protein kinases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
[[Category:EC 2.7.11]]


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Latest revision as of 17:56, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

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

RAC-gamma serine/threonine-protein kinase is an enzyme that in humans is encoded by the AKT3 gene.[1][2]

Function

The protein encoded by this gene is a member of the AKT subfamily of serine/threonine protein kinases. AKT kinases are known to be regulators of cell signaling in response to insulin and growth factors. They are involved in a wide variety of biological processes including cell proliferation, differentiation, apoptosis, tumorigenesis, as well as glycogen synthesis and glucose uptake. This kinase has been shown to be stimulated by platelet-derived growth factor (PDGF), insulin, and insulin-like growth factor 1 (IGF1). Alternatively splice transcript variants encoding distinct isoforms have been described.[3] Mice lacking Akt3 have a normal glucose metabolism (no diabetes), have approximately normal body weight, but have a 25% reduction in brain mass. Incidentally, Akt3 is highly expressed in the brain.

Interactions

AKT3 has been shown to interact with Protein kinase Mζ.[4]

References

  1. Brodbeck D, Cron P, Hemmings BA (Apr 1999). "A human protein kinase Bgamma with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain". J Biol Chem. 274 (14): 9133–6. doi:10.1074/jbc.274.14.9133. PMID 10092583.
  2. Nakatani K, Sakaue H, Thompson DA, Weigel RJ, Roth RA (Jun 1999). "Identification of a human Akt3 (protein kinase B gamma) which contains the regulatory serine phosphorylation site". Biochem Biophys Res Commun. 257 (3): 906–10. doi:10.1006/bbrc.1999.0559. PMID 10208883.
  3. "Entrez Gene: AKT3 v-akt murine thymoma viral oncogene homolog 3 (protein kinase B, gamma)".
  4. Hodgkinson CP, Sale EM, Sale GJ (2002). "Characterization of PDK2 activity against protein kinase B gamma". Biochemistry. 41 (32): 10351–9. doi:10.1021/bi026065r. PMID 12162751.

Further reading

External links