AKT1

Protein-coding gene in the species Homo sapiens

AKT1

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1H10, 1UNP, 1UNQ, 1UNR, 2UVM, 2UZR, 2UZS, 3CQU, 3CQW, 3MV5, 3MVH, 3O96, 3OCB, 3OW4, 3QKK, 3QKL, 3QKM, 4EJN, 4EKK, 4EKL, 4GV1, 5KCV

Identifiers

Aliases

AKT1, AKT, CWS6, PKB, PKB-ALPHA, PRKBA, RAC, RAC-ALPHA, AKT serine/threonine kinase 1

External IDs

OMIM: 164730; MGI: 87986; HomoloGene: 3785; GeneCards: AKT1; OMA:AKT1 - orthologs

Gene location (Human)

Chr.	Chromosome 14 (human)^[1]

Band	14q32.33	Start	104,769,349 bp^[1]
Band	14q32.33	End	104,795,751 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 12 (mouse)^[2]

Band	12 F1\|12 61.2 cM	Start	112,620,255 bp^[2]
Band	12 F1\|12 61.2 cM	End	112,641,318 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

stromal cell of endometrium

ganglionic eminence

left adrenal cortex

right adrenal gland

right adrenal cortex

ventricular zone

right coronary artery

gallbladder

body of stomach

muscle layer of sigmoid colon

Top expressed in

ventricular zone

granulocyte

atrium

molar

human fetus

efferent ductule

endothelial cell of lymphatic vessel

submandibular gland

stroma of bone marrow

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	GTPase activating protein binding kinase activity nitric-oxide synthase regulator activity ATP binding protein kinase activity protein phosphatase 2A binding enzyme binding phosphatidylinositol-3,4,5-trisphosphate binding transferase activity 14-3-3 protein binding protein binding protein serine/threonine/tyrosine kinase activity protein kinase binding protein kinase C binding nucleotide binding phosphatidylinositol-3,4-bisphosphate binding identical protein binding protein serine/threonine kinase activity protein homodimerization activity calmodulin binding
Cellular component	cytoplasm cytosol membrane cell-cell junction mitochondrion nucleus ciliary basal body microtubule cytoskeleton plasma membrane spindle nucleoplasm vesicle postsynapse protein-containing complex
Biological process	germ cell development positive regulation of glucose import cellular response to nerve growth factor stimulus positive regulation of protein phosphorylation positive regulation of lipid biosynthetic process regulation of neuron projection development activation-induced cell death of T cells response to heat regulation of cell cycle checkpoint response to organic substance response to insulin-like growth factor stimulus positive regulation of endodeoxyribonuclease activity cellular response to DNA damage stimulus regulation of protein localization platelet activation protein phosphorylation cellular response to mechanical stimulus negative regulation of long-chain fatty acid import across plasma membrane negative regulation of fatty acid beta-oxidation cell projection organization cellular response to granulocyte macrophage colony-stimulating factor stimulus positive regulation of blood vessel endothelial cell migration glucose metabolic process glycogen metabolic process regulation of glycogen biosynthetic process glycogen cell differentiation involved in embryonic placenta development cell population proliferation negative regulation of autophagy cellular response to hypoxia negative regulation of cell size endocrine pancreas development carbohydrate transport negative regulation of proteolysis insulin-like growth factor receptor signaling pathway positive regulation of protein metabolic process positive regulation of glycogen biosynthetic process glucose homeostasis labyrinthine layer blood vessel development response to oxidative stress negative regulation of gene expression positive regulation of peptidyl-serine phosphorylation cellular response to prostaglandin E stimulus positive regulation of cell growth positive regulation of nitric-oxide synthase activity maternal placenta development regulation of myelination protein ubiquitination positive regulation of vasoconstriction hyaluronan metabolic process spinal cord development cellular response to insulin stimulus cellular response to decreased oxygen levels protein autophosphorylation inflammatory response positive regulation of fat cell differentiation positive regulation of proteasomal ubiquitin-dependent protein catabolic process negative regulation of neuron death G protein-coupled receptor signaling pathway cell differentiation cellular response to peptide negative regulation of protein kinase activity phosphorylation regulation of mRNA stability negative regulation of release of cytochrome c from mitochondria execution phase of apoptosis cellular response to organic cyclic compound positive regulation of DNA-binding transcription factor activity positive regulation of glucose metabolic process nervous system development response to fluid shear stress maintenance of protein location in mitochondrion protein catabolic process negative regulation of protein kinase activity by protein phosphorylation osteoblast differentiation response to UV-A response to hormone peptidyl-threonine phosphorylation lipopolysaccharide-mediated signaling pathway positive regulation of protein localization to nucleus negative regulation of cysteine-type endopeptidase activity involved in apoptotic process intracellular signal transduction regulation of cell migration peripheral nervous system myelin maintenance nitric oxide biosynthetic process positive regulation of endothelial cell proliferation protein biosynthesis positive regulation of nitric oxide biosynthetic process cellular response to growth factor stimulus T cell costimulation regulation of nitric-oxide synthase activity human ageing mammary gland epithelial cell differentiation cellular response to epidermal growth factor stimulus multicellular organism development negative regulation of JNK cascade glycogen biosynthetic process establishment of protein localization to mitochondrion apoptotic mitochondrial changes peptidyl-serine phosphorylation positive regulation of sodium ion transport response to growth hormone positive regulation of apoptotic process response to food cellular response to vascular endothelial growth factor stimulus striated muscle cell differentiation negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway negative regulation of extrinsic apoptotic signaling pathway in absence of ligand positive regulation of fibroblast migration regulation of translation positive regulation of transcription by RNA polymerase II signal transduction negative regulation of endopeptidase activity apoptotic process positive regulation of epidermal growth factor receptor signaling pathway interleukin-18-mediated signaling pathway insulin receptor signaling pathway positive regulation of smooth muscle cell proliferation regulation of signal transduction by p53 class mediator negative regulation of macroautophagy TOR signaling anoikis positive regulation of organ growth I-kappaB kinase/NF-kappaB signaling phosphatidylinositol 3-kinase signaling cellular response to reactive oxygen species NIK/NF-kappaB signaling positive regulation of transcription, DNA-templated cellular response to cadmium ion positive regulation of I-kappaB phosphorylation epidermal growth factor receptor signaling pathway positive regulation of cell population proliferation positive regulation of mitochondrial membrane potential regulation of apoptotic process negative regulation of apoptotic process positive regulation of protein localization to plasma membrane carbohydrate metabolic process activation of protein kinase B activity protein kinase B signaling negative regulation of protein kinase B signaling excitatory postsynaptic potential cellular response to tumor necrosis factor cell migration involved in sprouting angiogenesis positive regulation of gene expression cytokine-mediated signaling pathway negative regulation of protein ubiquitination negative regulation of protein binding positive regulation of cyclin-dependent protein serine/threonine kinase activity negative regulation of Notch signaling pathway negative regulation of protein serine/threonine kinase activity cellular response to oxidised low-density lipoprotein particle stimulus positive regulation of G1/S transition of mitotic cell cycle negative regulation of leukocyte cell-cell adhesion positive regulation of protein localization to cell surface negative regulation of lymphocyte migration protein import into nucleus
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


207


11651

Ensembl


ENSG00000142208


ENSMUSG00000001729

UniProt


P31749


P31750

RefSeq (mRNA)

NM_001014431 NM_001014432 NM_005163 NM_001382430 NM_001382431
NM_001382432 NM_001382433


NM_001165894 NM_009652 NM_001331107

RefSeq (protein)

NP_001014431 NP_001014432 NP_005154 NP_001369359 NP_001369360
NP_001369361 NP_001369362


NP_001159366 NP_001318036 NP_033782

Location (UCSC)

Chr 14: 104.77 – 104.8 Mb

Chr 12: 112.62 – 112.64 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

RAC(Rho family)-alpha serine/threonine-protein kinase is an enzyme that in humans is encoded by the AKT1 gene. This enzyme belongs to the AKT subfamily of serine/threonine kinases that contain SH2 (Src homology 2-like) protein domains.^[5] It is commonly referred to as PKB, or by both names as "Akt/PKB".

Function

The serine-threonine protein kinase AKT1 is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase. In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components of the apoptotic machinery. Mice lacking Akt1 display a 25% reduction in body mass, indicating that Akt1 is critical for transmitting growth-promoting signals, most likely via the IGF1 receptor. Mice lacking Akt1 are also resistant to cancer: They experience considerable delay in tumor growth initiated by the large T antigen or the Neu oncogene. A single-nucleotide polymorphism in this gene causes Proteus syndrome.^[6]^[7]

History

AKT (now also called AKT1) was originally identified as the oncogene in the transforming retrovirus, AKT8.^[8] AKT8 was isolated from a spontaneous thymoma cell line derived from AKR mice by cocultivation with an indicator mink cell line. The transforming cellular sequences, v-akt, were cloned from a transformed mink cell clone and these sequences were used to identify Akt1 and Akt2 in a human clone library. AKT8 was isolated by Stephen Staal in the laboratory of Wallace P. Rowe; he subsequently cloned v-akt and human AKT1 and AKT2 while on staff at the Johns Hopkins Oncology Center.^[9]

In 2011, a mutation in AKT1 was strongly associated with Proteus syndrome, the disease that probably affected the Elephant Man.^[10]

The name Akt stands for Ak strain transforming. The origins of the Akt name date back to 1928, when J. Furth performed experimental studies on mice that developed spontaneous thymic lymphomas. Mice from three different stocks were studied, and the stocks were designated A, R, and S. Stock A was noted to yield many cancers, and inbred families were subsequently designated by a second small letter (Aa, Ab, Ac, etc.), and thus came the Ak strain of mice. Further inbreeding was undertaken with Ak mice at the Rockefeller Institute in 1936, leading to the designation of the AKR mouse strain. In 1977, a transforming retrovirus was isolated from the AKR mouse. This virus was named Akt-8, the "t" representing its transforming capabilities.

Interactions

AKT1 has been shown to interact with:

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000142208 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000001729 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: AKT1 v-akt murine thymoma viral oncogene homolog 1".
^ Lindhurst MJ, Sapp JC, Teer JK, Johnston JJ, Finn EM, Peters K, Turner J, Cannons JL, Bick D, Blakemore L, Blumhorst C, Brockmann K, Calder P, Cherman N, Deardorff MA, Everman DB, Golas G, Greenstein RM, Kato BM, Keppler-Noreuil KM, Kuznetsov SA, Miyamoto RT, Newman K, Ng D, O'Brien K, Rothenberg S, Schwartzentruber DJ, Singhal V, Tirabosco R, Upton J, Wientroub S, Zackai EH, Hoag K, Whitewood-Neal T, Robey PG, Schwartzberg PL, Darling TN, Tosi LL, Mullikin JC, Biesecker LG (2011). "A mosaic activating mutation in AKT1 associated with the Proteus syndrome". N. Engl. J. Med. 365 (7): 611–9. doi:10.1056/NEJMoa1104017. PMC 3170413. PMID 21793738.
^ Cohen MM (2014). "Proteus syndrome review: molecular, clinical, and pathologic features". Clin. Genet. 85 (2): 111–9. doi:10.1111/cge.12266. PMID 23992099. S2CID 204999819.
^ Staal SP, Hartley JW, Rowe WP (July 1977). "Isolation of transforming murine leukemia viruses from mice with a high incidence of spontaneous lymphoma". Proc. Natl. Acad. Sci. U.S.A. 74 (7): 3065–7. Bibcode:1977PNAS...74.3065S. doi:10.1073/pnas.74.7.3065. PMC 431413. PMID 197531.
^ Staal SP (July 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. Bibcode:1987PNAS...84.5034S. doi:10.1073/pnas.84.14.5034. PMC 305241. PMID 3037531.
^ Lindhurst MJ, Sapp JC, Teer JK, Johnston JJ, Finn EM, Peters K, Turner J, Cannons JL, Bick D, Blakemore L, Blumhorst C, Brockmann K, Calder P, Cherman N, Deardorff MA, Everman DB, Golas G, Greenstein RM, Kato BM, Keppler-Noreuil KM, Kuznetsov SA, Miyamoto RT, Newman K, Ng D, O'Brien K, Rothenberg S, Schwartzentruber DJ, Singhal V, Tirabosco R, Upton J, Wientroub S, Zackai EH, Hoag K, Whitewood-Neal T, Robey PG, Schwartzberg PL, Darling TN, Tosi LL, Mullikin JC, Biesecker LG (27 July 2011). "A Mosaic Activating Mutation in Associated with the Proteus Syndrome". New England Journal of Medicine. 365 (7): 611–619. doi:10.1056/NEJMoa1104017. PMC 3170413. PMID 21793738.
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^ Lynch DK, Daly RJ (Jan 2002). "PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2". EMBO J. 21 (1–2): 72–82. doi:10.1093/emboj/21.1.72. PMC 125816. PMID 11782427.
^ Haendeler J, Hoffmann J, Rahman S, Zeiher AM, Dimmeler S (Feb 2003). "Regulation of telomerase activity and anti-apoptotic function by protein-protein interaction and phosphorylation". FEBS Lett. 536 (1–3): 180–6. doi:10.1016/s0014-5793(03)00058-9. PMID 12586360. S2CID 26111467.
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^ ^a ^b Persad S, Attwell S, Gray V, Mawji N, Deng JT, Leung D, Yan J, Sanghera J, Walsh MP, Dedhar S (Jul 2001). "Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343". J. Biol. Chem. 276 (29): 27462–9. doi:10.1074/jbc.M102940200. PMID 11313365.
^ Delcommenne M, Tan C, Gray V, Rue L, Woodgett J, Dedhar S (Sep 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. Bibcode:1998PNAS...9511211D. doi:10.1073/pnas.95.19.11211. PMC 21621. PMID 9736715.
^ Paramio JM, Segrelles C, Ruiz S, Jorcano JL (Nov 2001). "Inhibition of protein kinase B (PKB) and PKCzeta mediates keratin K10-induced cell cycle arrest". Mol. Cell. Biol. 21 (21): 7449–59. doi:10.1128/MCB.21.21.7449-7459.2001. PMC 99917. PMID 11585925.
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^ ^a ^b Dan HC, Sun M, Yang L, Feldman RI, Sui XM, Ou CC, Nellist M, Yeung RS, Halley DJ, Nicosia SV, Pledger WJ, Cheng JQ (Sep 2002). "Phosphatidylinositol 3-kinase/Akt pathway regulates tuberous sclerosis tumor suppressor complex by phosphorylation of tuberin". J. Biol. Chem. 277 (38): 35364–70. doi:10.1074/jbc.M205838200. PMID 12167664.
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