[1]	NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY. DOI=10.1073/pnas.88.10.4171; PubMed=1851997 [NCBI, ExPASy, EBI, Israel, Japan] Jones P.F., Jakubowicz T., Pitossi F.J., Maurer F., Hemmings B.A.; "Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily."; Proc. Natl. Acad. Sci. U.S.A. 88:4171-4175(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/s001250100577; PubMed=11508278 [NCBI, ExPASy, EBI, Israel, Japan] Matsubara A., Wasson J.C., Donelan S.S., Welling C.M., Glaser B., Permutt M.A.; "Isolation and characterization of the human AKT1 gene, identification of 13 single nucleotide polymorphisms (SNPs), and their lack of association with Type II diabetes."; Diabetologia 44:910-913(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Muscle, and Ovary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 63-480, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. TISSUE=Foreskin; DOI=10.1111/j.1432-1033.1991.tb16305.x; PubMed=1718748 [NCBI, ExPASy, EBI, Israel, Japan] Coffer P.J., Woodgett J.R.; "Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families."; Eur. J. Biochem. 201:475-481(1991).
[5]	ERRATUM, AND SEQUENCE REVISION. PubMed=1533586 [NCBI, ExPASy, EBI, Israel, Japan] Coffer P.J., Woodgett J.R.; Eur. J. Biochem. 205:1217-1218(1992).
[6]	ENZYME REGULATION, AND PHOSPHORYLATION AT SER-473. DOI=10.1073/pnas.95.19.11211; PubMed=9736715 [NCBI, ExPASy, EBI, Israel, Japan] Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S.; "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. 95:11211-11216(1998).
[7]	MUTAGENESIS OF THR-308 AND SER-473, AND PHOSPHORYLATION AT THR-308 AND SER-473. PubMed=8978681 [NCBI, ExPASy, EBI, Israel, Japan] Alessi D.R., Andjelkovic M., Caudwell F.B., Cron P., Morrice N., Cohen P., Hemmings B.A.; "Mechanism of activation of protein kinase B by insulin and IGF-1."; EMBO J. 15:6541-6551(1996).
[8]	FUNCTION, ENZYME REGULATION, AND PHOSPHORYLATION AT THR-308 BY PDPK1. PubMed=9512493 [NCBI, ExPASy, EBI, Israel, Japan] Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., Alessi D.R.; "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. 331:299-308(1998).
[9]	INTERACTION WITH MTCP1; TCL1A AND TCL1B. DOI=10.1016/S1097-2765(00)00039-3; PubMed=10983986 [NCBI, ExPASy, EBI, Israel, Japan] Laine J., Kuenstle G., Obata T., Sha M., Noguchi M.; "The protooncogene TCL1 is an Akt kinase coactivator."; Mol. Cell 6:395-407(2000).
[10]	INTERACTION WITH TCL1A. DOI=10.1073/pnas.040557697; PubMed=10716693 [NCBI, ExPASy, EBI, Israel, Japan] Pekarsky Y., Koval A., Hallas C., Bichi R., Tresini M., Malstrom S., Russo G., Tsichlis P., Croce C.M.; "Tcl1 enhances Akt kinase activity and mediates its nuclear translocation."; Proc. Natl. Acad. Sci. U.S.A. 97:3028-3033(2000).
[11]	INTERACTION WITH THEM4, AND SUBCELLULAR LOCATION. DOI=10.1126/science.1062030; PubMed=11598301 [NCBI, ExPASy, EBI, Israel, Japan] Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.; "Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."; Science 294:374-380(2001).
[12]	FUNCTION IN PHOSPHORYLATION OF TBC1D4. DOI=10.1074/jbc.C200198200; PubMed=11994271 [NCBI, ExPASy, EBI, Israel, Japan] Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C., Lienhard G.E.; "A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain."; J. Biol. Chem. 277:22115-22118(2002).
[13]	INTERACTION WITH CDKN1B, AND FUNCTION. DOI=10.1074/jbc.M203668200; PubMed=12042314 [NCBI, ExPASy, EBI, Israel, Japan] Fujita N., Sato S., Katayama K., Tsuruo T.; "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization."; J. Biol. Chem. 277:28706-28713(2002).
[14]	PHOSPHORYLATION AT TYR-474, AND MUTAGENESIS OF TYR-474. DOI=10.1074/jbc.M203387200; PubMed=12149249 [NCBI, ExPASy, EBI, Israel, Japan] Conus N.M., Hannan K.M., Cristiano B.E., Hemmings B.A., Pearson R.B.; "Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase."; J. Biol. Chem. 277:38021-38028(2002).
[15]	INTERACTION WITH TCL1A. DOI=10.1128/MCB.22.5.1513-1525.2002; PubMed=11839817 [NCBI, ExPASy, EBI, Israel, Japan] Kuenstle G., Laine J., Pierron G., Kagami S., Nakajima H., Hoh F., Roumestand C., Stern M.H., Noguchi M.; "Identification of Akt association and oligomerization domains of the Akt kinase coactivator TCL1."; Mol. Cell. Biol. 22:1513-1525(2002).
[16]	INTERACTION WITH CDKN1B, FUNCTION, AND MUTAGENESIS OF THR-308 AND SER-473. DOI=10.1038/nm759; PubMed=12244301 [NCBI, ExPASy, EBI, Israel, Japan] Shin I., Yakes F.M., Rojo F., Shin N.-Y., Bakin A.V., Baselga J., Arteaga C.L.; "PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization."; Nat. Med. 8:1145-1152(2002).
[17]	INTERACTION WITH AGAP2, AND PHOSPHORYLATION AT SER-473. DOI=10.1074/jbc.M312175200; PubMed=14761976 [NCBI, ExPASy, EBI, Israel, Japan] Ahn J.-Y., Rong R., Kroll T.G., Van Meir E.G., Snyder S.H., Ye K.; "PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Akt activity and mediates cellular invasion."; J. Biol. Chem. 279:16441-16451(2004).
[18]	INTERACTION WITH AKTIP. DOI=10.1128/MCB.24.4.1493-1504.2004; PubMed=14749367 [NCBI, ExPASy, EBI, Israel, Japan] Remy I., Michnick S.W.; "Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt."; Mol. Cell. Biol. 24:1493-1504(2004).
[19]	INTERACTION WITH AGAP2. DOI=10.1073/pnas.0400921101; PubMed=15118108 [NCBI, ExPASy, EBI, Israel, Japan] Ahn J.-Y., Hu Y., Kroll T.G., Allard P., Ye K.; "PIKE-A is amplified in human cancers and prevents apoptosis by up-regulating Akt."; Proc. Natl. Acad. Sci. U.S.A. 101:6993-6998(2004).
[20]	FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH CCDC88A. DOI=10.1016/j.devcel.2005.08.001; PubMed=16139227 [NCBI, ExPASy, EBI, Israel, Japan] Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.; "Akt/PKB regulates actin organization and cell motility via Girdin/APE."; Dev. Cell 9:389-402(2005).
[21]	PHOSPHORYLATION AT THR-308 AND SER-473. DOI=10.1126/science.1106148; PubMed=15718470 [NCBI, ExPASy, EBI, Israel, Japan] Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.; "Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex."; Science 307:1098-1101(2005).
[22]	PHOSPHORYLATION AT SER-473. DOI=10.1007/s00401-006-0128-y; PubMed=17013611 [NCBI, ExPASy, EBI, Israel, Japan] Schick V., Majores M., Engels G., Spitoni S., Koch A., Elger C.E., Simon M., Knobbe C., Bluemcke I., Becker A.J.; "Activation of Akt independent of PTEN and CTMP tumor-suppressor gene mutations in epilepsy-associated Taylor-type focal cortical dysplasias."; Acta Neuropathol. 112:715-725(2006).
[23]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-126 AND SER-129, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[24]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-126 AND SER-129, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[26]	VARIANT BREAST CANCER LYS-17, AND CHARACTERIZATION OF VARIANT BREAST CANCER LYS-17. DOI=10.1038/nature05933; PubMed=17611497 [NCBI, ExPASy, EBI, Israel, Japan] Carpten J.D., Faber A.L., Horn C., Donoho G.P., Briggs S.L., Robbins C.M., Hostetter G., Boguslawski S., Moses T.Y., Savage S., Uhlik M., Lin A., Du J., Qian Y.-W., Zeckner D.J., Tucker-Kellogg G., Touchman J., Patel K., Mousses S., Bittner M., Schevitz R., Lai M.-H.T., Blanchard K.L., Thomas J.E.; "A transforming mutation in the pleckstrin homology domain of AKT1 in cancer."; Nature 448:439-444(2007).

Comments

FUNCTION: General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis, partly by playing a role in both insulin-induced phosphorylation of 4E-BP1 and in insulin-induced activation of p70 S6 kinase. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
ENZYME REGULATION: Three specific sites, one in the kinase domain (Thr-308) and the two other ones in the C-terminal regulatory region (Ser-473 and Tyr-474), need to be phosphorylated for its full activation.
SUBUNIT: Interacts with AGAP2 isoform 2 (PIKE-A) in the presence of guanine nucleotides. The C-terminus interacts with CCDC88A/GRDN and THEM4. Interacts with AKTIP. Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B. Interacts with CDKN1B; the interaction phosphorylates CDKN1B promoting 14-3-3 binding and cell-cycle progression.
INTERACTION:
Self; NbExp=1; IntAct=EBI-296087, EBI-296087;
P29067:Arrb2 (xeno); NbExp=2; IntAct=EBI-296087, EBI-1636616;
Q8IXJ9:ASXL1; NbExp=1; IntAct=EBI-296087, EBI-1646500;
O95999:BCL10; NbExp=3; IntAct=EBI-296087, EBI-958922;
O43521-1:BCL2L11; NbExp=1; IntAct=EBI-296087, EBI-526416;
Q16543:CDC37; NbExp=1; IntAct=EBI-296087, EBI-295634;
P49841:GSK3B; NbExp=1; IntAct=EBI-296087, EBI-373586;
Q99683:MAP3K5; NbExp=2; IntAct=EBI-296087, EBI-476263;
O60437:PPL; NbExp=1; IntAct=EBI-296087, EBI-368321;
Q15047:SETDB1; NbExp=6; IntAct=EBI-296087, EBI-79691;
Q7Z6J0:SH3RF1; NbExp=1; IntAct=EBI-296087, EBI-311339;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A.
TISSUE SPECIFICITY: In all human cell types so far analyzed.
DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI(3)K) results in its targeting to the plasma membrane.
DOMAIN: The AGC-kinase C-terminal mediates interaction with THEM4.
PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity. Ser-473 phosphorylation by the Rictor-mTor complex favors Thr-308 phosphorylation by PDPK1. Ser-473 phosphorylation is enhanced by interaction with AGAP2 isoform 2 (PIKE-A). Ser-473 phosphorylation is enhanced in focal cortical dysplasias with Taylor-type balloon cells.
DISEASE: Defects in AKT1 are associated with breast cancer (BC) [MIM:114480]. BC is an extremely common malignancy, affecting one in eight women during their lifetime.
DISEASE: Defects in AKT1 are associated with colorectal cancer (CRC) [MIM:114500].
DISEASE: Defects in AKT1 are associated with susceptibility to ovarian cancer [MIM:604370]; also called susceptibility to familial breast-ovarian cancer type 1 (BROVCA1).
SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.
SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
SIMILARITY: Contains 1 PH domain.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M63167; AAA36539.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283830; AAL55732.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283819; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283820; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283821; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283822; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283823; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283824; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283825; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283826; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283827; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283828; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283829; AAL55732.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000479; AAH00479.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC084538; AAH84538.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X61037; CAA43372.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00012866; -.

PIR

A39360; A39360.

RefSeq

NP_001014431.1; -.
NP_001014432.1; -.
NP_005154.2; -.

UniGene

Hs.525622

3D structure databases

PDB

1H10; X-ray; 1.40 A; A=1-123.	[ExPASy / RCSB / EBI]
1UNP; X-ray; 1.65 A; A=1-121.	[ExPASy / RCSB / EBI]
1UNQ; X-ray; 0.98 A; A=1-123.	[ExPASy / RCSB / EBI]
1UNR; X-ray; 1.25 A; A=1-123.	[ExPASy / RCSB / EBI]
2UVM; X-ray; 1.94 A; A=1-123.	[ExPASy / RCSB / EBI]
2UZR; X-ray; 1.94 A; A=1-123.	[ExPASy / RCSB / EBI]
2UZS; X-ray; 2.46 A; A=1-123.	[ExPASy / RCSB / EBI]
3CQU; X-ray; 2.20 A; A=144-480.	[ExPASy / RCSB / EBI]
3CQW; X-ray; 2.00 A; A=144-480.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1H10; -.
1UNP; -.
1UNQ; -.
1UNR; -.
2UVM; -.
2UZR; -.
2UZS; -.
3CQU; -.
3CQW; -.

ModBase

P31749.

Protein-protein interaction databases

DIP

DIP:24269N; -.

IntAct

P31749; 18.

PTM databases

PhosphoSite

P31749; -.

Enzyme and pathway databases

BRENDA

2.7.11.1; 247.

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
amb2_neutrophils_pathway; amb2 Integrin signaling.
angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
aurora_a_pathway; Aurora A signaling.
bcr_5pathway; BCR signaling pathway.
ceramidepathway; Ceramide signaling pathway.
pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
ar_pathway; Coregulation of Androgen receptor activity.
endothelinpathway; Endothelins.
fcer1pathway; Fc-epsilon receptor I signaling in mast cells.
fgf_pathway; FGF signaling pathway.
hnf3bpathway; FOXA2 and FOXA3 transcription factor networks.
foxopathway; FoxO family signaling.
hedgehog_glipathway; Hedgehog signaling events mediated by Gli proteins.
hif1_tfpathway; HIF-1-alpha transcription factor network.
ifngpathway; IFN-gamma pathway.
igf1_pathway; IGF1 pathway.
il2_pi3kpathway; IL2 signaling events mediated by PI3K.
il4_2pathway; IL4-mediated signaling events.
il6_7pathway; IL6-mediated signaling events.
insulin_pathway; Insulin Pathway.
insulin_glucose_pathway; Insulin-mediated glucose transport.
avb3_integrin_pathway; Integrins in angiogenesis.
lysophospholipid_pathway; LPA receptor mediated events.
mtor_4pathway; mTOR signaling pathway.
p75ntrpathway; p75(NTR)-mediated signaling.
pdgfrbpathway; PDGFR-beta signaling pathway.
er_nongenomic_pathway; Plasma membrane estrogen receptor signaling.
reelinpathway; Reelin signaling pathway.
smad2_3nuclearpathway; Regulation of nuclear SMAD2/3 signaling.
telomerasepathway; Regulation of Telomerase.
retinoic_acid_pathway; Retinoic acid receptors-mediated signaling.
s1p_s1p3_pathway; S1P3 pathway.
met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
ptp1bpathway; Signaling events mediated by PTP1B.
kitpathway; Signaling events mediated by Stem cell factor receptor (c-Kit).
hedgehog_2pathway; Signaling events mediated by the Hedgehog family.
vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2.
tcrpathway; TCR signaling in naive CD4+ T cells.
cd8tcrpathway; TCR signaling in naive CD8+ T cells.
txa2pathway; Thromboxane A2 receptor signaling.
pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
vegfr1_pathway; VEGFR1 specific signals.
lymphangiogenesis_pathway; VEGFR3 signaling in lymphatic endothelium.

Reactome

REACT_11061; Signalling by NGF.
REACT_12508; Metabolism of nitric oxide.
REACT_13698; Regulation of beta-cell development.
REACT_578; Apoptosis.
REACT_6900; Signaling in Immune system.

Organism-specific databases

GC14M104361; -.

HIX0012019; -.

HGNC:391; AKT1.

CAB003765; -.
HPA002891; -.

MIM

114480; phenotype. [NCBI / EBI]
114500; phenotype. [NCBI / EBI]
164730; gene. [NCBI / EBI]
604370; phenotype. [NCBI / EBI]

PharmGKB

PA24684; -.

Gene expression databases

P31749; -.

P31749; -.

HS_AKT1; -.

ENSG00000142208; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654;	Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005886;	Cellular component: plasma membrane (inferred from direct assay from UniProtKB).
GO:0005524;	Molecular function: ATP binding (inferred by curator from UniProtKB).
GO:0019899;	Molecular function: enzyme binding (inferred from sequence or structural similarity from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0030235;	Molecular function: nitric-oxide synthase regulator activity (inferred from mutant phenotype from UniProtKB).
GO:0005547;	Molecular function: phosphatidylinositol-3,4,5-trisphosphate binding (inferred from direct assay from UniProtKB).
GO:0043325;	Molecular function: phosphatidylinositol-3,4-bisphosphate binding (inferred from direct assay from UniProtKB).
GO:0004674;	Molecular function: protein serine/threonine kinase activity (inferred from direct assay from UniProtKB).
GO:0005351;	Molecular function: sugar:hydrogen symporter activity (inferred from electronic annotation from UniProtKB-KW).
GO:0008633;	Biological process: activation of pro-apoptotic gene products (inferred from experiment from Reactome).
GO:0006924;	Biological process: activation-induced cell death of T cells (inferred from mutant phenotype from MGI).
GO:0007186;	Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from ProtInc).
GO:0006006;	Biological process: glucose metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0005978;	Biological process: glycogen biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0008286;	Biological process: insulin receptor signaling pathway (inferred from mutant phenotype from UniProtKB).
GO:0048009;	Biological process: insulin-like growth factor receptor signaling pathway (inferred from mutant phenotype from UniProtKB).
GO:0031999;	Biological process: negative regulation of fatty acid beta-oxidation (inferred from mutant phenotype from UniProtKB).
GO:0010748;	Biological process: negative regulation of plasma membrane long-chain fatty acid transport (inferred from mutant phenotype from UniProtKB).
GO:0006469;	Biological process: negative regulation of protein kinase activity (inferred from mutant phenotype from UniProtKB).
GO:0006809;	Biological process: nitric oxide biosynthetic process (traceable author statement from ProtInc).
GO:0018105;	Biological process: peptidyl-serine phosphorylation (inferred from direct assay from UniProtKB).
GO:0030307;	Biological process: positive regulation of cell growth (inferred from direct assay from UniProtKB).
GO:0031659;	Biological process: positive regulation of cyclin-dependent protein kinase activity during G1/S (inferred from direct assay from UniProtKB).
GO:0045600;	Biological process: positive regulation of fat cell differentiation (inferred from mutant phenotype from UniProtKB).
GO:0046326;	Biological process: positive regulation of glucose import (inferred from mutant phenotype from UniProtKB).
GO:0010907;	Biological process: positive regulation of glucose metabolic process (inferred from mutant phenotype from UniProtKB).
GO:0045725;	Biological process: positive regulation of glycogen biosynthetic process (inferred from mutant phenotype from UniProtKB).
GO:0046889;	Biological process: positive regulation of lipid biosynthetic process (inferred from mutant phenotype from UniProtKB).
GO:0045429;	Biological process: positive regulation of nitric oxide biosynthetic process (inferred from mutant phenotype from UniProtKB).
GO:0051000;	Biological process: positive regulation of nitric-oxide synthase activity (inferred from mutant phenotype from UniProtKB).
GO:0046777;	Biological process: protein amino acid autophosphorylation (traceable author statement from UniProtKB).
GO:0000060;	Biological process: protein import into nucleus, translocation (inferred from mutant phenotype from UniProtKB).
GO:0070201;	Biological process: regulation of establishment of protein localization (inferred from mutant phenotype from UniProtKB).
GO:0006417;	Biological process: regulation of translation (inferred from electronic annotation from UniProtKB-KW).
GO:0034405;	Biological process: response to fluid shear stress (inferred from mutant phenotype from UniProtKB).
GO:0009408;	Biological process: response to heat (traceable author statement from ProtInc).
GO:0070141;	Biological process: response to UV-A (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000961; AGC-kinase_C.
IPR011993; PH_type.
IPR017892; Pkinase_C.
IPR001849; Pleckstrin_homology.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
IPR015744; Serine/threonine_Kinase_Rac.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.29.30; PH_type; 1.

PANTHER

PTHR22985:SF69; Akt; 1.

Pfam

PF00169; PH; 1.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00233; PH; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS51285; AGC_KINASE_CTER; 1.
PS50003; PH_DOMAIN; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P31749; -.

Genome annotation databases

Ensembl

ENSG00000142208; Homo sapiens. [Contig view]

GeneID

207; -.

KEGG

hsa:207; -.

Phylogenomic databases

HOGENOM

P31749; -.

HOVERGEN

P31749; -.

OMA

P31749; KLSPPFK.

Other

BindingDB

P31749; -.

DrugBank

DB00171; Adenosine triphosphate.
DB01169; Arsenic trioxide.

828; -.

P31749; -.

AKT1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Apoptosis; ATP-binding; Carbohydrate metabolism; Cell membrane; Cytoplasm; Disease mutation; Glucose metabolism; Glycogen biosynthesis; Glycogen metabolism; Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Sugar transport; Transferase; Translation regulation; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 480`	`480`	`RAC-alpha serine/threonine-protein kinase.`	`PRO_0000085605`
`DOMAIN`	`5 108`	`104`	`PH.`
`DOMAIN`	`150 408`	`259`	`Protein kinase.`
`DOMAIN`	`409 480`	`72`	`AGC-kinase C-terminal.`
`NP_BIND`	`156 164`	`9`	`ATP (By similarity).`
`ACT_SITE`	`274 274`		`Proton acceptor (By similarity).`
`BINDING`	`179 179`		`ATP (By similarity).`
`MOD_RES`	`124 124`		`Phosphoserine.`
`MOD_RES`	`126 126`		`Phosphoserine.`
`MOD_RES`	`129 129`		`Phosphoserine.`
`MOD_RES`	`308 308`		`Phosphothreonine; by PDPK1.`
`MOD_RES`	`473 473`		`Phosphoserine.`
`MOD_RES`	`474 474`		`Phosphotyrosine.`
`VARIANT`	`17 17`	`1`	`E -> K (in breast cancer, colorectal cancer and ovarian cancer; somatic mutation; alters the PH domain conformation; results in activation of the protein; alters the subcellular location of the protein to the plasma membrane).`	`VAR_055422 [3D]`
`VARIANT`	`167 167`	`1`	`V -> A (in dbSNP:rs11555433 [NCBI]).`	`VAR_051617`
`MUTAGEN`	`308 308`		`T->D: 5-fold activation and 18-fold activation; when associated with D-473.`
`MUTAGEN`	`473 473`		`S->D: 7-fold activation and 25-fold activation; when associated with D-308.`
`MUTAGEN`	`474 474`		`Y->F: 55% inhibition of activation.`
`CONFLICT`	`173 174`		`GR -> A (in Ref. 4; CAA43372).`
`CONFLICT`	`202 202`		`L -> Q (in Ref. 4; CAA43372).`
`CONFLICT`	`212 212`		`A -> R (in Ref. 4; CAA43372).`
`CONFLICT`	`246 246`		`S -> A (in Ref. 4; CAA43372).`
`CONFLICT`	`409 409`		`A -> T (in Ref. 4; CAA43372).`
`CONFLICT`	`476 476`		`A -> P (in Ref. 4; CAA43372).`
`CONFLICT`	`478 478`		`G -> A (in Ref. 4; CAA43372).`
`CONFLICT`	`478 478`		`G -> S (in Ref. 1; AAA36539 and 2; AAL55732).`
`STRAND`	`6 15`	`10`
`STRAND`	`17 19`	`3`
`STRAND`	`22 30`	`9`
`STRAND`	`33 40`	`8`
`STRAND`	`52 56`	`5`
`STRAND`	`61 65`	`5`
`STRAND`	`67 79`	`13`
`STRAND`	`82 89`	`8`
`HELIX`	`93 118`	`26`
`HELIX`	`147 149`	`3`
`STRAND`	`150 159`	`10`
`STRAND`	`162 169`	`8`
`TURN`	`170 172`	`3`
`STRAND`	`175 182`	`8`
`HELIX`	`183 188`	`6`
`HELIX`	`192 204`	`13`
`STRAND`	`213 218`	`6`
`STRAND`	`220 228`	`9`
`HELIX`	`235 242`	`8`
`HELIX`	`247 266`	`20`
`HELIX`	`277 279`	`3`
`STRAND`	`280 282`	`3`
`STRAND`	`288 290`	`3`
`HELIX`	`313 315`	`3`
`HELIX`	`318 321`	`4`
`HELIX`	`329 344`	`16`
`HELIX`	`354 363`	`10`
`HELIX`	`374 383`	`10`
`HELIX`	`388 390`	`3`
`TURN`	`396 398`	`3`
`HELIX`	`399 403`	`5`
`HELIX`	`406 408`	`3`
`HELIX`	`413 418`	`6`
`HELIX`	`440 443`	`4`

Sequence information

Length: 480 AA [This is the length of the unprocessed precursor]

Molecular weight: 55686 Da [This is the MW of the unprocessed precursor]

CRC64: 6EAFF4F8AD436714 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDVDQREA PLNNFSVAQC 

        70         80         90        100        110        120 
QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWT TAIQTVADGL KKQEEEEMDF 

       130        140        150        160        170        180 
RSGSPSDNSG AEEMEVSLAK PKHRVTMNEF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI 

       190        200        210        220        230        240 
LKKEVIVAKD EVAHTLTENR VLQNSRHPFL TALKYSFQTH DRLCFVMEYA NGGELFFHLS 

       250        260        270        280        290        300 
RERVFSEDRA RFYGAEIVSA LDYLHSEKNV VYRDLKLENL MLDKDGHIKI TDFGLCKEGI 

       310        320        330        340        350        360 
KDGATMKTFC GTPEYLAPEV LEDNDYGRAV DWWGLGVVMY EMMCGRLPFY NQDHEKLFEL 

       370        380        390        400        410        420 
ILMEEIRFPR TLGPEAKSLL SGLLKKDPKQ RLGGGSEDAK EIMQHRFFAG IVWQHVYEKK 

       430        440        450        460        470        480 
LSPPFKPQVT SETDTRYFDE EFTAQMITIT PPDQDDSMEC VDSERRPHFP QFSYSASGTA

P31749 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools