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Reviewed, UniProtKB/Swiss-Prot P31749 (AKT1_HUMAN)

Last modified June 16, 2009. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    RAC-alpha serine/threonine-protein kinase
    EC=2.7.11.1
Alternative name(s):
    RAC-PK-alpha
    Protein kinase B
      Short name=PKB
    C-AKT
Gene names
Name: AKT1
Synonyms: PKB, RAC
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) 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. Ref.4 Ref.8 Ref.12 Ref.13 Ref.16 Ref.20

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.4 Ref.20 Ref.1

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. Ref.8 Ref.6

Subunit structure

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. Ref.13 Ref.16 Ref.20 Ref.9 Ref.10 Ref.11 Ref.15 Ref.17 Ref.18 Ref.19

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. Ref.11

Tissue specificity

In all human cell types so far analyzed. Ref.4

Domain

Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI3K) results in its targeting to the plasma membrane.

The AGC-kinase C-terminal mediates interaction with THEM4.

Post-translational modification

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.

Involvement in 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.

Defects in AKT1 are associated with colorectal cancer (CRC) [MIM:114500].

Defects in AKT1 are associated with susceptibility to ovarian cancer [MIM:604370]; also called susceptibility to familial breast-ovarian cancer type 1 (BROVCA1).

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 PH domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Carbohydrate metabolism
Glucose metabolism
Glycogen biosynthesis
Glycogen metabolism
Sugar transport
Translation regulation
Transport
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processG-protein coupled receptor protein signaling pathway

Traceable author statement. Source: ProtInc

activation of pro-apoptotic gene products

Inferred from Experiment. Source: Reactome

activation-induced cell death of T cells Ref.18

Inferred from mutant phenotype. Source: MGI

glucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

glycogen biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

insulin receptor signaling pathway Ref.7

Inferred from mutant phenotype. Source: UniProtKB

insulin-like growth factor receptor signaling pathway Ref.7

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of fatty acid beta-oxidation

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of plasma membrane long-chain fatty acid transport

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from mutant phenotype. Source: UniProtKB

nitric oxide biosynthetic process

Traceable author statement. Source: ProtInc

peptidyl-serine phosphorylation Ref.20

Inferred from direct assay. Source: UniProtKB

positive regulation of cell growth

Inferred from direct assay. Source: UniProtKB

positive regulation of cyclin-dependent protein kinase activity during G1/S

Inferred from direct assay. Source: UniProtKB

positive regulation of fat cell differentiation

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of glucose import

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of glucose metabolic process

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of glycogen biosynthetic process

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of lipid biosynthetic process

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of nitric oxide biosynthetic process

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of nitric-oxide synthase activity

Inferred from mutant phenotype. Source: UniProtKB

protein amino acid autophosphorylation

Traceable author statement. Source: UniProtKB

protein import into nucleus, translocation

Inferred from mutant phenotype. Source: UniProtKB

regulation of establishment of protein localization

Inferred from mutant phenotype. Source: UniProtKB

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

response to UV-A

Inferred from direct assay. Source: UniProtKB

response to fluid shear stress

Inferred from mutant phenotype. Source: UniProtKB

response to heat

Traceable author statement. Source: ProtInc

   Cellular componentcytosol Ref.21

Inferred from Experiment. Source: Reactome

nucleoplasm

Inferred from Experiment. Source: Reactome

plasma membrane Ref.18

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding Ref.12

Inferred by curator. Source: UniProtKB

enzyme binding

Inferred from sequence or structural similarity. Source: UniProtKB

identical protein binding

Inferred from physical interaction. Source: IntAct

nitric-oxide synthase regulator activity

Inferred from mutant phenotype. Source: UniProtKB

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from direct assay. Source: UniProtKB

phosphatidylinositol-3,4-bisphosphate binding

Inferred from direct assay. Source: UniProtKB

protein serine/threonine kinase activity Ref.12 Ref.20

Inferred from direct assay. Source: UniProtKB

sugar:hydrogen symporter activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480RAC-alpha serine/threonine-protein kinase
PRO_0000085605

Regions

Domain5 – 108104PH
Domain150 – 408259Protein kinase
Domain409 – 48072AGC-kinase C-terminal
Nucleotide binding156 – 1649ATP By similarity

Sites

Active site2741Proton acceptor By similarity
Binding site1791ATP By similarity

Amino acid modifications

Modified residue1241Phosphoserine Ref.23 Ref.24
Modified residue1261Phosphoserine Ref.23 Ref.24
Modified residue1291Phosphoserine Ref.23 Ref.24
Modified residue3081Phosphothreonine; by PDPK1 Ref.8 Ref.7 Ref.21
Modified residue4731Phosphoserine Ref.6 Ref.17 Ref.7 Ref.21 Ref.22
Modified residue4741Phosphotyrosine Ref.14

Natural variations

Natural variant171E → 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
Natural variant1671V → A: dbSNP rs11555433.
VAR_051617

Experimental info

Mutagenesis3081T → D: 5-fold activation and 18-fold activation; when associated with D-473. Ref.16 Ref.7
Mutagenesis4731S → D: 7-fold activation and 25-fold activation; when associated with D-308. Ref.16 Ref.7
Mutagenesis4741Y → F: 55% inhibition of activation. Ref.14
Sequence conflict173 – 1742GR → A in CAA43372. Ref.4
Sequence conflict2021L → Q in CAA43372. Ref.4
Sequence conflict2121A → R in CAA43372. Ref.4
Sequence conflict2461S → A in CAA43372. Ref.4
Sequence conflict4091A → T in CAA43372. Ref.4
Sequence conflict4761A → P in CAA43372. Ref.4
Sequence conflict4781G → A in CAA43372. Ref.4
Sequence conflict4781G → S in AAA36539. Ref.1
Sequence conflict4781G → S in AAL55732. Ref.2

Secondary structure

................................................................ 480
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31749-1 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 6EAFF4F8AD436714

FASTA48055,686
        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 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily."
Jones P.F., Jakubowicz T., Pitossi F.J., Maurer F., Hemmings B.A.
Proc. Natl. Acad. Sci. U.S.A. 88:4171-4175(1991) [PubMed: 1851997] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
[2]"Isolation and characterization of the human AKT1 gene, identification of 13 single nucleotide polymorphisms (SNPs), and their lack of association with Type II diabetes."
Matsubara A., Wasson J.C., Donelan S.S., Welling C.M., Glaser B., Permutt M.A.
Diabetologia 44:910-913(2001) [PubMed: 11508278] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle and Ovary.
[4]"Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families."
Coffer P.J., Woodgett J.R.
Eur. J. Biochem. 201:475-481(1991) [PubMed: 1718748] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-480, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
Tissue: Foreskin.
[5]Erratum
Coffer P.J., Woodgett J.R.
Eur. J. Biochem. 205:1217-1218(1992) [PubMed: 1533586] [Abstract]
Cited for: SEQUENCE REVISION.
[6]"Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase."
Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S.
Proc. Natl. Acad. Sci. U.S.A. 95:11211-11216(1998) [PubMed: 9736715] [Abstract]
Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-473.
[7]"Mechanism of activation of protein kinase B by insulin and IGF-1."
Alessi D.R., Andjelkovic M., Caudwell F.B., Cron P., Morrice N., Cohen P., Hemmings B.A.
EMBO J. 15:6541-6551(1996) [PubMed: 8978681] [Abstract]
Cited for: MUTAGENESIS OF THR-308 AND SER-473, PHOSPHORYLATION AT THR-308 AND SER-473.
[8]"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."
Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., Alessi D.R.
Biochem. J. 331:299-308(1998) [PubMed: 9512493] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-308 BY PDPK1.
[9]"The protooncogene TCL1 is an Akt kinase coactivator."
Laine J., Kuenstle G., Obata T., Sha M., Noguchi M.
Mol. Cell 6:395-407(2000) [PubMed: 10983986] [Abstract]
Cited for: INTERACTION WITH MTCP1; TCL1A AND TCL1B.
[10]"Tcl1 enhances Akt kinase activity and mediates its nuclear translocation."
Pekarsky Y., Koval A., Hallas C., Bichi R., Tresini M., Malstrom S., Russo G., Tsichlis P., Croce C.M.
Proc. Natl. Acad. Sci. U.S.A. 97:3028-3033(2000) [PubMed: 10716693] [Abstract]
Cited for: INTERACTION WITH TCL1A.
[11]"Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.
Science 294:374-380(2001) [PubMed: 11598301] [Abstract]
Cited for: INTERACTION WITH THEM4, SUBCELLULAR LOCATION.
[12]"A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain."
Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C., Lienhard G.E.
J. Biol. Chem. 277:22115-22118(2002) [PubMed: 11994271] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TBC1D4.
[13]"Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization."
Fujita N., Sato S., Katayama K., Tsuruo T.
J. Biol. Chem. 277:28706-28713(2002) [PubMed: 12042314] [Abstract]
Cited for: INTERACTION WITH CDKN1B, FUNCTION.
[14]"Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase."
Conus N.M., Hannan K.M., Cristiano B.E., Hemmings B.A., Pearson R.B.
J. Biol. Chem. 277:38021-38028(2002) [PubMed: 12149249] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-474, MUTAGENESIS OF TYR-474.
[15]"Identification of Akt association and oligomerization domains of the Akt kinase coactivator TCL1."
Kuenstle G., Laine J., Pierron G., Kagami S., Nakajima H., Hoh F., Roumestand C., Stern M.H., Noguchi M.
Mol. Cell. Biol. 22:1513-1525(2002) [PubMed: 11839817] [Abstract]
Cited for: INTERACTION WITH TCL1A.
[16]"PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization."
Shin I., Yakes F.M., Rojo F., Shin N.-Y., Bakin A.V., Baselga J., Arteaga C.L.
Nat. Med. 8:1145-1152(2002) [PubMed: 12244301] [Abstract]
Cited for: INTERACTION WITH CDKN1B, FUNCTION, MUTAGENESIS OF THR-308 AND SER-473.
[17]"PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Akt activity and mediates cellular invasion."
Ahn J.-Y., Rong R., Kroll T.G., Van Meir E.G., Snyder S.H., Ye K.
J. Biol. Chem. 279:16441-16451(2004) [PubMed: 14761976] [Abstract]
Cited for: INTERACTION WITH AGAP2, PHOSPHORYLATION AT SER-473.
[18]"Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt."
Remy I., Michnick S.W.
Mol. Cell. Biol. 24:1493-1504(2004) [PubMed: 14749367] [Abstract]
Cited for: INTERACTION WITH AKTIP.
[19]"PIKE-A is amplified in human cancers and prevents apoptosis by up-regulating Akt."
Ahn J.-Y., Hu Y., Kroll T.G., Allard P., Ye K.
Proc. Natl. Acad. Sci. U.S.A. 101:6993-6998(2004) [PubMed: 15118108] [Abstract]
Cited for: INTERACTION WITH AGAP2.
[20]"Akt/PKB regulates actin organization and cell motility via Girdin/APE."
Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
Dev. Cell 9:389-402(2005) [PubMed: 16139227] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CCDC88A.
[21]"Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex."
Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.
Science 307:1098-1101(2005) [PubMed: 15718470] [Abstract]
Cited for: PHOSPHORYLATION AT THR-308 AND SER-473.
[22]"Activation of Akt independent of PTEN and CTMP tumor-suppressor gene mutations in epilepsy-associated Taylor-type focal cortical dysplasias."
Schick V., Majores M., Engels G., Spitoni S., Koch A., Elger C.E., Simon M., Knobbe C., Bluemcke I., Becker A.J.
Acta Neuropathol. 112:715-725(2006) [PubMed: 17013611] [Abstract]
Cited for: PHOSPHORYLATION AT SER-473.
[23]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-126 AND SER-129, MASS SPECTROMETRY.
Tissue: Epithelium.
[24]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-126 AND SER-129, MASS SPECTROMETRY.
[25]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[26]"A transforming mutation in the pleckstrin homology domain of AKT1 in cancer."
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. expand/collapse author list , Mousses S., Bittner M., Schevitz R., Lai M.-H.T., Blanchard K.L., Thomas J.E.
Nature 448:439-444(2007) [PubMed: 17611497] [Abstract]
Cited for: VARIANT BREAST CANCER LYS-17, CHARACTERIZATION OF VARIANT BREAST CANCER LYS-17.
+Additional computationally mapped references.

Cross-references

Sequence databases

M63167 mRNA. Translation: AAA36539.1.
AF283830 expand/collapse EMBL AC list , AF283819, AF283820, AF283821, AF283822, AF283823, AF283824, AF283825, AF283826, AF283827, AF283828, AF283829 Genomic DNA. Translation: AAL55732.1.
BC000479 mRNA. Translation: AAH00479.1.
BC084538 mRNA. Translation: AAH84538.1.
X61037 mRNA. Translation: CAA43372.1.
IPIIPI00012866.
PIRA39360.
RefSeqNP_001014431.1.
NP_001014432.1.
NP_005154.2.
UniGeneHs.525622

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1H10X-ray1.40A1-123[»]
1UNPX-ray1.65A1-121[»]
1UNQX-ray0.98A1-123[»]
1UNRX-ray1.25A1-123[»]
2UVMX-ray1.94A1-123[»]
2UZRX-ray1.94A1-123[»]
2UZSX-ray2.46A1-123[»]
3CQUX-ray2.20A144-480[»]
3CQWX-ray2.00A144-480[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:24269N.
IntActP31749. 18 interactions.

PTM databases

PhosphoSiteP31749.

Proteomic databases

PRIDEP31749.

Genome annotation databases

EnsemblENSG00000142208. Homo sapiens. [Contig view]
GeneID207.
KEGGhsa:207.

Organism-specific databases

GeneCardsGC14M104361.
H-InvDBHIX0012019.
HGNCHGNC:391. AKT1.
HPACAB003765.
HPA002891.
MIM114480. phenotype.
114500. phenotype.
164730. gene.
604370. phenotype.
PharmGKBPA24684.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP31749.
HOVERGENP31749.
OMAP31749. KLSPPFK.

Enzyme and pathway databases

BRENDA2.7.11.1. 247.
Pathway_Interaction_DBa6b1_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.
ReactomeREACT_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.

Gene expression databases

ArrayExpressP31749.
BgeeP31749.
CleanExHS_AKT1.
GermOnlineENSG00000142208. Homo sapiens.

Family and domain databases

InterProIPR000961. 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]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
PANTHERPTHR22985:SF69. Akt. 1 hit.
PfamPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP31749.
DrugBankDB00171. Adenosine triphosphate.
DB01169. Arsenic trioxide.
NextBio828.
PMAP-CutDBP31749.
SOURCESearch...

Entry information

Entry nameAKT1_HUMAN
AccessionPrimary (citable) accession number: P31749
Secondary accession number(s): Q9BWB6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 2005
Last modified: June 16, 2009
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents