Reviewed, UniProtKB/Swiss-Prot P31749 (AKT1_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	Apoptosis Carbohydrate metabolism Glucose metabolism Glycogen biosynthesis Glycogen metabolism Sugar transport Translation regulation Transport
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	G-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 component	cytosol Ref.21 Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome plasma membrane Ref.18 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-296087,EBI-296087
Arrb2	P29067	2	EBI-296087,EBI-1636616	From a different organism.
ASXL1	Q8IXJ9	1	EBI-296087,EBI-1646500
BCL10	O95999	3	EBI-296087,EBI-958922
BCL2L11	O43521-1	1	EBI-296087,EBI-526416
CDC37	Q16543	1	EBI-296087,EBI-295634
GSK3B	P49841	1	EBI-296087,EBI-373586
MAP3K5	Q99683	2	EBI-296087,EBI-476263
PPL	O60437	1	EBI-296087,EBI-368321
SETDB1	Q15047	6	EBI-296087,EBI-79691
SH3RF1	Q7Z6J0	1	EBI-296087,EBI-311339

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 480

480

RAC-alpha serine/threonine-protein kinase

PRO_0000085605

Regions

Domain

5 – 108

104

PH

Domain

150 – 408

259

Protein kinase

Domain

409 – 480

72

AGC-kinase C-terminal

Nucleotide binding

156 – 164

9

ATP By similarity

Sites

Active site

274

1

Proton acceptor By similarity

Binding site

179

1

ATP By similarity

Amino acid modifications

Modified residue

124

1

Phosphoserine Ref.23 Ref.24

Modified residue

126

1

Phosphoserine Ref.23 Ref.24

Modified residue

129

1

Phosphoserine Ref.23 Ref.24

Modified residue

308

1

Phosphothreonine; by PDPK1 Ref.8 Ref.7 Ref.21

Modified residue

473

1

Phosphoserine Ref.6 Ref.17 Ref.7 Ref.21 Ref.22

Modified residue

474

1

Phosphotyrosine Ref.14

Natural variations

Natural variant

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

Natural variant

167

1

V → A: dbSNP rs11555433.

VAR_051617

Experimental info

Mutagenesis

308

1

T → D: 5-fold activation and 18-fold activation; when associated with D-473. Ref.16 Ref.7

Mutagenesis

473

1

S → D: 7-fold activation and 25-fold activation; when associated with D-308. Ref.16 Ref.7

Mutagenesis

474

1

Y → F: 55% inhibition of activation. Ref.14

Sequence conflict

173 – 174

2

GR → A in CAA43372. Ref.4

Sequence conflict

202

1

L → Q in CAA43372. Ref.4

Sequence conflict

212

1

A → R in CAA43372. Ref.4

Sequence conflict

246

1

S → A in CAA43372. Ref.4

Sequence conflict

409

1

A → T in CAA43372. Ref.4

Sequence conflict

476

1

A → P in CAA43372. Ref.4

Sequence conflict

478

1

G → A in CAA43372. Ref.4

Sequence conflict

478

1

G → S in AAA36539. Ref.1

Sequence conflict

478

1

G → S in AAL55732. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

480

Helix Strand Turn

Details...

Beta strand

6 – 15

10

Beta strand

17 – 19

3

Beta strand

22 – 30

9

Beta strand

33 – 40

8

Beta strand

52 – 56

5

Beta strand

61 – 65

5

Beta strand

67 – 79

13

Beta strand

82 – 89

8

Helix

93 – 118

26

Helix

147 – 149

3

Beta strand

150 – 159

10

Beta strand

162 – 169

8

Turn

170 – 172

3

Beta strand

175 – 182

8

Helix

183 – 188

6

Helix

192 – 204

13

Beta strand

213 – 218

6

Beta strand

220 – 228

9

Helix

235 – 242

8

Helix

247 – 266

20

Helix

277 – 279

3

Beta strand

280 – 282

3

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	P31749-1 [UniParc]. Last modified February 1, 2005. Version 2. Checksum: 6EAFF4F8AD436714	FASTA	480	55,686
	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

References

	« Hide 'large scale' referencesShow '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. , 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

EMBLGenBankDDBJ

M63167 mRNA. Translation: AAA36539.1.
AF283830 , 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.

IPI

IPI00012866.

PIR

A39360.

RefSeq

NP_001014431.1.
NP_001014432.1.
NP_005154.2.

UniGene

Hs.525622

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H10	X-ray	1.40	A	1-123	[»]
1UNP	X-ray	1.65	A	1-121	[»]
1UNQ	X-ray	0.98	A	1-123	[»]
1UNR	X-ray	1.25	A	1-123	[»]
2UVM	X-ray	1.94	A	1-123	[»]
2UZR	X-ray	1.94	A	1-123	[»]
2UZS	X-ray	2.46	A	1-123	[»]
3CQU	X-ray	2.20	A	144-480	[»]
3CQW	X-ray	2.00	A	144-480	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:24269N.

IntAct

P31749. 18 interactions.

PTM databases

PhosphoSite

P31749.

Proteomic databases

PRIDE

P31749.

Genome annotation databases

Ensembl

ENSG00000142208. Homo sapiens. [Contig view]

GeneID

207.

KEGG

hsa:207.

Organism-specific databases

GeneCards

GC14M104361.

H-InvDB

HIX0012019.

HGNC

HGNC:391. AKT1.

HPA

CAB003765.
HPA002891.

MIM

114480. phenotype.
114500. phenotype.
164730. gene.
604370. phenotype.

PharmGKB

PA24684.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P31749.

HOVERGEN

P31749.

OMA

P31749. KLSPPFK.

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.

Gene expression databases

ArrayExpress

P31749.

Bgee

P31749.

CleanEx

HS_AKT1.

GermOnline

ENSG00000142208. Homo sapiens.

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]

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.

PANTHER

PTHR22985:SF69. Akt. 1 hit.

Pfam

PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS51285. 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]

ProtoNet

Search...

Other Resources

BindingDB

P31749.

DrugBank

DB00171. Adenosine triphosphate.
DB01169. Arsenic trioxide.

NextBio

828.

PMAP-CutDB

P31749.

SOURCE

Search...

Entry information

Entry name

AKT1_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)