LOCUS NP_001014431 480 aa linear PRI 16-NOV-2008
DEFINITION v-akt murine thymoma viral oncogene homolog 1 [Homo sapiens].
ACCESSION NP_001014431
VERSION NP_001014431.1 GI:62241013
DBSOURCE REFSEQ: accession NM_001014431.1
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 480)
AUTHORS Zai,C.C., Romano-Silva,M.A., Hwang,R., Zai,G.C., Deluca,V.,
Muller,D.J., King,N., Voineskos,A.N., Meltzer,H.Y., Lieberman,J.A.,
Potkin,S.G., Remington,G. and Kennedy,J.L.
TITLE Genetic study of eight AKT1 gene polymorphisms and their
interaction with DRD2 gene polymorphisms in tardive dyskinesia
JOURNAL Schizophr. Res. (2008) In press
PUBMED 18838251
REMARK GeneRIF: Observational study of gene-disease association. (HuGE
Navigator)
Publication Status: Available-Online prior to print
REFERENCE 2 (residues 1 to 480)
AUTHORS Ikeda,M., Yamanouchi,Y., Kinoshita,Y., Kitajima,T., Yoshimura,R.,
Hashimoto,S., O'Donovan,M.C., Nakamura,J., Ozaki,N. and Iwata,N.
TITLE Variants of dopamine and serotonin candidate genes as predictors of
response to risperidone treatment in first-episode schizophrenia
JOURNAL Pharmacogenomics 9 (10), 1437-1443 (2008)
PUBMED 18855532
REMARK GeneRIF: Clinical trial of gene-disease association,
gene-environment interaction, and pharmacogenomic / toxicogenomic.
(HuGE Navigator)
REFERENCE 3 (residues 1 to 480)
AUTHORS Han,J.K., Lee,H.S., Yang,H.M., Hur,J., Jun,S.I., Kim,J.Y.,
Cho,C.H., Koh,G.Y., Peters,J.M., Park,K.W., Cho,H.J., Lee,H.Y.,
Kang,H.J., Oh,B.H., Park,Y.B. and Kim,H.S.
TITLE Peroxisome proliferator-activated receptor-delta agonist enhances
vasculogenesis by regulating endothelial progenitor cells through
genomic and nongenomic activations of the phosphatidylinositol
3-kinase/Akt pathway
JOURNAL Circulation 118 (10), 1021-1033 (2008)
PUBMED 18711014
REMARK GeneRIF: Peroxisome proliferator-activated receptor-delta agonist
enhances vasculogenesis by regulating endothelial progenitor cells
through genomic and nongenomic activations of the
phosphatidylinositol 3-kinase/Akt pathway
REFERENCE 4 (residues 1 to 480)
AUTHORS Cao,Z., Song,J.H., Kim,C.J., Cho,Y.G., Kim,S.Y., Nam,S.W., Lee,J.Y.
and Park,W.S.
TITLE Absence of E17K mutation in the pleckstrin homology domain of AKT1
in gastrointestinal and liver cancers in the Korean population
JOURNAL APMIS 116 (6), 530-533 (2008)
PUBMED 18754328
REMARK GeneRIF: no aberrant SSCP pattern in exon 2 of the AKT1 gene was
found, indicating that there were no E17K mutations of the AKT1
gene in these samples of gastrointestinal and liver cancers in the
Korean patients
REFERENCE 5 (residues 1 to 480)
AUTHORS Kohrenhagen,N., Voelker,H.U., Schmidt,M., Kapp,M.,
Krockenberger,M., Frambach,T., Dietl,J. and Kammerer,U.
TITLE Expression of transketolase-like 1 (TKTL1) and p-Akt correlates
with the progression of cervical neoplasia
JOURNAL J. Obstet. Gynaecol. Res. 34 (3), 293-300 (2008)
PUBMED 18686341
REMARK GeneRIF: results suggest that both Transketolase-like enzyme 1
(TKTL1) and p-Akt protein play an important role in the progression
of cervical neoplasia
REFERENCE 6 (sites)
AUTHORS Shenoy,N.G., Gleich,G.J. and Thomas,L.L.
TITLE Eosinophil major basic protein stimulates neutrophil superoxide
production by a class IA phosphoinositide 3-kinase and protein
kinase C-zeta-dependent pathway
JOURNAL J. Immunol. 171 (7), 3734-3741 (2003)
PUBMED 14500673
REFERENCE 7 (sites)
AUTHORS Pankov,R., Cukierman,E., Clark,K., Matsumoto,K., Hahn,C., Poulin,B.
and Yamada,K.M.
TITLE Specific beta1 integrin site selectively regulates Akt/protein
kinase B signaling via local activation of protein phosphatase 2A
JOURNAL J. Biol. Chem. 278 (20), 18671-18681 (2003)
PUBMED 12637511
REFERENCE 8 (sites)
AUTHORS Conus,N.M., Hannan,K.M., Cristiano,B.E., Hemmings,B.A. and
Pearson,R.B.
TITLE Direct identification of tyrosine 474 as a regulatory
phosphorylation site for the Akt protein kinase
JOURNAL J. Biol. Chem. 277 (41), 38021-38028 (2002)
PUBMED 12149249
REFERENCE 9 (sites)
AUTHORS Xu,J., Liu,D. and Songyang,Z.
TITLE The role of Asp-462 in regulating Akt activity
JOURNAL J. Biol. Chem. 277 (38), 35561-35566 (2002)
PUBMED 12124386
REFERENCE 10 (sites)
AUTHORS Hill,M.M., Feng,J. and Hemmings,B.A.
TITLE Identification of a plasma membrane Raft-associated PKB Ser473
kinase activity that is distinct from ILK and PDK1
JOURNAL Curr. Biol. 12 (14), 1251-1255 (2002)
PUBMED 12176337
REFERENCE 11 (sites)
AUTHORS Chen,R., Kim,O., Yang,J., Sato,K., Eisenmann,K.M., McCarthy,J.,
Chen,H. and Qiu,Y.
TITLE Regulation of Akt/PKB activation by tyrosine phosphorylation
JOURNAL J. Biol. Chem. 276 (34), 31858-31862 (2001)
PUBMED 11445557
REFERENCE 12 (sites)
AUTHORS Matsumoto,M., Ogawa,W., Hino,Y., Furukawa,K., Ono,Y., Takahashi,M.,
Ohba,M., Kuroki,T. and Kasuga,M.
TITLE Inhibition of insulin-induced activation of Akt by a
kinase-deficient mutant of the epsilon isozyme of protein kinase C
JOURNAL J. Biol. Chem. 276 (17), 14400-14406 (2001)
PUBMED 11278835
REFERENCE 13 (sites)
AUTHORS Okuno,S., Kitani,T., Matsuzaki,H., Konishi,H., Kikkawa,U. and
Fujisawa,H.
TITLE Studies on the phosphorylation of protein kinase B by
Ca(2+)/calmodulin-dependent protein kinases
JOURNAL J. Biochem. 127 (6), 965-970 (2000)
PUBMED 10833263
REFERENCE 14 (sites)
AUTHORS Balendran,A., Casamayor,A., Deak,M., Paterson,A., Gaffney,P.,
Currie,R., Downes,C.P. and Alessi,D.R.
TITLE PDK1 acquires PDK2 activity in the presence of a synthetic peptide
derived from the carboxyl terminus of PRK2
JOURNAL Curr. Biol. 9 (8), 393-404 (1999)
PUBMED 10226025
REFERENCE 15 (sites)
AUTHORS Delcommenne,M., Tan,C., Gray,V., Rue,L., Woodgett,J. and Dedhar,S.
TITLE Phosphoinositide-3-OH kinase-dependent regulation of glycogen
synthase kinase 3 and protein kinase B/AKT by the integrin-linked
kinase
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 95 (19), 11211-11216 (1998)
PUBMED 9736715
REFERENCE 16 (sites)
AUTHORS Alessi,D.R., Deak,M., Casamayor,A., Caudwell,F.B., Morrice,N.,
Norman,D.G., Gaffney,P., Reese,C.B., MacDougall,C.N., Harbison,D.,
Ashworth,A. and Bownes,M.
TITLE 3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural
and functional homology with the Drosophila DSTPK61 kinase
JOURNAL Curr. Biol. 7 (10), 776-789 (1997)
PUBMED 9368760
REFERENCE 17 (residues 1 to 480)
AUTHORS Coffer,P.J. and Woodgett,J.R.
TITLE Molecular cloning and characterisation of a novel putative
protein-serine kinase related to the cAMP-dependent and protein
kinase C families
JOURNAL Eur. J. Biochem. 205 (3), 1217 (1992)
PUBMED 1533586
REMARK Correction to:[Eur J Biochem. 1991 Oct 15;201(2):475-81. PMID:
1718748]
REFERENCE 18 (residues 1 to 480)
AUTHORS Coffer,P.J. and Woodgett,J.R.
TITLE Molecular cloning and characterisation of a novel putative
protein-serine kinase related to the cAMP-dependent and protein
kinase C families
JOURNAL Eur. J. Biochem. 201 (2), 475-481 (1991)
PUBMED 1718748
REMARK Erratum:[Eur J Biochem. 1992 May 1;205(3):1217. PMID: 1533586]
REFERENCE 19 (residues 1 to 480)
AUTHORS Jones,P.F., Jakubowicz,T., Pitossi,F.J., Maurer,F. and
Hemmings,B.A.
TITLE Molecular cloning and identification of a serine/threonine protein
kinase of the second-messenger subfamily
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 88 (10), 4171-4175 (1991)
PUBMED 1851997
REFERENCE 20 (residues 1 to 480)
AUTHORS Staal,S.P., Huebner,K., Croce,C.M., Parsa,N.Z. and Testa,J.R.
TITLE The AKT1 proto-oncogene maps to human chromosome 14, band q32
JOURNAL Genomics 2 (1), 96-98 (1988)
PUBMED 3384441
REFERENCE 21 (residues 1 to 480)
AUTHORS Staal,S.P.
TITLE Molecular cloning of the akt oncogene and its human homologues AKT1
and AKT2: amplification of AKT1 in a primary human gastric
adenocarcinoma
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 84 (14), 5034-5037 (1987)
PUBMED 3037531
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from CN414251.1 and BC000479.2.
Summary: The serine-threonine protein kinase encoded by the AKT1
gene 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. Multiple alternatively spliced
transcript variants have been found for this gene. [provided by
RefSeq].
Transcript Variant: This variant (3) lacks the 5' exon, but has an
upstream alternate 5' exon, as compared to variant 1. Variants 1
and 3 encode the same protein.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the
Entrez Gene record to access additional publications.
FEATURES Location/Qualifiers
source 1..480
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="14"
/map="14q32.32"
Protein 1..480
/product="v-akt murine thymoma viral oncogene homolog 1"
/EC_number="2.7.11.1"
/note="murine thymoma viral (v-akt) oncogene homolog-1;
rac protein kinase alpha; protein kinase B; RAC-alpha
serine/threonine-protein kinase"
/calculated_mol_wt=55556
Site 124
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[8]
Site 129
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[8]
Site 308
/site_type="modified"
/experiment="experimental evidence, no additional details
recorded"
/note="dephosphorylation site"
/citation=[7]
/db_xref="HPRD:08912"
Site 308
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[12]
/db_xref="HPRD:03954"
Site 308
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[14]
/citation=[16]
/db_xref="HPRD:05556"
Site 308
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[6]
/citation=[8]
/citation=[11]
Site 308
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[13]
/db_xref="HPRD:13000"
Site 315
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[11]
/db_xref="HPRD:01819"
Site 326
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[11]
/db_xref="HPRD:01819"
Site 450
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[8]
Site 462
/site_type="modified"
/experiment="experimental evidence, no additional details
recorded"
/note="proteolytic cleavage site"
/citation=[9]
/db_xref="HPRD:02799"
Site 473
/site_type="modified"
/experiment="experimental evidence, no additional details
recorded"
/note="dephosphorylation site"
/citation=[7]
/db_xref="HPRD:08912"
Site 473
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[15]
/db_xref="HPRD:03842"
Site 473
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[14]
/db_xref="HPRD:05556"
Site 473
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[6]
/citation=[8]
/citation=[10]
/citation=[11]
Site 473
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[12]
/db_xref="HPRD:03954"
Site 474
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[8]
CDS 1..480
/gene="AKT1"
/gene_synonym="AKT"
/gene_synonym="PKB"
/gene_synonym="RAC"
/gene_synonym="PRKBA"
/gene_synonym="MGC99656"
/gene_synonym="PKB-ALPHA"
/gene_synonym="RAC-ALPHA"
/coded_by="NM_001014431.1:341..1783"
/db_xref="CCDS:CCDS9994.1"
/db_xref="GeneID:207"
/db_xref="HGNC:391"
/db_xref="HPRD:01261"
/db_xref="MIM:164730"
ORIGIN
1 msdvaivkeg wlhkrgeyik twrpryfllk ndgtfigyke rpqdvdqrea plnnfsvaqc
61 qlmkterprp ntfiirclqw ttviertfhv etpeereewt taiqtvadgl kkqeeeemdf
121 rsgspsdnsg aeemevslak pkhrvtmnef eylkllgkgt fgkvilvkek atgryyamki
181 lkkevivakd evahtltenr vlqnsrhpfl talkysfqth drlcfvmeya nggelffhls
241 rervfsedra rfygaeivsa ldylhseknv vyrdlklenl mldkdghiki tdfglckegi
301 kdgatmktfc gtpeylapev ledndygrav dwwglgvvmy emmcgrlpfy nqdheklfel
361 ilmeeirfpr tlgpeaksll sgllkkdpkq rlgggsedak eimqhrffag ivwqhvyekk
421 lsppfkpqvt setdtryfde eftaqmitit ppdqddsmec vdserrphfp qfsysasgta
//