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UniProtKB/Swiss-Prot entry Q9Y243


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AKT3_HUMAN
Primary accession number Q9Y243
Secondary accession numbers Q0VAA6 Q5VTI1 Q5VTI2 Q96QV3 Q9UFP5
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 97)
Name and origin of the protein
Protein name RAC-gamma serine/threonine-protein kinase
Synonyms EC 2.7.11.1
RAC-PK-gamma
Protein kinase Akt-3
Protein kinase B, gamma
PKB gamma
STK-2
Gene name
Name: AKT3
Synonyms: PKBG
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
DOI=10.1074/jbc.274.14.9133; PubMed=10092583 [NCBI, ExPASy, EBI, Israel, Japan]
Brodbeck D., Cron P., Hemmings B.A.;
"A human protein kinase B gamma with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain.";
J. Biol. Chem. 274:9133-9136(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1006/bbrc.1999.0559; PubMed=10208883 [NCBI, ExPASy, EBI, Israel, Japan]
Nakatani K., Sakaue H., Thompson D.A., Weigel R.J., Roth R.A.;
"Identification of a human Akt3 (protein kinase B gamma) which contains the regulatory serine phosphorylation site.";
Biochem. Biophys. Res. Commun. 257:906-910(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1046/j.1432-1327.1999.00774.x; PubMed=10491192 [NCBI, ExPASy, EBI, Israel, Japan]
Masure S., Haefner B., Wesselink J.-J., Hoefnagel E., Mortier E., Verhasselt P., Tuytelaars A., Gordon R., Richardson A.;
"Molecular cloning, expression and characterization of the human serine/threonine kinase Akt-3.";
Eur. J. Biochem. 265:353-360(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Li X., Yu L., Huang H., Zhang M., Zhao Y., Zhao S.;
"Cloning of a novel human cDNA, STK-2, which encodes a rat serine-threonine protein kinase (STK) homolog.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan]
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND MUTAGENESIS OF THR-305 AND THR-447.
DOI=10.1074/jbc.M104633200; PubMed=11387345 [NCBI, ExPASy, EBI, Israel, Japan]
Brodbeck D., Hill M.M., Hemmings B.A.;
"Two splice variants of PKB gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site Ser-472 in the C-terminal hydrophobic domain.";
J. Biol. Chem. 276:29550-29558(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[10]
CHARACTERIZATION, AND PHOSPHORYLATION AT THR-305 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).
[11]
INTERACTION WITH TCL1A.
DOI=10.1074/jbc.M107069200; PubMed=11707444 [NCBI, ExPASy, EBI, Israel, Japan]
Laine J., Kuenstle G., Obata T., Noguchi M.;
"Differential regulation of Akt kinase isoforms by the members of the TCL1 oncogene family.";
J. Biol. Chem. 277:3743-3751(2002).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[14]
VARIANT [LARGE SCALE ANALYSIS] ARG-171.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
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
AF124141; AAD29089.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF135794; AAD24196.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF085234; AAL40392.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ245709; CAB53537.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL117525; CAB55977.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY005799; AAF91073.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591721; CAH71866.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC096539; CAH71866.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592151; CAH71866.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662889; CAH71866.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591721; CAH71867.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC096539; CAH71867.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592151; CAH71867.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662889; CAH71867.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592151; CAH72891.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC096539; CAH72891.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591721; CAH72891.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662889; CAH72891.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592151; CAH72892.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC096539; CAH72892.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591721; CAH72892.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662889; CAH72892.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662889; CAH73072.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC096539; CAH73072.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591721; CAH73072.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592151; CAH73072.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662889; CAH73073.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC096539; CAH73073.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591721; CAH73073.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592151; CAH73073.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471148; EAW77093.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471148; EAW77094.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC121154; AAI21155.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00031747; -.
IPI00219411; -.
PIR A59380; A59380.
T17287; T17287.
RefSeq NP_005456.1; -.
NP_859029.1; -.
UniGene Hs.498292
3D structure databases
HSSP P31751; 1GZK. [HSSP ENTRY / PDB]
SMR Q9Y243; 1-115.
ModBase Q9Y243.
Protein-protein interaction databases
IntAct Q9Y243; 1.
PTM databases
PhosphoSite Q9Y243; -.
Enzyme and pathway databases
BRENDA 2.7.11.1; 247.
Pathway_Interaction_DB pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
s1p_s1p3_pathway; S1P3 pathway.
Reactome REACT_11061; Signalling by NGF.
REACT_13698; Regulation of beta-cell development.
Organism-specific databases
GeneCards GC01M241718; -.
H-InvDB HIX0001744; -.
HGNC HGNC:393; AKT3.
GenAtlas AKT3.
HPA CAB013090; -.
MIM 611223; gene. [NCBI / EBI]
PharmGKB PA24686; -.
Gene expression databases
ArrayExpress Q9Y243; -.
Bgee Q9Y243; -.
CleanEx HS_AKT3; -.
GermOnline ENSG00000117020; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006468; Biological process: protein amino acid phosphorylation (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
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 Q9Y243; -.
Genome annotation databases
Ensembl ENSG00000117020; Homo sapiens. [Contig view]
GeneID 10000; -.
KEGG hsa:10000; -.
NMPDR fig|9606.3.peg.3340; -.
Phylogenomic databases
HOGENOM Q9Y243; -.
HOVERGEN Q9Y243; -.
Other
BindingDB Q9Y243; -.
NextBio 37765; -.
SOURCE AKT3; Homo sapiens.
ProtoNet Q9Y243.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Cytoplasm; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   479  479     RAC-gamma serine/threonine-protein kinase. PRO_0000085611
DOMAIN   5   107  103     PH. 
DOMAIN   148   405  258     Protein kinase. 
DOMAIN   406   479  74     AGC-kinase C-terminal. 
NP_BIND   154   162  9     ATP (By similarity). 
ACT_SITE   271   271        Proton acceptor (By similarity). 
BINDING   177   177        ATP (By similarity). 
MOD_RES   120   120        Phosphoserine. 
MOD_RES   123   123        Phosphoserine. 
MOD_RES   305   305        Phosphothreonine; by PDPK1. 
MOD_RES   472   472        Phosphoserine (By similarity). 
VAR_SEQ   452   479        YDEDGMDCMDNERRPHFPQFSYSASGRE -> CQQSDCGMLGNWKK (in isoform 2). VSP_004947
VARIANT   171   171  1     G -> R (in a glioblastoma multiforme sample; somatic mutation). VAR_040358 [3D]
MUTAGEN   305   305        T->A: No activation after pervanadate treatment. 
MUTAGEN   305   305        T->D: 2-fold increase of phosphorylation steady state level, no activation after pervanadate treatment. 
MUTAGEN   447   447        T->A: No effect. 
MUTAGEN   447   447        T->D: No effect. 
MUTAGEN   472   472        S->A: 67% decrease of activity after pervanadate treatment. 
MUTAGEN   472   472        S->D: 1.4-fold increase of phosphorylation steady state level, 50% decrease of activity after pervanadate treatment. 
CONFLICT   279   279        L -> R (in Ref. 9; AAI21155). 
Sequence information
Length: 479 AA [This is the length of the unprocessed precursor] Molecular weight: 55775 Da [This is the MW of the unprocessed precursor] CRC64: F08BDDE6502E78FB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSDVTIVKEG WVQKRGEYIK NWRPRYFLLK TDGSFIGYKE KPQDVDLPYP LNNFSVAKCQ 

        70         80         90        100        110        120 
LMKTERPKPN TFIIRCLQWT TVIERTFHVD TPEEREEWTE AIQAVADRLQ RQEEERMNCS 

       130        140        150        160        170        180 
PTSQIDNIGE EEMDASTTHH KRKTMNDFDY LKLLGKGTFG KVILVREKAS GKYYAMKILK 

       190        200        210        220        230        240 
KEVIIAKDEV AHTLTESRVL KNTRHPFLTS LKYSFQTKDR LCFVMEYVNG GELFFHLSRE 

       250        260        270        280        290        300 
RVFSEDRTRF YGAEIVSALD YLHSGKIVYR DLKLENLMLD KDGHIKITDF GLCKEGITDA 

       310        320        330        340        350        360 
ATMKTFCGTP EYLAPEVLED NDYGRAVDWW GLGVVMYEMM CGRLPFYNQD HEKLFELILM 

       370        380        390        400        410        420 
EDIKFPRTLS SDAKSLLSGL LIKDPNKRLG GGPDDAKEIM RHSFFSGVNW QDVYDKKLVP 

       430        440        450        460        470 
PFKPQVTSET DTRYFDEEFT AQTITITPPE KYDEDGMDCM DNERRPHFPQ FSYSASGRE 

Q9Y243 in FASTA format

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