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UniProtKB/Swiss-Prot entry Q8INB9


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

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Entry information
Entry name AKT1_DROME
Primary accession number Q8INB9
Secondary accession numbers Q0KI65 Q24293 Q24469 Q24470 Q7JN11 Q8T9A5 Q9VEY7
Integrated into Swiss-Prot on January 24, 2006
Sequence was last modified on December 7, 2004 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 59)
Name and origin of the protein
Protein name RAC serine/threonine-protein kinase
Synonyms DRAC-PK
Dakt1
DAkt
EC 2.7.11.1
Akt
Protein kinase B
PKB
Gene name
Name: Akt1
ORFNames: CG4006
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=8302573 [NCBI, ExPASy, EBI, Israel, Japan]
Franke T.F., Tartof K.D., Tsichlis P.N.;
"The SH2-like Akt homology (AH) domain of c-akt is present in multiple copies in the genome of vertebrate and invertebrate eucaryotes. Cloning and characterisation of the Drosophila melanogaster c-akt homolog Dakt1.";
Oncogene 9:141-148(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE INITIATION (ISOFORMS A AND C), ENZYME ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
DOI=10.1074/jbc.270.8.4066; PubMed=7876156 [NCBI, ExPASy, EBI, Israel, Japan]
Andjelkovic M., Jones P.F., Grossniklaus U., Cron P., Schier A.F., Dick M., Bilbe G., Hemmings B.A.;
"Developmental regulation of expression and activity of multiple forms of the Drosophila RAC protein kinase.";
J. Biol. Chem. 270:4066-4075(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE INITIATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
FUNCTION, AND MUTAGENESIS OF PHE-408.
DOI=10.1016/S0960-9822(98)70231-3; PubMed=9601646 [NCBI, ExPASy, EBI, Israel, Japan]
Staveley B.E., Ruel L., Jin J., Stambolic V., Mastronardi F.G., Heitzler P., Woodgett J.R., Manoukian A.S.;
"Genetic analysis of protein kinase B (AKT) in Drosophila.";
Curr. Biol. 8:599-602(1998).
[7]
FUNCTION, AND MUTAGENESIS OF LYS-295.
DOI=10.1038/70293; PubMed=10587646 [NCBI, ExPASy, EBI, Israel, Japan]
Verdu J., Buratovich M.A., Wilder E.L., Birnbaum M.J.;
"Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/PKB.";
Nat. Cell Biol. 1:500-506(1999).
[8]
FUNCTION, AND PHOSPHORYLATION AT SER-586.
DOI=10.1038/sj.onc.1203739; PubMed=10962553 [NCBI, ExPASy, EBI, Israel, Japan]
Scanga S.E., Ruel L., Binari R.C., Snow B., Stambolic V., Bouchard D., Peters M., Calvieri B., Mak T.W., Woodgett J.R., Manoukian A.S.;
"The conserved PI3'K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila.";
Oncogene 19:3971-3977(2000).
[9]
FUNCTION.
DOI=10.1016/S1534-5807(01)00090-9; PubMed=11740943 [NCBI, ExPASy, EBI, Israel, Japan]
Jin J., Anthopoulos N., Wetsch B., Binari R.C., Isaac D.D., Andrew D.J., Woodgett J.R., Manoukian A.S.;
"Regulation of Drosophila tracheal system development by protein kinase B.";
Dev. Cell 1:817-827(2001).
[10]
PHOSPHORYLATION.
DOI=10.1073/pnas.101596998; PubMed=11344272 [NCBI, ExPASy, EBI, Israel, Japan]
Cho K.S., Lee J.H., Kim S., Kim D., Koh H., Lee J., Kim C., Kim J., Chung J.;
"Drosophila phosphoinositide-dependent kinase-1 regulates apoptosis and growth via the phosphoinositide 3-kinase-dependent signaling pathway.";
Proc. Natl. Acad. Sci. U.S.A. 98:6144-6149(2001).
[11]
FUNCTION.
DOI=10.1073/pnas.011318098; PubMed=11752451 [NCBI, ExPASy, EBI, Israel, Japan]
Rintelen F., Stocker H., Thomas G., Hafen E.;
"PDK1 regulates growth through Akt and S6K in Drosophila.";
Proc. Natl. Acad. Sci. U.S.A. 98:15020-15025(2001).
[12]
FUNCTION.
DOI=10.1038/ncb840; PubMed=12172554 [NCBI, ExPASy, EBI, Israel, Japan]
Potter C.J., Pedraza L.G., Xu T.;
"Akt regulates growth by directly phosphorylating Tsc2.";
Nat. Cell Biol. 4:658-665(2002).
[13]
FUNCTION, AND MUTAGENESIS OF GLY-180 AND PHE-408.
DOI=10.1126/science.1068094; PubMed=11872800 [NCBI, ExPASy, EBI, Israel, Japan]
Stocker H., Andjelkovic M., Oldham S., Laffargue M., Wymann M.P., Hemmings B.A., Hafen E.;
"Living with lethal PIP3 levels: viability of flies lacking PTEN restored by a PH domain mutation in Akt/PKB.";
Science 295:2088-2091(2002).
[14]
FUNCTION.
DOI=10.1096/fj.03-0040fje; PubMed=14525946 [NCBI, ExPASy, EBI, Israel, Japan]
Lavenburg K.R., Ivey J., Hsu T., Muise-Helmericks R.C.;
"Coordinated functions of Akt/PKB and ETS1 in tubule formation.";
FASEB J. 17:2278-2280(2003).
[15]
FUNCTION.
DOI=10.1101/gad.1098703; PubMed=12893776 [NCBI, ExPASy, EBI, Israel, Japan]
Puig O., Marr M.T., Ruhf M.L., Tjian R.;
"Control of cell number by Drosophila FOXO: downstream and feedback regulation of the insulin receptor pathway.";
Genes Dev. 17:2006-2020(2003).
[16]
FUNCTION.
DOI=10.1101/gad.1240504; PubMed=15466161 [NCBI, ExPASy, EBI, Israel, Japan]
Dong J., Pan D.;
"Tsc2 is not a critical target of Akt during normal Drosophila development.";
Genes Dev. 18:2479-2484(2004).
[17]
FUNCTION, AND DEVELOPMENTAL STAGE.
DOI=10.1002/dvdy.20333; PubMed=15712201 [NCBI, ExPASy, EBI, Israel, Japan]
Cavaliere V., Donati A., Hsouna A., Hsu T., Gargiulo G.;
"dAkt kinase controls follicle cell size during Drosophila oogenesis.";
Dev. Dyn. 232:845-854(2005).
[18]
DEPHOSPHORYLATION AT SER-586.
DOI=10.1016/j.molcel.2005.03.008; PubMed=15808505 [NCBI, ExPASy, EBI, Israel, Japan]
Gao T., Furnari F., Newton A.C.;
"PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth.";
Mol. Cell 18:13-24(2005).
[19]
PHOSPHORYLATION AT SER-586.
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS SPECTROMETRY.
TISSUE=Embryo;
DOI=10.1021/pr700696a; PubMed=18327897 [NCBI, ExPASy, EBI, Israel, Japan]
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
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
Z26242; CAA81204.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X83510; CAA58499.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X83510; CAA58500.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAF55275.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAN13699.3; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY069856; AAL40001.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A55888; A55888.
RefSeq NP_732113.3; -.
NP_732114.1; -.
UniGene Dm.1219
3D structure databases
HSSP Q63450; 1A06. [HSSP ENTRY / PDB]
ModBase Q8INB9.
Protein-protein interaction databases
IntAct Q8INB9; 42.
Organism-specific databases
FlyBase FBgn0010379; Akt1.
Gene expression databases
ArrayExpress Q8INB9; -.
GermOnline CG4006; Drosophila melanogaster.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from FlyBase).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0035091; Molecular function: phosphoinositide binding (non-traceable author statement from FlyBase).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from direct assay from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (inferred from mutant phenotype from FlyBase).
GO:0008362; Biological process: chitin-based embryonic cuticle biosynthetic process (inferred from genetic interaction from FlyBase).
GO:0007427; Biological process: epithelial cell migration, open tracheal system (inferred from mutant phenotype from UniProtKB).
GO:0008286; Biological process: insulin receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0007242; Biological process: intracellular signaling cascade (inferred from genetic interaction from UniProtKB).
GO:0030307; Biological process: positive regulation of cell growth (inferred from mutant phenotype from UniProtKB).
GO:0040018; Biological process: positive regulation of multicellular organism growth (traceable author statement from FlyBase).
GO:0046622; Biological process: positive regulation of organ growth (inferred from mutant phenotype from UniProtKB).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from UniProtKB).
GO:0008360; Biological process: regulation of cell shape (inferred from mutant phenotype from FlyBase).
GO:0042306; Biological process: regulation of protein import into nucleus (traceable author statement from FlyBase).
GO:0019915; Biological process: sequestering of lipid (inferred from genetic interaction from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR015744; Akt.
IPR001849; PH.
IPR011993; PH_type.
IPR000961; Pkinase_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
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).
Genome annotation databases
Ensembl CG4006; Drosophila melanogaster. [Contig view]
GeneID 41957; -.
KEGG dme:Dmel_CG4006; -.
Other
NextBio 826461; -.
ProtoNet Q8INB9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative initiation; Apoptosis; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Developmental protein; Growth regulation; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   611  611     RAC serine/threonine-protein kinase. PRO_0000045784
DOMAIN   106   211  106     PH. 
DOMAIN   266   523  258     Protein kinase. 
DOMAIN   524   597  74     AGC-kinase C-terminal. 
NP_BIND   272   280  9     ATP (By similarity). 
ACT_SITE   389   389        Proton acceptor (By similarity). 
BINDING   295   295        ATP (Probable). 
MOD_RES   30    30        Phosphoserine. 
MOD_RES   586   586        Phosphoserine. 
VAR_SEQ   1    81        Missing (in isoform A). VSP_018833
MUTAGEN   180   180        G->S: Fails to be recruited at the membrane upon activation. 
MUTAGEN   260   260        K->A: Abolishes enzymatic activity. 
MUTAGEN   295   295        K->M: Abolishes enzymatic activity. 
MUTAGEN   408   408        F->I: Abolishes enzymatic activity. 
CONFLICT   73    73        A -> T (in Ref. 2; CAA58499). 
CONFLICT   200   201        QQ -> HE (in Ref. 1; CAA81204). 
Sequence information
Length: 611 AA [This is the length of the unprocessed precursor] Molecular weight: 68485 Da [This is the MW of the unprocessed precursor] CRC64: C139380152580934 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNYLPFVLQR RSTVVASAPA PGSASRIPES PTTTGSNIIN IIYSQSTHPN SSPTSGSAEK 

        70         80         90        100        110        120 
FSWQQSWPSR TSAAPTHDSG TMSINTTFDL SSPSVTSGHA LTEQTQVVKE GWLMKRGEHI 

       130        140        150        160        170        180 
KNWRQRYFVL HSDGRLMGYR SKPADSASTP SDFLLNNFTV RGCQIMTVDR PKPFTFIIRG 

       190        200        210        220        230        240 
LQWTTVIERT FAVESELERQ QWTEAIRNVS SRLIDVGEVA MTPSEQTDMT DVDMATIAED 

       250        260        270        280        290        300 
ELSEQFSVQG TTCNSSGVKK VTLENFEFLK VLGKGTFGKV ILCREKATAK LYAIKILKKE 

       310        320        330        340        350        360 
VIIQKDEVAH TLTESRVLKS TNHPFLISLK YSFQTNDRLC FVMQYVNGGE LFWHLSHERI 

       370        380        390        400        410        420 
FTEDRTRFYG AEIISALGYL HSQGIIYRDL KLENLLLDKD GHIKVADFGL CKEDITYGRT 

       430        440        450        460        470        480 
TKTFCGTPEY LAPEVLDDND YGQAVDWWGT GVVMYEMICG RLPFYNRDHD VLFTLILVEE 

       490        500        510        520        530        540 
VKFPRNITDE AKNLLAGLLA KDPKKRLGGG KDDVKEIQAH PFFASINWTD LVLKKIPPPF 

       550        560        570        580        590        600 
KPQVTSDTDT RYFDKEFTGE SVELTPPDPT GPLGSIAEEP LFPQFSYQGD MASTLGTSSH 

       610 
ISTSTSLASM Q 

Q8INB9 in FASTA format

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