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Q8INB9

- AKT1_DROME

UniProt

Q8INB9 - AKT1_DROME

Protein

RAC serine/threonine-protein kinase

Gene

Akt1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase involved in various developmental processes. During early embryogenesis, acts as a survival protein. During mid-embryogenesis, phosphorylates and activates trh, a transcription factor required for tracheal cell fate determination. Also regulates tracheal cell migration. Later in development, acts downstream of PI3K and Pk61C/PDK1 in the insulin receptor transduction pathway which regulates cell growth and organ size, by phosphorylating and antagonizing FOXO transcription factor. Controls follicle cell size during oogenesis. May also stimulate cell growth by phosphorylating Gig/Tsc2 and inactivating the Tsc complex. Dephosphorylation of 'Ser-586' by Phlpp triggers apoptosis and suppression of tumor growth.11 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei295 – 2951ATPCurated
    Active sitei389 – 3891Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi272 – 2809ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatidylinositol binding Source: FlyBase
    3. protein binding Source: UniProtKB
    4. protein kinase activity Source: FlyBase
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. chitin-based embryonic cuticle biosynthetic process Source: FlyBase
    3. circadian rhythm Source: FlyBase
    4. dendrite regeneration Source: FlyBase
    5. epithelial cell migration, open tracheal system Source: UniProtKB
    6. insulin receptor signaling pathway Source: UniProtKB
    7. intracellular signal transduction Source: UniProtKB
    8. lipid storage Source: FlyBase
    9. long term synaptic depression Source: FlyBase
    10. negative regulation of apoptotic process Source: FlyBase
    11. negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
    12. open tracheal system development Source: FlyBase
    13. positive regulation of axon regeneration Source: FlyBase
    14. positive regulation of cell growth Source: UniProtKB
    15. positive regulation of cell size Source: FlyBase
    16. positive regulation of multicellular organism growth Source: FlyBase
    17. positive regulation of organ growth Source: UniProtKB
    18. protein phosphorylation Source: UniProtKB
    19. regulation of cell shape Source: FlyBase
    20. regulation of cell size Source: FlyBase
    21. regulation of dendrite development Source: FlyBase
    22. regulation of hemocyte proliferation Source: FlyBase
    23. regulation of multicellular organism growth Source: FlyBase
    24. regulation of organ growth Source: FlyBase
    25. regulation of protein import into nucleus Source: FlyBase
    26. response to oxidative stress Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Growth regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_180302. KSRP destabilizes mRNA.
    REACT_180799. Downregulation of ERBB2:ERBB3 signaling.
    REACT_180852. Translocation of GLUT4 to the plasma membrane.
    REACT_184384. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_207784. Inhibition of TSC complex formation by PKB.
    REACT_208852. Activation of PKB.
    REACT_219214. GPVI-mediated activation cascade.
    SignaLinkiQ8INB9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RAC serine/threonine-protein kinase (EC:2.7.11.1)
    Short name:
    DAkt
    Short name:
    DRAC-PK
    Short name:
    Dakt1
    Alternative name(s):
    Akt
    Protein kinase B
    Short name:
    PKB
    Gene namesi
    Name:Akt1
    ORF Names:CG4006
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0010379. Akt1.

    Subcellular locationi

    Cytoplasmcytosol. Cell membrane
    Note: Recruited to plasma membrane upon activation.

    GO - Cellular componenti

    1. cell surface Source: FlyBase
    2. cytoplasm Source: FlyBase
    3. cytosol Source: Reactome
    4. neuronal cell body Source: FlyBase
    5. plasma membrane Source: FlyBase

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Death at the first instar larval stage.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi180 – 1801G → S: Fails to be recruited at the membrane upon activation. 1 Publication
    Mutagenesisi260 – 2601K → A: Abolishes enzymatic activity.
    Mutagenesisi295 – 2951K → M: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi408 – 4081F → I: Abolishes enzymatic activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 611611RAC serine/threonine-protein kinasePRO_0000045784Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei30 – 301Phosphoserine2 Publications
    Modified residuei586 – 5861Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated and activated by Pk61C/PDK1. Phosphorylated on Ser-586 by the rictor-Tor complex.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ8INB9.
    PRIDEiQ8INB9.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Present in ovary, where it is concentrated at the basal side of follicle cells.1 Publication

    Developmental stagei

    Expressed both maternally and zygotically. Strongly expressed in embryo and pupa. Weakly expressed in larva. Mildly expressed in adult.2 Publications

    Gene expression databases

    BgeeiQ8INB9.

    Interactioni

    Protein-protein interaction databases

    BioGridi67008. 51 interactions.
    DIPiDIP-49060N.
    IntActiQ8INB9. 40 interactions.
    MINTiMINT-291950.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8INB9.
    SMRiQ8INB9. Positions 107-591.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini106 – 211106PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini266 – 523258Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini524 – 59774AGC-kinase C-terminalAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000114960.
    InParanoidiQ8INB9.
    KOiK04456.
    OMAiCNSSGVK.
    OrthoDBiEOG7Q5HCW.
    PhylomeDBiQ8INB9.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform C (identifier: Q8INB9-1) [UniParc]FASTAAdd to Basket

    Also known as: PK85

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNYLPFVLQR RSTVVASAPA PGSASRIPES PTTTGSNIIN IIYSQSTHPN    50
    SSPTSGSAEK FSWQQSWPSR TSAAPTHDSG TMSINTTFDL SSPSVTSGHA 100
    LTEQTQVVKE GWLMKRGEHI KNWRQRYFVL HSDGRLMGYR SKPADSASTP 150
    SDFLLNNFTV RGCQIMTVDR PKPFTFIIRG LQWTTVIERT FAVESELERQ 200
    QWTEAIRNVS SRLIDVGEVA MTPSEQTDMT DVDMATIAED ELSEQFSVQG 250
    TTCNSSGVKK VTLENFEFLK VLGKGTFGKV ILCREKATAK LYAIKILKKE 300
    VIIQKDEVAH TLTESRVLKS TNHPFLISLK YSFQTNDRLC FVMQYVNGGE 350
    LFWHLSHERI FTEDRTRFYG AEIISALGYL HSQGIIYRDL KLENLLLDKD 400
    GHIKVADFGL CKEDITYGRT TKTFCGTPEY LAPEVLDDND YGQAVDWWGT 450
    GVVMYEMICG RLPFYNRDHD VLFTLILVEE VKFPRNITDE AKNLLAGLLA 500
    KDPKKRLGGG KDDVKEIQAH PFFASINWTD LVLKKIPPPF KPQVTSDTDT 550
    RYFDKEFTGE SVELTPPDPT GPLGSIAEEP LFPQFSYQGD MASTLGTSSH 600
    ISTSTSLASM Q 611
    Length:611
    Mass (Da):68,485
    Last modified:December 7, 2004 - v3
    Checksum:iC139380152580934
    GO
    Isoform A (identifier: Q8INB9-2) [UniParc]FASTAAdd to Basket

    Also known as: PK66

    The sequence of this isoform differs from the canonical sequence as follows:
         1-81: Missing.

    Note: Major form.

    Show »
    Length:530
    Mass (Da):59,911
    Checksum:iF7508582C7F4A288
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731A → T in CAA58499. (PubMed:7876156)Curated
    Sequence conflicti200 – 2012QQ → HE in CAA81204. (PubMed:8302573)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8181Missing in isoform A. 2 PublicationsVSP_018833Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z26242 mRNA. Translation: CAA81204.1.
    X83510 Genomic DNA. Translation: CAA58499.2.
    X83510 Genomic DNA. Translation: CAA58500.1.
    AE014297 Genomic DNA. Translation: AAF55275.1.
    AE014297 Genomic DNA. Translation: AAN13699.3.
    AY069856 mRNA. Translation: AAL40001.1.
    PIRiA55888.
    RefSeqiNP_732113.3. NM_169705.1. [Q8INB9-1]
    NP_732114.1. NM_169706.1. [Q8INB9-2]
    NP_732115.1. NM_169707.1. [Q8INB9-2]
    UniGeneiDm.1219.

    Genome annotation databases

    EnsemblMetazoaiFBtr0083228; FBpp0082682; FBgn0010379. [Q8INB9-1]
    GeneIDi41957.
    KEGGidme:Dmel_CG4006.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z26242 mRNA. Translation: CAA81204.1 .
    X83510 Genomic DNA. Translation: CAA58499.2 .
    X83510 Genomic DNA. Translation: CAA58500.1 .
    AE014297 Genomic DNA. Translation: AAF55275.1 .
    AE014297 Genomic DNA. Translation: AAN13699.3 .
    AY069856 mRNA. Translation: AAL40001.1 .
    PIRi A55888.
    RefSeqi NP_732113.3. NM_169705.1. [Q8INB9-1 ]
    NP_732114.1. NM_169706.1. [Q8INB9-2 ]
    NP_732115.1. NM_169707.1. [Q8INB9-2 ]
    UniGenei Dm.1219.

    3D structure databases

    ProteinModelPortali Q8INB9.
    SMRi Q8INB9. Positions 107-591.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67008. 51 interactions.
    DIPi DIP-49060N.
    IntActi Q8INB9. 40 interactions.
    MINTi MINT-291950.

    Proteomic databases

    PaxDbi Q8INB9.
    PRIDEi Q8INB9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0083228 ; FBpp0082682 ; FBgn0010379 . [Q8INB9-1 ]
    GeneIDi 41957.
    KEGGi dme:Dmel_CG4006.

    Organism-specific databases

    CTDi 207.
    FlyBasei FBgn0010379. Akt1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000114960.
    InParanoidi Q8INB9.
    KOi K04456.
    OMAi CNSSGVK.
    OrthoDBi EOG7Q5HCW.
    PhylomeDBi Q8INB9.

    Enzyme and pathway databases

    Reactomei REACT_180302. KSRP destabilizes mRNA.
    REACT_180799. Downregulation of ERBB2:ERBB3 signaling.
    REACT_180852. Translocation of GLUT4 to the plasma membrane.
    REACT_184384. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_207784. Inhibition of TSC complex formation by PKB.
    REACT_208852. Activation of PKB.
    REACT_219214. GPVI-mediated activation cascade.
    SignaLinki Q8INB9.

    Miscellaneous databases

    GenomeRNAii 41957.
    NextBioi 826461.
    PROi Q8INB9.

    Gene expression databases

    Bgeei Q8INB9.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Franke T.F., Tartof K.D., Tsichlis P.N.
      Oncogene 9:141-148(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    2. "Developmental regulation of expression and activity of multiple forms of the Drosophila RAC protein kinase."
      Andjelkovic M., Jones P.F., Grossniklaus U., Cron P., Schier A.F., Dick M., Bilbe G., Hemmings B.A.
      J. Biol. Chem. 270:4066-4075(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE INITIATION (ISOFORMS A AND C), ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    3. "The genome sequence of Drosophila melanogaster."
      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.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION, ALTERNATIVE INITIATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Strain: Berkeley.
      Tissue: Embryo.
    6. Cited for: FUNCTION, MUTAGENESIS OF PHE-408, DISRUPTION PHENOTYPE.
    7. "Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/PKB."
      Verdu J., Buratovich M.A., Wilder E.L., Birnbaum M.J.
      Nat. Cell Biol. 1:500-506(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-295.
    8. "The conserved PI3'K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila."
      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.
      Oncogene 19:3971-3977(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-586.
    9. "Regulation of Drosophila tracheal system development by protein kinase B."
      Jin J., Anthopoulos N., Wetsch B., Binari R.C., Isaac D.D., Andrew D.J., Woodgett J.R., Manoukian A.S.
      Dev. Cell 1:817-827(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Drosophila phosphoinositide-dependent kinase-1 regulates apoptosis and growth via the phosphoinositide 3-kinase-dependent signaling pathway."
      Cho K.S., Lee J.H., Kim S., Kim D., Koh H., Lee J., Kim C., Kim J., Chung J.
      Proc. Natl. Acad. Sci. U.S.A. 98:6144-6149(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    11. Cited for: FUNCTION.
    12. "Akt regulates growth by directly phosphorylating Tsc2."
      Potter C.J., Pedraza L.G., Xu T.
      Nat. Cell Biol. 4:658-665(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Living with lethal PIP3 levels: viability of flies lacking PTEN restored by a PH domain mutation in Akt/PKB."
      Stocker H., Andjelkovic M., Oldham S., Laffargue M., Wymann M.P., Hemmings B.A., Hafen E.
      Science 295:2088-2091(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-180 AND PHE-408.
    14. "Coordinated functions of Akt/PKB and ETS1 in tubule formation."
      Lavenburg K.R., Ivey J., Hsu T., Muise-Helmericks R.C.
      FASEB J. 17:2278-2280(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Control of cell number by Drosophila FOXO: downstream and feedback regulation of the insulin receptor pathway."
      Puig O., Marr M.T., Ruhf M.L., Tjian R.
      Genes Dev. 17:2006-2020(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Tsc2 is not a critical target of Akt during normal Drosophila development."
      Dong J., Pan D.
      Genes Dev. 18:2479-2484(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "dAkt kinase controls follicle cell size during Drosophila oogenesis."
      Cavaliere V., Donati A., Hsouna A., Hsu T., Gargiulo G.
      Dev. Dyn. 232:845-854(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    18. "PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth."
      Gao T., Furnari F., Newton A.C.
      Mol. Cell 18:13-24(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEPHOSPHORYLATION AT SER-586.
    19. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-586.
    20. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiAKT1_DROME
    AccessioniPrimary (citable) accession number: Q8INB9
    Secondary accession number(s): Q0KI65
    , Q24293, Q24469, Q24470, Q7JN11, Q8T9A5, Q9VEY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 115 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3