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Q8INB9

- AKT1_DROME

UniProt

Q8INB9 - AKT1_DROME

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Protein

RAC serine/threonine-protein kinase

Gene
Akt1, CG4006
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 2951ATP Inferred
Active sitei389 – 3891Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi272 – 2809ATP By similarity

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
Complete GO annotation...

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
Complete GO annotation...

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 – 301Phosphoserine1 Publication
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini106 – 211106PHAdd
BLAST
Domaini266 – 523258Protein kinaseAdd
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 Inferred.

Sequence similaritiesi

Contains 1 PH domain.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8181Missing in isoform A. VSP_018833Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731A → T in CAA58499. 1 Publication
Sequence conflicti200 – 2012QQ → HE in CAA81204. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 114 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

Similar proteinsi