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Q8INB9 (AKT1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RAC serine/threonine-protein kinase

Short name=DAkt
Short name=DRAC-PK
Short name=Dakt1
EC=2.7.11.1
Alternative name(s):
Akt
Protein kinase B
Short name=PKB
Gene names
Name:Akt1
ORF Names:CG4006
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.2

Subcellular location

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

Tissue specificity

Ubiquitously expressed. Present in ovary, where it is concentrated at the basal side of follicle cells. Ref.2

Developmental stage

Expressed both maternally and zygotically. Strongly expressed in embryo and pupa. Weakly expressed in larva. Mildly expressed in adult. Ref.2 Ref.17

Domain

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

Post-translational modification

Phosphorylated and activated by Pk61C/PDK1. Phosphorylated on Ser-586 by the rictor-Tor complex. Ref.8 Ref.10 Ref.18 Ref.19

Disruption phenotype

Death at the first instar larval stage. Ref.6

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 PH domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Growth regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative initiation
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

chitin-based embryonic cuticle biosynthetic process

Inferred from genetic interaction Ref.9. Source: FlyBase

circadian rhythm

Inferred from mutant phenotype PubMed 17895391. Source: FlyBase

dendrite regeneration

Inferred from mutant phenotype PubMed 22759636. Source: FlyBase

epithelial cell migration, open tracheal system

Inferred from mutant phenotype Ref.14. Source: UniProtKB

insulin receptor signaling pathway

Inferred from direct assay Ref.7. Source: UniProtKB

intracellular signal transduction

Inferred from genetic interaction Ref.8. Source: UniProtKB

lipid storage

Inferred from genetic interaction PubMed 17079271. Source: FlyBase

long term synaptic depression

Inferred from mutant phenotype PubMed 16611817. Source: FlyBase

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.6. Source: FlyBase

negative regulation of synaptic growth at neuromuscular junction

Inferred from mutant phenotype PubMed 23393158. Source: FlyBase

open tracheal system development

Inferred from mutant phenotype Ref.9. Source: FlyBase

positive regulation of axon regeneration

Inferred from mutant phenotype PubMed 22759636. Source: FlyBase

positive regulation of cell growth

Inferred from mutant phenotype Ref.7Ref.8Ref.12Ref.17. Source: UniProtKB

positive regulation of cell size

Inferred from mutant phenotype Ref.7Ref.8. Source: FlyBase

positive regulation of multicellular organism growth

Traceable author statement PubMed 10679387PubMed 11128988PubMed 12559758. Source: FlyBase

positive regulation of organ growth

Inferred from mutant phenotype Ref.7. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of cell shape

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

regulation of cell size

Non-traceable author statement PubMed 11897402. Source: FlyBase

regulation of dendrite development

Inferred from mutant phenotype PubMed 19778508. Source: FlyBase

regulation of hemocyte proliferation

Inferred from mutant phenotype PubMed 20688956. Source: FlyBase

regulation of multicellular organism growth

Inferred from mutant phenotype Ref.8. Source: FlyBase

regulation of organ growth

Non-traceable author statement PubMed 10679387PubMed 11897402. Source: FlyBase

regulation of protein import into nucleus

Traceable author statement PubMed 14570584. Source: FlyBase

response to oxidative stress

Inferred from mutant phenotype PubMed 17895391. Source: FlyBase

   Cellular_componentcell surface

Inferred from direct assay PubMed 17079271. Source: FlyBase

cytoplasm

Inferred from direct assay PubMed 17079271. Source: FlyBase

cytosol

Traceable author statement. Source: Reactome

neuronal cell body

Inferred from direct assay PubMed 24068890. Source: FlyBase

plasma membrane

Non-traceable author statement PubMed 12559758. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol binding

Non-traceable author statement PubMed 12559758. Source: FlyBase

protein kinase activity

Inferred from direct assay Ref.2. Source: FlyBase

protein serine/threonine kinase activity

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform C (identifier: Q8INB9-1)

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.
Isoform A (identifier: Q8INB9-2)

Also known as: PK66;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 611611RAC serine/threonine-protein kinase
PRO_0000045784

Regions

Domain106 – 211106PH
Domain266 – 523258Protein kinase
Domain524 – 59774AGC-kinase C-terminal
Nucleotide binding272 – 2809ATP By similarity

Sites

Active site3891Proton acceptor By similarity
Binding site2951ATP Probable

Amino acid modifications

Modified residue301Phosphoserine Ref.20
Modified residue5861Phosphoserine Ref.8 Ref.18 Ref.19

Natural variations

Alternative sequence1 – 8181Missing in isoform A.
VSP_018833

Experimental info

Mutagenesis1801G → S: Fails to be recruited at the membrane upon activation. Ref.13
Mutagenesis2601K → A: Abolishes enzymatic activity.
Mutagenesis2951K → M: Abolishes enzymatic activity. Ref.7
Mutagenesis4081F → I: Abolishes enzymatic activity. Ref.6 Ref.13
Sequence conflict731A → T in CAA58499. Ref.2
Sequence conflict200 – 2012QQ → HE in CAA81204. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform C (PK85) [UniParc].

Last modified December 7, 2004. Version 3.
Checksum: C139380152580934

FASTA61168,485
        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 

« Hide

Isoform A (PK66) [UniParc].

Checksum: F7508582C7F4A288
Show »

FASTA53059,911

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE INITIATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Embryo.
[6]"Genetic analysis of protein kinase B (AKT) in Drosophila."
Staveley B.E., Ruel L., Jin J., Stambolic V., Mastronardi F.G., Heitzler P., Woodgett J.R., Manoukian A.S.
Curr. Biol. 8:599-602(1998) [PubMed] [Europe PMC] [Abstract]
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]"PDK1 regulates growth through Akt and S6K in Drosophila."
Rintelen F., Stocker H., Thomas G., Hafen E.
Proc. Natl. Acad. Sci. U.S.A. 98:15020-15025(2001) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA55888.
RefSeqNP_732113.3. NM_169705.1.
NP_732114.1. NM_169706.1.
NP_732115.1. NM_169707.1.
UniGeneDm.1219.

3D structure databases

ProteinModelPortalQ8INB9.
SMRQ8INB9. Positions 107-591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67008. 51 interactions.
IntActQ8INB9. 39 interactions.
MINTMINT-291950.

Proteomic databases

PaxDbQ8INB9.
PRIDEQ8INB9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0083228; FBpp0082682; FBgn0010379. [Q8INB9-1]
GeneID41957.
KEGGdme:Dmel_CG4006.

Organism-specific databases

CTD207.
FlyBaseFBgn0010379. Akt1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000114960.
InParanoidQ8INB9.
KOK04456.
OMAYRSKPAD.
OrthoDBEOG7Q5HCW.
PhylomeDBQ8INB9.

Enzyme and pathway databases

ReactomeREACT_6313. Insulin receptor mediated signaling.
SignaLinkQ8INB9.

Gene expression databases

BgeeQ8INB9.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR001849. Pleckstrin_homology.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

GenomeRNAi41957.
NextBio826461.
PROQ8INB9.

Entry information

Entry nameAKT1_DROME
AccessionPrimary (citable) accession number: Q8INB9
Secondary accession number(s): Q0KI65 expand/collapse secondary AC list , Q24293, Q24469, Q24470, Q7JN11, Q8T9A5, Q9VEY7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase