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Protein

RAC serine/threonine-protein kinase

Gene

Akt1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei295ATPCurated1
Active sitei389Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi272 – 280ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • phosphatidylinositol binding Source: FlyBase
  • protein kinase activity Source: FlyBase
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • chitin-based embryonic cuticle biosynthetic process Source: FlyBase
  • circadian rhythm Source: FlyBase
  • dendrite regeneration Source: FlyBase
  • epithelial cell migration, open tracheal system Source: UniProtKB
  • insulin receptor signaling pathway Source: UniProtKB
  • intracellular signal transduction Source: UniProtKB
  • lipid metabolic process Source: FlyBase
  • lipid storage Source: FlyBase
  • long term synaptic depression Source: FlyBase
  • multicellular organism growth Source: FlyBase
  • myoblast fusion Source: FlyBase
  • negative regulation of apoptotic process Source: FlyBase
  • negative regulation of neuron death Source: FlyBase
  • negative regulation of peptide hormone secretion Source: FlyBase
  • negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • oogenesis Source: FlyBase
  • open tracheal system development Source: FlyBase
  • peptidyl-serine phosphorylation Source: GO_Central
  • positive regulation of axon regeneration Source: FlyBase
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of cell size Source: FlyBase
  • positive regulation of multicellular organism growth Source: FlyBase
  • positive regulation of organ growth Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of cell shape Source: FlyBase
  • regulation of cell size Source: FlyBase
  • regulation of dendrite development Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • regulation of hemocyte proliferation Source: FlyBase
  • regulation of multicellular organism growth Source: FlyBase
  • regulation of organ growth Source: FlyBase
  • regulation of protein import into nucleus Source: FlyBase
  • response to oxidative stress Source: FlyBase
  • somatic muscle development 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

ReactomeiR-DME-114604. GPVI-mediated activation cascade.
R-DME-1257604. PIP3 activates AKT signaling.
R-DME-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-DME-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-DME-165158. Activation of AKT2.
R-DME-165159. mTOR signalling.
R-DME-165181. Inhibition of TSC complex formation by PKB.
R-DME-198323. AKT phosphorylates targets in the cytosol.
R-DME-198693. AKT phosphorylates targets in the nucleus.
R-DME-199418. Negative regulation of the PI3K/AKT network.
R-DME-203615. eNOS activation.
R-DME-211163. AKT-mediated inactivation of FOXO1A.
R-DME-354192. Integrin alphaIIb beta3 signaling.
R-DME-389357. CD28 dependent PI3K/Akt signaling.
R-DME-392451. G beta:gamma signalling through PI3Kgamma.
R-DME-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-DME-450604. KSRP (KHSRP) binds and destabilizes mRNA.
R-DME-5218920. VEGFR2 mediated vascular permeability.
R-DME-5628897. TP53 Regulates Metabolic Genes.
R-DME-6804758. Regulation of TP53 Activity through Acetylation.
R-DME-6804759. Regulation of TP53 Activity through Association with Co-factors.
R-DME-8876198. RAB GEFs exchange GTP for GDP on RABs.
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:Akt1Imported
ORF Names:CG4006Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0010379. Akt1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: FlyBase
  • cytoplasm Source: FlyBase
  • cytosol Source: UniProtKB-SubCell
  • neuronal cell body Source: FlyBase
  • 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 (PubMed:9601646). Conditional RNAi-mediated knockdown in the female germline reduces ovary size (PubMed:24786828).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi180G → S: Fails to be recruited at the membrane upon activation. 1 Publication1
Mutagenesisi260K → A: Abolishes enzymatic activity. 1
Mutagenesisi295K → M: Abolishes enzymatic activity. 1 Publication1
Mutagenesisi408F → I: Abolishes enzymatic activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000457841 – 611RAC serine/threonine-protein kinaseAdd BLAST611

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei30Phosphoserine1 Publication1
Modified residuei586Phosphoserine2 Publications1

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.

PTM databases

iPTMnetiQ8INB9.

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

BgeeiFBgn0010379.
GenevisibleiQ8INB9. DM.

Interactioni

Protein-protein interaction databases

BioGridi67008. 51 interactors.
DIPiDIP-49060N.
IntActiQ8INB9. 41 interactors.
MINTiMINT-291950.
STRINGi7227.FBpp0082682.

Structurei

3D structure databases

ProteinModelPortaliQ8INB9.
SMRiQ8INB9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini106 – 211PHPROSITE-ProRule annotationAdd BLAST106
Domaini266 – 523Protein kinasePROSITE-ProRule annotationAdd BLAST258
Domaini524 – 597AGC-kinase C-terminalAdd BLAST74

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

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
InParanoidiQ8INB9.
KOiK04456.
OrthoDBiEOG091G06FF.
PhylomeDBiQ8INB9.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. 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. AlignAdd to basket

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

        10         20         30         40         50
MNYLPFVLQR RSTVVASAPA PGSASRIPES PTTTGSNIIN IIYSQSTHPN
60 70 80 90 100
SSPTSGSAEK FSWQQSWPSR TSAAPTHDSG TMSINTTFDL SSPSVTSGHA
110 120 130 140 150
LTEQTQVVKE GWLMKRGEHI KNWRQRYFVL HSDGRLMGYR SKPADSASTP
160 170 180 190 200
SDFLLNNFTV RGCQIMTVDR PKPFTFIIRG LQWTTVIERT FAVESELERQ
210 220 230 240 250
QWTEAIRNVS SRLIDVGEVA MTPSEQTDMT DVDMATIAED ELSEQFSVQG
260 270 280 290 300
TTCNSSGVKK VTLENFEFLK VLGKGTFGKV ILCREKATAK LYAIKILKKE
310 320 330 340 350
VIIQKDEVAH TLTESRVLKS TNHPFLISLK YSFQTNDRLC FVMQYVNGGE
360 370 380 390 400
LFWHLSHERI FTEDRTRFYG AEIISALGYL HSQGIIYRDL KLENLLLDKD
410 420 430 440 450
GHIKVADFGL CKEDITYGRT TKTFCGTPEY LAPEVLDDND YGQAVDWWGT
460 470 480 490 500
GVVMYEMICG RLPFYNRDHD VLFTLILVEE VKFPRNITDE AKNLLAGLLA
510 520 530 540 550
KDPKKRLGGG KDDVKEIQAH PFFASINWTD LVLKKIPPPF KPQVTSDTDT
560 570 580 590 600
RYFDKEFTGE SVELTPPDPT GPLGSIAEEP LFPQFSYQGD MASTLGTSSH
610
ISTSTSLASM Q
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)DescriptionActionsGraphical viewLength
Sequence conflicti73A → T in CAA58499 (PubMed:7876156).Curated1
Sequence conflicti200 – 201QQ → HE in CAA81204 (PubMed:8302573).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0188331 – 81Missing in isoform A. 2 PublicationsAdd BLAST81

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001287353.1. NM_001300424.1. [Q8INB9-2]
NP_001287354.1. NM_001300425.1. [Q8INB9-2]
NP_732113.3. NM_169705.2. [Q8INB9-1]
NP_732114.1. NM_169706.2. [Q8INB9-2]
NP_732115.1. NM_169707.2. [Q8INB9-2]
UniGeneiDm.1219.

Genome annotation databases

GeneIDi41957.
KEGGidme:Dmel_CG4006.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001287353.1. NM_001300424.1. [Q8INB9-2]
NP_001287354.1. NM_001300425.1. [Q8INB9-2]
NP_732113.3. NM_169705.2. [Q8INB9-1]
NP_732114.1. NM_169706.2. [Q8INB9-2]
NP_732115.1. NM_169707.2. [Q8INB9-2]
UniGeneiDm.1219.

3D structure databases

ProteinModelPortaliQ8INB9.
SMRiQ8INB9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67008. 51 interactors.
DIPiDIP-49060N.
IntActiQ8INB9. 41 interactors.
MINTiMINT-291950.
STRINGi7227.FBpp0082682.

PTM databases

iPTMnetiQ8INB9.

Proteomic databases

PaxDbiQ8INB9.
PRIDEiQ8INB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi41957.
KEGGidme:Dmel_CG4006.

Organism-specific databases

CTDi207.
FlyBaseiFBgn0010379. Akt1.

Phylogenomic databases

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
InParanoidiQ8INB9.
KOiK04456.
OrthoDBiEOG091G06FF.
PhylomeDBiQ8INB9.

Enzyme and pathway databases

ReactomeiR-DME-114604. GPVI-mediated activation cascade.
R-DME-1257604. PIP3 activates AKT signaling.
R-DME-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-DME-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-DME-165158. Activation of AKT2.
R-DME-165159. mTOR signalling.
R-DME-165181. Inhibition of TSC complex formation by PKB.
R-DME-198323. AKT phosphorylates targets in the cytosol.
R-DME-198693. AKT phosphorylates targets in the nucleus.
R-DME-199418. Negative regulation of the PI3K/AKT network.
R-DME-203615. eNOS activation.
R-DME-211163. AKT-mediated inactivation of FOXO1A.
R-DME-354192. Integrin alphaIIb beta3 signaling.
R-DME-389357. CD28 dependent PI3K/Akt signaling.
R-DME-392451. G beta:gamma signalling through PI3Kgamma.
R-DME-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-DME-450604. KSRP (KHSRP) binds and destabilizes mRNA.
R-DME-5218920. VEGFR2 mediated vascular permeability.
R-DME-5628897. TP53 Regulates Metabolic Genes.
R-DME-6804758. Regulation of TP53 Activity through Acetylation.
R-DME-6804759. Regulation of TP53 Activity through Association with Co-factors.
R-DME-8876198. RAB GEFs exchange GTP for GDP on RABs.
SignaLinkiQ8INB9.

Miscellaneous databases

ChiTaRSiAkt1. fly.
GenomeRNAii41957.
PROiQ8INB9.

Gene expression databases

BgeeiFBgn0010379.
GenevisibleiQ8INB9. DM.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 139 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.