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RAC serine/threonine-protein kinase (DAkt) (DRAC-PK) (Dakt1) (EC 2.7.11.1) (Akt) (Protein kinase B) (PKB)

 AKT1_DROME              Reviewed;         611 AA.
Q8INB9; Q0KI65; Q24293; Q24469; Q24470; Q7JN11; Q8T9A5; Q9VEY7;
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 3.
12-SEP-2018, entry version 157.
RecName: Full=RAC serine/threonine-protein kinase;
Short=DAkt;
Short=DRAC-PK;
Short=Dakt1;
EC=2.7.11.1;
AltName: Full=Akt;
AltName: Full=Protein kinase B;
Short=PKB;
Name=Akt1 {ECO:0000312|FlyBase:FBgn0010379};
ORFNames=CG4006 {ECO:0000312|FlyBase:FBgn0010379};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=8302573;
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.
PubMed=7876156; DOI=10.1074/jbc.270.8.4066;
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;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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; DOI=10.1186/gb-2002-3-12-research0080;
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, MUTAGENESIS OF PHE-408, AND DISRUPTION PHENOTYPE.
PubMed=9601646; DOI=10.1016/S0960-9822(98)70231-3;
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.
PubMed=10587646; DOI=10.1038/70293;
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.
PubMed=10962553; DOI=10.1038/sj.onc.1203739;
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.
PubMed=11740943; DOI=10.1016/S1534-5807(01)00090-9;
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.
PubMed=11344272; DOI=10.1073/pnas.101596998;
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.
PubMed=11752451; DOI=10.1073/pnas.011318098;
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.
PubMed=12172554; DOI=10.1038/ncb840;
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.
PubMed=11872800; DOI=10.1126/science.1068094;
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.
PubMed=14525946; DOI=10.1096/fj.03-0040fje;
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.
PubMed=12893776; DOI=10.1101/gad.1098703;
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.
PubMed=15466161; DOI=10.1101/gad.1240504;
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.
PubMed=15712201; DOI=10.1002/dvdy.20333;
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.
PubMed=15808505; DOI=10.1016/j.molcel.2005.03.008;
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.
PubMed=15718470; DOI=10.1126/science.1106148;
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 IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
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).
[21]
PHOSPHORYLATION.
PubMed=22493059; DOI=10.1128/MCB.06474-11;
Wang T., Blumhagen R., Lao U., Kuo Y., Edgar B.A.;
"LST8 regulates cell growth via target-of-rapamycin complex 2
(TORC2).";
Mol. Cell. Biol. 32:2203-2213(2012).
[22]
DISRUPTION PHENOTYPE.
PubMed=24786828; DOI=10.1038/cdd.2014.63;
Wei Y., Lilly M.A.;
"The TORC1 inhibitors Nprl2 and Nprl3 mediate an adaptive response to
amino-acid starvation in Drosophila.";
Cell Death Differ. 21:1460-1468(2014).
[23]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24603715; DOI=10.1371/journal.pgen.1004172;
Liu Y., Wang W., Shui G., Huang X.;
"CDP-diacylglycerol synthetase coordinates cell growth and fat storage
through phosphatidylinositol metabolism and the insulin pathway.";
PLoS Genet. 10:E1004172-E1004172(2014).
[24]
FUNCTION, AND PHOSPHORYLATION AT SER-586.
PubMed=25329475; DOI=10.1371/journal.pone.0109530;
Das R., Sebo Z., Pence L., Dobens L.L.;
"Drosophila tribbles antagonizes insulin signaling-mediated growth and
metabolism via interactions with Akt kinase.";
PLoS ONE 9:E109530-E109530(2014).
[25]
FUNCTION, AND INTERACTION WITH TRBL.
PubMed=29025897; DOI=10.1242/dmm.030619;
Fischer Z., Das R., Shipman A., Fan J.Y., Pence L., Bouyain S.,
Dobens L.L.;
"A Drosophila model of insulin resistance associated with the human
Trib3 Q/R polymorphism.";
Dis. Model. Mech. 10:1453-1464(2017).
-!- FUNCTION: Serine/threonine kinase involved in various
developmental processes (PubMed:9601646, PubMed:10587646,
PubMed:10962553, PubMed:11740943, PubMed:12172554,
PubMed:11872800, PubMed:14525946, PubMed:12893776,
PubMed:15466161, PubMed:15712201). During early embryogenesis,
acts as a survival protein (PubMed:9601646, PubMed:10962553).
During mid-embryogenesis, phosphorylates and activates trh, a
transcription factor required for tracheal cell fate determination
(PubMed:11740943). Also regulates tracheal cell migration
(PubMed:11740943, PubMed:14525946). 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
(PubMed:10587646, PubMed:10962553, PubMed:11752451,
PubMed:12893776, PubMed:25329475, PubMed:29025897,
PubMed:24603715). Controls follicle cell size during oogenesis
(PubMed:15712201). May also stimulate cell growth by
phosphorylating Gig/Tsc2 and inactivating the Tsc complex
(PubMed:12172554, PubMed:15466161). Dephosphorylation of 'Ser-586'
by Phlpp triggers apoptosis and suppression of tumor growth
(PubMed:10962553). {ECO:0000269|PubMed:10587646,
ECO:0000269|PubMed:10962553, ECO:0000269|PubMed:11740943,
ECO:0000269|PubMed:11752451, ECO:0000269|PubMed:11872800,
ECO:0000269|PubMed:12172554, ECO:0000269|PubMed:12893776,
ECO:0000269|PubMed:14525946, ECO:0000269|PubMed:15466161,
ECO:0000269|PubMed:15712201, ECO:0000269|PubMed:24603715,
ECO:0000269|PubMed:25329475, ECO:0000269|PubMed:29025897,
ECO:0000269|PubMed:9601646}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:7876156}.
-!- SUBUNIT: Interacts with trbl. {ECO:0000269|PubMed:29025897}.
-!- INTERACTION:
Q9VDE3:slmb; NbExp=4; IntAct=EBI-162210, EBI-91763;
P68198:Ubi-p63E; NbExp=2; IntAct=EBI-162210, EBI-86340;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane.
Note=Recruited to plasma membrane upon activation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=C; Synonyms=PK85;
IsoId=Q8INB9-1; Sequence=Displayed;
Name=A; Synonyms=PK66;
IsoId=Q8INB9-2; Sequence=VSP_018833;
Note=Major form.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Present in ovary,
where it is concentrated at the basal side of follicle cells.
{ECO:0000269|PubMed:7876156}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Strongly expressed in embryo and pupa. Weakly expressed in larva.
Mildly expressed in adult. {ECO:0000269|PubMed:15712201,
ECO:0000269|PubMed:7876156}.
-!- DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-
kinase alpha (PI(3)K) results in its targeting to the plasma
membrane. {ECO:0000305}.
-!- PTM: Phosphorylated and activated by Pk61C/PDK1 (PubMed:11344272).
Phosphorylated on Ser-586 by the TORC2 complex (PubMed:10962553,
PubMed:15718470, PubMed:22493059). {ECO:0000269|PubMed:10962553,
ECO:0000269|PubMed:11344272, ECO:0000269|PubMed:15718470,
ECO:0000269|PubMed:22493059}.
-!- DISRUPTION PHENOTYPE: Death at the first instar larval stage
(PubMed:9601646). Conditional RNAi-mediated knockdown in the
female germline reduces ovary size (PubMed:24786828). RNAi-
mediated knockdown in both larval salivary glands and fat body,
results in small salivary glands displaying ectopic lipid storage
and reduced expression of CdsA (PubMed:24603715).
{ECO:0000269|PubMed:24603715, ECO:0000269|PubMed:24786828,
ECO:0000269|PubMed:9601646}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. RAC subfamily. {ECO:0000305}.
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EMBL; Z26242; CAA81204.1; -; mRNA.
EMBL; X83510; CAA58499.2; -; Genomic_DNA.
EMBL; X83510; CAA58500.1; -; Genomic_DNA.
EMBL; AE014297; AAF55275.1; -; Genomic_DNA.
EMBL; AE014297; AAN13699.3; -; Genomic_DNA.
EMBL; AY069856; AAL40001.1; -; mRNA.
PIR; A55888; A55888.
RefSeq; NP_001287353.1; NM_001300424.1. [Q8INB9-2]
RefSeq; NP_001287354.1; NM_001300425.1. [Q8INB9-2]
RefSeq; NP_732113.3; NM_169705.2. [Q8INB9-1]
RefSeq; NP_732114.1; NM_169706.2. [Q8INB9-2]
RefSeq; NP_732115.1; NM_169707.2. [Q8INB9-2]
UniGene; Dm.1219; -.
ProteinModelPortal; Q8INB9; -.
SMR; Q8INB9; -.
BioGrid; 67008; 197.
DIP; DIP-49060N; -.
IntAct; Q8INB9; 43.
MINT; Q8INB9; -.
STRING; 7227.FBpp0082682; -.
iPTMnet; Q8INB9; -.
PaxDb; Q8INB9; -.
PRIDE; Q8INB9; -.
EnsemblMetazoa; FBtr0083226; FBpp0082680; FBgn0010379. [Q8INB9-2]
EnsemblMetazoa; FBtr0083227; FBpp0082681; FBgn0010379. [Q8INB9-2]
EnsemblMetazoa; FBtr0083228; FBpp0082682; FBgn0010379. [Q8INB9-1]
EnsemblMetazoa; FBtr0344470; FBpp0310841; FBgn0010379. [Q8INB9-2]
EnsemblMetazoa; FBtr0344717; FBpp0311050; FBgn0010379. [Q8INB9-2]
GeneID; 41957; -.
KEGG; dme:Dmel_CG4006; -.
CTD; 207; -.
FlyBase; FBgn0010379; Akt1.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00920000148938; -.
InParanoid; Q8INB9; -.
KO; K04456; -.
OrthoDB; EOG091G06FF; -.
PhylomeDB; Q8INB9; -.
Reactome; R-DME-110478; Insulin signaling pathway.
Reactome; R-DME-110523; TOR signaling pathway.
Reactome; R-DME-1257604; PIP3 activates AKT signaling.
Reactome; R-DME-1358803; Downregulation of ERBB2:ERBB3 signaling.
Reactome; R-DME-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-DME-165158; Activation of AKT2.
Reactome; R-DME-165159; mTOR signalling.
Reactome; R-DME-165181; Inhibition of TSC complex formation by PKB.
Reactome; R-DME-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-DME-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-DME-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-DME-203615; eNOS activation.
Reactome; R-DME-211163; AKT-mediated inactivation of FOXO1A.
Reactome; R-DME-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-DME-389513; CTLA4 inhibitory signaling.
Reactome; R-DME-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-DME-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-DME-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-DME-6804759; Regulation of TP53 Activity through Association with Co-factors.
Reactome; R-DME-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-DME-8876198; RAB GEFs exchange GTP for GDP on RABs.
Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
Reactome; R-DME-9604323; Negative regulation of NOTCH4 signaling.
SignaLink; Q8INB9; -.
ChiTaRS; Akt1; fly.
GenomeRNAi; 41957; -.
PRO; PR:Q8INB9; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0010379; Expressed in 48 organ(s), highest expression level in embryo.
ExpressionAtlas; Q8INB9; baseline and differential.
Genevisible; Q8INB9; DM.
GO; GO:0005938; C:cell cortex; IDA:FlyBase.
GO; GO:0005829; C:cytosol; IDA:FlyBase.
GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0035091; F:phosphatidylinositol binding; NAS:FlyBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:FlyBase.
GO; GO:0008362; P:chitin-based embryonic cuticle biosynthetic process; IGI:FlyBase.
GO; GO:0042632; P:cholesterol homeostasis; IMP:FlyBase.
GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
GO; GO:0031104; P:dendrite regeneration; IMP:FlyBase.
GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IGI:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; IMP:FlyBase.
GO; GO:0060292; P:long term synaptic depression; IMP:FlyBase.
GO; GO:0035264; P:multicellular organism growth; IMP:FlyBase.
GO; GO:0007520; P:myoblast fusion; IMP:FlyBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
GO; GO:1901215; P:negative regulation of neuron death; IGI:FlyBase.
GO; GO:0090278; P:negative regulation of peptide hormone secretion; IMP:FlyBase.
GO; GO:0045886; P:negative regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:1904262; P:negative regulation of TORC1 signaling; IGI:FlyBase.
GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0048680; P:positive regulation of axon regeneration; IMP:FlyBase.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:FlyBase.
GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
GO; GO:0010884; P:positive regulation of lipid storage; IMP:FlyBase.
GO; GO:0046622; P:positive regulation of organ growth; IMP:UniProtKB.
GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:FlyBase.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0050773; P:regulation of dendrite development; IMP:FlyBase.
GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:FlyBase.
GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
CDD; cd01241; PH_PKB; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR039026; PH_PKB.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR039029; RAC_gamma-like.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24356:SF190; PTHR24356:SF190; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
SMART; SM00233; PH; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative initiation; Apoptosis; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Developmental protein;
Growth regulation; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 611 RAC serine/threonine-protein kinase.
/FTId=PRO_0000045784.
DOMAIN 106 211 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 266 523 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 524 597 AGC-kinase C-terminal.
NP_BIND 272 280 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 389 389 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 295 295 ATP. {ECO:0000305}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 586 586 Phosphoserine.
{ECO:0000269|PubMed:10962553,
ECO:0000269|PubMed:15718470,
ECO:0000269|PubMed:25329475}.
VAR_SEQ 1 81 Missing (in isoform A).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:8302573}.
/FTId=VSP_018833.
MUTAGEN 180 180 G->S: Fails to be recruited at the
membrane upon activation.
{ECO:0000269|PubMed:11872800}.
MUTAGEN 260 260 K->A: Abolishes enzymatic activity.
MUTAGEN 295 295 K->M: Abolishes enzymatic activity.
{ECO:0000269|PubMed:10587646}.
MUTAGEN 408 408 F->I: Abolishes enzymatic activity.
{ECO:0000269|PubMed:11872800,
ECO:0000269|PubMed:9601646}.
CONFLICT 73 73 A -> T (in Ref. 2; CAA58499).
{ECO:0000305}.
CONFLICT 200 201 QQ -> HE (in Ref. 1; CAA81204).
{ECO:0000305}.
SEQUENCE 611 AA; 68485 MW; C139380152580934 CRC64;
MNYLPFVLQR RSTVVASAPA PGSASRIPES PTTTGSNIIN IIYSQSTHPN SSPTSGSAEK
FSWQQSWPSR TSAAPTHDSG TMSINTTFDL SSPSVTSGHA LTEQTQVVKE GWLMKRGEHI
KNWRQRYFVL HSDGRLMGYR SKPADSASTP SDFLLNNFTV RGCQIMTVDR PKPFTFIIRG
LQWTTVIERT FAVESELERQ QWTEAIRNVS SRLIDVGEVA MTPSEQTDMT DVDMATIAED
ELSEQFSVQG TTCNSSGVKK VTLENFEFLK VLGKGTFGKV ILCREKATAK LYAIKILKKE
VIIQKDEVAH TLTESRVLKS TNHPFLISLK YSFQTNDRLC FVMQYVNGGE LFWHLSHERI
FTEDRTRFYG AEIISALGYL HSQGIIYRDL KLENLLLDKD GHIKVADFGL CKEDITYGRT
TKTFCGTPEY LAPEVLDDND YGQAVDWWGT GVVMYEMICG RLPFYNRDHD VLFTLILVEE
VKFPRNITDE AKNLLAGLLA KDPKKRLGGG KDDVKEIQAH PFFASINWTD LVLKKIPPPF
KPQVTSDTDT RYFDKEFTGE SVELTPPDPT GPLGSIAEEP LFPQFSYQGD MASTLGTSSH
ISTSTSLASM Q


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