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RAC-alpha serine/threonine-protein kinase (EC 2.7.11.1) (AKT1 kinase) (Protein kinase B) (PKB) (Protein kinase B alpha) (PKB alpha) (Proto-oncogene c-Akt) (RAC-PK-alpha) (Thymoma viral proto-oncogene)

 AKT1_MOUSE              Reviewed;         480 AA.
P31750; Q62274; Q6GSA6;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
27-SEP-2017, entry version 193.
RecName: Full=RAC-alpha serine/threonine-protein kinase;
EC=2.7.11.1;
AltName: Full=AKT1 kinase;
AltName: Full=Protein kinase B;
Short=PKB;
AltName: Full=Protein kinase B alpha;
Short=PKB alpha;
AltName: Full=Proto-oncogene c-Akt;
AltName: Full=RAC-PK-alpha;
AltName: Full=Thymoma viral proto-oncogene;
Name=Akt1; Synonyms=Akt, Rac;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=AKR/J; TISSUE=Thymus;
PubMed=8437858;
Bellacosa A., Franke T.F., Gonzalez-Portal M.E., Datta K., Taguchi T.,
Gardner J., Cheng J.Q., Testa J.R., Tsichlis P.N.;
"Structure, expression and chromosomal mapping of c-akt: relationship
to v-akt and its implications.";
Oncogene 8:745-754(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION AT
SER-473, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
STRAIN=129/SvJ;
PubMed=12783884; DOI=10.1074/jbc.M302847200;
Yang Z.Z., Tschopp O., Hemmings-Mieszczak M., Feng J., Brodbeck D.,
Perentes E., Hemmings B.A.;
"Protein kinase B alpha/Akt1 regulates placental development and fetal
growth.";
J. Biol. Chem. 278:32124-32131(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Bousquets X., Powell C.T.;
"Complete nucleotide coding sequence for murine rac (related to A and
C kinases) protein kinase.";
Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND MUTAGENESIS OF LYS-179.
PubMed=9415393; DOI=10.1210/mend.11.13.0027;
Cong L.N., Chen H., Li Y., Zhou L., McGibbon M.A., Taylor S.I.,
Quon M.J.;
"Physiological role of Akt in insulin-stimulated translocation of
GLUT4 in transfected rat adipose cells.";
Mol. Endocrinol. 11:1881-1890(1997).
[9]
FUNCTION IN PHOSPHORYLATION OF PDE3B.
PubMed=10454575; DOI=10.1128/MCB.19.9.6286;
Kitamura T., Kitamura Y., Kuroda S., Hino Y., Ando M., Kotani K.,
Konishi H., Matsuzaki H., Kikkawa U., Ogawa W., Kasuga M.;
"Insulin-induced phosphorylation and activation of cyclic nucleotide
phosphodiesterase 3B by the serine-threonine kinase Akt.";
Mol. Cell. Biol. 19:6286-6296(1999).
[10]
PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
PubMed=11090077;
Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C.,
Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T.,
Kienast J., Kanakura Y., Berdel W.E., Serve H.;
"Flt3 mutations from patients with acute myeloid leukemia induce
transformation of 32D cells mediated by the Ras and STAT5 pathways.";
Blood 96:3907-3914(2000).
[11]
SUBCELLULAR LOCATION.
PubMed=10716693; DOI=10.1073/pnas.97.7.3028;
Pekarsky Y., Koval A., Hallas C., Bichi R., Tresini M., Malstrom S.,
Russo G., Tsichlis P., Croce C.M.;
"Tcl1 enhances Akt kinase activity and mediates its nuclear
translocation.";
Proc. Natl. Acad. Sci. U.S.A. 97:3028-3033(2000).
[12]
FUNCTION.
PubMed=11282895; DOI=10.1161/01.RES.88.6.609;
Yamashita K., Kajstura J., Discher D.J., Wasserlauf B.J.,
Bishopric N.H., Anversa P., Webster K.A.;
"Reperfusion-activated Akt kinase prevents apoptosis in transgenic
mouse hearts overexpressing insulin-like growth factor-1.";
Circ. Res. 88:609-614(2001).
[13]
FUNCTION IN PHOSPHORYLATION OF PTPN1.
PubMed=11579209; DOI=10.1210/mend.15.10.0711;
Ravichandran L.V., Chen H., Li Y., Quon M.J.;
"Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to
dephosphorylate the insulin receptor.";
Mol. Endocrinol. 15:1768-1780(2001).
[14]
INTERACTION WITH THEM4.
PubMed=11598301; DOI=10.1126/science.1062030;
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M.,
Hemmings B.A.;
"Carboxyl-terminal modulator protein (CTMP), a negative regulator of
PKB/Akt and v-Akt at the plasma membrane.";
Science 294:374-380(2001).
[15]
FUNCTION IN PHOSPHORYLATION OF TBC1D4.
PubMed=11994271; DOI=10.1074/jbc.C200198200;
Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C.,
Lienhard G.E.;
"A method to identify serine kinase substrates. Akt phosphorylates a
novel adipocyte protein with a Rab GTPase-activating protein (GAP)
domain.";
J. Biol. Chem. 277:22115-22118(2002).
[16]
INTERACTION WITH CCDC88A, AND PHOSPHORYLATION AT THR-308 AND SER-473.
PubMed=15753085; DOI=10.1074/jbc.M500586200;
Anai M., Shojima N., Katagiri H., Ogihara T., Sakoda H., Onishi Y.,
Ono H., Fujishiro M., Fukushima Y., Horike N., Viana A., Kikuchi M.,
Noguchi N., Takahashi S., Takata K., Oka Y., Uchijima Y., Kurihara H.,
Asano T.;
"A novel protein kinase B (PKB)/AKT-binding protein enhances PKB
kinase activity and regulates DNA synthesis.";
J. Biol. Chem. 280:18525-18535(2005).
[17]
INTERACTION WITH GRB10.
PubMed=15722337; DOI=10.1074/jbc.M501477200;
Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.;
"Phosphorylation of grb10 regulates its interaction with 14-3-3.";
J. Biol. Chem. 280:16987-16993(2005).
[18]
INTERACTION WITH WDFY2.
PubMed=16792529; DOI=10.1042/BJ20060511;
Fritzius T., Burkard G., Haas E., Heinrich J., Schweneker M.,
Bosse M., Zimmermann S., Frey A.D., Caelers A., Bachmann A.S.,
Moelling K.;
"A WD-FYVE protein binds to the kinases Akt and PKCzeta/lambda.";
Biochem. J. 399:9-20(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[20]
INTERACTION WITH BTBD10.
PubMed=18160256; DOI=10.1016/j.cellsig.2007.11.004;
Nawa M., Kanekura K., Hashimoto Y., Aiso S., Matsuoka M.;
"A novel Akt/PKB-interacting protein promotes cell adhesion and
inhibits familial amyotrophic lateral sclerosis-linked mutant SOD1-
induced neuronal death via inhibition of PP2A-mediated
dephosphorylation of Akt/PKB.";
Cell. Signal. 20:493-505(2008).
[21]
COMPLEX FORMATION WITH WDFY2 AND FOXO1, SUBUNIT, AND SUBCELLULAR
LOCATION.
PubMed=18388859; DOI=10.1038/emboj.2008.67;
Fritzius T., Moelling K.;
"Akt- and Foxo1-interacting WD-repeat-FYVE protein promotes
adipogenesis.";
EMBO J. 27:1399-1410(2008).
[22]
GLYCOSYLATION AT SER-473.
PubMed=18570920; DOI=10.1016/j.yexcr.2008.04.014;
Kang E.S., Han D., Park J., Kwak T.K., Oh M.A., Lee S.A., Choi S.,
Park Z.Y., Kim Y., Lee J.W.;
"O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of
murine pancreatic beta cells.";
Exp. Cell Res. 314:2238-2248(2008).
[23]
FUNCTION, GLYCOSYLATION AT SER-473, AND PHOSPHORYLATION AT THR-308.
PubMed=18288188; DOI=10.1038/nature06668;
Yang X., Ongusaha P.P., Miles P.D., Havstad J.C., Zhang F., So W.V.,
Kudlow J.E., Michell R.H., Olefsky J.M., Field S.J., Evans R.M.;
"Phosphoinositide signalling links O-GlcNAc transferase to insulin
resistance.";
Nature 451:964-969(2008).
[24]
FUNCTION.
PubMed=19778506; DOI=10.1016/j.neuron.2009.08.008;
Kim J.Y., Duan X., Liu C.Y., Jang M.H., Guo J.U., Pow-anpongkul N.,
Kang E., Song H., Ming G.L.;
"DISC1 regulates new neuron development in the adult brain via
modulation of AKT-mTOR signaling through KIAA1212.";
Neuron 63:761-773(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[26]
INTERACTION WITH CLK2.
PubMed=20074525; DOI=10.1016/j.cmet.2009.11.006;
Rodgers J.T., Haas W., Gygi S.P., Puigserver P.;
"Cdc2-like kinase 2 is an insulin-regulated suppressor of hepatic
gluconeogenesis.";
Cell Metab. 11:23-34(2010).
[27]
PHOSPHORYLATION AT THR-450.
PubMed=21045808; DOI=10.1038/emboj.2010.271;
Oh W.J., Wu C.C., Kim S.J., Facchinetti V., Julien L.A., Finlan M.,
Roux P.P., Su B., Jacinto E.;
"mTORC2 can associate with ribosomes to promote cotranslational
phosphorylation and stability of nascent Akt polypeptide.";
EMBO J. 29:3939-3951(2010).
[28]
INTERACTION WITH WDFY2, AND SUBCELLULAR LOCATION.
PubMed=20189988; DOI=10.1074/jbc.M110.110536;
Walz H.A., Shi X., Chouinard M., Bue C.A., Navaroli D.M., Hayakawa A.,
Zhou Q.L., Nadler J., Leonard D.M., Corvera S.;
"Isoform-specific regulation of Akt signaling by the endosomal protein
WDFY2.";
J. Biol. Chem. 285:14101-14108(2010).
[29]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-176; THR-308
AND SER-473, MUTAGENESIS OF TYR-176, AND INTERACTION WITH TNK2.
PubMed=20333297; DOI=10.1371/journal.pone.0009646;
Mahajan K., Coppola D., Challa S., Fang B., Chen Y.A., Zhu W.,
Lopez A.S., Koomen J., Engelman R.W., Rivera C., Muraoka-Cook R.S.,
Cheng J.Q., Schoenbrunn E., Sebti S.M., Earp H.S., Mahajan N.P.;
"Ack1 mediated AKT/PKB tyrosine 176 phosphorylation regulates its
activation.";
PLoS ONE 5:E9646-E9646(2010).
[30]
PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
PubMed=21262971; DOI=10.1074/jbc.M110.205021;
Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K.,
Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D.,
Muller J.P.;
"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase
FLT3 signaling.";
J. Biol. Chem. 286:10918-10929(2011).
[31]
FUNCTION, UBIQUITINATION BY ZNRF1, AND MUTAGENESIS OF THR-308 AND
SER-473.
PubMed=22057101; DOI=10.1038/ncb2373;
Wakatsuki S., Saitoh F., Araki T.;
"ZNRF1 promotes Wallerian degeneration by degrading AKT to induce
GSK3B-dependent CRMP2 phosphorylation.";
Nat. Cell Biol. 13:1415-1423(2011).
[32]
REVIEW ON FUNCTION.
PubMed=11882383; DOI=10.1016/S0898-6568(01)00271-6;
Nicholson K.M., Anderson N.G.;
"The protein kinase B/Akt signalling pathway in human malignancy.";
Cell. Signal. 14:381-395(2002).
[33]
REVIEW ON FUNCTION.
PubMed=21620960; DOI=10.1016/j.cellsig.2011.05.004;
Hers I., Vincent E.E., Tavare J.M.;
"Akt signalling in health and disease.";
Cell. Signal. 23:1515-1527(2011).
[34]
REVIEW ON FUNCTION.
PubMed=21432781; DOI=10.14670/HH-26.651;
Heron-Milhavet L., Khouya N., Fernandez A., Lamb N.J.;
"Akt1 and Akt2: differentiating the aktion.";
Histol. Histopathol. 26:651-662(2011).
[35]
INTERACTION WITH KCTD20.
PubMed=24156551; DOI=10.1186/1471-2091-14-27;
Nawa M., Matsuoka M.;
"KCTD20, a relative of BTBD10, is a positive regulator of Akt.";
BMC Biochem. 14:27-27(2013).
-!- FUNCTION: AKT1 is one of 3 closely related serine/threonine-
protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and
which regulate many processes including metabolism, proliferation,
cell survival, growth and angiogenesis. This is mediated through
serine and/or threonine phosphorylation of a range of downstream
substrates. Over 100 substrate candidates have been reported so
far, but for most of them, no isoform specificity has been
reported. AKT is responsible of the regulation of glucose uptake
by mediating insulin-induced translocation of the SLC2A4/GLUT4
glucose transporter to the cell surface. Phosphorylation of PTPN1
at 'Ser-50' negatively modulates its phosphatase activity
preventing dephosphorylation of the insulin receptor and the
attenuation of insulin signaling. Phosphorylation of TBC1D4
triggers the binding of this effector to inhibitory 14-3-3
proteins, which is required for insulin-stimulated glucose
transport. AKT regulates also the storage of glucose in the form
of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at
'Ser-9', resulting in inhibition of its kinase activity.
Phosphorylation of GSK3 isoforms by AKT is also thought to be one
mechanism by which cell proliferation is driven. AKT regulates
also cell survival via the phosphorylation of MAP3K5 (apoptosis
signal-related kinase). Phosphorylation of 'Ser-83' decreases
MAP3K5 kinase activity stimulated by oxidative stress and thereby
prevents apoptosis. AKT mediates insulin-stimulated protein
synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462',
thereby activating mTORC1 signaling and leading to both
phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is
involved in the phosphorylation of members of the FOXO factors
(Forkhead family of transcription factors), leading to binding of
14-3-3 proteins and cytoplasmic localization. In particular, FOXO1
is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and
FOXO4 are phosphorylated on equivalent sites. AKT has an important
role in the regulation of NF-kappa-B-dependent gene transcription
and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-
response element binding protein). The phosphorylation of CREB1
induces the binding of accessory proteins that are necessary for
the transcription of pro-survival genes such as BCL2 and MCL1. AKT
phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby
potentially regulating ACLY activity and fatty acid synthesis.
Activates the 3B isoform of cyclic nucleotide phosphodiesterase
(PDE3B) via phosphorylation of 'Ser-273', resulting in reduced
cyclic AMP levels and inhibition of lipolysis. Phosphorylates
PIKFYVE on 'Ser-318', which results in increased PI(3)P-5
activity. The Rho GTPase-activating protein DLC1 is another
substrate and its phosphorylation is implicated in the regulation
cell proliferation and cell growth. AKT plays a role as key
modulator of the AKT-mTOR signaling pathway controlling the tempo
of the process of newborn neurons integration during adult
neurogenesis, including correct neuron positioning, dendritic
development and synapse formation. Signals downstream of
phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of
various growth factors such as platelet-derived growth factor
(PDGF), epidermal growth factor (EGF), insulin and insulin-like
growth factor I (IGF-I). AKT mediates the antiapoptotic effects of
IGF-I. Essential for the SPATA13-mediated regulation of cell
migration and adhesion assembly and disassembly. May be involved
in the regulation of the placental development. Phosphorylates
STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its:
kinase activity, nuclear translocation, autophosphorylation and
ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-
117' and 'Thr-384' leading to inhibition of its: cleavage, kinase
activity, autophosphorylation at Thr-180, binding to RASSF1 and
nuclear translocation. Phosphorylates SRPK2 and enhances its
kinase activity towards SRSF2 and ACIN1 and promotes its nuclear
translocation (By similarity). Phosphorylates RAF1 at 'Ser-259'
and negatively regulates its activity (By similarity).
Phosphorylates KAT6A at 'Thr-369' and this phosphorylation
inhibits the interaction of KAT6A with PML and negatively
regulates its acetylation activity towards p53/TP53 (By
similarity). {ECO:0000250}.
-!- FUNCTION: AKT1-specific substrates have been recently identified,
including palladin (PALLD), which phosphorylation modulates
cytoskeletal organization and cell motility; prohibitin (PHB),
playing an important role in cell metabolism and proliferation;
and CDKN1A, for which phosphorylation at 'Thr-145' induces its
release from CDK2 and cytoplasmic relocalization. These recent
findings indicate that the AKT1 isoform has a more specific role
in cell motility and proliferation. Phosphorylates CLK2 thereby
controlling cell survival to ionizing radiation.
{ECO:0000269|PubMed:10454575, ECO:0000269|PubMed:11282895,
ECO:0000269|PubMed:11579209, ECO:0000269|PubMed:11994271,
ECO:0000269|PubMed:12783884, ECO:0000269|PubMed:18288188,
ECO:0000269|PubMed:19778506, ECO:0000269|PubMed:20333297,
ECO:0000269|PubMed:22057101, ECO:0000269|PubMed:9415393}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Three specific sites, one in the kinase domain
(Thr-308) and the two other ones in the C-terminal regulatory
region (Ser-473 and Tyr-474), need to be phosphorylated for its
full activation.
-!- SUBUNIT: Interacts with and phosphorylated by PDPK1 (By
similarity). Interacts with AGAP2 (isoform 2/PIKE-A); the
interaction occurs in the presence of guanine nucleotides.
Interacts with AKTIP. Interacts (via PH domain) with MTCP1, TCL1A
AND TCL1B. Interacts with CDKN1B; the interaction phosphorylates
CDKN1B promoting 14-3-3 binding and cell-cycle progression.
Interacts with MAP3K5 and TRAF6. Interacts with BAD, PPP2R5B, STK3
and STK4. Interacts (via PH domain) with SIRT1. Interacts with
SRPK2 in a phosphorylation-dependent manner. Interacts with
TRIM13; the interaction ubiquitinates AKT1 leading to its
proteasomal degradation. Interacts with RAF1 (By similarity).
Interacts (via the C-terminus) with CCDC88A (via its C-terminus)
and THEM4 (via its C-terminus). Interacts with GRB10; the
interaction leads to GRB10 phosphorylation thus promoting YWHAE-
binding. Interacts with KCTD20 (PubMed:24156551). Interacts with
BTBD10 (PubMed:18160256). Interacts with PA2G4 (By similarity).
Interacts with KIF14; the interaction is detected in the plasma
membrane upon INS stimulation and promotes AKT1 phosphorylation
(By similarity). Interacts with FAM83B; activates the PI3K/AKT
signaling cascade (By similarity). Interacts with WDFY2 (via WD
repeats 1-3) (PubMed:16792529, PubMed:20189988). Forms a complex
with WDFY2 and FOXO1 (PubMed:18388859). Interacts with FAM168A (By
similarity). {ECO:0000250|UniProtKB:P31749,
ECO:0000250|UniProtKB:P47196, ECO:0000269|PubMed:11598301,
ECO:0000269|PubMed:15722337, ECO:0000269|PubMed:15753085,
ECO:0000269|PubMed:16792529, ECO:0000269|PubMed:18160256,
ECO:0000269|PubMed:18388859, ECO:0000269|PubMed:20074525,
ECO:0000269|PubMed:20189988, ECO:0000269|PubMed:20333297,
ECO:0000269|PubMed:24156551}.
-!- INTERACTION:
P32121:ARRB2 (xeno); NbExp=3; IntAct=EBI-298707, EBI-714559;
Q1W6H9:FAM110C (xeno); NbExp=3; IntAct=EBI-298707, EBI-3942563;
P07901:Hsp90aa1; NbExp=6; IntAct=EBI-298707, EBI-78930;
Q8TCU6:PREX1 (xeno); NbExp=2; IntAct=EBI-298707, EBI-1046542;
Q8K4K2:Trib3; NbExp=5; IntAct=EBI-298707, EBI-448962;
P62991:Ubc; NbExp=3; IntAct=EBI-298707, EBI-413074;
P03165:X (xeno); NbExp=2; IntAct=EBI-298707, EBI-7683985;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18388859,
ECO:0000269|PubMed:20189988}. Nucleus
{ECO:0000269|PubMed:18388859, ECO:0000269|PubMed:20189988}. Cell
membrane {ECO:0000250}. Note=Nucleus after activation by integrin-
linked protein kinase 1 (ILK1) (By similarity). Nuclear
translocation is enhanced by interaction with TCL1A.
Phosphorylation on Tyr-176 by TNK2 results in its localization to
the cell membrane where it is targeted for further
phosphorylations on Thr-308 and Ser-473 leading to its activation
and the activated form translocates to the nucleus. Colocalizes
with WDFY2 in intracellular vesicles.
{ECO:0000250|UniProtKB:P31749}.
-!- TISSUE SPECIFICITY: Widely expressed. Low levels found in liver
with slightly higher levels present in thymus and testis.
{ECO:0000269|PubMed:8437858}.
-!- DEVELOPMENTAL STAGE: Expressed in trophoblast and vessel
endothelial cells of the placenta and in the brain at 14.5 dpc (at
protein level). {ECO:0000269|PubMed:12783884}.
-!- DOMAIN: Binding of the PH domain to phosphatidylinositol 3,4,5-
trisphosphate (PI(3,4,5)P3) following phosphatidylinositol 3-
kinase alpha (PIK3CA) activity results in its targeting to the
plasma membrane. The PH domain mediates interaction with TNK2 and
Tyr-176 is also essential for this interaction.
-!- DOMAIN: The AGC-kinase C-terminal mediates interaction with THEM4.
{ECO:0000250}.
-!- PTM: O-GlcNAcylation at Thr-305 and Thr-312 inhibits activating
phosphorylation at Thr-308 via disrupting the interaction between
AKT1 and PDPK1. O-GlcNAcylation at Ser-473 also probably
interferes with phosphorylation at this site (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required
for full activity. Activated TNK2 phosphorylates it on Tyr-176
resulting in its binding to the anionic plasma membrane
phospholipid PA. This phosphorylated form localizes to the plasma
membrane, where it is targeted by PDPK1 and PDPK2 for further
phosphorylations on Thr-308 and Ser-473 leading to its activation.
Ser-473 phosphorylation by mTORC2 favors Thr-308 phosphorylation
by PDPK1. Phosphorylated at Thr-308 and Ser-473 by IKBKE and TBK1.
Ser-473 phosphorylation is enhanced by signaling through activated
FLT3. Dephosphorylated at Thr-308 and Ser-473 by PP2A phosphatase.
The phosphorylated form of PPP2R5B is required for bridging AKT1
with PP2A phosphatase. Ser-473 is dephosphorylated by CPPED1,
leading to termination of signaling (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT1
ubiquitination is critical for phosphorylation and activation.
When ubiquitinated, it translocates to the plasma membrane, where
it becomes phosphorylated. When fully phosphorylated and
translocated into the nucleus, undergoes 'Lys-48'-
polyubiquitination catalyzed by TTC3, leading to its degradation
by the proteasome. Also ubiquitinated by TRIM13 leading to its
proteasomal degradation. Ubiquitinated via 'Lys-48'-linked
polyubiquitination by ZNRF1, leading to its degradation by the
proteasome. Phosphorylated, undergoes 'Lys-48'-linked
polyubiquitination preferentially at Lys-284 catalyzed by MUL1,
leading to its proteasomal degradation.
{ECO:0000269|PubMed:11090077, ECO:0000269|PubMed:12783884,
ECO:0000269|PubMed:15753085, ECO:0000269|PubMed:18288188,
ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:21045808,
ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:22057101}.
-!- PTM: Acetylated on Lys-14 and Lys-20 by the histone
acetyltransferases EP300 and KAT2B. Acetylation results in reduced
phosphorylation and inhibition of activity. Deacetylated at Lys-14
and Lys-20 by SIRT1. SIRT1-mediated deacetylation relieves the
inhibition (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Show fetal growth impairment and reduced
vascularization in the placenta; majority of pups died within 10
days. {ECO:0000269|PubMed:12783884}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. RAC subfamily. {ECO:0000305}.
-!- CAUTION: In light of strong homologies in the primary amino acid
sequence, the 3 AKT kinases were long surmised to play redundant
and overlapping roles. More recent studies has brought into
question the redundancy within AKT kinase isoforms and instead
pointed to isoform specific functions in different cellular events
and diseases. AKT1 is more specifically involved in cellular
survival pathways, by inhibiting apoptotic processes; whereas AKT2
is more specific for the insulin receptor signaling pathway.
Moreover, while AKT1 and AKT2 are often implicated in many aspects
of cellular transformation, the 2 isoforms act in a complementary
opposing manner. The role of AKT3 is less clear, though it appears
to be predominantly expressed in brain. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X65687; CAA46620.1; -; mRNA.
EMBL; AF534134; AAN04036.1; -; Genomic_DNA.
EMBL; M94335; AAA18254.1; -; mRNA.
EMBL; AK154936; BAE32937.1; -; mRNA.
EMBL; CH466549; EDL18586.1; -; Genomic_DNA.
EMBL; BC066018; AAH66018.1; -; mRNA.
CCDS; CCDS26194.1; -.
PIR; S33364; S33364.
RefSeq; NP_001159366.1; NM_001165894.1.
RefSeq; NP_001318036.1; NM_001331107.1.
RefSeq; NP_033782.1; NM_009652.3.
RefSeq; XP_006515478.1; XM_006515415.1.
UniGene; Mm.6645; -.
ProteinModelPortal; P31750; -.
SMR; P31750; -.
BioGrid; 198056; 32.
CORUM; P31750; -.
DIP; DIP-736N; -.
ELM; P31750; -.
IntAct; P31750; 24.
MINT; MINT-4049532; -.
STRING; 10090.ENSMUSP00000001780; -.
BindingDB; P31750; -.
ChEMBL; CHEMBL5859; -.
iPTMnet; P31750; -.
PhosphoSitePlus; P31750; -.
SwissPalm; P31750; -.
EPD; P31750; -.
MaxQB; P31750; -.
PaxDb; P31750; -.
PeptideAtlas; P31750; -.
PRIDE; P31750; -.
Ensembl; ENSMUST00000001780; ENSMUSP00000001780; ENSMUSG00000001729.
GeneID; 11651; -.
KEGG; mmu:11651; -.
UCSC; uc007pex.2; mouse.
CTD; 207; -.
MGI; MGI:87986; Akt1.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00890000139324; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P31750; -.
KO; K04456; -.
OMA; QHRFFAS; -.
OrthoDB; EOG091G06FF; -.
TreeFam; TF102004; -.
BRENDA; 2.7.11.1; 3474.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-1358803; Downregulation of ERBB2:ERBB3 signaling.
Reactome; R-MMU-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-MMU-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-MMU-165159; mTOR signalling.
Reactome; R-MMU-165160; PDE3B signalling.
Reactome; R-MMU-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-MMU-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-MMU-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-MMU-203615; eNOS activation.
Reactome; R-MMU-211163; AKT-mediated inactivation of FOXO1A.
Reactome; R-MMU-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-MMU-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-MMU-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
Reactome; R-MMU-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
ChiTaRS; Akt1; mouse.
PRO; PR:P31750; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000001729; -.
CleanEx; MM_AKT1; -.
ExpressionAtlas; P31750; baseline and differential.
Genevisible; P31750; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0036064; C:ciliary basal body; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005819; C:spindle; IDA:MGI.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0032794; F:GTPase activating protein binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0016301; F:kinase activity; EXP:Reactome.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISO:MGI.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0006924; P:activation-induced cell death of T cells; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
GO; GO:0030030; P:cell projection organization; ISO:MGI.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
GO; GO:0036294; P:cellular response to decreased oxygen levels; IDA:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:MGI.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISO:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:1901653; P:cellular response to peptide; IDA:MGI.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:MGI.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:MGI.
GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0072655; P:establishment of protein localization to mitochondrion; ISO:MGI.
GO; GO:0097194; P:execution phase of apoptosis; IDA:MGI.
GO; GO:0007281; P:germ cell development; IDA:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
GO; GO:0015758; P:glucose transport; IMP:UniProtKB.
GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0060709; P:glycogen cell differentiation involved in embryonic placenta development; IMP:MGI.
GO; GO:0005977; P:glycogen metabolic process; IMP:MGI.
GO; GO:0030212; P:hyaluronan metabolic process; IEA:Ensembl.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0006954; P:inflammatory response; IDA:MGI.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:UniProtKB.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0035655; P:interleukin-18-mediated signaling pathway; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
GO; GO:0072656; P:maintenance of protein location in mitochondrion; ISO:MGI.
GO; GO:0001893; P:maternal placenta development; IMP:MGI.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
GO; GO:0045792; P:negative regulation of cell size; ISO:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:MGI.
GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0046329; P:negative regulation of JNK cascade; IEA:Ensembl.
GO; GO:0010748; P:negative regulation of plasma membrane long-chain fatty acid transport; ISO:MGI.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
GO; GO:0045861; P:negative regulation of proteolysis; ISO:MGI.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
GO; GO:0038061; P:NIK/NF-kappaB signaling; ISO:MGI.
GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:MGI.
GO; GO:0016310; P:phosphorylation; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0031659; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; ISO:MGI.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; ISO:MGI.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:MGI.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:MGI.
GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
GO; GO:0010907; P:positive regulation of glucose metabolic process; ISO:MGI.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:MGI.
GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; ISO:MGI.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISO:MGI.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:MGI.
GO; GO:0046622; P:positive regulation of organ growth; IMP:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0010765; P:positive regulation of sodium ion transport; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0030163; P:protein catabolic process; IDA:MGI.
GO; GO:0000060; P:protein import into nucleus, translocation; ISO:MGI.
GO; GO:0043491; P:protein kinase B signaling; IGI:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
GO; GO:0005979; P:regulation of glycogen biosynthetic process; ISO:MGI.
GO; GO:0031641; P:regulation of myelination; IMP:MGI.
GO; GO:0010975; P:regulation of neuron projection development; IDA:UniProtKB.
GO; GO:0032880; P:regulation of protein localization; IDA:MGI.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0034405; P:response to fluid shear stress; ISO:MGI.
GO; GO:0032094; P:response to food; IDA:MGI.
GO; GO:0060416; P:response to growth hormone; ISS:AgBase.
GO; GO:0009725; P:response to hormone; IDA:UniProtKB.
GO; GO:1990418; P:response to insulin-like growth factor stimulus; ISS:AgBase.
GO; GO:0010033; P:response to organic substance; IDA:MGI.
GO; GO:0006979; P:response to oxidative stress; ISS:ParkinsonsUK-UCL.
GO; GO:0070141; P:response to UV-A; ISO:MGI.
GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
GO; GO:0006412; P:translation; IEA:Ensembl.
CDD; cd05594; STKc_PKB_alpha; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR034676; Akt1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
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; SSF50729; SSF50729; 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;
Acetylation; Apoptosis; ATP-binding; Carbohydrate metabolism;
Cell membrane; Complete proteome; Cytoplasm; Developmental protein;
Disulfide bond; Glucose metabolism; Glycogen biosynthesis;
Glycogen metabolism; Glycoprotein; Isopeptide bond; Kinase; Membrane;
Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Sugar transport;
Transferase; Translation regulation; Transport; Ubl conjugation.
CHAIN 1 480 RAC-alpha serine/threonine-protein
kinase.
/FTId=PRO_0000085606.
DOMAIN 5 108 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 150 408 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 409 480 AGC-kinase C-terminal.
NP_BIND 156 164 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 14 19 Inositol-(1,3,4,5)-tetrakisphosphate
binding. {ECO:0000250}.
REGION 23 25 Inositol-(1,3,4,5)-tetrakisphosphate
binding. {ECO:0000250}.
REGION 228 230 Inhibitor binding. {ECO:0000250}.
ACT_SITE 274 274 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 53 53 Inositol-(1,3,4,5)-tetrakisphosphate.
{ECO:0000250}.
BINDING 86 86 Inositol-(1,3,4,5)-tetrakisphosphate.
{ECO:0000250}.
BINDING 161 161 Inhibitor; via amide nitrogen.
{ECO:0000250}.
BINDING 179 179 ATP.
BINDING 230 230 Inhibitor; via amide nitrogen.
{ECO:0000250}.
BINDING 234 234 Inhibitor. {ECO:0000250}.
BINDING 292 292 Inhibitor. {ECO:0000250}.
MOD_RES 14 14 N6-acetyllysine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 20 20 N6-acetyllysine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 126 126 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 129 129 Phosphoserine; alternate.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 176 176 Phosphotyrosine; by TNK2.
{ECO:0000269|PubMed:20333297}.
MOD_RES 308 308 Phosphothreonine; by IKKE, PDPK1 and
TBK1. {ECO:0000269|PubMed:15753085,
ECO:0000269|PubMed:18288188,
ECO:0000269|PubMed:20333297}.
MOD_RES 448 448 Phosphothreonine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 450 450 Phosphothreonine; by MTOR.
{ECO:0000269|PubMed:21045808}.
MOD_RES 473 473 Phosphoserine; by IKKE, MTOR and TBK1;
alternate. {ECO:0000305|PubMed:12783884,
ECO:0000305|PubMed:15753085,
ECO:0000305|PubMed:20333297}.
MOD_RES 474 474 Phosphotyrosine.
{ECO:0000250|UniProtKB:P31749}.
CARBOHYD 126 126 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 129 129 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 305 305 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 312 312 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 473 473 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
DISULFID 60 77 {ECO:0000250}.
DISULFID 296 310 {ECO:0000250}.
CROSSLNK 284 284 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P31749}.
MUTAGEN 176 176 Y->F: Significant loss of interaction
with TNK2. Loss of membrane localization.
Significant reduction in phosphorylation
on Ser-473.
{ECO:0000269|PubMed:20333297}.
MUTAGEN 179 179 K->A: Lacks kinase activity.
Overexpression inhibits insulin-
stimulated translocation of SLC2A4/GLUT4
in a dominant negative manner.
{ECO:0000269|PubMed:9415393}.
MUTAGEN 308 308 T->A: Does not affect ubiquitination by
ZNRF1. {ECO:0000269|PubMed:22057101}.
MUTAGEN 473 473 S->A: Does not affect ubiquitination by
ZNRF1. {ECO:0000269|PubMed:22057101}.
CONFLICT 367 367 R -> A (in Ref. 3; AAA18254).
{ECO:0000305}.
SEQUENCE 480 AA; 55707 MW; 98DF28E5EFE03730 CRC64;
MNDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDVDQRES PLNNFSVAQC
QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWA TAIQTVADGL KRQEEETMDF
RSGSPSDNSG AEEMEVSLAK PKHRVTMNEF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI
LKKEVIVAKD EVAHTLTENR VLQNSRHPFL TALKYSFQTH DRLCFVMEYA NGGELFFHLS
RERVFSEDRA RFYGAEIVSA LDYLHSEKNV VYRDLKLENL MLDKDGHIKI TDFGLCKEGI
KDGATMKTFC GTPEYLAPEV LEDNDYGRAV DWWGLGVVMY EMMCGRLPFY NQDHEKLFEL
ILMEEIRFPR TLGPEAKSLL SGLLKKDPTQ RLGGGSEDAK EIMQHRFFAN IVWQDVYEKK
LSPPFKPQVT SETDTRYFDE EFTAQMITIT PPDQDDSMEC VDSERRPHFP QFSYSASGTA


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