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RAC-beta serine/threonine-protein kinase (EC 2.7.11.1) (Protein kinase Akt-2) (Protein kinase B beta) (PKB beta) (RAC-PK-beta)

 AKT2_HUMAN              Reviewed;         481 AA.
P31751; B2RBD8; Q05BV0; Q0VAN0; Q0VAN1; Q68GC0;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
22-NOV-2017, entry version 195.
RecName: Full=RAC-beta serine/threonine-protein kinase;
EC=2.7.11.1;
AltName: Full=Protein kinase Akt-2;
AltName: Full=Protein kinase B beta;
Short=PKB beta;
AltName: Full=RAC-PK-beta;
Name=AKT2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Epithelium;
PubMed=1801921;
Jones P.F., Jakubowicz T., Hemmings B.A.;
"Molecular cloning of a second form of rac protein kinase.";
Cell Regul. 2:1001-1009(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1409633; DOI=10.1073/pnas.89.19.9267;
Cheng J.Q., Godwin A.K., Bellacosa A., Taguchi T., Franke T.F.,
Hamilton T.C., Tsichlis P.N., Testa J.R.;
"AKT2, a putative oncogene encoding a member of a subfamily of
protein-serine/threonine kinases, is amplified in human ovarian
carcinomas.";
Proc. Natl. Acad. Sci. U.S.A. 89:9267-9271(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lymph;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-277.
NIEHS SNPs program;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[7]
CHARACTERIZATION, AND PHOSPHORYLATION AT THR-309 BY PDPK1.
PubMed=9512493; DOI=10.1042/bj3310299;
Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., Alessi D.R.;
"Activation of protein kinase B beta and gamma isoforms by insulin in
vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro:
comparison with protein kinase B alpha.";
Biochem. J. 331:299-308(1998).
[8]
INTERACTION WITH MTCP1; TCL1A AND TCL1B.
PubMed=10983986; DOI=10.1016/S1097-2765(00)00039-3;
Laine J., Kuenstle G., Obata T., Sha M., Noguchi M.;
"The protooncogene TCL1 is an Akt kinase coactivator.";
Mol. Cell 6:395-407(2000).
[9]
MUTAGENESIS OF THR-309 AND SER-474, AND PHOSPHORYLATION AT THR-309 AND
SER-474.
PubMed=15890450; DOI=10.1016/j.bbagen.2005.04.002;
Baer K., Lisinski I., Gompert M., Stuhlmann D., Schmolz K.,
Klein H.W., Al-Hasani H.;
"Activation of a GST-tagged AKT2/PKBbeta.";
Biochim. Biophys. Acta 1725:340-347(2005).
[10]
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).
[11]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16540465; DOI=10.1074/jbc.M601384200;
Zhang X., Zhang S., Yamane H., Wahl R., Ali A., Lofgren J.A.,
Kendall R.L.;
"Kinetic mechanism of AKT/PKB enzyme family.";
J. Biol. Chem. 281:13949-13956(2006).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PBH2.
PubMed=17565718; DOI=10.1002/jcp.21177;
Heron-Milhavet L., Mamaeva D., Rochat A., Lamb N.J., Fernandez A.;
"Akt2 is implicated in skeletal muscle differentiation and
specifically binds Prohibitin2/REA.";
J. Cell. Physiol. 214:158-165(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
UBIQUITINATION BY TTC3, PHOSPHORYLATION AT THR-309 AND SER-474, AND
MUTAGENESIS OF THR-309 AND SER-474.
PubMed=20059950; DOI=10.1016/j.devcel.2009.09.007;
Suizu F., Hiramuki Y., Okumura F., Matsuda M., Okumura A.J.,
Hirata N., Narita M., Kohno T., Yokota J., Bohgaki M., Obuse C.,
Hatakeyama S., Obata T., Noguchi M.;
"The E3 ligase TTC3 facilitates ubiquitination and degradation of
phosphorylated Akt.";
Dev. Cell 17:800-810(2009).
[15]
INTERACTION WITH CLIP3, AND SUBCELLULAR LOCATION.
PubMed=19139280; DOI=10.1128/MCB.00754-08;
Ding J., Du K.;
"ClipR-59 interacts with Akt and regulates Akt cellular
compartmentalization.";
Mol. Cell. Biol. 29:1459-1471(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447; THR-451; SER-474
AND SER-478, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
UBIQUITINATION, AND INTERACTION WITH TRAF6.
PubMed=19713527; DOI=10.1126/science.1175065;
Yang W.-L., Wang J., Chan C.-H., Lee S.-W., Campos A.D., Lamothe B.,
Hur L., Grabiner B.C., Lin X., Darnay B.G., Lin H.-K.;
"The E3 ligase TRAF6 regulates Akt ubiquitination and activation.";
Science 325:1134-1138(2009).
[18]
INVOLVEMENT IN CANCER.
PubMed=20167810; DOI=10.1093/neuonc/nop026;
Mure H., Matsuzaki K., Kitazato K.T., Mizobuchi Y., Kuwayama K.,
Kageji T., Nagahiro S.;
"Akt2 and Akt3 play a pivotal role in malignant gliomas.";
Neuro-oncol. 12:221-232(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
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).
[21]
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).
[22]
FUNCTION IN MUSCLE DIFFERENTIATION, AND INTERACTION WITH ANKRD2.
PubMed=21737686; DOI=10.1091/mbc.E10-11-0928;
Cenni V., Bavelloni A., Beretti F., Tagliavini F., Manzoli L.,
Lattanzi G., Maraldi N.M., Cocco L., Marmiroli S.;
"Ankrd2/ARPP is a novel Akt2 specific substrate and regulates myogenic
differentiation upon cellular exposure to H(2)O(2).";
Mol. Biol. Cell 22:2946-2956(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-126, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND THR-451, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 146-480.
PubMed=12086620; DOI=10.1016/S1097-2765(02)00550-6;
Yang J., Cron P., Thompson V., Good V.M., Hess D., Hemmings B.A.,
Barford D.;
"Molecular mechanism for the regulation of protein kinase B/Akt by
hydrophobic motif phosphorylation.";
Mol. Cell 9:1227-1240(2002).
[27]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 146-467 IN COMPLEX WITH
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER AND MANGANESE, AND
PHOSPHORYLATION AT THR-309.
PubMed=12434148; DOI=10.1038/nsb870;
Yang J., Cron P., Good V.M., Thompson V., Hemmings B.A., Barford D.;
"Crystal structure of an activated Akt/protein kinase B ternary
complex with GSK3-peptide and AMP-PNP.";
Nat. Struct. Biol. 9:940-944(2002).
[28]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 143-481, ATP-BINDING,
SUBSTRATE-BINDING, AND DISULFIDE BOND.
PubMed=12517337; DOI=10.1016/S0969-2126(02)00937-1;
Huang X., Begley M., Morgenstern K.A., Gu Y., Rose P., Zhao H.,
Zhu X.;
"Crystal structure of an inactive Akt2 kinase domain.";
Structure 11:21-30(2003).
[29]
STRUCTURE BY NMR OF 1-111.
PubMed=14755158; DOI=10.1023/B:JNMR.0000013836.62154.c2;
Auguin D., Barthe P., Auge-Senegas M.T., Stern M.H., Noguchi M.,
Roumestand C.;
"Solution structure and backbone dynamics of the pleckstrin homology
domain of the human protein kinase B (PKB/Akt). Interaction with
inositol phosphates.";
J. Biomol. NMR 28:137-155(2004).
[30]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 146-467, AND
INHIBITOR-BINDING.
PubMed=17275837; DOI=10.1016/j.jmb.2007.01.004;
Davies T.G., Verdonk M.L., Graham B., Saalau-Bethell S., Hamlett C.C.,
McHardy T., Collins I., Garrett M.D., Workman P., Woodhead S.J.,
Jhoti H., Barford D.;
"A structural comparison of inhibitor binding to PKB, PKA and PKA-PKB
chimera.";
J. Mol. Biol. 367:882-894(2007).
[31]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 146-480, AND ENZYME
REGULATION.
PubMed=18800763; DOI=10.1021/jm8004527;
Heerding D.A., Rhodes N., Leber J.D., Clark T.J., Keenan R.M.,
Lafrance L.V., Li M., Safonov I.G., Takata D.T., Venslavsky J.W.,
Yamashita D.S., Choudhry A.E., Copeland R.A., Lai Z., Schaber M.D.,
Tummino P.J., Strum S.L., Wood E.R., Duckett D.R., Eberwein D.,
Knick V.B., Lansing T.J., McConnell R.T., Zhang S., Minthorn E.A.,
Concha N.O., Warren G.L., Kumar R.;
"Identification of 4-(2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-
7-{[(3S)-3-piperidinylmethyl]oxy}-1H-imidazo[4,5-c]pyridin-4-yl)-2-
methyl-3-butyn-2-ol (GSK690693), a novel inhibitor of AKT kinase.";
J. Med. Chem. 51:5663-5679(2008).
[32]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 146-480, AND ENZYME
REGULATION.
PubMed=19179070; DOI=10.1016/j.bmcl.2009.01.002;
Rouse M.B., Seefeld M.A., Leber J.D., McNulty K.C., Sun L.,
Miller W.H., Zhang S., Minthorn E.A., Concha N.O., Choudhry A.E.,
Schaber M.D., Heerding D.A.;
"Aminofurazans as potent inhibitors of AKT kinase.";
Bioorg. Med. Chem. Lett. 19:1508-1511(2009).
[33]
VARIANT NIDDM HIS-274.
PubMed=15166380; DOI=10.1126/science.1096706;
George S., Rochford J.J., Wolfrum C., Gray S.L., Schinner S.,
Wilson J.C., Soos M.A., Murgatroyd P.R., Williams R.M., Acerini C.L.,
Dunger D.B., Barford D., Umpleby A.M., Wareham N.J., Davies H.A.,
Schafer A.J., Stoffel M., O'Rahilly S., Barroso I.;
"A family with severe insulin resistance and diabetes due to a
mutation in AKT2.";
Science 304:1325-1328(2004).
[34]
VARIANTS [LARGE SCALE ANALYSIS] VAL-188 AND LYS-208.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[35]
ASSOCIATION OF VARIANT NIDDM HIS-274 WITH TYPICAL METABOLIC
DYSLIPIDEMIA.
PubMed=19164855; DOI=10.1172/JCI37432;
Semple R.K., Sleigh A., Murgatroyd P.R., Adams C.A., Bluck L.,
Jackson S., Vottero A., Kanabar D., Charlton-Menys V., Durrington P.,
Soos M.A., Carpenter T.A., Lomas D.J., Cochran E.K., Gorden P.,
O'Rahilly S., Savage D.B.;
"Postreceptor insulin resistance contributes to human dyslipidemia and
hepatic steatosis.";
J. Clin. Invest. 119:315-322(2009).
[36]
VARIANT HIHGHH LYS-17.
PubMed=21979934; DOI=10.1126/science.1210878;
Hussain K., Challis B., Rocha N., Payne F., Minic M., Thompson A.,
Daly A., Scott C., Harris J., Smillie B.J., Savage D.B., Ramaswami U.,
De Lonlay P., O'Rahilly S., Barroso I., Semple R.K.;
"An activating mutation of AKT2 and human hypoglycemia.";
Science 334:474-474(2011).
-!- FUNCTION: AKT2 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.
-!- FUNCTION: One of the few specific substrates of AKT2 identified
recently is PITX2. Phosphorylation of PITX2 impairs its
association with the CCND1 mRNA-stabilizing complex thus
shortening the half-life of CCND1. AKT2 seems also to be the
principal isoform responsible of the regulation of glucose uptake.
Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated
adipocytes. AKT2 is also specifically involved in skeletal muscle
differentiation, one of its substrates in this process being
ANKRD2. Down-regulation by RNA interference reduces the expression
of the phosphorylated form of BAD, resulting in the induction of
caspase-dependent apoptosis. Phosphorylates CLK2 on 'Thr-343'.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Two specific sites, one in the kinase domain
(Thr-309) and the other in the C-terminal regulatory region (Ser-
474), need to be phosphorylated for its full activation.
Aminofurazans are potent AKT2 inhibitors.
{ECO:0000269|PubMed:18800763, ECO:0000269|PubMed:19179070}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=358.4 uM for ATP (for purified and in vitro activated AKT2)
{ECO:0000269|PubMed:16540465};
KM=3.4 uM for peptide substrate (for purified and in vitro
activated AKT2) {ECO:0000269|PubMed:16540465};
KM=564 uM for ATP (for recombinant myristoylated AKT2 expressed
and immunoprecipitated from Rat-1 cells)
{ECO:0000269|PubMed:16540465};
KM=2.3 uM for peptide substrate (for recombinant myristoylated
AKT2 expressed and immunoprecipitated from Rat-1 cells)
{ECO:0000269|PubMed:16540465};
-!- SUBUNIT: Interacts with BTBD10 (By similarity). Interacts with
KCTD20 (By similarity). Interacts (via PH domain) with MTCP1,
TCL1A AND TCL1B. Interacts with CLK2, PBH2 and TRAF6. Interacts
(when phosphorylated) with CLIP3, the interaction promotes cell
membrane localization (PubMed:19139280). Interacts with WDFY2 (via
WD repeats 1-3) (PubMed:16792529). {ECO:0000250|UniProtKB:Q60823,
ECO:0000269|PubMed:10983986, ECO:0000269|PubMed:12434148,
ECO:0000269|PubMed:16792529, ECO:0000269|PubMed:17565718,
ECO:0000269|PubMed:19139280, ECO:0000269|PubMed:19713527,
ECO:0000269|PubMed:21737686}.
-!- INTERACTION:
P49841:GSK3B; NbExp=2; IntAct=EBI-296058, EBI-373586;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-296058, EBI-352572;
Q15118-1:PDK1; NbExp=2; IntAct=EBI-12562336, EBI-12562315;
O60504:SORBS3; NbExp=4; IntAct=EBI-296058, EBI-741237;
P08670:VIM; NbExp=6; IntAct=EBI-296058, EBI-353844;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane;
Peripheral membrane protein. Early endosome
{ECO:0000250|UniProtKB:Q60823}. Note=Localizes within both nucleus
and cytoplasm of proliferative primary myoblasts and mostly within
the nucleus of differentiated primary myoblasts. By virtue of the
N-terminal PH domain, is recruited to sites of the plasma membrane
containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane
targeting is also facilitared by interaction with CLIP3.
Colocalizes with WDFY2 in early endosomes (By similarity).
{ECO:0000250|UniProtKB:Q60823}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P31751-1; Sequence=Displayed;
Name=2;
IsoId=P31751-2; Sequence=VSP_056930;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all cell types so far analyzed.
-!- 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.
-!- PTM: Phosphorylation on Thr-309 and Ser-474 is required for full
activity. {ECO:0000269|PubMed:12434148,
ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950,
ECO:0000269|PubMed:9512493}.
-!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT2
ubiquitination. When fully phosphorylated and translocated into
the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by
TTC3, leading to its degradation by the proteasome.
{ECO:0000269|PubMed:19713527, ECO:0000269|PubMed:20059950}.
-!- PTM: O-GlcNAcylation at Thr-306 and Thr-313 inhibits activating
phosphorylation at Thr-309 via disrupting the interaction between
AKT and PDK1. {ECO:0000250}.
-!- DISEASE: Note=Defects in AKT2 are a cause of susceptibility to
breast cancer (BC). AKT2 promotes metastasis of tumor cells
without affecting the latency of tumor development. With AKT3,
plays also a pivotal role in the biology of glioblastoma.
-!- DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM)
[MIM:125853]: A multifactorial disorder of glucose homeostasis
caused by a lack of sensitivity to the body's own insulin.
Affected individuals usually have an obese body habitus and
manifestations of a metabolic syndrome characterized by diabetes,
insulin resistance, hypertension and hypertriglyceridemia. The
disease results in long-term complications that affect the eyes,
kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:15166380,
ECO:0000269|PubMed:19164855}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Hypoinsulinemic hypoglycemia with hemihypertrophy
(HIHGHH) [MIM:240900]: A disorder characterized by hypoglycemia,
low insulin levels, low serum levels of ketone bodies and
branched-chain amino acids, left-sided hemihypertrophy, neonatal
macrosomia, reduced consciousness and hypoglycemic seizures.
{ECO:0000269|PubMed:21979934}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AKT2ID517ch19q13.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/akt2/";
-----------------------------------------------------------------------
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EMBL; M77198; AAA36585.1; -; mRNA.
EMBL; M95936; AAA58364.1; -; mRNA.
EMBL; AK314619; BAG37185.1; -; mRNA.
EMBL; AC118344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032709; AAH32709.1; -; mRNA.
EMBL; BC120995; AAI20996.1; -; mRNA.
EMBL; BC120994; AAI20995.1; -; mRNA.
EMBL; AY708392; AAT97984.1; -; Genomic_DNA.
CCDS; CCDS12552.1; -. [P31751-1]
CCDS; CCDS82350.1; -. [P31751-2]
PIR; A46288; A46288.
RefSeq; NP_001317440.1; NM_001330511.1. [P31751-2]
RefSeq; NP_001617.1; NM_001626.5. [P31751-1]
RefSeq; XP_011524916.1; XM_011526614.1. [P31751-1]
RefSeq; XP_011524917.1; XM_011526615.1. [P31751-1]
RefSeq; XP_011524918.1; XM_011526616.1. [P31751-1]
RefSeq; XP_011524920.1; XM_011526618.1. [P31751-1]
RefSeq; XP_011524921.1; XM_011526619.1. [P31751-1]
RefSeq; XP_011524922.1; XM_011526620.1. [P31751-1]
RefSeq; XP_016881959.1; XM_017026470.1. [P31751-1]
UniGene; Hs.631535; -.
PDB; 1GZK; X-ray; 2.30 A; A=146-460.
PDB; 1GZN; X-ray; 2.50 A; A=146-480.
PDB; 1GZO; X-ray; 2.75 A; A=146-460.
PDB; 1MRV; X-ray; 2.80 A; A=143-481.
PDB; 1MRY; X-ray; 2.80 A; A=143-481.
PDB; 1O6K; X-ray; 1.70 A; A=146-481.
PDB; 1O6L; X-ray; 1.60 A; A=146-467.
PDB; 1P6S; NMR; -; A=1-111.
PDB; 2JDO; X-ray; 1.80 A; A=146-467.
PDB; 2JDR; X-ray; 2.30 A; A=146-467.
PDB; 2UW9; X-ray; 2.10 A; A=146-467.
PDB; 2X39; X-ray; 1.93 A; A=146-467.
PDB; 2XH5; X-ray; 2.72 A; A=146-479.
PDB; 3D0E; X-ray; 2.00 A; A/B=146-480.
PDB; 3E87; X-ray; 2.30 A; A/B=146-480.
PDB; 3E88; X-ray; 2.50 A; A/B=146-480.
PDB; 3E8D; X-ray; 2.70 A; A/B=146-480.
PDBsum; 1GZK; -.
PDBsum; 1GZN; -.
PDBsum; 1GZO; -.
PDBsum; 1MRV; -.
PDBsum; 1MRY; -.
PDBsum; 1O6K; -.
PDBsum; 1O6L; -.
PDBsum; 1P6S; -.
PDBsum; 2JDO; -.
PDBsum; 2JDR; -.
PDBsum; 2UW9; -.
PDBsum; 2X39; -.
PDBsum; 2XH5; -.
PDBsum; 3D0E; -.
PDBsum; 3E87; -.
PDBsum; 3E88; -.
PDBsum; 3E8D; -.
DisProt; DP00304; -.
ProteinModelPortal; P31751; -.
SMR; P31751; -.
BioGrid; 106711; 59.
CORUM; P31751; -.
DIP; DIP-32583N; -.
ELM; P31751; -.
IntAct; P31751; 33.
MINT; MINT-87790; -.
STRING; 9606.ENSP00000375892; -.
BindingDB; P31751; -.
ChEMBL; CHEMBL2431; -.
DrugBank; DB08073; (2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE.
DrugBank; DB07859; 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE.
DrugBank; DB07947; ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE.
GuidetoPHARMACOLOGY; 1480; -.
iPTMnet; P31751; -.
PhosphoSitePlus; P31751; -.
BioMuta; AKT2; -.
DMDM; 1170703; -.
EPD; P31751; -.
MaxQB; P31751; -.
PaxDb; P31751; -.
PeptideAtlas; P31751; -.
PRIDE; P31751; -.
DNASU; 208; -.
Ensembl; ENST00000311278; ENSP00000309428; ENSG00000105221. [P31751-2]
Ensembl; ENST00000392038; ENSP00000375892; ENSG00000105221. [P31751-1]
Ensembl; ENST00000424901; ENSP00000399532; ENSG00000105221. [P31751-2]
GeneID; 208; -.
KEGG; hsa:208; -.
UCSC; uc002onf.3; human. [P31751-1]
CTD; 208; -.
DisGeNET; 208; -.
EuPathDB; HostDB:ENSG00000105221.16; -.
GeneCards; AKT2; -.
HGNC; HGNC:392; AKT2.
HPA; CAB004204; -.
HPA; HPA064521; -.
MalaCards; AKT2; -.
MIM; 125853; phenotype.
MIM; 164731; gene.
MIM; 240900; phenotype.
neXtProt; NX_P31751; -.
OpenTargets; ENSG00000105221; -.
Orphanet; 79085; Familial partial lipodystrophy due to AKT2 mutations.
Orphanet; 293964; Hypoinsulinemic hypoglycemia and body hemihypertrophy.
PharmGKB; PA24685; -.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00890000139324; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P31751; -.
KO; K04456; -.
OrthoDB; EOG091G06FF; -.
PhylomeDB; P31751; -.
TreeFam; TF102004; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-165158; Activation of AKT2.
Reactome; R-HSA-165160; PDE3B signalling.
Reactome; R-HSA-165181; Inhibition of TSC complex formation by PKB.
Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-HSA-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-HSA-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-HSA-211163; AKT-mediated inactivation of FOXO1A.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
Reactome; R-HSA-8941332; RUNX2 regulates genes involved in cell migration.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
SABIO-RK; P31751; -.
SignaLink; P31751; -.
SIGNOR; P31751; -.
ChiTaRS; AKT2; human.
EvolutionaryTrace; P31751; -.
GeneWiki; AKT2; -.
GenomeRNAi; 208; -.
PRO; PR:P31751; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105221; -.
CleanEx; HS_AKT2; -.
ExpressionAtlas; P31751; baseline and differential.
Genevisible; P31751; HS.
GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; IEA:Ensembl.
GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0071486; P:cellular response to high light intensity; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
GO; GO:0045444; P:fat cell differentiation; TAS:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0065002; P:intracellular protein transmembrane transport; ISS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0060644; P:mammary gland epithelial cell differentiation; TAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0010748; P:negative regulation of plasma membrane long-chain fatty acid transport; IMP:BHF-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:2000147; P:positive regulation of cell motility; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:BHF-UCL.
GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IEA:Ensembl.
GO; GO:0010907; P:positive regulation of glucose metabolic process; IMP:BHF-UCL.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IMP:BHF-UCL.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
GO; GO:0031340; P:positive regulation of vesicle fusion; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0071156; P:regulation of cell cycle arrest; TAS:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; TAS:UniProtKB.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0097473; P:retinal rod cell apoptotic process; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
CDD; cd05595; STKc_PKB_beta; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR034677; Akt2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
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;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Carbohydrate metabolism; Cell membrane;
Complete proteome; Cytoplasm; Developmental protein;
Diabetes mellitus; Disease mutation; Disulfide bond; Endosome;
Glucose metabolism; Glycogen biosynthesis; Glycogen metabolism;
Glycoprotein; Isopeptide bond; Kinase; Manganese; Membrane;
Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome;
Serine/threonine-protein kinase; Sugar transport; Transferase;
Translation regulation; Transport; Ubl conjugation.
CHAIN 1 481 RAC-beta serine/threonine-protein kinase.
/FTId=PRO_0000085608.
DOMAIN 5 108 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 152 409 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 410 481 AGC-kinase C-terminal.
NP_BIND 158 166 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 230 232 Inhibitor binding.
REGION 277 279 Inhibitor binding.
REGION 292 293 Inhibitor binding.
ACT_SITE 275 275 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 280 280 Manganese. {ECO:0000269|PubMed:12434148}.
METAL 293 293 Manganese. {ECO:0000269|PubMed:12434148}.
BINDING 181 181 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 181 181 Inhibitor.
BINDING 200 200 Inhibitor.
BINDING 232 232 Inhibitor; via amide nitrogen.
BINDING 236 236 Inhibitor.
BINDING 279 279 Inhibitor; via carbonyl oxygen.
BINDING 293 293 Inhibitor.
BINDING 294 294 Inhibitor; via amide nitrogen.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 14 14 N6-acetyllysine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 20 20 N6-acetyllysine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 128 128 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 131 131 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 178 178 Phosphotyrosine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 309 309 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:12434148,
ECO:0000269|PubMed:15890450,
ECO:0000269|PubMed:20059950,
ECO:0000269|PubMed:9512493}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 449 449 Phosphothreonine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 451 451 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 474 474 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:15890450,
ECO:0000269|PubMed:20059950}.
MOD_RES 475 475 Phosphotyrosine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
CARBOHYD 128 128 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 131 131 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 306 306 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 313 313 O-linked (GlcNAc) threonine.
{ECO:0000250}.
DISULFID 60 77 {ECO:0000250}.
DISULFID 297 311 {ECO:0000269|PubMed:12517337}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P31749}.
VAR_SEQ 278 320 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056930.
VARIANT 17 17 E -> K (in HIHGHH; exhibits plasma
membrane localization in serum-starved
cells and produced inappropriate tonic
nuclear exclusion of FOXO1 in
preadipocytes; dbSNP:rs387906659).
{ECO:0000269|PubMed:21979934}.
/FTId=VAR_067309.
VARIANT 188 188 I -> V (in dbSNP:rs55859611).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040356.
VARIANT 208 208 R -> K (in dbSNP:rs35817154).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040357.
VARIANT 274 274 R -> H (in NIDDM; associated with typical
metabolic dyslipidemia with elevated
fastin triglyceride, high VLDL
triglyceride/cholesterol ratios, low HDL
cholesterol levels and high small dense
LDL levels; de novo lipogenesis and liver
fat are also significantly elevated in
this subject; dbSNP:rs121434593).
{ECO:0000269|PubMed:15166380}.
/FTId=VAR_067310.
MUTAGEN 309 309 T->A: Impairs interaction with TTC3; when
associated with A-474.
{ECO:0000269|PubMed:15890450,
ECO:0000269|PubMed:20059950}.
MUTAGEN 309 309 T->E: Constitutively active; when
associated with D-474.
{ECO:0000269|PubMed:15890450,
ECO:0000269|PubMed:20059950}.
MUTAGEN 474 474 S->A: Impairs interaction with TTC3; when
associated with A-309.
{ECO:0000269|PubMed:15890450,
ECO:0000269|PubMed:20059950}.
MUTAGEN 474 474 S->D: Constitutively active; when
associated with E-309.
{ECO:0000269|PubMed:15890450,
ECO:0000269|PubMed:20059950}.
CONFLICT 478 481 SIRE -> FREEKDLLMSLFVSLILFSDFSSLKSHSFSSNF
ILLSFSSLKK (in Ref. 1; AAA36585).
{ECO:0000305}.
STRAND 6 15 {ECO:0000244|PDB:1P6S}.
STRAND 17 20 {ECO:0000244|PDB:1P6S}.
STRAND 22 30 {ECO:0000244|PDB:1P6S}.
TURN 31 33 {ECO:0000244|PDB:1P6S}.
STRAND 34 40 {ECO:0000244|PDB:1P6S}.
STRAND 45 47 {ECO:0000244|PDB:1P6S}.
STRAND 52 56 {ECO:0000244|PDB:1P6S}.
STRAND 58 60 {ECO:0000244|PDB:1P6S}.
STRAND 62 65 {ECO:0000244|PDB:1P6S}.
STRAND 67 75 {ECO:0000244|PDB:1P6S}.
STRAND 86 92 {ECO:0000244|PDB:1P6S}.
HELIX 93 110 {ECO:0000244|PDB:1P6S}.
HELIX 149 151 {ECO:0000244|PDB:1O6L}.
STRAND 152 160 {ECO:0000244|PDB:1O6L}.
STRAND 162 171 {ECO:0000244|PDB:1O6L}.
TURN 172 174 {ECO:0000244|PDB:1O6L}.
STRAND 177 184 {ECO:0000244|PDB:1O6L}.
HELIX 185 190 {ECO:0000244|PDB:1O6L}.
HELIX 194 205 {ECO:0000244|PDB:1O6L}.
STRAND 215 220 {ECO:0000244|PDB:1O6L}.
STRAND 222 230 {ECO:0000244|PDB:1O6L}.
HELIX 237 244 {ECO:0000244|PDB:1O6L}.
HELIX 249 268 {ECO:0000244|PDB:1O6L}.
STRAND 280 283 {ECO:0000244|PDB:1O6L}.
STRAND 289 291 {ECO:0000244|PDB:1O6L}.
STRAND 298 300 {ECO:0000244|PDB:2UW9}.
STRAND 310 312 {ECO:0000244|PDB:2JDO}.
HELIX 314 316 {ECO:0000244|PDB:1O6L}.
HELIX 319 322 {ECO:0000244|PDB:1O6L}.
STRAND 323 325 {ECO:0000244|PDB:1O6L}.
HELIX 331 345 {ECO:0000244|PDB:1O6L}.
STRAND 351 353 {ECO:0000244|PDB:1GZK}.
HELIX 355 364 {ECO:0000244|PDB:1O6L}.
STRAND 371 373 {ECO:0000244|PDB:1GZN}.
HELIX 375 384 {ECO:0000244|PDB:1O6L}.
TURN 389 391 {ECO:0000244|PDB:1O6L}.
TURN 393 395 {ECO:0000244|PDB:2X39}.
TURN 397 399 {ECO:0000244|PDB:1O6L}.
HELIX 400 404 {ECO:0000244|PDB:1O6L}.
HELIX 407 409 {ECO:0000244|PDB:1O6L}.
HELIX 414 418 {ECO:0000244|PDB:1O6L}.
STRAND 431 434 {ECO:0000244|PDB:2JDR}.
STRAND 437 439 {ECO:0000244|PDB:1GZO}.
HELIX 441 444 {ECO:0000244|PDB:1O6L}.
STRAND 474 476 {ECO:0000244|PDB:3D0E}.
TURN 477 479 {ECO:0000244|PDB:3D0E}.
SEQUENCE 481 AA; 55769 MW; B18C87A7246BFB24 CRC64;
MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP PLNNFSVAEC
QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM RAIQMVANSL KQRAPGEDPM
DYKCGSPSDS STTEEMEVAV SKARAKVTMN DFDYLKLLGK GTFGKVILVR EKATGRYYAM
KILRKEVIIA KDEVAHTVTE SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH
LSRERVFTEE RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG
ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF YNQDHERLFE
LILMEEIRFP RTLSPEAKSL LAGLLKKDPK QRLGGGPSDA KEVMEHRFFL SINWQDVVQK
KLLPPFKPQV TSEVDTRYFD DEFTAQSITI TPPDRYDSLG LLELDQRTHF PQFSYSASIR
E


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