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Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1)

 GSK3B_HUMAN             Reviewed;         420 AA.
P49841; D3DN89; Q9BWH3; Q9UL47;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
02-MAY-2002, sequence version 2.
25-OCT-2017, entry version 219.
RecName: Full=Glycogen synthase kinase-3 beta;
Short=GSK-3 beta;
EC=2.7.11.26;
AltName: Full=Serine/threonine-protein kinase GSK3B;
EC=2.7.11.1;
Name=GSK3B;
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), AND MUTAGENESIS OF SER-9.
PubMed=7980435; DOI=10.1042/bj3030701;
Stambolic V., Woodgett J.R.;
"Mitogen inactivation of glycogen synthase kinase-3 beta in intact
cells via serine 9 phosphorylation.";
Biochem. J. 303:701-704(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Eye, and Placenta;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
PubMed=10486203; DOI=10.1006/geno.1999.5875;
Lau K.F., Miller C.C.J., Anderton B.H., Shaw P.C.;
"Molecular cloning and characterization of the human glycogen synthase
kinase-3beta promoter.";
Genomics 60:121-128(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-202.
PubMed=10523816; DOI=10.1038/sj.mp.4000538;
Rhoads A.R., Karkera J.D., Detera-Wadleigh S.D.;
"Radiation hybrid mapping of genes in the lithium-sensitive wnt
signaling pathway.";
Mol. Psychiatry 4:437-442(1999).
[6]
FUNCTION IN PHOSPHORYLATION OF JUN.
PubMed=1846781; DOI=10.1016/0092-8674(91)90241-P;
Boyle W.J., Smeal T., Defize L.H., Angel P., Woodgett J.R., Karin M.,
Hunter T.;
"Activation of protein kinase C decreases phosphorylation of c-Jun at
sites that negatively regulate its DNA-binding activity.";
Cell 64:573-584(1991).
[7]
FUNCTION IN PHOSPHORYLATION OF EIF2BE/EIF2B5.
PubMed=8397507; DOI=10.1042/bj2940625;
Welsh G.I., Proud C.G.;
"Glycogen synthase kinase-3 is rapidly inactivated in response to
insulin and phosphorylates eukaryotic initiation factor eIF-2B.";
Biochem. J. 294:625-629(1993).
[8]
PHOSPHORYLATION AT SER-9.
PubMed=8250835; DOI=10.1042/bj2960015;
Sutherland C., Leighton I.A., Cohen P.;
"Inactivation of glycogen synthase kinase-3 beta by phosphorylation:
new kinase connections in insulin and growth-factor signalling.";
Biochem. J. 296:15-19(1993).
[9]
ENZYME REGULATION BY AKT1.
PubMed=8524413; DOI=10.1038/378785a0;
Cross D.A., Alessi D.R., Cohen P., Andjelkovich M., Hemmings B.A.;
"Inhibition of glycogen synthase kinase-3 by insulin mediated by
protein kinase B.";
Nature 378:785-789(1995).
[10]
FUNCTION IN PHOSPHORYLATION OF NFATC1/NFATC.
PubMed=9072970; DOI=10.1126/science.275.5308.1930;
Beals C.R., Sheridan C.M., Turck C.W., Gardner P., Crabtree G.R.;
"Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3.";
Science 275:1930-1934(1997).
[11]
INTERACTION WITH DNM1L.
TISSUE=Liver;
PubMed=9731200; DOI=10.1006/bbrc.1998.9253;
Hong Y.-R., Chen C.-H., Cheng D.-S., Howng S.-L., Chow C.-C.;
"Human dynamin-like protein interacts with the glycogen synthase
kinase 3beta.";
Biochem. Biophys. Res. Commun. 249:697-703(1998).
[12]
INTERACTION WITH MUC1, AND FUNCTION.
PubMed=9819408; DOI=10.1128/MCB.18.12.7216;
Li Y., Bharti A., Chen D., Gong J., Kufe D.;
"Interaction of glycogen synthase kinase 3beta with the DF3/MUC1
carcinoma-associated antigen and beta-catenin.";
Mol. Cell. Biol. 18:7216-7224(1998).
[13]
CHARACTERIZATION.
PubMed=9736715; DOI=10.1073/pnas.95.19.11211;
Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S.;
"Phosphoinositide-3-OH kinase-dependent regulation of glycogen
synthase kinase 3 and protein kinase B/AKT by the integrin-linked
kinase.";
Proc. Natl. Acad. Sci. U.S.A. 95:11211-11216(1998).
[14]
INTERACTION WITH NIN.
PubMed=11004522; DOI=10.1016/S0167-4781(00)00127-5;
Hong Y.-R., Chen C.-H., Chang J.-H., Wang S.-K., Sy W.-D., Chou C.-K.,
Howng S.-L.;
"Cloning and characterization of a novel human ninein protein that
interacts with the glycogen synthase kinase 3beta.";
Biochim. Biophys. Acta 1492:513-516(2000).
[15]
ASSOCIATION WITH DIABETES MELLITUS.
PubMed=10868943; DOI=10.2337/diabetes.49.2.263;
Nikoulina S.E., Ciaraldi T.P., Mudaliar S., Mohideen P., Carter L.,
Henry R.R.;
"Potential role of glycogen synthase kinase-3 in skeletal muscle
insulin resistance of type 2 diabetes.";
Diabetes 49:263-271(2000).
[16]
FUNCTION, AND MUTAGENESIS OF ARG-96 AND LEU-128.
PubMed=11430833; DOI=10.1016/S1097-2765(01)00253-2;
Frame S., Cohen P., Biondi R.M.;
"A common phosphate binding site explains the unique substrate
specificity of GSK3 and its inactivation by phosphorylation.";
Mol. Cell 7:1321-1327(2001).
[17]
PHOSPHORYLATION AT SER-9 BY SGK3, AND INTERACTION WITH SGK3.
PubMed=12054501; DOI=10.1016/S0006-291X(02)00349-2;
Dai F., Yu L., He H., Chen Y., Yu J., Yang Y., Xu Y., Ling W.,
Zhao S.;
"Human serum and glucocorticoid-inducible kinase-like kinase (SGKL)
phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-
9 through direct interaction.";
Biochem. Biophys. Res. Commun. 293:1191-1196(2002).
[18]
FUNCTION IN PHOSPHORYLATION OF MAPT/TAU.
PubMed=14690523;
Cho J.H., Johnson G.V.;
"Primed phosphorylation of tau at Thr231 by glycogen synthase kinase
3beta (GSK3beta) plays a critical role in regulating tau's ability to
bind and stabilize microtubules.";
J. Neurochem. 88:349-358(2004).
[19]
FUNCTION, INTERACTION WITH SNAI1, AND SUBCELLULAR LOCATION.
PubMed=15448698; DOI=10.1038/ncb1173;
Zhou B.P., Deng J., Xia W., Xu J., Li Y.M., Gunduz M., Hung M.C.;
"Dual regulation of Snail by GSK-3beta-mediated phosphorylation in
control of epithelial-mesenchymal transition.";
Nat. Cell Biol. 6:931-940(2004).
[20]
INTERACTION WITH CABYR.
PubMed=15752768; DOI=10.1016/j.bbrc.2005.02.089;
Hsu H.-C., Lee Y.-L., Cheng T.-S., Howng S.-L., Chang L.-K., Lu P.-J.,
Hong Y.-R.;
"Characterization of two non-testis-specific CABYR variants that bind
to GSK3beta with a proline-rich extensin-like domain.";
Biochem. Biophys. Res. Commun. 329:1108-1117(2005).
[21]
FUNCTION, AND INTERACTION WITH SNAI1.
PubMed=15647282; DOI=10.1074/jbc.M413878200;
Yook J.I., Li X.Y., Ota I., Fearon E.R., Weiss S.J.;
"Wnt-dependent regulation of the E-cadherin repressor snail.";
J. Biol. Chem. 280:11740-11748(2005).
[22]
INTERACTION WITH GSKIP.
PubMed=16981698; DOI=10.1021/bi061147r;
Chou H.-Y., Howng S.-L., Cheng T.-S., Hsiao Y.-L., Lieu A.-S.,
Loh J.-K., Hwang S.-L., Lin C.-C., Hsu C.-M., Wang C., Lee C.-I.,
Lu P.-J., Chou C.-K., Huang C.-Y., Hong Y.-R.;
"GSKIP is homologous to the axin GSK3beta interaction domain and
functions as a negative regulator of GSK3beta.";
Biochemistry 45:11379-11389(2006).
[23]
INTERACTION WITH PRUNE1.
PubMed=16428445; DOI=10.1128/MCB.26.3.898-911.2006;
Kobayashi T., Hino S., Oue N., Asahara T., Zollo M., Yasui W.,
Kikuchi A.;
"Glycogen synthase kinase 3 and h-prune regulate cell migration by
modulating focal adhesions.";
Mol. Cell. Biol. 26:898-911(2006).
[24]
FUNCTION, AND PHOSPHORYLATION AT SER-9.
PubMed=16484495; DOI=10.1126/science.1121613;
Yin L., Wang J., Klein P.S., Lazar M.A.;
"Nuclear receptor Rev-erbalpha is a critical lithium-sensitive
component of the circadian clock.";
Science 311:1002-1005(2006).
[25]
INTERACTION WITH AXIN1.
PubMed=17318175; DOI=10.1038/sj.emboj.7601607;
Luo W., Peterson A., Garcia B.A., Coombs G., Kofahl B., Heinrich R.,
Shabanowitz J., Hunt D.F., Yost H.J., Virshup D.M.;
"Protein phosphatase 1 regulates assembly and function of the beta-
catenin degradation complex.";
EMBO J. 26:1511-1521(2007).
[26]
FUNCTION IN PHOSPHORYLATION OF SIK1.
PubMed=18348280; DOI=10.1002/jcb.21737;
Hashimoto Y.K., Satoh T., Okamoto M., Takemori H.;
"Importance of autophosphorylation at Ser186 in the A-loop of salt
inducible kinase 1 for its sustained kinase activity.";
J. Cell. Biochem. 104:1724-1739(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-402, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390, 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).
[29]
INTERACTION WITH MMP2.
PubMed=19493954; DOI=10.1093/cvr/cvp175;
Kandasamy A.D., Schulz R.;
"Glycogen synthase kinase-3beta is activated by matrix
metalloproteinase-2 mediated proteolysis in cardiomyoblasts.";
Cardiovasc. Res. 83:698-706(2009).
[30]
FUNCTION, AND INTERACTION WITH CLOCK-ARNTL/BMAL1.
PubMed=19946213; DOI=10.4161/cc.8.24.10273;
Spengler M.L., Kuropatwinski K.K., Schumer M., Antoch M.P.;
"A serine cluster mediates BMAL1-dependent CLOCK phosphorylation and
degradation.";
Cell Cycle 8:4138-4146(2009).
[31]
INTERACTION WITH CTNND2.
PubMed=19706605; DOI=10.1074/jbc.M109.002659;
Oh M., Kim H., Yang I., Park J.H., Cong W.T., Baek M.C., Bareiss S.,
Ki H., Lu Q., No J., Kwon I., Choi J.K., Kim K.;
"GSK-3 phosphorylates delta-catenin and negatively regulates its
stability via ubiquitination/proteosome-mediated proteolysis.";
J. Biol. Chem. 284:28579-28589(2009).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[33]
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).
[34]
ALTERNATIVE SPLICING.
PubMed=20067585; DOI=10.1111/j.1471-4159.2010.06581.x;
Castano Z., Gordon-Weeks P.R., Kypta R.M.;
"The neuron-specific isoform of glycogen synthase kinase-3beta is
required for axon growth.";
J. Neurochem. 113:117-130(2010).
[35]
FUNCTION.
PubMed=20932480; DOI=10.1016/j.molcel.2010.09.013;
Heyd F., Lynch K.W.;
"Phosphorylation-dependent regulation of PSF by GSK3 controls CD45
alternative splicing.";
Mol. Cell 40:126-137(2010).
[36]
INTERACTION WITH DAB2IP AND PPP2CA.
PubMed=20080667; DOI=10.1073/pnas.0908133107;
Xie D., Gore C., Liu J., Pong R.C., Mason R., Hao G., Long M.,
Kabbani W., Yu L., Zhang H., Chen H., Sun X., Boothman D.A., Min W.,
Hsieh J.T.;
"Role of DAB2IP in modulating epithelial-to-mesenchymal transition and
prostate cancer metastasis.";
Proc. Natl. Acad. Sci. U.S.A. 107:2485-2490(2010).
[37]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-9.
PubMed=20937854; DOI=10.1073/pnas.1000975107;
Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
"ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
plasma membrane of migrating cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
[38]
REVIEW ON FUNCTION, AND ENZYME REGULATION.
PubMed=11749387; DOI=10.1021/cr000110o;
Ali A., Hoeflich K.P., Woodgett J.R.;
"Glycogen synthase kinase-3: properties, functions, and regulation.";
Chem. Rev. 101:2527-2540(2001).
[39]
REVIEW ON FUNCTION.
PubMed=17478001; DOI=10.1016/j.diabres.2007.01.033;
Lee J., Kim M.S.;
"The role of GSK3 in glucose homeostasis and the development of
insulin resistance.";
Diabetes Res. Clin. Pract. 77:S49-S57(2007).
[40]
REVIEW ON FUNCTION, AND ENZYME REGULATION.
PubMed=19366350; DOI=10.1111/j.1476-5381.2008.00085.x;
Rayasam G.V., Tulasi V.K., Sodhi R., Davis J.A., Ray A.;
"Glycogen synthase kinase 3: more than a namesake.";
Br. J. Pharmacol. 156:885-898(2009).
[41]
INTERACTION WITH GSKIP, AND COMPLEX FORMATION WITH PRKAR2A AND GSKIP.
PubMed=20007971; DOI=10.1074/jbc.M109.047944;
Hundsrucker C., Skroblin P., Christian F., Zenn H.M., Popara V.,
Joshi M., Eichhorst J., Wiesner B., Herberg F.W., Reif B.,
Rosenthal W., Klussmann E.;
"Glycogen synthase kinase 3beta interaction protein functions as an A-
kinase anchoring protein.";
J. Biol. Chem. 285:5507-5521(2010).
[42]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[43]
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).
[44]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
PubMed=21029237; DOI=10.1111/j.1750-3639.2010.00437.x;
Bose A., Mouton-Liger F., Paquet C., Mazot P., Vigny M., Gray F.,
Hugon J.;
"Modulation of tau phosphorylation by the kinase PKR: implications in
Alzheimer's disease.";
Brain Pathol. 21:189-200(2011).
[45]
FUNCTION.
PubMed=22514281; DOI=10.1074/jbc.M111.306373;
Sun L., Lv F., Guo X., Gao G.;
"Glycogen synthase kinase 3? (GSK3?) modulates antiviral activity of
zinc-finger antiviral protein (ZAP).";
J. Biol. Chem. 287:22882-22888(2012).
[46]
ADP-RIBOSYLATION BY PARP10.
PubMed=23332125; DOI=10.1186/1478-811X-11-5;
Feijs K.L., Kleine H., Braczynski A., Forst A.H., Herzog N.,
Verheugd P., Linzen U., Kremmer E., Luscher B.;
"ARTD10 substrate identification on protein microarrays: regulation of
GSK3beta by mono-ADP-ribosylation.";
Cell Commun. Signal. 11:5-5(2013).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390, 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).
[48]
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).
[49]
FUNCTION, INTERACTION WITH NCYM, AND PHOSPHORYLATION AT SER-9.
PubMed=24391509; DOI=10.1371/journal.pgen.1003996;
Suenaga Y., Islam S.M., Alagu J., Kaneko Y., Kato M., Tanaka Y.,
Kawana H., Hossain S., Matsumoto D., Yamamoto M., Shoji W., Itami M.,
Shibata T., Nakamura Y., Ohira M., Haraguchi S., Takatori A.,
Nakagawara A.;
"NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein
that inhibits GSK3beta resulting in the stabilization of MYCN in human
neuroblastomas.";
PLoS Genet. 10:E1003996-E1003996(2014).
[50]
PHOSPHORYLATION AT SER-9 AND TYR-216, INTERACTION WITH JPT1, AND
SUBCELLULAR LOCATION.
PubMed=25169422; DOI=10.1002/jcb.24956;
Varisli L., Ozturk B.E., Akyuz G.K., Korkmaz K.S.;
"HN1 negatively influences the beta-catenin/E-cadherin interaction,
and contributes to migration in prostate cells.";
J. Cell. Biochem. 116:170-178(2015).
[51]
INTERACTION WITH GSKIP, AND COMPLEX FORMATION WITH PRKAR2B AND GSKIP.
PubMed=25920809; DOI=10.1016/j.bbamcr.2015.04.013;
Loh J.K., Lin C.C., Yang M.C., Chou C.H., Chen W.S., Hong M.C.,
Cho C.L., Hsu C.M., Cheng J.T., Chou A.K., Chang C.H., Tseng C.N.,
Wang C.H., Lieu A.S., Howng S.L., Hong Y.R.;
"GSKIP- and GSK3-mediated anchoring strengthens cAMP/PKA/Drp1 axis
signaling in the regulation of mitochondrial elongation.";
Biochim. Biophys. Acta 1853:1796-1807(2015).
[52]
INTERACTION WITH GSKIP, AND COMPLEX FORMATION WITH PRKAR2A AND GSKIP.
PubMed=27484798; DOI=10.1074/jbc.M116.738047;
Dema A., Schroeter M.F., Perets E., Skroblin P., Moutty M.C.,
Deak V.A., Birchmeier W., Klussmann E.;
"The A-Kinase Anchoring Protein (AKAP) Glycogen Synthase Kinase 3beta
Interaction Protein (GSKIP) Regulates beta-Catenin through Its
Interactions with Both Protein Kinase A (PKA) and GSK3beta.";
J. Biol. Chem. 291:19618-19630(2016).
[53]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-386.
PubMed=11440715; DOI=10.1016/S0092-8674(01)00374-9;
Dajani R., Fraser E., Roe S.M., Young N., Good V., Dale T.C.,
Pearl L.H.;
"Crystal structure of glycogen synthase kinase 3 beta: structural
basis for phosphate-primed substrate specificity and autoinhibition.";
Cell 105:721-732(2001).
[54]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 27-393 OF PHOSPHORYLATED
GSK3B.
PubMed=11738041; DOI=10.1016/S0969-2126(01)00679-7;
Bax B., Carter P.S., Lewis C., Guy A.R., Bridges A., Tanner R.,
Pettman G., Mannix C., Culbert A.A., Brown M.J.B., Smith D.G.,
Reith A.D.;
"The structure of phosphorylated GSK-3beta complexed with a peptide,
FRATtide, that inhibits beta-catenin phosphorylation.";
Structure 9:1143-1152(2001).
[55]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 35-384 IN COMPLEX WITH AXIN1,
INTERACTION WITH AXIN1 AND FRAT1, FUNCTION, ENZYME REGULATION, AND
PHOSPHORYLATION AT TYR-216.
PubMed=12554650; DOI=10.1093/emboj/cdg068;
Dajani R., Fraser E., Roe S.M., Yeo M., Good V.M., Thompson V.,
Dale T.C., Pearl L.H.;
"Structural basis for recruitment of glycogen synthase kinase 3beta to
the axin-APC scaffold complex.";
EMBO J. 22:494-501(2003).
-!- FUNCTION: Constitutively active protein kinase that acts as a
negative regulator in the hormonal control of glucose homeostasis,
Wnt signaling and regulation of transcription factors and
microtubules, by phosphorylating and inactivating glycogen
synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1,
DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires
primed phosphorylation of the majority of its substrates. In
skeletal muscle, contributes to insulin regulation of glycogen
synthesis by phosphorylating and inhibiting GYS1 activity and
hence glycogen synthesis. May also mediate the development of
insulin resistance by regulating activation of transcription
factors. Regulates protein synthesis by controlling the activity
of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as
glycogen synthase. In Wnt signaling, GSK3B forms a multimeric
complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates
the N-terminus of CTNNB1 leading to its degradation mediated by
ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its
DNA-binding domain, thereby reducing its affinity for DNA.
Phosphorylates NFATC1/NFATC on conserved serine residues promoting
NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene
regulation, and thereby opposing the action of calcineurin.
Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly
MAPT/TAU ability to bind and stabilize microtubules. MAPT/TAU is
the principal component of neurofibrillary tangles in Alzheimer
disease. Plays an important role in ERBB2-dependent stabilization
of microtubules at the cell cortex. Phosphorylates MACF1,
inhibiting its binding to microtubules which is critical for its
role in bulge stem cell migration and skin wound repair. Probably
regulates NF-kappa-B (NFKB1) at the transcriptional level and is
required for the NF-kappa-B-mediated anti-apoptotic response to
TNF-alpha (TNF/TNFA). Negatively regulates replication in
pancreatic beta-cells, resulting in apoptosis, loss of beta-cells
and diabetes. Through phosphorylation of the anti-apoptotic
protein MCL1, may control cell apoptosis in response to growth
factors deprivation. Phosphorylates MUC1 in breast cancer cells,
decreasing the interaction of MUC1 with CTNNB1/beta-catenin. Is
necessary for the establishment of neuronal polarity and axon
outgrowth. Phosphorylates MARK2, leading to inhibit its activity.
Phosphorylates SIK1 at 'Thr-182', leading to sustain its activity.
Phosphorylates ZC3HAV1 which enhances its antiviral activity.
Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination
and proteasomal degradation. Phosphorylates SFPQ at 'Thr-687' upon
T-cell activation. Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59'
and stabilizes it by protecting it from proteasomal degradation.
Regulates the circadian clock via phosphorylation of the major
clock components including ARNTL/BMAL1, CLOCK and PER2.
Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal
degradation. Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21'
and primes it for ubiquitination and proteasomal degradation.
Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively
regulates its activity. Phosphorylates MYCN in neuroblastoma cells
which may promote its degradation (PubMed:24391509).
{ECO:0000269|PubMed:11430833, ECO:0000269|PubMed:12554650,
ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15448698,
ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:16484495,
ECO:0000269|PubMed:18348280, ECO:0000269|PubMed:1846781,
ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20932480,
ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:22514281,
ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:8397507,
ECO:0000269|PubMed:9072970, ECO:0000269|PubMed:9819408}.
-!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
phosphate.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by phosphorylation at Tyr-216. In
response to insulin, inhibited by phosphorylation at Ser-9 by
PKB/AKT1 and RPS6KA3; phosphorylation at this site causes a
conformational change, preventing access of substrates to the
active site. Inhibited by lithium. {ECO:0000269|PubMed:11749387,
ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:19366350,
ECO:0000269|PubMed:8524413}.
-!- SUBUNIT: Monomer. Interacts with ARRB2, DISC1 and ZBED3 (By
similarity). Interacts with CABYR, MMP2, MUC1, NIN and PRUNE1.
Interacts with AXIN1; the interaction mediates
hyperphosphorylation of CTNNB1 leading to its ubiquitination and
destruction. Interacts with and phosphorylates SNAI1. Interacts
with DNM1L (via a C-terminal domain). Found in a complex composed
of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). Interacts
with SGK3. Interacts with DAB2IP (via C2 domain); the interaction
stimulates GSK3B kinase activation. Interacts (via C2 domain) with
PPP2CA. Interacts with the CLOCK-ARNTL/BMAL1 heterodimer.
Interacts with the ARNTL/BMAL1. Interacts with CTNND2
(PubMed:19706605). Interacts with NCYM (PubMed:24391509). The
complex composed, at least, of APC, CTNNB1 and GSK3B interacts
with JPT1; the interaction requires the inactive form of GSK3B
(phosphorylated at 'Ser-9') (PubMed:25169422). Forms a complex
composed of PRKAR2A or PRKAR2B, GSK3B and GSKIP through GSKIP
interaction; facilitates PKA-induced phosphorylation and regulates
GSK3B activity (PubMed:27484798, PubMed:20007971,
PubMed:25920809). Interacts with GSK3B; induces GSK3B-mediated
phosphorylation of GSKIP (PubMed:16981698).
{ECO:0000250|UniProtKB:Q9WV60, ECO:0000269|PubMed:11004522,
ECO:0000269|PubMed:12054501, ECO:0000269|PubMed:12554650,
ECO:0000269|PubMed:15448698, ECO:0000269|PubMed:15647282,
ECO:0000269|PubMed:15752768, ECO:0000269|PubMed:16428445,
ECO:0000269|PubMed:16981698, ECO:0000269|PubMed:17318175,
ECO:0000269|PubMed:19493954, ECO:0000269|PubMed:19706605,
ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20007971,
ECO:0000269|PubMed:20080667, ECO:0000269|PubMed:24391509,
ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:25920809,
ECO:0000269|PubMed:27484798, ECO:0000269|PubMed:9731200,
ECO:0000269|PubMed:9819408}.
-!- INTERACTION:
P31749:AKT1; NbExp=4; IntAct=EBI-373586, EBI-296087;
P31751:AKT2; NbExp=2; IntAct=EBI-373586, EBI-296058;
O15169:AXIN1; NbExp=48; IntAct=EBI-373586, EBI-710484;
O35625:Axin1 (xeno); NbExp=5; IntAct=EBI-373586, EBI-2365912;
Q14DJ8:Axin1 (xeno); NbExp=2; IntAct=EBI-373586, EBI-4312125;
Q96G01:BICD1; NbExp=7; IntAct=EBI-373586, EBI-1104509;
O75952-3:CABYR; NbExp=3; IntAct=EBI-373586, EBI-10900795;
O75952-5:CABYR; NbExp=3; IntAct=EBI-373586, EBI-10898671;
P35222:CTNNB1; NbExp=16; IntAct=EBI-373586, EBI-491549;
Q02248:Ctnnb1 (xeno); NbExp=3; IntAct=EBI-373586, EBI-397872;
Q5VWQ8:DAB2IP; NbExp=2; IntAct=EBI-373586, EBI-2871881;
Q5VWQ8-2:DAB2IP; NbExp=2; IntAct=EBI-373586, EBI-9543020;
Q9NYF0:DACT1; NbExp=3; IntAct=EBI-373586, EBI-3951744;
O75398:DEAF1; NbExp=2; IntAct=EBI-373586, EBI-718185;
Q811T9:Disc1 (xeno); NbExp=4; IntAct=EBI-373586, EBI-2298259;
Q8BMD2-1:Dzip1 (xeno); NbExp=3; IntAct=EBI-15870655, EBI-16153101;
Q13144:EIF2B5; NbExp=2; IntAct=EBI-373586, EBI-4401110;
Q92837:FRAT1; NbExp=4; IntAct=EBI-373586, EBI-3934879;
P13807:GYS1; NbExp=4; IntAct=EBI-373586, EBI-740553;
O75581:LRP6; NbExp=4; IntAct=EBI-373586, EBI-910915;
Q5S007:LRRK2; NbExp=7; IntAct=EBI-373586, EBI-5323863;
P63085:Mapk1 (xeno); NbExp=2; IntAct=EBI-373586, EBI-397697;
P10636:MAPT; NbExp=2; IntAct=EBI-373586, EBI-366182;
P10636-8:MAPT; NbExp=9; IntAct=EBI-373586, EBI-366233;
P01106:MYC; NbExp=3; IntAct=EBI-15870655, EBI-447544;
Q8N4C6:NIN; NbExp=3; IntAct=EBI-373586, EBI-1164022;
P17612:PRKACA; NbExp=5; IntAct=EBI-373586, EBI-476586;
Q01201:RELB; NbExp=4; IntAct=EBI-373586, EBI-357837;
Q15797:SMAD1; NbExp=2; IntAct=EBI-373586, EBI-1567153;
O95863:SNAI1; NbExp=5; IntAct=EBI-373586, EBI-1045459;
P37840:SNCA; NbExp=2; IntAct=EBI-373586, EBI-985879;
Q6J9G0:STYK1; NbExp=2; IntAct=EBI-373586, EBI-6424915;
P04637:TP53; NbExp=3; IntAct=EBI-373586, EBI-366083;
Q14134:TRIM29; NbExp=2; IntAct=EBI-373586, EBI-702370;
O95071:UBR5; NbExp=8; IntAct=EBI-373586, EBI-358329;
P63104:YWHAZ; NbExp=4; IntAct=EBI-373586, EBI-347088;
Q8IX07:ZFPM1; NbExp=2; IntAct=EBI-373586, EBI-3942619;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25169422}.
Nucleus. Cell membrane. Note=The phosphorylated form shows
localization to cytoplasm and cell membrane. The MEMO1-RHOA-DIAPH1
signaling pathway controls localization of the phosphorylated form
to the cell membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=GSK-3beta1;
IsoId=P49841-1; Sequence=Displayed;
Name=2; Synonyms=GSK-3beta2, neuron-specific;
IsoId=P49841-2; Sequence=VSP_004790;
Note=May play a specific role in axon growth and neurite
outgrowth. Reduced binding to AXIN1, reduced ability to
phosphorylate MAPT/TAU. {ECO:0000269|PubMed:20067585};
-!- TISSUE SPECIFICITY: Expressed in testis, thymus, prostate and
ovary and weakly expressed in lung, brain and kidney. Colocalizes
with EIF2AK2/PKR and TAU in the Alzheimer disease (AD) brain.
{ECO:0000269|PubMed:21029237}.
-!- PTM: Phosphorylated by AKT1 and ILK1. Upon insulin-mediated
signaling, the activated PKB/AKT1 protein kinase phosphorylates
and desactivates GSK3B, resulting in the dephosphorylation and
activation of GYS1. Activated by phosphorylation at Tyr-216
(PubMed:25169422). Inactivated by phosphorylation at Ser-9
(Probable). {ECO:0000269|PubMed:12054501,
ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:16484495,
ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:21029237,
ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:8250835,
ECO:0000305|PubMed:25169422}.
-!- PTM: Mono-ADP-ribosylation by PARP10 negatively regulates kinase
activity.
-!- MISCELLANEOUS: Higher expression and activity of GSK3B are found
in the skeletal muscle (vastus lateralis) of patients with type 2
diabetes (PubMed:10868943). Several potent GSK3 (GSK3A and GSK3B)
inhibitors have been identified and characterized in preclinical
models for treatments of type 2 diabetes (PubMed:19366350).
{ECO:0000305|PubMed:10868943, ECO:0000305|PubMed:19366350}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. GSK-3 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GSK3BID40761ch3q13.html";
-----------------------------------------------------------------------
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EMBL; L33801; AAA66475.1; -; mRNA.
EMBL; CH471052; EAW79533.1; -; Genomic_DNA.
EMBL; CH471052; EAW79536.1; -; Genomic_DNA.
EMBL; BC000251; AAH00251.1; -; mRNA.
EMBL; BC012760; AAH12760.1; -; mRNA.
EMBL; AF074333; AAD48517.1; -; Genomic_DNA.
EMBL; AF098789; AAC69340.1; -; Genomic_DNA.
CCDS; CCDS2996.1; -. [P49841-2]
CCDS; CCDS54628.1; -. [P49841-1]
PIR; S53324; S53324.
RefSeq; NP_001139628.1; NM_001146156.1. [P49841-1]
RefSeq; NP_002084.2; NM_002093.3. [P49841-2]
UniGene; Hs.445733; -.
PDB; 1GNG; X-ray; 2.60 A; A/B=27-393.
PDB; 1H8F; X-ray; 2.80 A; A/B=35-386.
PDB; 1I09; X-ray; 2.70 A; A/B=1-420.
PDB; 1J1B; X-ray; 1.80 A; A/B=1-420.
PDB; 1J1C; X-ray; 2.10 A; A/B=1-420.
PDB; 1O6K; X-ray; 1.70 A; C=3-12.
PDB; 1O6L; X-ray; 1.60 A; C=3-12.
PDB; 1O9U; X-ray; 2.40 A; A=35-384.
PDB; 1PYX; X-ray; 2.40 A; A/B=1-420.
PDB; 1Q3D; X-ray; 2.20 A; A/B=2-420.
PDB; 1Q3W; X-ray; 2.30 A; A/B=2-420.
PDB; 1Q41; X-ray; 2.10 A; A/B=2-420.
PDB; 1Q4L; X-ray; 2.77 A; A/B=2-420.
PDB; 1Q5K; X-ray; 1.94 A; A/B=7-420.
PDB; 1R0E; X-ray; 2.25 A; A/B=35-420.
PDB; 1UV5; X-ray; 2.80 A; A=35-384.
PDB; 2JDO; X-ray; 1.80 A; C=3-12.
PDB; 2JDR; X-ray; 2.30 A; C=3-12.
PDB; 2JLD; X-ray; 2.35 A; A/B=1-420.
PDB; 2O5K; X-ray; 3.20 A; A=29-393.
PDB; 2OW3; X-ray; 2.80 A; A/B=35-386.
PDB; 2UW9; X-ray; 2.10 A; C=3-12.
PDB; 2X39; X-ray; 1.93 A; C=3-12.
PDB; 2XH5; X-ray; 2.72 A; C=3-12.
PDB; 3CQU; X-ray; 2.20 A; C=3-12.
PDB; 3CQW; X-ray; 2.00 A; C=3-12.
PDB; 3DU8; X-ray; 2.20 A; A/B=1-420.
PDB; 3E87; X-ray; 2.30 A; C/D=3-12.
PDB; 3E88; X-ray; 2.50 A; C/D=3-12.
PDB; 3E8D; X-ray; 2.70 A; C/D=3-12.
PDB; 3F7Z; X-ray; 2.40 A; A/B=35-383.
PDB; 3F88; X-ray; 2.60 A; A/B=35-383.
PDB; 3GB2; X-ray; 2.40 A; A=34-383.
PDB; 3I4B; X-ray; 2.30 A; A/B=7-420.
PDB; 3L1S; X-ray; 2.90 A; A/B=7-420.
PDB; 3M1S; X-ray; 3.13 A; A/B=1-420.
PDB; 3MV5; X-ray; 2.47 A; C=3-12.
PDB; 3OW4; X-ray; 2.60 A; C/D=3-12.
PDB; 3PUP; X-ray; 2.99 A; A/B=1-420.
PDB; 3Q3B; X-ray; 2.70 A; A/B=2-420.
PDB; 3QKK; X-ray; 2.30 A; C=3-12.
PDB; 3SAY; X-ray; 2.23 A; A/B=1-420.
PDB; 3SD0; X-ray; 2.70 A; A/B=35-384.
PDB; 3ZDI; X-ray; 2.64 A; A=35-384.
PDB; 3ZRK; X-ray; 2.37 A; A/B=23-393.
PDB; 3ZRL; X-ray; 2.48 A; A/B=23-393.
PDB; 3ZRM; X-ray; 2.49 A; A/B=23-393.
PDB; 4ACC; X-ray; 2.21 A; A/B=1-420.
PDB; 4ACD; X-ray; 2.60 A; A/B=1-420.
PDB; 4ACG; X-ray; 2.60 A; A/B=1-420.
PDB; 4ACH; X-ray; 2.60 A; A/B=1-420.
PDB; 4AFJ; X-ray; 1.98 A; A/B=27-393.
PDB; 4B7T; X-ray; 2.77 A; A=35-384.
PDB; 4DIT; X-ray; 2.60 A; A=27-393.
PDB; 4EKK; X-ray; 2.80 A; C/D=3-12.
PDB; 4IQ6; X-ray; 3.12 A; A/B=1-420.
PDB; 4J1R; X-ray; 2.70 A; A/B/C/D=1-420.
PDB; 4J71; X-ray; 2.31 A; A/B=1-420.
PDB; 4NM0; X-ray; 2.50 A; A=1-383.
PDB; 4NM3; X-ray; 2.10 A; A=1-383.
PDB; 4NM5; X-ray; 2.30 A; A=13-383.
PDB; 4NM7; X-ray; 2.30 A; A=13-383.
PDB; 4PTC; X-ray; 2.71 A; A/B=1-420.
PDB; 4PTE; X-ray; 2.03 A; A/B=1-420.
PDB; 4PTG; X-ray; 2.36 A; A/B=1-420.
PDB; 5F94; X-ray; 2.51 A; A/B=36-385.
PDB; 5F95; X-ray; 2.52 A; A/B=36-385.
PDB; 5HLN; X-ray; 3.10 A; A/B=1-420.
PDB; 5HLP; X-ray; 2.45 A; A/B=1-420.
PDB; 5K5N; X-ray; 2.20 A; A/B=28-384.
PDBsum; 1GNG; -.
PDBsum; 1H8F; -.
PDBsum; 1I09; -.
PDBsum; 1J1B; -.
PDBsum; 1J1C; -.
PDBsum; 1O6K; -.
PDBsum; 1O6L; -.
PDBsum; 1O9U; -.
PDBsum; 1PYX; -.
PDBsum; 1Q3D; -.
PDBsum; 1Q3W; -.
PDBsum; 1Q41; -.
PDBsum; 1Q4L; -.
PDBsum; 1Q5K; -.
PDBsum; 1R0E; -.
PDBsum; 1UV5; -.
PDBsum; 2JDO; -.
PDBsum; 2JDR; -.
PDBsum; 2JLD; -.
PDBsum; 2O5K; -.
PDBsum; 2OW3; -.
PDBsum; 2UW9; -.
PDBsum; 2X39; -.
PDBsum; 2XH5; -.
PDBsum; 3CQU; -.
PDBsum; 3CQW; -.
PDBsum; 3DU8; -.
PDBsum; 3E87; -.
PDBsum; 3E88; -.
PDBsum; 3E8D; -.
PDBsum; 3F7Z; -.
PDBsum; 3F88; -.
PDBsum; 3GB2; -.
PDBsum; 3I4B; -.
PDBsum; 3L1S; -.
PDBsum; 3M1S; -.
PDBsum; 3MV5; -.
PDBsum; 3OW4; -.
PDBsum; 3PUP; -.
PDBsum; 3Q3B; -.
PDBsum; 3QKK; -.
PDBsum; 3SAY; -.
PDBsum; 3SD0; -.
PDBsum; 3ZDI; -.
PDBsum; 3ZRK; -.
PDBsum; 3ZRL; -.
PDBsum; 3ZRM; -.
PDBsum; 4ACC; -.
PDBsum; 4ACD; -.
PDBsum; 4ACG; -.
PDBsum; 4ACH; -.
PDBsum; 4AFJ; -.
PDBsum; 4B7T; -.
PDBsum; 4DIT; -.
PDBsum; 4EKK; -.
PDBsum; 4IQ6; -.
PDBsum; 4J1R; -.
PDBsum; 4J71; -.
PDBsum; 4NM0; -.
PDBsum; 4NM3; -.
PDBsum; 4NM5; -.
PDBsum; 4NM7; -.
PDBsum; 4PTC; -.
PDBsum; 4PTE; -.
PDBsum; 4PTG; -.
PDBsum; 5F94; -.
PDBsum; 5F95; -.
PDBsum; 5HLN; -.
PDBsum; 5HLP; -.
PDBsum; 5K5N; -.
DisProt; DP00385; -.
ProteinModelPortal; P49841; -.
SMR; P49841; -.
BioGrid; 109187; 294.
CORUM; P49841; -.
DIP; DIP-878N; -.
ELM; P49841; -.
IntAct; P49841; 198.
MINT; MINT-105006; -.
STRING; 9606.ENSP00000324806; -.
BindingDB; P49841; -.
ChEMBL; CHEMBL262; -.
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; DB04014; Alsterpaullone.
DrugBank; DB01793; I-5.
DrugBank; DB02052; Indirubin-3'-Monoxime.
DrugBank; DB07947; ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE.
DrugBank; DB01356; Lithium.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB02010; Staurosporine.
GuidetoPHARMACOLOGY; 2030; -.
iPTMnet; P49841; -.
PhosphoSitePlus; P49841; -.
BioMuta; GSK3B; -.
DMDM; 20455502; -.
EPD; P49841; -.
PaxDb; P49841; -.
PeptideAtlas; P49841; -.
PRIDE; P49841; -.
DNASU; 2932; -.
Ensembl; ENST00000264235; ENSP00000264235; ENSG00000082701. [P49841-1]
Ensembl; ENST00000316626; ENSP00000324806; ENSG00000082701. [P49841-2]
GeneID; 2932; -.
KEGG; hsa:2932; -.
UCSC; uc003edn.4; human. [P49841-1]
CTD; 2932; -.
DisGeNET; 2932; -.
EuPathDB; HostDB:ENSG00000082701.14; -.
GeneCards; GSK3B; -.
HGNC; HGNC:4617; GSK3B.
HPA; CAB016263; -.
HPA; HPA028017; -.
MIM; 605004; gene.
neXtProt; NX_P49841; -.
OpenTargets; ENSG00000082701; -.
PharmGKB; PA29009; -.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00520000055635; -.
HOGENOM; HOG000233017; -.
HOVERGEN; HBG014652; -.
InParanoid; P49841; -.
KO; K03083; -.
OMA; YSNGDKK; -.
OrthoDB; EOG091G099S; -.
PhylomeDB; P49841; -.
TreeFam; TF101104; -.
BRENDA; 2.7.11.26; 2681.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5339716; Misspliced GSK3beta mutants stabilize beta-catenin.
Reactome; R-HSA-5358747; S33 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358749; S37 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358751; S45 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358752; T41 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
SignaLink; P49841; -.
SIGNOR; P49841; -.
ChiTaRS; GSK3B; human.
EvolutionaryTrace; P49841; -.
GeneWiki; GSK3B; -.
GenomeRNAi; 2932; -.
PRO; PR:P49841; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000082701; -.
CleanEx; HS_GSK3B; -.
ExpressionAtlas; P49841; baseline and differential.
Genevisible; P49841; HS.
GO; GO:0030877; C:beta-catenin destruction complex; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:1990909; C:Wnt signalosome; TAS:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
GO; GO:0002039; F:p53 binding; IDA:MGI.
GO; GO:0002020; F:protease binding; IPI:ParkinsonsUK-UCL.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:BHF-UCL.
GO; GO:0004672; F:protein kinase activity; TAS:ParkinsonsUK-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:UniProtKB.
GO; GO:0050321; F:tau-protein kinase activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:1904885; P:beta-catenin destruction complex assembly; TAS:Reactome.
GO; GO:1904886; P:beta-catenin destruction complex disassembly; TAS:Reactome.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:1904646; P:cellular response to amyloid-beta; ISS:ARUK-UCL.
GO; GO:0036016; P:cellular response to interleukin-3; ISS:UniProtKB.
GO; GO:0099565; P:chemical synaptic transmission, postsynaptic; NAS:ParkinsonsUK-UCL.
GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
GO; GO:0007212; P:dopamine receptor signaling pathway; NAS:ParkinsonsUK-UCL.
GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:0006983; P:ER overload response; IDA:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISS:UniProtKB.
GO; GO:0005977; P:glycogen metabolic process; IDA:BHF-UCL.
GO; GO:0021766; P:hippocampus development; IMP:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:UniProtKB.
GO; GO:1904339; P:negative regulation of dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
GO; GO:2000466; P:negative regulation of glycogen (starch) synthase activity; TAS:UniProtKB.
GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; TAS:UniProtKB.
GO; GO:1901215; P:negative regulation of neuron death; IDA:UniProtKB.
GO; GO:0051534; P:negative regulation of NFAT protein import into nucleus; IMP:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL.
GO; GO:0031333; P:negative regulation of protein complex assembly; IMP:BHF-UCL.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISS:BHF-UCL.
GO; GO:2000077; P:negative regulation of type B pancreatic cell development; TAS:UniProtKB.
GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:BHF-UCL.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:BHF-UCL.
GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0010822; P:positive regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:1901216; P:positive regulation of neuron death; IDA:ParkinsonsUK-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IC:ParkinsonsUK-UCL.
GO; GO:0032092; P:positive regulation of protein binding; ISS:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IC:BHF-UCL.
GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
GO; GO:0071109; P:superior temporal gyrus development; IMP:BHF-UCL.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
InterPro; IPR033573; GSK3B.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24057:SF8; PTHR24057:SF8; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 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; ADP-ribosylation; Alternative splicing;
Alzheimer disease; ATP-binding; Biological rhythms;
Carbohydrate metabolism; Cell membrane; Complete proteome; Cytoplasm;
Developmental protein; Diabetes mellitus; Differentiation;
Glycogen metabolism; Kinase; Membrane; Neurogenesis;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Signal transduction inhibitor;
Transferase; Wnt signaling pathway.
CHAIN 1 420 Glycogen synthase kinase-3 beta.
/FTId=PRO_0000085980.
DOMAIN 56 340 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 62 70 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 181 181 Proton acceptor.
BINDING 85 85 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 9 9 Phosphoserine; by PKB/AKT1, RPS6KA3 and
SGK3. {ECO:0000269|PubMed:12054501,
ECO:0000269|PubMed:16484495,
ECO:0000269|PubMed:20937854,
ECO:0000269|PubMed:24391509,
ECO:0000269|PubMed:25169422,
ECO:0000269|PubMed:8250835}.
MOD_RES 216 216 Phosphotyrosine.
{ECO:0000269|PubMed:12554650,
ECO:0000269|PubMed:25169422}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WV60}.
MOD_RES 390 390 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 402 402 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
VAR_SEQ 303 303 K -> KDSSGTGHFTSGVR (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_004790.
MUTAGEN 9 9 S->A: Loss of phosphorylation; No
inhibition of activity and constitutively
active. {ECO:0000269|PubMed:7980435}.
MUTAGEN 96 96 R->A: Prevents the phosphorylation of
phosphate-primed glycogen synthase.
{ECO:0000269|PubMed:11430833}.
MUTAGEN 128 128 L->A: Abolishes activity toward AXIN1.
{ECO:0000269|PubMed:11430833}.
CONFLICT 28 28 V -> G (in Ref. 4; AAD48517).
{ECO:0000305}.
CONFLICT 350 350 L -> H (in Ref. 1; AAA66475).
{ECO:0000305}.
STRAND 10 12 {ECO:0000244|PDB:2JDO}.
STRAND 26 30 {ECO:0000244|PDB:1J1B}.
STRAND 32 34 {ECO:0000244|PDB:4NM5}.
STRAND 38 48 {ECO:0000244|PDB:1J1B}.
STRAND 52 64 {ECO:0000244|PDB:1J1B}.
STRAND 66 75 {ECO:0000244|PDB:1J1B}.
TURN 76 78 {ECO:0000244|PDB:1J1B}.
STRAND 81 88 {ECO:0000244|PDB:1J1B}.
STRAND 91 93 {ECO:0000244|PDB:1Q5K}.
HELIX 96 102 {ECO:0000244|PDB:1J1B}.
STRAND 112 120 {ECO:0000244|PDB:1J1B}.
TURN 121 124 {ECO:0000244|PDB:1J1B}.
STRAND 125 133 {ECO:0000244|PDB:1J1B}.
STRAND 136 138 {ECO:0000244|PDB:1Q5K}.
HELIX 139 148 {ECO:0000244|PDB:1J1B}.
HELIX 155 173 {ECO:0000244|PDB:1J1B}.
TURN 174 176 {ECO:0000244|PDB:1J1B}.
HELIX 184 186 {ECO:0000244|PDB:1J1B}.
STRAND 187 190 {ECO:0000244|PDB:1J1B}.
TURN 191 194 {ECO:0000244|PDB:1J1B}.
STRAND 195 198 {ECO:0000244|PDB:1J1B}.
STRAND 209 211 {ECO:0000244|PDB:4DIT}.
HELIX 220 222 {ECO:0000244|PDB:4AFJ}.
HELIX 225 228 {ECO:0000244|PDB:1J1B}.
HELIX 237 252 {ECO:0000244|PDB:1J1B}.
HELIX 262 273 {ECO:0000244|PDB:1J1B}.
HELIX 278 284 {ECO:0000244|PDB:1J1B}.
HELIX 286 288 {ECO:0000244|PDB:4NM3}.
STRAND 289 291 {ECO:0000244|PDB:4ACC}.
HELIX 301 304 {ECO:0000244|PDB:1J1B}.
HELIX 311 320 {ECO:0000244|PDB:1J1B}.
HELIX 325 327 {ECO:0000244|PDB:1J1B}.
HELIX 331 335 {ECO:0000244|PDB:1J1B}.
HELIX 338 344 {ECO:0000244|PDB:1J1B}.
STRAND 345 347 {ECO:0000244|PDB:1UV5}.
HELIX 364 367 {ECO:0000244|PDB:1J1B}.
HELIX 371 373 {ECO:0000244|PDB:1J1B}.
HELIX 374 377 {ECO:0000244|PDB:1J1B}.
TURN 380 383 {ECO:0000244|PDB:1J1B}.
SEQUENCE 420 AA; 46744 MW; 4ACC24D00CDBB9C3 CRC64;
MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK
VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG
EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR
DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV
WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP
WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF
NFTTQELSSN PPLATILIPP HARIQAAAST PTNATAASDA NTGDRGQTNN AASASASNST


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