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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_MOUSE             Reviewed;         420 AA.
Q9WV60;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 2.
27-SEP-2017, entry version 184.
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;
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].
TISSUE=Testis;
Salameh W.A., Guo T.B., Chan K.C., Mitchell A.P.;
"Testicular expression and hormonal control of glycogen synthase
kinase 3, a homologue of yeast RIM11.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
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).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10894547; DOI=10.1038/35017574;
Hoeflich K.P., Luo J., Rubie E.A., Tsao M.S., Jin O., Woodgett J.R.;
"Requirement for glycogen synthase kinase-3beta in cell survival and
NF-kappaB activation.";
Nature 406:86-90(2000).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[5]
INTERACTION WITH ARRB2.
PubMed=16051150; DOI=10.1016/j.cell.2005.05.012;
Beaulieu J.-M., Sotnikova T.D., Marion S., Lefkowitz R.J.,
Gainetdinov R.R., Caron M.G.;
"An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic
neurotransmission and behavior.";
Cell 122:261-273(2005).
[6]
FUNCTION, AND MUTAGENESIS OF SER-9.
PubMed=15791206; DOI=10.1038/sj.emboj.7600633;
McManus E.J., Sakamoto K., Armit L.J., Ronaldson L., Shpiro N.,
Marquez R., Alessi D.R.;
"Role that phosphorylation of GSK3 plays in insulin and Wnt signalling
defined by knockin analysis.";
EMBO J. 24:1571-1583(2005).
[7]
FUNCTION IN MCL1 PHOSPHORYLATION.
PubMed=16543145; DOI=10.1016/j.molcel.2006.02.009;
Maurer U., Charvet C., Wagman A.S., Dejardin E., Green D.R.;
"Glycogen synthase kinase-3 regulates mitochondrial outer membrane
permeabilization and apoptosis by destabilization of MCL-1.";
Mol. Cell 21:749-760(2006).
[8]
FUNCTION IN AXON FORMATION.
PubMed=17391670; DOI=10.1016/j.febslet.2007.03.018;
Garrido J.J., Simon D., Varea O., Wandosell F.;
"GSK3 alpha and GSK3 beta are necessary for axon formation.";
FEBS Lett. 581:1579-1586(2007).
[9]
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).
[10]
FUNCTION IN REGULATION OF PANCREATIC BETA-CELLS.
PubMed=18288891; DOI=10.1371/journal.pbio.0060037;
Tanabe K., Liu Z., Patel S., Doble B.W., Li L., Cras-Meneur C.,
Martinez S.C., Welling C.M., White M.F., Bernal-Mizrachi E.,
Woodgett J.R., Permutt M.A.;
"Genetic deficiency of glycogen synthase kinase-3beta corrects
diabetes in mouse models of insulin resistance.";
PLoS Biol. 6:E37-E37(2008).
[11]
INTERACTION WITH DISC1.
PubMed=19303846; DOI=10.1016/j.cell.2008.12.044;
Mao Y., Ge X., Frank C.L., Madison J.M., Koehler A.N., Doud M.K.,
Tassa C., Berry E.M., Soda T., Singh K.K., Biechele T.,
Petryshen T.L., Moon R.T., Haggarty S.J., Tsai L.H.;
"Disrupted in schizophrenia 1 regulates neuronal progenitor
proliferation via modulation of GSK3beta/beta-catenin signaling.";
Cell 136:1017-1031(2009).
[12]
INTERACTION WITH AXIN1 AND ZBED3, AND MUTAGENESIS OF LYS-85.
PubMed=19141611; DOI=10.1074/jbc.M807753200;
Chen T., Li M., Ding Y., Zhang L.S., Xi Y., Pan W.J., Tao D.L.,
Wang J.Y., Li L.;
"Identification of zinc-finger BED domain-containing 3 (Zbed3) as a
novel Axin-interacting protein that activates Wnt/beta-catenin
signaling.";
J. Biol. Chem. 284:6683-6689(2009).
[13]
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).
[14]
FUNCTION.
PubMed=20123978; DOI=10.1128/MCB.01047-09;
Kurabayashi N., Hirota T., Sakai M., Sanada K., Fukada Y.;
"DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism
directing proteasomal degradation of CRY2 for circadian timekeeping.";
Mol. Cell. Biol. 30:1757-1768(2010).
[15]
FUNCTION, AND INTERACTION WITH ARNTL/BMAL1.
PubMed=20049328; DOI=10.1371/journal.pone.0008561;
Sahar S., Zocchi L., Kinoshita C., Borrelli E., Sassone-Corsi P.;
"Regulation of BMAL1 protein stability and circadian function by
GSK3beta-mediated phosphorylation.";
PLoS ONE 5:E8561-E8561(2010).
[16]
FUNCTION.
PubMed=21295697; DOI=10.1016/j.cell.2010.12.033;
Wu X., Shen Q.T., Oristian D.S., Lu C.P., Zheng Q., Wang H.W.,
Fuchs E.;
"Skin stem cells orchestrate directional migration by regulating
microtubule-ACF7 connections through GSK3beta.";
Cell 144:341-352(2011).
[17]
FUNCTION IN PHOSPHORYLATION OF DPYSL2, PHOSPHORYLATION AT SER-9, AND
MUTAGENESIS OF SER-9.
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).
[18]
FUNCTION, AND PHOSPHORYLATION AT SER-9.
PubMed=23395175; DOI=10.1016/j.cmet.2012.12.017;
Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K.,
Kissel H., Burlingame A.L., Shokat K.M., Ptacek L.J., Fu Y.H.;
"Glucose sensor O-GlcNAcylation coordinates with phosphorylation to
regulate circadian clock.";
Cell Metab. 17:291-302(2013).
-!- 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. 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. 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 SFPQ at 'Thr-679' upon T-cell activation.
Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination
and proteasomal degradation. 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. {ECO:0000269|PubMed:10894547,
ECO:0000269|PubMed:15791206, ECO:0000269|PubMed:16543145,
ECO:0000269|PubMed:17391670, ECO:0000269|PubMed:18288891,
ECO:0000269|PubMed:20049328, ECO:0000269|PubMed:20123978,
ECO:0000269|PubMed:21295697, ECO:0000269|PubMed:22057101,
ECO:0000269|PubMed:23395175}.
-!- 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.
-!- SUBUNIT: Monomer. Interacts with DAB2IP (via C2 domain); the
interaction stimulates GSK3B kinase activation. Interacts (via C2
domain) with PPP2CA (By similarity). Interacts with CABYR, MMP2,
MUC1, NIN and PRUNE1 (By similarity). 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) (By
similarity). Interacts with ARRB2 and DISC1. Found in a complex
composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity).
Interacts with SGK3. Interacts with the CLOCK-ARNTL/BMAL1
heterodimer (By similarity). Interacts with AXIN1 and ZBED3.
Interacts with the ARNTL/BMAL1. 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')
(By similarity). {ECO:0000250|UniProtKB:P49841,
ECO:0000269|PubMed:16051150, ECO:0000269|PubMed:19141611,
ECO:0000269|PubMed:19303846, ECO:0000269|PubMed:20049328}.
-!- INTERACTION:
Q02248:Ctnnb1; NbExp=2; IntAct=EBI-400793, EBI-397872;
Q9WUA5:Epm2a; NbExp=2; IntAct=EBI-400793, EBI-1040928;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Cell membrane {ECO:0000250}. 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 (By
similarity). {ECO:0000250}.
-!- 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.
Phosphorylation of Ser-9 in the hippocampus peaks at CT0, whereas
in the liver it peaks at CT12. Inactivated by phosphorylation at
Ser-9 (By similarity). {ECO:0000250|UniProtKB:P49841,
ECO:0000269|PubMed:22057101, ECO:0000269|PubMed:23395175}.
-!- PTM: Mono-ADP-ribosylation by PARP10 negatively regulates kinase
activity. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality at E16 due to hepatocyte
apoptosis. {ECO:0000269|PubMed:10894547}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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EMBL; AF156099; AAD39258.2; -; mRNA.
EMBL; BC006936; AAH06936.1; -; mRNA.
EMBL; BC060743; AAH60743.1; -; mRNA.
CCDS; CCDS28163.1; -.
RefSeq; NP_062801.1; NM_019827.6.
UniGene; Mm.394930; -.
PDB; 4NU1; X-ray; 2.50 A; A=1-383.
PDB; 5AIR; X-ray; 2.53 A; A/B=4-420.
PDBsum; 4NU1; -.
PDBsum; 5AIR; -.
ProteinModelPortal; Q9WV60; -.
SMR; Q9WV60; -.
BioGrid; 208115; 60.
CORUM; Q9WV60; -.
DIP; DIP-32446N; -.
ELM; Q9WV60; -.
IntAct; Q9WV60; 46.
MINT; MINT-4096935; -.
STRING; 10090.ENSMUSP00000023507; -.
BindingDB; Q9WV60; -.
ChEMBL; CHEMBL1075321; -.
iPTMnet; Q9WV60; -.
PhosphoSitePlus; Q9WV60; -.
EPD; Q9WV60; -.
MaxQB; Q9WV60; -.
PaxDb; Q9WV60; -.
PRIDE; Q9WV60; -.
Ensembl; ENSMUST00000023507; ENSMUSP00000023507; ENSMUSG00000022812.
GeneID; 56637; -.
UCSC; uc007zen.1; mouse.
CTD; 2932; -.
MGI; MGI:1861437; Gsk3b.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00520000055635; -.
HOGENOM; HOG000233017; -.
HOVERGEN; HBG014652; -.
InParanoid; Q9WV60; -.
PhylomeDB; Q9WV60; -.
TreeFam; TF101104; -.
BRENDA; 2.7.11.26; 3474.
Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-MMU-69229; Ubiquitin-dependent degradation of Cyclin D1.
ChiTaRS; Gsk3b; mouse.
PMAP-CutDB; Q9WV60; -.
PRO; PR:Q9WV60; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022812; -.
CleanEx; MM_GSK3B; -.
ExpressionAtlas; Q9WV60; baseline and differential.
Genevisible; Q9WV60; MM.
GO; GO:0030877; C:beta-catenin destruction complex; IDA:MGI.
GO; GO:0044297; C:cell body; IDA:MGI.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0043198; C:dendritic shaft; IDA:MGI.
GO; GO:0030426; C:growth cone; IDA:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0043227; C:membrane-bounded organelle; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density of dendrite; IDA:MGI.
GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
GO; GO:0070840; F:dynein complex binding; IPI:CAFA.
GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0050321; F:tau-protein kinase activity; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0007409; P:axonogenesis; IGI:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
GO; GO:0044337; P:canonical Wnt signaling pathway involved in positive regulation of apoptotic process; IMP:BHF-UCL.
GO; GO:0016477; P:cell migration; IGI:MGI.
GO; GO:0008283; P:cell proliferation; TAS:MGI.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI.
GO; GO:0036016; P:cellular response to interleukin-3; IDA:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0006983; P:ER overload response; IDA:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:UniProtKB.
GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
GO; GO:0005977; P:glycogen metabolic process; ISO:MGI.
GO; GO:0021766; P:hippocampus development; ISO:MGI.
GO; GO:0044027; P:hypermethylation of CpG island; IMP:BHF-UCL.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:CAFA.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IDA:CACAO.
GO; GO:0007520; P:myoblast fusion; IDA:MGI.
GO; GO:0014902; P:myotube differentiation; IGI:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IDA:MGI.
GO; GO:0014043; P:negative regulation of neuron maturation; IGI:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:MGI.
GO; GO:0051534; P:negative regulation of NFAT protein import into nucleus; ISS:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:0031333; P:negative regulation of protein complex assembly; ISO:MGI.
GO; GO:1904780; P:negative regulation of protein localization to centrosome; IMP:CAFA.
GO; GO:0032007; P:negative regulation of TOR signaling; IGI:BHF-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0016310; P:phosphorylation; IMP:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IGI:BHF-UCL.
GO; GO:0045773; P:positive regulation of axon extension; IGI:MGI.
GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IMP:BHF-UCL.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0010822; P:positive regulation of mitochondrion organization; ISO:MGI.
GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IGI:MGI.
GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
GO; GO:0031334; P:positive regulation of protein complex assembly; ISO:MGI.
GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:MGI.
GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
GO; GO:0035372; P:protein localization to microtubule; IGI:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0000320; P:re-entry into mitotic cell cycle; IDA:MGI.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:BHF-UCL.
GO; GO:0032886; P:regulation of microtubule-based process; IDA:UniProtKB.
GO; GO:0010975; P:regulation of neuron projection development; IGI:MGI.
GO; GO:0071109; P:superior temporal gyrus development; ISO:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IGI:MGI.
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:SF26; PTHR24057:SF26; 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; ATP-binding; Biological rhythms;
Carbohydrate metabolism; Cell membrane; Complete proteome; Cytoplasm;
Developmental protein; 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_0000085981.
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. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 85 85 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 9 9 Phosphoserine; by PKB/AKT1, RPS6KA3 and
SGK3. {ECO:0000269|PubMed:22057101,
ECO:0000269|PubMed:23395175}.
MOD_RES 216 216 Phosphotyrosine.
{ECO:0000250|UniProtKB:P49841}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000244|PubMed:15345747}.
MUTAGEN 9 9 S->A: Loss of phosphorylation; No
inhibition of activity and constitutively
active. {ECO:0000269|PubMed:15791206,
ECO:0000269|PubMed:22057101}.
MUTAGEN 85 85 K->R: Inhibits interaction with AXIN1 and
ZBED3. {ECO:0000269|PubMed:19141611}.
STRAND 27 29 {ECO:0000244|PDB:5AIR}.
STRAND 38 48 {ECO:0000244|PDB:4NU1}.
STRAND 52 64 {ECO:0000244|PDB:4NU1}.
STRAND 69 75 {ECO:0000244|PDB:4NU1}.
TURN 76 78 {ECO:0000244|PDB:4NU1}.
STRAND 81 88 {ECO:0000244|PDB:4NU1}.
HELIX 97 101 {ECO:0000244|PDB:4NU1}.
STRAND 112 118 {ECO:0000244|PDB:4NU1}.
STRAND 121 124 {ECO:0000244|PDB:5AIR}.
STRAND 127 133 {ECO:0000244|PDB:4NU1}.
HELIX 139 148 {ECO:0000244|PDB:4NU1}.
HELIX 155 173 {ECO:0000244|PDB:4NU1}.
TURN 174 176 {ECO:0000244|PDB:4NU1}.
HELIX 184 186 {ECO:0000244|PDB:4NU1}.
STRAND 187 190 {ECO:0000244|PDB:4NU1}.
TURN 191 194 {ECO:0000244|PDB:4NU1}.
STRAND 195 198 {ECO:0000244|PDB:4NU1}.
HELIX 201 203 {ECO:0000244|PDB:5AIR}.
HELIX 220 222 {ECO:0000244|PDB:5AIR}.
HELIX 225 228 {ECO:0000244|PDB:4NU1}.
HELIX 237 252 {ECO:0000244|PDB:4NU1}.
HELIX 262 273 {ECO:0000244|PDB:4NU1}.
HELIX 278 284 {ECO:0000244|PDB:4NU1}.
HELIX 286 288 {ECO:0000244|PDB:4NU1}.
HELIX 301 304 {ECO:0000244|PDB:4NU1}.
HELIX 311 320 {ECO:0000244|PDB:4NU1}.
HELIX 325 327 {ECO:0000244|PDB:4NU1}.
HELIX 331 335 {ECO:0000244|PDB:4NU1}.
HELIX 338 340 {ECO:0000244|PDB:4NU1}.
HELIX 341 344 {ECO:0000244|PDB:4NU1}.
TURN 364 367 {ECO:0000244|PDB:4NU1}.
HELIX 371 373 {ECO:0000244|PDB:4NU1}.
HELIX 374 377 {ECO:0000244|PDB:4NU1}.
HELIX 380 382 {ECO:0000244|PDB:4NU1}.
SEQUENCE 420 AA; 46710 MW; 200C3FD1B38B4883 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 HARIQAAASP PANATAASDT NAGDRGQTNN AASASASNST


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