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Glycogen synthase kinase-3 alpha (GSK-3 alpha) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3A) (EC 2.7.11.1)

 GSK3A_HUMAN             Reviewed;         483 AA.
P49840; O14959;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
20-DEC-2017, entry version 179.
RecName: Full=Glycogen synthase kinase-3 alpha;
Short=GSK-3 alpha;
EC=2.7.11.26;
AltName: Full=Serine/threonine-protein kinase GSK3A;
EC=2.7.11.1;
Name=GSK3A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Foreskin;
He X., Saint-Jeannet J.P., Woodgett J.R., Varmus H.E., Dawid I.B.;
"Glycogen synthase kinase 3 and dorsoventral patterning in Xenopus
embryos.";
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Hoshino T., Kondo K., Ishiguro K., Takashima A., Imahori K.;
"Isolation of cDNA clones for human glycogen synthase kinase 3alpha.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Pancreas;
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).
[5]
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).
[6]
ASSOCIATION WITH ALZHEIMER DISEASE, AND FUNCTION.
PubMed=12761548; DOI=10.1038/nature01640;
Phiel C.J., Wilson C.A., Lee V.M., Klein P.S.;
"GSK-3alpha regulates production of Alzheimer's disease amyloid-beta
peptides.";
Nature 423:435-439(2003).
[7]
FUNCTION IN WNT SIGNALING, AND INTERACTION WITH AXIN1 AND
CTNNB1/BETA-CATENIN.
PubMed=17229088; DOI=10.1111/j.1460-9568.2006.05243.x;
Asuni A.A., Hooper C., Reynolds C.H., Lovestone S., Anderton B.H.,
Killick R.;
"GSK3alpha exhibits beta-catenin and tau directed kinase activities
that are modulated by Wnt.";
Eur. J. Neurosci. 24:3387-3392(2006).
[8]
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).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-72, 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).
[11]
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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
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).
[14]
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).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2; SER-77 AND SER-97, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[16]
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]
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).
[18]
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).
[19]
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).
[20]
VARIANT [LARGE SCALE ANALYSIS] PHE-461.
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).
-!- 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), CTNNB1/beta-catenin, APC and AXIN1.
Requires primed phosphorylation of the majority of its substrates.
Contributes to insulin regulation of glycogen synthesis by
phosphorylating and inhibiting GYS1 activity and hence glycogen
synthesis. Regulates glycogen metabolism in liver, but not in
muscle. May also mediate the development of insulin resistance by
regulating activation of transcription factors. In Wnt signaling,
regulates the level and transcriptional activity of nuclear
CTNNB1/beta-catenin. Facilitates amyloid precursor protein (APP)
processing and the generation of APP-derived amyloid plaques found
in Alzheimer disease. May be involved in the regulation of
replication in pancreatic beta-cells. Is necessary for the
establishment of neuronal polarity and axon outgrowth. Through
phosphorylation of the anti-apoptotic protein MCL1, may control
cell apoptosis in response to growth factors deprivation.
{ECO:0000269|PubMed:12761548, ECO:0000269|PubMed:17229088}.
-!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
phosphate.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by phosphorylation at Tyr-279. In
response to insulin, inhibited by phosphorylation at Ser-21 by
PKB/AKT1; 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:19366350}.
-!- SUBUNIT: Monomer. Interacts with ARRB2 (By similarity). Interacts
with AXIN1 and CTNNB1/beta-catenin. Interacts with CTNND2
(PubMed:19706605). {ECO:0000250, ECO:0000269|PubMed:17229088,
ECO:0000269|PubMed:19706605}.
-!- INTERACTION:
O15169:AXIN1; NbExp=3; IntAct=EBI-1044067, EBI-710484;
O75398:DEAF1; NbExp=2; IntAct=EBI-1044067, EBI-718185;
Q92837:FRAT1; NbExp=3; IntAct=EBI-1044067, EBI-3934879;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-1044067, EBI-352572;
O75581:LRP6; NbExp=2; IntAct=EBI-1044067, EBI-910915;
Q8IUH5:ZDHHC17; NbExp=3; IntAct=EBI-1044067, EBI-524753;
-!- PTM: Phosphorylated by AKT1 at Ser-21: upon insulin-mediated
signaling, the activated PKB/AKT1 protein kinase phosphorylates
and desactivates GSK3A, resulting in the dephosphorylation and
activation of GYS1. Activated by phosphorylation at Tyr-279.
-!- MISCELLANEOUS: Higher expression and activity of GSK3A 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}.
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EMBL; L40027; AAA62432.1; -; mRNA.
EMBL; D63424; BAA23608.1; -; mRNA.
EMBL; AC006486; AAD11986.1; -; Genomic_DNA.
EMBL; BC027984; AAH27984.1; -; mRNA.
EMBL; BC051865; AAH51865.1; -; mRNA.
CCDS; CCDS12599.1; -.
RefSeq; NP_063937.2; NM_019884.2.
UniGene; Hs.466828; -.
PDB; 2DFM; Model; -; A=98-449.
PDBsum; 2DFM; -.
ProteinModelPortal; P49840; -.
SMR; P49840; -.
BioGrid; 109186; 72.
ELM; P49840; -.
IntAct; P49840; 43.
MINT; MINT-1688290; -.
STRING; 9606.ENSP00000222330; -.
BindingDB; P49840; -.
ChEMBL; CHEMBL2850; -.
GuidetoPHARMACOLOGY; 2029; -.
iPTMnet; P49840; -.
PhosphoSitePlus; P49840; -.
BioMuta; GSK3A; -.
DMDM; 12644292; -.
EPD; P49840; -.
MaxQB; P49840; -.
PaxDb; P49840; -.
PeptideAtlas; P49840; -.
PRIDE; P49840; -.
DNASU; 2931; -.
Ensembl; ENST00000222330; ENSP00000222330; ENSG00000105723.
Ensembl; ENST00000453535; ENSP00000412663; ENSG00000105723.
GeneID; 2931; -.
KEGG; hsa:2931; -.
UCSC; uc002otb.2; human.
CTD; 2931; -.
DisGeNET; 2931; -.
EuPathDB; HostDB:ENSG00000105723.11; -.
GeneCards; GSK3A; -.
HGNC; HGNC:4616; GSK3A.
HPA; CAB004422; -.
HPA; HPA028423; -.
MIM; 606784; gene.
neXtProt; NX_P49840; -.
OpenTargets; ENSG00000105723; -.
PharmGKB; PA29008; -.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00520000055635; -.
HOGENOM; HOG000233017; -.
HOVERGEN; HBG014652; -.
InParanoid; P49840; -.
KO; K08822; -.
OMA; FDELRCP; -.
OrthoDB; EOG091G099S; -.
PhylomeDB; P49840; -.
TreeFam; TF101104; -.
Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
SignaLink; P49840; -.
SIGNOR; P49840; -.
ChiTaRS; GSK3A; human.
GeneWiki; GSK3A; -.
GenomeRNAi; 2931; -.
PRO; PR:P49840; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105723; -.
CleanEx; HS_GSK3A; -.
ExpressionAtlas; P49840; baseline and differential.
Genevisible; P49840; HS.
GO; GO:0097440; C:apical dendrite; NAS:ARUK-UCL.
GO; GO:0030877; C:beta-catenin destruction complex; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:BHF-UCL.
GO; GO:0005874; C:microtubule; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0043025; C:neuronal cell body; NAS:ARUK-UCL.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:1990635; C:proximal dendrite; NAS:ARUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0005102; F:receptor binding; IPI:ARUK-UCL.
GO; GO:0050321; F:tau-protein kinase activity; TAS:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISS:BHF-UCL.
GO; GO:0016477; P:cell migration; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
GO; GO:0036016; P:cellular response to interleukin-3; ISS:UniProtKB.
GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0099565; P:chemical synaptic transmission, postsynaptic; NAS:ParkinsonsUK-UCL.
GO; GO:0007212; P:dopamine receptor signaling pathway; NAS:ParkinsonsUK-UCL.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISS:UniProtKB.
GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
GO; GO:0044027; P:hypermethylation of CpG island; IEA:Ensembl.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:UniProtKB.
GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISS:BHF-UCL.
GO; GO:2000171; P:negative regulation of dendrite development; IEA:Ensembl.
GO; GO:0046325; P:negative regulation of glucose import; IMP:BHF-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:1904227; P:negative regulation of glycogen synthase activity, transferring glucose-1-phosphate; IMP:BHF-UCL.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0032007; P:negative regulation of TOR signaling; ISS:BHF-UCL.
GO; GO:2000077; P:negative regulation of type B pancreatic cell development; TAS:UniProtKB.
GO; GO:0010905; P:negative regulation of UDP-glucose catabolic process; IC:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0071879; P:positive regulation of adrenergic receptor signaling pathway; ISS:BHF-UCL.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IMP:ARUK-UCL.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; ISS:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; ISS:BHF-UCL.
GO; GO:0045823; P:positive regulation of heart contraction; ISS:BHF-UCL.
GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; NAS:BHF-UCL.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; ISS:ARUK-UCL.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IEA:Ensembl.
GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISS:BHF-UCL.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
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; Acetylation; Alzheimer disease; ATP-binding;
Carbohydrate metabolism; Complete proteome; Diabetes mellitus;
Glycogen metabolism; Kinase; Neurogenesis; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Signal transduction inhibitor;
Transferase; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330}.
CHAIN 2 483 Glycogen synthase kinase-3 alpha.
/FTId=PRO_0000085978.
DOMAIN 119 403 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 125 133 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 3 83 Gly-rich.
ACT_SITE 244 244 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 148 148 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 21 21 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:Q2NL51}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 279 279 Phosphotyrosine.
{ECO:0000250|UniProtKB:P18265}.
VARIANT 109 109 Q -> E (in dbSNP:rs35978177).
/FTId=VAR_051625.
VARIANT 461 461 L -> F (in dbSNP:rs35454502).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040539.
CONFLICT 449 449 A -> S (in Ref. 1; AAA62432).
{ECO:0000305}.
SEQUENCE 483 AA; 50981 MW; F18C012C03B7D786 CRC64;
MSGGGPSGGG PGGSGRARTS SFAEPGGGGG GGGGGPGGSA SGPGGTGGGK ASVGAMGGGV
GASSSGGGPG GSGGGGSGGP GAGTSFPPPG VKLGRDSGKV TTVVATLGQG PERSQEVAYT
DIKVIGNGSF GVVYQARLAE TRELVAIKKV LQDKRFKNRE LQIMRKLDHC NIVRLRYFFY
SSGEKKDELY LNLVLEYVPE TVYRVARHFT KAKLTIPILY VKVYMYQLFR SLAYIHSQGV
CHRDIKPQNL LVDPDTAVLK LCDFGSAKQL VRGEPNVSYI CSRYYRAPEL IFGATDYTSS
IDVWSAGCVL AELLLGQPIF PGDSGVDQLV EIIKVLGTPT REQIREMNPN YTEFKFPQIK
AHPWTKVFKS RTPPEAIALC SSLLEYTPSS RLSPLEACAH SFFDELRCLG TQLPNNRPLP
PLFNFSAGEL SIQPSLNAIL IPPHLRSPAG TTTLTPSSQA LTETPTSSDW QSTDATPTLT
NSS


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