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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_MOUSE             Reviewed;         490 AA.
Q2NL51;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 2.
22-NOV-2017, entry version 109.
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;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 227-490.
TISSUE=Eye;
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]
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).
[4]
FUNCTION, MUTAGENESIS OF SER-21, AND PHOSPHORYLATION AT SER-21.
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).
[5]
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).
[6]
FUNCTION IN AXON FORMATION, AND TISSUE SPECIFICITY.
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).
[7]
FUNCTION IN HEPATIC GLYCOGEN METABOLISM, AND DISRUPTION PHENOTYPE.
PubMed=17908561; DOI=10.1016/j.cmet.2007.08.013;
MacAulay K., Doble B.W., Patel S., Hansotia T., Sinclair E.M.,
Drucker D.J., Nagy A., Woodgett J.R.;
"Glycogen synthase kinase 3alpha-specific regulation of murine hepatic
glycogen metabolism.";
Cell Metab. 6:329-337(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Lung, 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).
-!- 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:15791206, ECO:0000269|PubMed:16543145,
ECO:0000269|PubMed:17391670, ECO:0000269|PubMed:17908561}.
-!- 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.
-!- SUBUNIT: Monomer. Interacts with AXIN1 and CTNNB1/beta-catenin (By
similarity). Interacts with ARRB2 (PubMed:16051150). Interacts
with CTNND2 (By similarity). {ECO:0000250|UniProtKB:P49840,
ECO:0000269|PubMed:16051150}.
-!- 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.
{ECO:0000269|PubMed:15791206}.
-!- DISRUPTION PHENOTYPE: Enhanced glucose tolerance and insulin
sensitivity, increased activity of hepatic glycogen synthase,
elevated hepatic glycogen storage and reduced fat mass.
{ECO:0000269|PubMed:17908561}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. GSK-3 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC156992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC111032; AAI11033.1; -; mRNA.
CCDS; CCDS20976.1; -.
RefSeq; NP_001026837.1; NM_001031667.1.
UniGene; Mm.491101; -.
ProteinModelPortal; Q2NL51; -.
SMR; Q2NL51; -.
BioGrid; 546781; 6.
IntAct; Q2NL51; 1.
STRING; 10090.ENSMUSP00000071654; -.
ChEMBL; CHEMBL2176843; -.
iPTMnet; Q2NL51; -.
PhosphoSitePlus; Q2NL51; -.
EPD; Q2NL51; -.
MaxQB; Q2NL51; -.
PaxDb; Q2NL51; -.
PRIDE; Q2NL51; -.
Ensembl; ENSMUST00000071739; ENSMUSP00000071654; ENSMUSG00000057177.
GeneID; 606496; -.
KEGG; mmu:606496; -.
UCSC; uc009frx.1; mouse.
CTD; 2931; -.
MGI; MGI:2152453; Gsk3a.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00520000055635; -.
HOGENOM; HOG000233017; -.
HOVERGEN; HBG014652; -.
InParanoid; Q2NL51; -.
KO; K08822; -.
OMA; FDELRCP; -.
OrthoDB; EOG091G099S; -.
PhylomeDB; Q2NL51; -.
TreeFam; TF101104; -.
PMAP-CutDB; Q2NL51; -.
PRO; PR:Q2NL51; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000057177; -.
CleanEx; MM_GSK3A; -.
ExpressionAtlas; Q2NL51; baseline and differential.
Genevisible; Q2NL51; MM.
GO; GO:0005874; C:microtubule; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:BHF-UCL.
GO; GO:0016477; P:cell migration; IGI:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
GO; GO:0036016; P:cellular response to interleukin-3; IDA:UniProtKB.
GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:UniProtKB.
GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
GO; GO:0044027; P:hypermethylation of CpG island; IMP:BHF-UCL.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IMP:BHF-UCL.
GO; GO:2000171; P:negative regulation of dendrite development; IEA:Ensembl.
GO; GO:0046325; P:negative regulation of glucose import; ISO:MGI.
GO; GO:1904227; P:negative regulation of glycogen synthase activity, transferring glucose-1-phosphate; ISO:MGI.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
GO; GO:0032007; P:negative regulation of TOR signaling; IMP:BHF-UCL.
GO; GO:0071879; P:positive regulation of adrenergic receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IMP:BHF-UCL.
GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; IMP:BHF-UCL.
GO; GO:0045823; P:positive regulation of heart contraction; IMP:BHF-UCL.
GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
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:1903955; P:positive regulation of protein targeting to mitochondrion; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; ISO:MGI.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:BHF-UCL.
GO; GO:0003073; P:regulation of systemic arterial blood pressure; IMP: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;
Acetylation; ATP-binding; Carbohydrate metabolism; Complete proteome;
Glycogen metabolism; Kinase; Neurogenesis; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Signal transduction inhibitor; Transferase; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P49840}.
CHAIN 2 490 Glycogen synthase kinase-3 alpha.
/FTId=PRO_0000280395.
DOMAIN 119 404 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:0000250|UniProtKB:P49840}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P49840}.
MOD_RES 21 21 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:15791206}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:P49840}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000250|UniProtKB:P49840}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:P49840}.
MOD_RES 279 279 Phosphotyrosine.
{ECO:0000250|UniProtKB:P18265}.
MUTAGEN 21 21 S->A: Loss of phosphorylation; No
inhibition of activity and constitutively
active. {ECO:0000269|PubMed:15791206}.
SEQUENCE 490 AA; 51661 MW; 739CDD86BBFB497B CRC64;
MSGGGPSGGG PGGSGRARTS SFAEPGGGGG GGGGGPGGSA SGPGGTGGGK ASVGAMGGGV
GASSSGGGPS GSGGGGSGGP GAGTSFPPPG VKLGRDSGKV TTVVATVGQG PERSQEVAYT
DIKVIGNGSF GVVYQARLAE TRELVAIKKV LQDKRFKNRE LQIMRKLDHC NIVRLRYFFY
SSGEKKDELY LNLVLEYVPE TVYRVARHFT KAKLITPIIY IKVYMYQLFR SLAYIHSQGV
CHRDIKPQNL LVDPDTAVLK LCDFGSAKQL VRGEPNVSYI CSRYYRAPEL IFGATDYTSS
IDVWSAGCVL AELLLGQPIF PGDSGVDQLV EIIKVLGTPT REQIREMNPN YTEFKFPQIK
AHPWTKVFKS SKTPPEAIAL CSSLLEYTPS SRLSPLEACA HSFFDELRRL GAQLPNDRPL
PPLFNFSPGE LSIQPSLNAI LIPPHLRSPA GPASPLTTSY NPSSQALTEA QTGQDWQPSD
ATTATLASSS


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