ID   E9QAQ5_MOUSE            Unreviewed;       433 AA.
AC   E9QAQ5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Glycogen synthase kinase-3 beta {ECO:0000256|ARBA:ARBA00015835};
DE            EC=2.7.11.26 {ECO:0000256|ARBA:ARBA00012407};
GN   Name=Gsk3b {ECO:0000313|Ensembl:ENSMUSP00000110398.2,
GN   ECO:0000313|MGI:MGI:1861437};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000110398.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:15345747}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [2] {ECO:0007829|PubMed:17242355}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000110398.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110398.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5] {ECO:0000313|Ensembl:ENSMUSP00000110398.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110398.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC         COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC         Evidence={ECO:0000256|ARBA:ARBA00023955};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC         Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26; Evidence={ECO:0000256|ARBA:ARBA00023915};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. GSK-3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005527}.
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DR   RefSeq; NP_001334161.1; NM_001347232.1.
DR   AlphaFoldDB; E9QAQ5; -.
DR   SMR; E9QAQ5; -.
DR   IntAct; E9QAQ5; 1.
DR   SwissPalm; E9QAQ5; -.
DR   jPOST; E9QAQ5; -.
DR   MaxQB; E9QAQ5; -.
DR   PeptideAtlas; E9QAQ5; -.
DR   ProteomicsDB; 308068; -.
DR   Antibodypedia; 4266; 1850 antibodies from 53 providers.
DR   DNASU; 56637; -.
DR   Ensembl; ENSMUST00000114750.2; ENSMUSP00000110398.2; ENSMUSG00000022812.15.
DR   GeneID; 56637; -.
DR   AGR; MGI:1861437; -.
DR   CTD; 2932; -.
DR   MGI; MGI:1861437; Gsk3b.
DR   VEuPathDB; HostDB:ENSMUSG00000022812; -.
DR   GeneTree; ENSGT00520000055635; -.
DR   OrthoDB; 2872909at2759; -.
DR   PhylomeDB; E9QAQ5; -.
DR   BioGRID-ORCS; 56637; 13 hits in 81 CRISPR screens.
DR   ChiTaRS; Gsk3b; mouse.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000022812; Expressed in spermatid and 251 other cell types or tissues.
DR   ExpressionAtlas; E9QAQ5; baseline and differential.
DR   GO; GO:0030877; C:beta-catenin destruction complex; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR   GO; GO:0034452; F:dynactin binding; IEA:Ensembl.
DR   GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR   GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:Ensembl.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:Ensembl.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:1904886; P:beta-catenin destruction complex disassembly; IEA:Ensembl.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0006983; P:ER overload response; IEA:Ensembl.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:2000740; P:negative regulation of mesenchymal stem cell differentiation; IEA:Ensembl.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
DR   GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0010822; P:positive regulation of mitochondrion organization; IEA:Ensembl.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl.
DR   GO; GO:1904781; P:positive regulation of protein localization to centrosome; IEA:Ensembl.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:Ensembl.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0150101; P:regulation of microtubule anchoring at centrosome; IEA:Ensembl.
DR   GO; GO:0071109; P:superior temporal gyrus development; IEA:Ensembl.
DR   CDD; cd14137; STKc_GSK3; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR039192; STKc_GSK3.
DR   PANTHER; PTHR24057; GLYCOGEN SYNTHASE KINASE-3 ALPHA; 1.
DR   PANTHER; PTHR24057:SF8; GLYCOGEN SYNTHASE KINASE-3 BETA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteomics identification {ECO:0007829|EPD:E9QAQ5,
KW   ECO:0007829|MaxQB:E9QAQ5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   DOMAIN          56..353
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   433 AA;  47990 MW;  901D4D23D958F2D4 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
     WTKDSPGAGH FTPGVRVFRP RTPPEAIALC SRLLEYTPTA RLTPLEACAH SFFDELRDPN
     VKLPNGRDTP ALFNFTTQEL SSNPPLATIL IPPHARIQAA ASPPANATAA SDTNAGDRGQ
     TNNAASASAS NST
//