GYS1_HUMAN
ID GYS1_HUMAN Reviewed; 737 AA.
AC P13807; Q9BTT9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Glycogen [starch] synthase, muscle {ECO:0000305};
DE EC=2.4.1.11 {ECO:0000250|UniProtKB:P13834};
GN Name=GYS1 {ECO:0000312|HGNC:HGNC:4706}; Synonyms=GYS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=2493642; DOI=10.1073/pnas.86.5.1443;
RA Browner M.F., Nakano K., Bang A.G., Fletterick R.J.;
RT "Human muscle glycogen synthase cDNA sequence: a negatively charged protein
RT with an asymmetric charge distribution.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1443-1447(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT NIDDM SER-464.
RX PubMed=7657035; DOI=10.2337/diab.44.9.1099;
RA Orho M., Nikula-Ijas P., Schalin-Jantti C., Permutt M.A., Groop L.C.;
RT "Isolation and characterization of the human muscle glycogen synthase
RT gene.";
RL Diabetes 44:1099-1105(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Endometrium;
RX PubMed=9010351; DOI=10.1016/s0960-0760(96)00138-0;
RA Su X., Schuler L., Shapiro S.S.;
RT "Cloning and characterization of a glycogen synthase cDNA from human
RT endometrium.";
RL J. Steroid Biochem. Mol. Biol. 59:459-465(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, Lymph, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH GYG1.
RX PubMed=17055998; DOI=10.1016/j.abb.2006.09.024;
RA Skurat A.V., Dietrich A.D., Roach P.J.;
RT "Interaction between glycogenin and glycogen synthase.";
RL Arch. Biochem. Biophys. 456:93-97(2006).
RN [8]
RP INVOLVEMENT IN GSD0B.
RX PubMed=17928598; DOI=10.1056/nejmoa066691;
RA Kollberg G., Tulinius M., Gilljam T., Oestman-Smith I., Forsander G.,
RA Jotorp P., Oldfors A., Holme E.;
RT "Cardiomyopathy and exercise intolerance in muscle glycogen storage disease
RT 0.";
RL N. Engl. J. Med. 357:1507-1514(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-645 AND SER-649, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP DEPHOSPHORYLATION AT SER-641 AND SER-645 BY PP1.
RX PubMed=21668450; DOI=10.1111/j.1471-4159.2011.07345.x;
RA Kelsall I.R., Voss M., Munro S., Cuthbertson D.J., Cohen P.T.;
RT "R3F, a novel membrane-associated glycogen targeting subunit of protein
RT phosphatase 1 regulates glycogen synthase in astrocytoma cells in response
RT to glucose and extracellular signals.";
RL J. Neurochem. 118:596-610(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-710 AND SER-727, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND THR-700, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC reducing end of alpha-1,4-glucan. {ECO:0000250|UniProtKB:P13834}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-
CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11;
CC Evidence={ECO:0000250|UniProtKB:P13834};
CC -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate.
CC Phosphorylation reduces the activity towards UDP-glucose. When in the
CC non-phosphorylated state, glycogen synthase does not require glucose-6-
CC phosphate as an allosteric activator; when phosphorylated it does (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000250|UniProtKB:P13834}.
CC -!- SUBUNIT: Interacts with GYG1. {ECO:0000269|PubMed:17055998}.
CC -!- INTERACTION:
CC P13807; Q13155: AIMP2; NbExp=3; IntAct=EBI-740553, EBI-745226;
CC P13807; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-740553, EBI-10181188;
CC P13807; Q53HL2: CDCA8; NbExp=3; IntAct=EBI-740553, EBI-979174;
CC P13807; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-740553, EBI-12357161;
CC P13807; O43186: CRX; NbExp=3; IntAct=EBI-740553, EBI-748171;
CC P13807; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-740553, EBI-2349927;
CC P13807; Q86W67: FAM228A; NbExp=3; IntAct=EBI-740553, EBI-12958227;
CC P13807; P49841: GSK3B; NbExp=4; IntAct=EBI-740553, EBI-373586;
CC P13807; P46976: GYG1; NbExp=7; IntAct=EBI-740553, EBI-740533;
CC P13807; P46976-2: GYG1; NbExp=3; IntAct=EBI-740553, EBI-12017394;
CC P13807; P17509: HOXB6; NbExp=3; IntAct=EBI-740553, EBI-741308;
CC P13807; P31273: HOXC8; NbExp=3; IntAct=EBI-740553, EBI-1752118;
CC P13807; Q8IYA8: IHO1; NbExp=6; IntAct=EBI-740553, EBI-8638439;
CC P13807; Q0VD86: INCA1; NbExp=3; IntAct=EBI-740553, EBI-6509505;
CC P13807; Q9H079: KATNBL1; NbExp=5; IntAct=EBI-740553, EBI-715394;
CC P13807; Q13351: KLF1; NbExp=3; IntAct=EBI-740553, EBI-8284732;
CC P13807; O43474: KLF4; NbExp=5; IntAct=EBI-740553, EBI-7232405;
CC P13807; P50221: MEOX1; NbExp=3; IntAct=EBI-740553, EBI-2864512;
CC P13807; P17568: NDUFB7; NbExp=3; IntAct=EBI-740553, EBI-1246238;
CC P13807; P49585: PCYT1A; NbExp=3; IntAct=EBI-740553, EBI-2563309;
CC P13807; Q96BK5: PINX1; NbExp=3; IntAct=EBI-740553, EBI-721782;
CC P13807; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-740553, EBI-2876622;
CC P13807; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-740553, EBI-10171633;
CC P13807; Q9UQK1: PPP1R3C; NbExp=2; IntAct=EBI-740553, EBI-2506727;
CC P13807; Q5RL73: RBM48; NbExp=3; IntAct=EBI-740553, EBI-473821;
CC P13807; Q8TAD8: SNIP1; NbExp=3; IntAct=EBI-740553, EBI-749336;
CC P13807; O60504: SORBS3; NbExp=3; IntAct=EBI-740553, EBI-741237;
CC P13807; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-740553, EBI-11952651;
CC P13807; Q08117-2: TLE5; NbExp=5; IntAct=EBI-740553, EBI-11741437;
CC P13807; Q86T24: ZBTB33; NbExp=3; IntAct=EBI-740553, EBI-2515625;
CC P13807; Q9UDV6: ZNF212; NbExp=3; IntAct=EBI-740553, EBI-1640204;
CC P13807; Q5BKZ1: ZNF326; NbExp=3; IntAct=EBI-740553, EBI-2560158;
CC P13807; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-740553, EBI-17269964;
CC P13807; Q9H707: ZNF552; NbExp=3; IntAct=EBI-740553, EBI-2555731;
CC P13807; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-740553, EBI-4395669;
CC P13807; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-740553, EBI-10251462;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P13807-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13807-2; Sequence=VSP_042745;
CC -!- PTM: Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity.
CC Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is
CC required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645
CC (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By
CC similarity). Phosphorylated at Ser-641 by DYRK2, leading to
CC inactivation (By similarity). Phosphorylated at Ser-641 by PASK,
CC leading to inactivation; phosphorylation by PASK is inhibited by
CC glycogen. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the
CC enzyme. {ECO:0000250|UniProtKB:P13834}.
CC -!- DISEASE: Muscle glycogen storage disease 0 (GSD0b) [MIM:611556]:
CC Metabolic disorder characterized by fasting hypoglycemia presenting in
CC infancy or early childhood. The role of muscle glycogen is to provide
CC critical energy during bursts of activity and sustained muscle work.
CC {ECO:0000269|PubMed:17928598}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 3 family. {ECO:0000305}.
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DR EMBL; J04501; AAA88046.1; -; mRNA.
DR EMBL; Z33622; CAA83916.1; -; Genomic_DNA.
DR EMBL; Z33623; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33609; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33624; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33625; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33626; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33610; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33627; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33628; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33629; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33630; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33631; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; Z33633; CAA83916.1; JOINED; Genomic_DNA.
DR EMBL; U32573; AAB60385.1; -; mRNA.
DR EMBL; AC008687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471177; EAW52424.1; -; Genomic_DNA.
DR EMBL; BC002617; AAH02617.1; -; mRNA.
DR EMBL; BC003182; AAH03182.1; -; mRNA.
DR EMBL; BC007688; AAH07688.1; -; mRNA.
DR CCDS; CCDS12747.1; -. [P13807-1]
DR CCDS; CCDS54292.1; -. [P13807-2]
DR PIR; A32156; A32156.
DR RefSeq; NP_001155059.1; NM_001161587.1. [P13807-2]
DR RefSeq; NP_002094.2; NM_002103.4. [P13807-1]
DR AlphaFoldDB; P13807; -.
DR SMR; P13807; -.
DR BioGRID; 109252; 93.
DR IntAct; P13807; 78.
DR MINT; P13807; -.
DR STRING; 9606.ENSP00000317904; -.
DR BindingDB; P13807; -.
DR ChEMBL; CHEMBL4000; -.
DR CAZy; GT3; Glycosyltransferase Family 3.
DR GlyGen; P13807; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P13807; -.
DR PhosphoSitePlus; P13807; -.
DR BioMuta; GYS1; -.
DR DMDM; 1351366; -.
DR EPD; P13807; -.
DR jPOST; P13807; -.
DR MassIVE; P13807; -.
DR MaxQB; P13807; -.
DR PaxDb; P13807; -.
DR PeptideAtlas; P13807; -.
DR PRIDE; P13807; -.
DR ProteomicsDB; 52994; -. [P13807-1]
DR ProteomicsDB; 52995; -. [P13807-2]
DR Antibodypedia; 3582; 416 antibodies from 39 providers.
DR DNASU; 2997; -.
DR Ensembl; ENST00000263276.6; ENSP00000263276.6; ENSG00000104812.15. [P13807-2]
DR Ensembl; ENST00000323798.8; ENSP00000317904.3; ENSG00000104812.15. [P13807-1]
DR GeneID; 2997; -.
DR KEGG; hsa:2997; -.
DR MANE-Select; ENST00000323798.8; ENSP00000317904.3; NM_002103.5; NP_002094.2.
DR UCSC; uc002plp.4; human. [P13807-1]
DR CTD; 2997; -.
DR DisGeNET; 2997; -.
DR GeneCards; GYS1; -.
DR HGNC; HGNC:4706; GYS1.
DR HPA; ENSG00000104812; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; GYS1; -.
DR MIM; 138570; gene.
DR MIM; 611556; phenotype.
DR neXtProt; NX_P13807; -.
DR OpenTargets; ENSG00000104812; -.
DR Orphanet; 137625; Glycogen storage disease due to muscle and heart glycogen synthase deficiency.
DR PharmGKB; PA29084; -.
DR VEuPathDB; HostDB:ENSG00000104812; -.
DR eggNOG; KOG3742; Eukaryota.
DR GeneTree; ENSGT00390000018612; -.
DR HOGENOM; CLU_015910_1_0_1; -.
DR InParanoid; P13807; -.
DR OMA; YFFTSGR; -.
DR OrthoDB; 264593at2759; -.
DR PhylomeDB; P13807; -.
DR TreeFam; TF300306; -.
DR BioCyc; MetaCyc:HS02622-MON; -.
DR BRENDA; 2.4.1.11; 2681.
DR PathwayCommons; P13807; -.
DR Reactome; R-HSA-3322077; Glycogen synthesis.
DR Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
DR Reactome; R-HSA-3814836; Glycogen storage disease type XV (GYG1).
DR Reactome; R-HSA-3828062; Glycogen storage disease type 0 (muscle GYS1).
DR SignaLink; P13807; -.
DR SIGNOR; P13807; -.
DR UniPathway; UPA00164; -.
DR BioGRID-ORCS; 2997; 105 hits in 1077 CRISPR screens.
DR ChiTaRS; GYS1; human.
DR GenomeRNAi; 2997; -.
DR Pharos; P13807; Tchem.
DR PRO; PR:P13807; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P13807; protein.
DR Bgee; ENSG00000104812; Expressed in hindlimb stylopod muscle and 165 other tissues.
DR ExpressionAtlas; P13807; baseline and differential.
DR Genevisible; P13807; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IEA:Ensembl.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:UniProtKB.
DR GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; EXP:Reactome.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR InterPro; IPR008631; Glycogen_synth.
DR PANTHER; PTHR10176; PTHR10176; 1.
DR Pfam; PF05693; Glycogen_syn; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Alternative splicing; Diabetes mellitus;
KW Disease variant; Glycogen biosynthesis; Glycosyltransferase;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..737
FT /note="Glycogen [starch] synthase, muscle"
FT /id="PRO_0000194763"
FT REGION 634..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="Phosphoserine; by AMPK and PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1E4"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13834"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2RRU1"
FT MOD_RES 653
FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:P13834"
FT MOD_RES 657
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P13834"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13834"
FT MOD_RES 700
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 721
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1E4"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 101..164
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042745"
FT VARIANT 108
FT /note="I -> M (in dbSNP:rs5455)"
FT /id="VAR_037958"
FT VARIANT 130
FT /note="K -> E (in dbSNP:rs5456)"
FT /id="VAR_014727"
FT VARIANT 283
FT /note="N -> S (in dbSNP:rs5461)"
FT /id="VAR_014728"
FT VARIANT 359
FT /note="E -> G (in dbSNP:rs5465)"
FT /id="VAR_014729"
FT VARIANT 416
FT /note="M -> V (in dbSNP:rs5447)"
FT /id="VAR_014730"
FT VARIANT 464
FT /note="G -> S (in NIDDM; dbSNP:rs200862074)"
FT /evidence="ECO:0000269|PubMed:7657035"
FT /id="VAR_007859"
FT VARIANT 619
FT /note="E -> Q (in dbSNP:rs5450)"
FT /id="VAR_014731"
FT VARIANT 691
FT /note="P -> A (in dbSNP:rs5453)"
FT /id="VAR_014732"
FT CONFLICT 136
FT /note="T -> I (in Ref. 1; AAA88046 and 3; AAB60385)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="Missing (in Ref. 3; AAB60385)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="A -> D (in Ref. 3; AAB60385)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="S -> R (in Ref. 1; AAA88046 and 3; AAB60385)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 83786 MW; 0E321BBFDEB0BD7F CRC64;
MPLNRTLSMS SLPGLEDWED EFDLENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
NYFLVGPYTE QGVRTQVELL EAPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH
EWLAGVGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ
TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF GRKLYESLLV GSLPDMNKML
DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE
FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE
HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
LGRYYMSARH MALSKAFPEH FTYEPNEADA AQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
EDPRNGPLEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT SSTSGSKRNS VDTATSSSLS
TPSEPLSPTS SLGEERN
