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 27-MAR-2024, entry version 218. DE RecName: Full=Glycogen [starch] synthase, muscle {ECO:0000305}; DE EC=2.4.1.11 {ECO:0000250|UniProtKB:P13834, ECO:0000305|PubMed:35835870}; DE AltName: Full=Glycogen synthase 1 {ECO:0000312|HGNC:HGNC:4706}; 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). RN [18] {ECO:0000312|PDB:7ZBN} RP STRUCTURE BY ELECTRON MICROSCOPY (2.62 ANGSTROMS) IN COMPLEX WITH GYG1, RP ACTIVITY REGULATION, SUBUNIT, AND PHOSPHORYLATION AT SER-8; SER-412; RP SER-641; SER-645; SER-652; SER-653; SER-657; SER-727 AND SER-731. RX PubMed=35690592; DOI=10.1038/s41467-022-31109-6; RA Marr L., Biswas D., Daly L.A., Browning C., Vial S.C.M., Maskell D.P., RA Hudson C., Bertrand J.A., Pollard J., Ranson N.A., Khatter H., Eyers C.E., RA Sakamoto K., Zeqiraj E.; RT "Mechanism of glycogen synthase inactivation and interaction with RT glycogenin."; RL Nat. Commun. 13:3372-3372(2022). RN [19] {ECO:0000312|PDB:7Q0B, ECO:0000312|PDB:7Q0S, ECO:0000312|PDB:7Q12, ECO:0000312|PDB:7Q13} RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH GYG1; UDP; RP ALPHA-D-GLUCOSE AND GLUCOSE-6-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, RP ACTIVITY REGULATION, PATHWAY, AND SUBUNIT. RX PubMed=35835870; DOI=10.1038/s41594-022-00799-3; RA McCorvie T.J., Loria P.M., Tu M., Han S., Shrestha L., Froese D.S., RA Ferreira I.M., Berg A.P., Yue W.W.; RT "Molecular basis for the regulation of human glycogen synthase by RT phosphorylation and glucose-6-phosphate."; RL Nat. Struct. Mol. Biol. 29:628-638(2022). CC -!- FUNCTION: Glycogen synthase participates in the glycogen biosynthetic CC process along with glycogenin and glycogen branching enzyme. Extends CC the primer composed of a few glucose units formed by glycogenin by CC adding new glucose units to it. In this context, glycogen synthase CC transfers the glycosyl residue from UDP-Glc to the non-reducing end of CC alpha-1,4-glucan. {ECO:0000269|PubMed:35835870}. 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:0000269|PubMed:35835870}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550; CC Evidence={ECO:0000269|PubMed:35835870}; CC -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate CC (PubMed:35690592, PubMed:35835870). Phosphorylation reduces enzyme CC activity by constraining a tense conformation of the tetramer through CC inter-subunit interaction (PubMed:35690592, PubMed:35835870). CC Phosphorylation reduces the activity towards UDP-glucose (By CC similarity). When in the non-phosphorylated state, glycogen synthase CC does not require glucose-6-phosphate as an allosteric activator; when CC phosphorylated it does (By similarity). {ECO:0000250|UniProtKB:P13834, CC ECO:0000250|UniProtKB:P54840, ECO:0000269|PubMed:35690592, CC ECO:0000269|PubMed:35835870}. CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000269|PubMed:35835870}. CC -!- SUBUNIT: Part of the GYS1-GYG1 complex, a heterooctamer composed of a CC tetramer of GYS1 and 2 dimers of GYG1, where each GYS1 protomer binds CC to one GYG1 subunit (via GYG1 C-terminus); the GYS1 tetramer may CC dissociate from GYG1 dimers to continue glycogen polymerization on its CC own. {ECO:0000269|PubMed:17055998, ECO:0000269|PubMed:35690592, CC ECO:0000269|PubMed:35835870}. 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 -!- TISSUE SPECIFICITY: Expressed in skeletal muscle and most other cell CC types where glycogen is present. {ECO:0000305|PubMed:2493642}. 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 (PubMed:35835870). {ECO:0000250|UniProtKB:P13834, CC ECO:0000305|PubMed:35835870}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7Q0B; EM; 3.00 A; A/B/C/D=1-737. DR PDB; 7Q0S; EM; 4.00 A; A/B/C/D=1-737. DR PDB; 7Q12; EM; 3.70 A; A/B/C/D=1-737. DR PDB; 7Q13; EM; 3.00 A; A/B/C/D=1-737. DR PDB; 7ZBN; EM; 2.62 A; A/B/C/D=1-737. DR PDB; 8CVX; EM; 3.50 A; A/B/C/D=1-634. DR PDB; 8CVY; EM; 3.60 A; A/B/C/D=1-634. DR PDB; 8CVZ; EM; 3.52 A; A/B/C/D=1-634. DR PDBsum; 7Q0B; -. DR PDBsum; 7Q0S; -. DR PDBsum; 7Q12; -. DR PDBsum; 7Q13; -. DR PDBsum; 7ZBN; -. DR PDBsum; 8CVX; -. DR PDBsum; 8CVY; -. DR PDBsum; 8CVZ; -. DR AlphaFoldDB; P13807; -. DR EMDB; EMD-13743; -. DR EMDB; EMD-13751; -. DR EMDB; EMD-13752; -. DR EMDB; EMD-13753; -. DR EMDB; EMD-14587; -. DR EMDB; EMD-27020; -. DR EMDB; EMD-27021; -. DR EMDB; EMD-27022; -. DR SMR; P13807; -. DR BioGRID; 109252; 110. DR IntAct; P13807; 80. 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 SwissPalm; P13807; -. DR BioMuta; GYS1; -. DR DMDM; 1351366; -. DR EPD; P13807; -. DR jPOST; P13807; -. DR MassIVE; P13807; -. DR MaxQB; P13807; -. DR PaxDb; 9606-ENSP00000317904; -. DR PeptideAtlas; P13807; -. DR ProteomicsDB; 52994; -. [P13807-1] DR ProteomicsDB; 52995; -. [P13807-2] DR Pumba; P13807; -. DR Antibodypedia; 3582; 498 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 AGR; HGNC:4706; -. 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; RDVRNHI; -. DR OrthoDB; 9432at2759; -. DR PhylomeDB; P13807; -. DR TreeFam; TF300306; -. DR BioCyc; MetaCyc:HS02622-MONOMER; -. 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; 106 hits in 1157 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 167 other cell types or tissues. DR ExpressionAtlas; P13807; baseline and differential. 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; EXP:Reactome. DR GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; EXP:Reactome. DR GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR CDD; cd03793; GT3_GSY2-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR008631; Glycogen_synth. DR PANTHER; PTHR10176:SF2; GLYCOGEN [STARCH] SYNTHASE, MUSCLE; 1. DR PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1. DR Pfam; PF05693; Glycogen_syn; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2. DR Genevisible; P13807; HS. PE 1: Evidence at protein level; KW 3D-structure; 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" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 205 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000305|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 211 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000305|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 291 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 292 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 294 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q12, ECO:0007744|PDB:7Q13" FT BINDING 297 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 301 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 331 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 331 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000305|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 501 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q12, ECO:0007744|PDB:7Q13" FT BINDING 510 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000305|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 512 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000305|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 513 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000305|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 515 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q13" FT BINDING 582 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q12, ECO:0007744|PDB:7Q13" FT BINDING 586 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000269|PubMed:35835870, FT ECO:0007744|PDB:7Q12, ECO:0007744|PDB:7Q13" FT MOD_RES 8 FT /note="Phosphoserine; by AMPK and PKA" FT /evidence="ECO:0000269|PubMed:35690592" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13834" FT MOD_RES 412 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:35690592, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 641 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:35690592, FT ECO:0007744|PubMed:18669648" FT MOD_RES 645 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:35690592, FT 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:0000269|PubMed:35690592" FT MOD_RES 653 FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta" FT /evidence="ECO:0000269|PubMed:35690592" FT MOD_RES 657 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:35690592" 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:0000269|PubMed:35690592, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 731 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:35690592" 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" FT TURN 16..21 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 28..32 FT /evidence="ECO:0007829|PDB:7ZBN" FT TURN 34..37 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 43..58 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 61..67 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 70..75 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 85..96 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 100..106 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:7Q0B" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 120..125 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 126..137 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 146..167 FT /evidence="ECO:0007829|PDB:7ZBN" FT TURN 169..171 FT /evidence="ECO:0007829|PDB:7Q13" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 182..194 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 197..206 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 208..216 FT /evidence="ECO:0007829|PDB:7ZBN" FT TURN 218..226 FT /evidence="ECO:0007829|PDB:8CVX" FT HELIX 229..235 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 239..250 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 253..259 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 260..269 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 294..311 FT /evidence="ECO:0007829|PDB:7ZBN" FT TURN 312..314 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 323..331 FT /evidence="ECO:0007829|PDB:7ZBN" FT TURN 334..338 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 339..355 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 361..367 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 372..375 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 377..409 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 416..419 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 422..435 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 443..448 FT /evidence="ECO:0007829|PDB:7ZBN" FT TURN 449..453 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 455..463 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 472..477 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 483..485 FT /evidence="ECO:0007829|PDB:8CVX" FT STRAND 487..490 FT /evidence="ECO:0007829|PDB:8CVX" FT HELIX 493..498 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 501..504 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 508..512 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 514..521 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 526..529 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 533..541 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 542..544 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 545..548 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 550..553 FT /evidence="ECO:0007829|PDB:7ZBN" FT STRAND 556..558 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 560..576 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 579..591 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 592..596 FT /evidence="ECO:0007829|PDB:7ZBN" FT HELIX 598..616 FT /evidence="ECO:0007829|PDB:7ZBN" FT TURN 618..620 FT /evidence="ECO:0007829|PDB:7ZBN" 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 //