ID GYS2_HUMAN Reviewed; 703 AA. AC P54840; A0AVD8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 09-FEB-2010, sequence version 2. DT 27-MAR-2024, entry version 189. DE RecName: Full=Glycogen [starch] synthase, liver {ECO:0000305|PubMed:9691087}; DE EC=2.4.1.11 {ECO:0000269|PubMed:1731614, ECO:0000269|PubMed:9691087}; DE AltName: Full=Glycogen synthase 2 {ECO:0000312|HGNC:HGNC:4707}; GN Name=GYS2 {ECO:0000303|PubMed:9691087, ECO:0000312|HGNC:HGNC:4707}; 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], AND VARIANT VAL-363. RC TISSUE=Liver; RX PubMed=8203908; DOI=10.1006/abbi.1994.1260; RA Nuttall F.Q., Gannon M.C., Bai G., Lee E.Y.; RT "Primary structure of human liver glycogen synthase deduced by cDNA RT cloning."; RL Arch. Biochem. Biophys. 311:443-449(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, RP VARIANTS GSD0 SER-39; PRO-339; VAL-363; ASP-446; GLN-479; PRO-483 AND RP ARG-491, AND CHARACTERIZATION OF VARIANTS GSD0 SER-39; PRO-339; VAL-363; RP ASP-446; GLN-479; PRO-483 AND ARG-491. RX PubMed=9691087; DOI=10.1172/jci2890; RA Orho M., Bosshard N.U., Buist N.R.M., Gitzelmann R., Aynsley-Green A., RA Blumel P., Gannon M.C., Nuttall F.Q., Groop L.C.; RT "Mutations in the liver glycogen synthase gene in children with RT hypoglycemia due to glycogen storage disease type 0."; RL J. Clin. Invest. 102:507-515(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-363. RC TISSUE=Liver; RA Nakabayashi H., Nakayama T.; RT "Human liver glycogen synthase cDNA."; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-363. 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 [6] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, PATHWAY, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=1731614; DOI=10.1016/0003-9861(92)90019-s; RA Westphal S.A., Nuttall F.Q.; RT "Comparative characterization of human and rat liver glycogen synthase."; RL Arch. Biochem. Biophys. 292:479-486(1992). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627 AND SER-683, 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: 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:1731614, CC ECO:0000269|PubMed:9691087}. 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:1731614, ECO:0000269|PubMed:9691087}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550; CC Evidence={ECO:0000269|PubMed:1731614, ECO:0000269|PubMed:9691087}; CC -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate CC (PubMed:1731614). Phosphorylation reduces the activity towards UDP- CC glucose (PubMed:1731614). When in the non-phosphorylated state, CC glycogen synthase does not require glucose-6-phosphate as an allosteric CC activator; when phosphorylated it does (PubMed:1731614). CC {ECO:0000269|PubMed:1731614}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.5 mM for UDP-alpha-D-glucose (UDPG) (in the absence of CC glucose-6-phosphate) (poorly and non-phosphorylated state) CC {ECO:0000269|PubMed:1731614}; CC KM=1.1 mM for UDP-alpha-D-glucose (UDPG) (in the presence of 50 uM of CC glucose-6-phosphate) (poorly or non-phosphorylated state) CC {ECO:0000269|PubMed:1731614}; CC KM=0.2 mM for UDP-alpha-D-glucose (UDPG) (in the presence of 7.2 mM CC glucose-6-phosphate) (poorly or non-phosphorylated state) CC {ECO:0000269|PubMed:1731614}; CC KM=33 mM for UDP-alpha-D-glucose (UDPG) (in the absence of CC glucose-6-phosphate) (most phosphorylated state) CC {ECO:0000269|PubMed:1731614}; CC KM=20 mM for UDP-alpha-D-glucose (UDPG) (in the presence of 70 uM of CC glucose-6-phosphate) (most phosphorylated state) CC {ECO:0000269|PubMed:1731614}; CC KM=8.9 mM for UDP-alpha-D-glucose (UDPG) (in the presence of 200 uM CC of glucose-6-phosphate) (most phosphorylated state) CC {ECO:0000269|PubMed:1731614}; CC KM=0.3 mM for UDP-alpha-D-glucose (UDPG) (in the presence of 7.2 mM CC glucose-6-phosphate) (most phosphorylated state) CC {ECO:0000269|PubMed:1731614}; CC pH dependence: CC Optimum pH is 7.5-8.5 (at 25 degrees Celsius) (non-phosphorylated CC state). Optimum pH is 8.5 (at 25 degrees Celsius) (most CC phosphorylated state). {ECO:0000269|PubMed:1731614}; CC Temperature dependence: CC Optimum temperature is 30-40 degrees Celsius. CC {ECO:0000269|PubMed:1731614}; CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000269|PubMed:1731614, ECO:0000269|PubMed:9691087}. CC -!- SUBUNIT: Part of the glycogen synthase (GS)-glycogenin complex, a CC heterooctamer composed of a tetramer of GS and 2 dimers of glycogenin, CC where each GS protomer binds to one glycogenin subunit (via glycogenin CC C-terminus); the GS tetramer may dissociate from glycogenin dimers to CC continue glycogen polymerization on its own (By similarity). May also CC form a heterooctamer complex with GYG1 (via GYG1 C-terminus) (By CC similarity). {ECO:0000250|UniProtKB:P13807, CC ECO:0000250|UniProtKB:Q8VCB3}. CC -!- TISSUE SPECIFICITY: Specifically expressed in liver (at protein level). CC {ECO:0000269|PubMed:1731614}. CC -!- PTM: Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 CC is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser- CC 645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an CC GSK3B. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the CC enzyme (By similarity). Phosphorylation at Ser-8 is not required for CC interaction with GYG1 (By similarity). Interaction with GYG1 does not CC regulate the phosphorylation at Ser-8 and Ser-641 (By similarity). CC {ECO:0000250|UniProtKB:P13807, ECO:0000250|UniProtKB:P13834, CC ECO:0000250|UniProtKB:Q8VCB3}. CC -!- DISEASE: Glycogen storage disease 0 (GSD0) [MIM:240600]: A metabolic CC disorder characterized by fasting hypoglycemia presenting in infancy or CC early childhood, high blood ketones and low alanine and lactate CC concentrations. Although feeding relieves symptoms, it often results in CC postprandial hyperglycemia and hyperlactatemia. CC {ECO:0000269|PubMed:9691087}. 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; S70004; AAB30886.1; -; mRNA. DR EMBL; AJ003087; CAA05859.1; -; Genomic_DNA. DR EMBL; AJ003088; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003089; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003090; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003091; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003092; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003093; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003094; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003095; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003096; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003097; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003098; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003099; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003100; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003101; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; AJ003102; CAA05859.1; JOINED; Genomic_DNA. DR EMBL; D29685; BAA06154.1; -; mRNA. DR EMBL; AC006559; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010197; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC022072; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC126310; AAI26311.1; -; mRNA. DR EMBL; BC126312; AAI26313.1; -; mRNA. DR CCDS; CCDS8690.1; -. DR PIR; S45686; S45686. DR RefSeq; NP_068776.2; NM_021957.3. DR AlphaFoldDB; P54840; -. DR SMR; P54840; -. DR BioGRID; 109253; 9. DR IntAct; P54840; 7. DR MINT; P54840; -. DR STRING; 9606.ENSP00000261195; -. DR BindingDB; P54840; -. DR ChEMBL; CHEMBL4523243; -. DR DrugCentral; P54840; -. DR CAZy; GT3; Glycosyltransferase Family 3. DR GlyGen; P54840; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P54840; -. DR PhosphoSitePlus; P54840; -. DR BioMuta; GYS2; -. DR DMDM; 288558811; -. DR EPD; P54840; -. DR jPOST; P54840; -. DR MassIVE; P54840; -. DR MaxQB; P54840; -. DR PaxDb; 9606-ENSP00000261195; -. DR PeptideAtlas; P54840; -. DR ProteomicsDB; 56737; -. DR Antibodypedia; 24071; 130 antibodies from 25 providers. DR DNASU; 2998; -. DR Ensembl; ENST00000261195.3; ENSP00000261195.2; ENSG00000111713.3. DR GeneID; 2998; -. DR KEGG; hsa:2998; -. DR MANE-Select; ENST00000261195.3; ENSP00000261195.2; NM_021957.4; NP_068776.2. DR UCSC; uc001rfb.3; human. DR AGR; HGNC:4707; -. DR CTD; 2998; -. DR DisGeNET; 2998; -. DR GeneCards; GYS2; -. DR HGNC; HGNC:4707; GYS2. DR HPA; ENSG00000111713; Tissue enriched (liver). DR MalaCards; GYS2; -. DR MIM; 138571; gene. DR MIM; 240600; phenotype. DR neXtProt; NX_P54840; -. DR OpenTargets; ENSG00000111713; -. DR Orphanet; 2089; Glycogen storage disease due to hepatic glycogen synthase deficiency. DR PharmGKB; PA29085; -. DR VEuPathDB; HostDB:ENSG00000111713; -. DR eggNOG; KOG3742; Eukaryota. DR GeneTree; ENSGT00390000018612; -. DR HOGENOM; CLU_015910_1_0_1; -. DR InParanoid; P54840; -. DR OMA; RMHKSNV; -. DR OrthoDB; 9432at2759; -. DR PhylomeDB; P54840; -. DR TreeFam; TF300306; -. DR PathwayCommons; P54840; -. DR Reactome; R-HSA-3322077; Glycogen synthesis. DR Reactome; R-HSA-3858516; Glycogen storage disease type 0 (liver GYS2). DR Reactome; R-HSA-3878781; Glycogen storage disease type IV (GBE1). DR SignaLink; P54840; -. DR SIGNOR; P54840; -. DR UniPathway; UPA00164; -. DR BioGRID-ORCS; 2998; 13 hits in 1147 CRISPR screens. DR ChiTaRS; GYS2; human. DR GenomeRNAi; 2998; -. DR Pharos; P54840; Tbio. DR PRO; PR:P54840; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P54840; Protein. DR Bgee; ENSG00000111713; Expressed in right lobe of liver and 40 other cell types or tissues. DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB. DR GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:UniProtKB. DR GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; TAS:Reactome. DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:UniProtKB. DR GO; GO:0009749; P:response to glucose; ISS:UniProtKB. 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:SF1; GLYCOGEN [STARCH] SYNTHASE, LIVER; 1. DR PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1. DR Pfam; PF05693; Glycogen_syn; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2. DR Genevisible; P54840; HS. PE 1: Evidence at protein level; KW Allosteric enzyme; Disease variant; Glycogen biosynthesis; KW Glycogen storage disease; Glycosyltransferase; Phosphoprotein; KW Reference proteome; Transferase. FT CHAIN 1..703 FT /note="Glycogen [starch] synthase, liver" FT /id="PRO_0000194768" FT REGION 628..703 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 658..672 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 689..703 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 40 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 205 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 211 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" 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:0000250|UniProtKB:P13807" 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:0000250|UniProtKB:P13807" 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:0000250|UniProtKB:P13807" 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:0000250|UniProtKB:P13807" 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:0000250|UniProtKB:P13807" FT BINDING 331 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 331 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" 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:0000250|UniProtKB:P13807" FT BINDING 510 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 512 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 513 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 515 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:P13807" 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:0000250|UniProtKB:P13807" 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:0000250|UniProtKB:P13807" FT MOD_RES 8 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000250|UniProtKB:P17625" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VCB3" FT MOD_RES 627 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 641 FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P13834" FT MOD_RES 645 FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P13834" FT MOD_RES 649 FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P13834" 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 683 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 39 FT /note="N -> S (in GSD0; loss of glycogen (starch) synthase FT activity; dbSNP:rs121918423)" FT /evidence="ECO:0000269|PubMed:9691087" FT /id="VAR_007860" FT VARIANT 193 FT /note="A -> T (in dbSNP:rs16924038)" FT /id="VAR_055885" FT VARIANT 339 FT /note="A -> P (in GSD0; loss of glycogen (starch) synthase FT activity; dbSNP:rs121918421)" FT /evidence="ECO:0000269|PubMed:9691087" FT /id="VAR_007861" FT VARIANT 363 FT /note="M -> V (in dbSNP:rs2306180)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8203908, ECO:0000269|PubMed:9691087, FT ECO:0000269|Ref.3" FT /id="VAR_058848" FT VARIANT 415 FT /note="D -> E (in dbSNP:rs16924002)" FT /id="VAR_055886" FT VARIANT 446 FT /note="H -> D (in GSD0; loss of glycogen (starch) synthase FT activity; dbSNP:rs121918425)" FT /evidence="ECO:0000269|PubMed:9691087" FT /id="VAR_007862" FT VARIANT 479 FT /note="P -> Q (in GSD0; loss of glycogen (starch) synthase FT activity; dbSNP:rs121918420)" FT /evidence="ECO:0000269|PubMed:9691087" FT /id="VAR_007863" FT VARIANT 483 FT /note="S -> P (in GSD0; loss of glycogen (starch) synthase FT activity; dbSNP:rs121918424)" FT /evidence="ECO:0000269|PubMed:9691087" FT /id="VAR_007864" FT VARIANT 491 FT /note="M -> R (in GSD0; loss of glycogen (starch) synthase FT activity; dbSNP:rs121918422)" FT /evidence="ECO:0000269|PubMed:9691087" FT /id="VAR_007865" FT CONFLICT 97 FT /note="K -> M (in Ref. 3; BAA06154)" FT /evidence="ECO:0000305" FT CONFLICT 178 FT /note="Q -> R (in Ref. 3; BAA06154)" FT /evidence="ECO:0000305" FT CONFLICT 186 FT /note="I -> V (in Ref. 3; BAA06154)" FT /evidence="ECO:0000305" FT CONFLICT 335..336 FT /note="SN -> FKT (in Ref. 3; BAA06154)" FT /evidence="ECO:0000305" FT CONFLICT 344 FT /note="E -> D (in Ref. 3; BAA06154)" FT /evidence="ECO:0000305" FT CONFLICT 441 FT /note="P -> A (in Ref. 3; BAA06154)" FT /evidence="ECO:0000305" FT CONFLICT 576..577 FT /note="KQ -> NM (in Ref. 3; BAA06154)" FT /evidence="ECO:0000305" FT CONFLICT 583 FT /note="I -> F (in Ref. 3; BAA06154)" FT /evidence="ECO:0000305" SQ SEQUENCE 703 AA; 80989 MW; 718F000D6D00CA4A CRC64; MLRGRSLSVT SLGGLPQWEV EELPVEELLL FEVAWEVTNK VGGIYTVIQT KAKTTADEWG ENYFLIGPYF EHNMKTQVEQ CEPVNDAVRR AVDAMNKHGC QVHFGRWLIE GSPYVVLFDI GYSAWNLDRW KGDLWEACSV GIPYHDREAN DMLIFGSLTA WFLKEVTDHA DGKYVVAQFH EWQAGIGLIL SRARKLPIAT IFTTHATLLG RYLCAANIDF YNHLDKFNID KEAGERQIYH RYCMERASVH CAHVFTTVSE ITAIEAEHML KRKPDVVTPN GLNVKKFSAV HEFQNLHAMY KARIQDFVRG HFYGHLDFDL EKTLFLFIAG RYEFSNKGAD IFLESLSRLN FLLRMHKSDI TVMVFFIMPA KTNNFNVETL KGQAVRKQLW DVAHSVKEKF GKKLYDALLR GEIPDLNDIL DRDDLTIMKR AIFSTQRQSL PPVTTHNMID DSTDPILSTI RRIGLFNNRT DRVKVILHPE FLSSTSPLLP MDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSVTTN LSGFGCFMQE HVADPTAYGI YIVDRRFRSP DDSCNQLTKF LYGFCKQSRR QRIIQRNRTE RLSDLLDWRY LGRYYQHARH LTLSRAFPDK FHVELTSPPT TEGFKYPRPS SVPPSPSGSQ ASSPQSSDVE DEVEDERYDE EEEAERDRLN IKSPFSLSHV PHGKKKLHGE YKN //