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 glucose-
CC 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=33.0 mM for UDP-alpha-D-glucose (UDPG) (in the absence of glucose-
CC 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}.
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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 Genevisible; P54840; HS.
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.
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
//
