ID GYS1_YEAST Reviewed; 708 AA. AC P23337; D6VTP6; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 205. DE RecName: Full=Glycogen [starch] synthase isoform 1; DE EC=2.4.1.11 {ECO:0000269|PubMed:2123485}; GN Name=GSY1; OrderedLocusNames=YFR015C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE OF 2-17; 52-62; RP 86-105; 377-391; 593-600; 602-608 AND 660-669, CLEAVAGE OF INITIATOR RP METHIONINE, FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=YPH52; RX PubMed=2123485; DOI=10.1016/s0021-9258(17)45298-7; RA Farkas I., Hardy T.A., Depaoli-Roach A.A., Roach P.J.; RT "Isolation of the GSY1 gene encoding yeast glycogen synthase and evidence RT for the existence of a second gene."; RL J. Biol. Chem. 265:20879-20886(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=YAL6B; RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., RA Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling RT pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non- CC reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis CC of glycogen. {ECO:0000269|PubMed:2123485}. 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:2123485}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550; CC Evidence={ECO:0000269|PubMed:2123485}; CC -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate, and CC phosphorylation by a cAMP-dependent kinase. CC {ECO:0000305|PubMed:2123485}. CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000305|PubMed:2123485}. CC -!- INTERACTION: CC P23337; P27472: GSY2; NbExp=3; IntAct=EBI-8031, EBI-8036; CC -!- DEVELOPMENTAL STAGE: Activity increases just before cells entry in the CC stationary phase. {ECO:0000305|PubMed:2123485}. CC -!- INDUCTION: Synthesized in response to growth limitation. CC {ECO:0000305|PubMed:2123485}. CC -!- MISCELLANEOUS: Present with 6300 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; M60919; AAA88715.1; -; Genomic_DNA. DR EMBL; D50617; BAA09254.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12456.1; -; Genomic_DNA. DR PIR; A38326; A38326. DR RefSeq; NP_116670.1; NM_001179980.1. DR AlphaFoldDB; P23337; -. DR SMR; P23337; -. DR BioGRID; 31167; 92. DR DIP; DIP-5354N; -. DR IntAct; P23337; 13. DR MINT; P23337; -. DR STRING; 4932.YFR015C; -. DR CAZy; GT3; Glycosyltransferase Family 3. DR iPTMnet; P23337; -. DR MaxQB; P23337; -. DR PaxDb; 4932-YFR015C; -. DR PeptideAtlas; P23337; -. DR DNASU; 850569; -. DR EnsemblFungi; YFR015C_mRNA; YFR015C; YFR015C. DR GeneID; 850569; -. DR KEGG; sce:YFR015C; -. DR AGR; SGD:S000001911; -. DR SGD; S000001911; GSY1. DR VEuPathDB; FungiDB:YFR015C; -. DR eggNOG; KOG3742; Eukaryota. DR GeneTree; ENSGT00390000018612; -. DR HOGENOM; CLU_015910_1_0_1; -. DR InParanoid; P23337; -. DR OMA; RDVRNHI; -. DR OrthoDB; 9432at2759; -. DR BioCyc; YEAST:YFR015C-MONOMER; -. DR Reactome; R-SCE-3322077; Glycogen synthesis. DR UniPathway; UPA00164; -. DR BioGRID-ORCS; 850569; 1 hit in 10 CRISPR screens. DR PRO; PR:P23337; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P23337; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:SGD. DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:SGD. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR008631; Glycogen_synth. DR PANTHER; PTHR10176:SF3; GLYCOGEN [STARCH] SYNTHASE; 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; Direct protein sequencing; Glycogen biosynthesis; KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2123485" FT CHAIN 2..708 FT /note="Glycogen [starch] synthase isoform 1" FT /id="PRO_0000194773" FT REGION 687..708 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 693..708 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 20 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250" FT MOD_RES 159 FT /note="Phosphoserine" FT /evidence="ECO:0000255" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0000255" FT MOD_RES 560 FT /note="Phosphoserine" FT /evidence="ECO:0000255" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 655 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15665377, FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 660 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000255" FT MOD_RES 662 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000255" SQ SEQUENCE 708 AA; 80510 MW; 9EF2D3858529E68A CRC64; MARDLQNHLL FEVATEVTNR VGGIYSVLKS KAPVTVAQYG DNYTLLGPLN KATYESEVEK LDWEDESIFP EELLPIQKTL MSMREKGVNF VYGNWLIEGA PRVILFELDS VRHFLNEWKA DLWSLVGIPS PEHDHETNDA ILLGYVVVWF LGEVSKLDSS HAIIGHFHEW LAGVALPLCR KKRIDVVTIF TTHATLLGRY LCAAGDVDFY NNLQYFDVDQ EAGKRGIYHR YCIERAAAHT ADVFTTVSQI TALEAEHLLK RKPDGILPNG LNVVKFQAVH EFQNLHALKK DKINDFVRGH FHGCFDFDLD NTVYFFIAGR YEYKNKGADM FIESLARLNY RLKVSGSKKT VVAFLIMPAK TNSFTVEALK SQAIVKSLEN TVNEVTASIG KRIFEHTMRY PHNGLESELP TNLDELLKSS EKVLLKKRVL ALRRPYGELP PVVTHNMCDD ANDPILNQIR HVRLFNDSSD RVKVIFHPEF LNANNPILGL DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGVPSITTNV SGFGAYMEDL IETDQAKDYG IYIVDRRFKS PDESVEQLAD YMEEFVNKTR RQRINQRNRT ERLSDLLDWK RMGLEYVKAR QLGLRRAYPE QFKQLVGETI SDANMNTLAG GKKFKIARPL SVPGSPKVRS NSTVYMTPGD LGTLQDANNA DDYFNLSTNG AIDNDDDDND TSAYYEDN //