ID GYS2_YEAST Reviewed; 705 AA. AC P27472; D6VYQ5; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 202. DE RecName: Full=Glycogen [starch] synthase isoform 2; DE EC=2.4.1.11 {ECO:0000250|UniProtKB:P23337}; GN Name=GSY2; OrderedLocusNames=YLR258W; ORFNames=L8479.8; 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], PROTEIN SEQUENCE OF 52-62; 378-391; RP 593-600; 602-608 AND 661-670, AND PROBABLE CLEAVAGE OF INITIATOR RP METHIONINE. RC STRAIN=YPH52; RX PubMed=1908457; DOI=10.1016/s0021-9258(18)98448-6; RA Farkast I., Hardy T.A., Roach P.J., Goebl M.G.; RT "Two glycogen synthase isoforms in Saccharomyces cerevisiae are coded by RT distinct genes that are differentially controlled."; RL J. Biol. Chem. 266:15602-15607(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). 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 PROTEIN SEQUENCE OF 96-99; 236-253; 549-556; 593-600 AND 617-623. RX PubMed=2114092; DOI=10.1042/bj2680401; RA Carabaza A., Arino J., Fox J.W., Villar-Palasi C., Guinovart J.J.; RT "Purification, characterization and partial amino acid sequence of glycogen RT synthase from Saccharomyces cerevisiae."; RL Biochem. J. 268:401-407(1990). RN [5] RP PHOSPHORYLATION AT SER-655 AND THR-668. RX PubMed=9584169; DOI=10.1128/mcb.18.6.3289; RA Huang D., Moffat J., Wilson W.A., Moore L., Cheng C., Roach P.J., RA Andrews B.J.; RT "Cyclin partners determine Pho85 protein kinase substrate specificity in RT vitro and in vivo: control of glycogen biosynthesis by Pcl8 and Pcl10."; RL Mol. Cell. Biol. 18:3289-3299(1998). RN [6] RP INTERACTION WITH PCL10. RX PubMed=10490639; DOI=10.1128/mcb.19.10.7020; RA Wilson W.A., Mahrenholz A.M., Roach P.J.; RT "Substrate targeting of the yeast cyclin-dependent kinase Pho85p by the RT cyclin Pcl10p."; RL Mol. Cell. Biol. 19:7020-7030(1999). RN [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, AND RP IDENTIFICATION BY 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651, AND IDENTIFICATION BY RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467; 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651, AND IDENTIFICATION BY RP 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. 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:P23337}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550; CC Evidence={ECO:0000250|UniProtKB:P23337}; CC -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate, and CC phosphorylation by a cAMP-dependent kinase. CC {ECO:0000250|UniProtKB:P23337}. CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000250|UniProtKB:P23337}. CC -!- SUBUNIT: Interacts with PCL10. {ECO:0000269|PubMed:10490639}. CC -!- INTERACTION: CC P27472; P23337: GSY1; NbExp=3; IntAct=EBI-8036, EBI-8031; CC P27472; P27472: GSY2; NbExp=3; IntAct=EBI-8036, EBI-8036; CC -!- PTM: Phosphorylated by the cyclin-CDK PCL10-PHO85. Phosphorylation CC causes inactivation of enzyme. {ECO:0000269|PubMed:9584169}. CC -!- MISCELLANEOUS: Present with 14600 molecules/cell in log phase SD CC medium. {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; M65206; AAA88716.1; -; Genomic_DNA. DR EMBL; U17244; AAB67378.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09571.1; -; Genomic_DNA. DR PIR; S51396; S51396. DR RefSeq; NP_013359.1; NM_001182145.1. DR PDB; 3NAZ; X-ray; 3.00 A; A/B/C/D=1-705. DR PDB; 3NB0; X-ray; 2.41 A; A/B/C/D=1-705. DR PDB; 3NCH; X-ray; 2.88 A; A/B/C/D=1-705. DR PDB; 3O3C; X-ray; 3.51 A; A/B/C/D=1-705. DR PDB; 3RSZ; X-ray; 3.01 A; A/B/C/D=1-705. DR PDB; 3RT1; X-ray; 2.80 A; A/B/C/D=1-705. DR PDB; 4KQ2; X-ray; 2.95 A; A/B/C/D=1-705. DR PDB; 4KQM; X-ray; 2.77 A; A/B/C/D=1-705. DR PDB; 5SUK; X-ray; 2.88 A; A/B/C/D=1-705. DR PDB; 5SUL; X-ray; 3.30 A; A/B=1-705. DR PDB; 5UW0; X-ray; 2.73 A; A/B/C/D=1-700. DR PDB; 5UW1; X-ray; 3.26 A; A/B/C/D=1-700. DR PDB; 5UW4; X-ray; 2.98 A; A/B/C/D=1-700. DR PDB; 5UX7; X-ray; 2.69 A; A/B/C/D=1-700. DR PDB; 5VNC; X-ray; 2.98 A; A/B/C/D=1-700. DR PDB; 6U77; X-ray; 2.85 A; A/B/C/D=1-705. DR PDBsum; 3NAZ; -. DR PDBsum; 3NB0; -. DR PDBsum; 3NCH; -. DR PDBsum; 3O3C; -. DR PDBsum; 3RSZ; -. DR PDBsum; 3RT1; -. DR PDBsum; 4KQ2; -. DR PDBsum; 4KQM; -. DR PDBsum; 5SUK; -. DR PDBsum; 5SUL; -. DR PDBsum; 5UW0; -. DR PDBsum; 5UW1; -. DR PDBsum; 5UW4; -. DR PDBsum; 5UX7; -. DR PDBsum; 5VNC; -. DR PDBsum; 6U77; -. DR AlphaFoldDB; P27472; -. DR SMR; P27472; -. DR BioGRID; 31526; 114. DR DIP; DIP-1255N; -. DR IntAct; P27472; 26. DR MINT; P27472; -. DR STRING; 4932.YLR258W; -. DR CAZy; GT3; Glycosyltransferase Family 3. DR iPTMnet; P27472; -. DR MaxQB; P27472; -. DR PaxDb; 4932-YLR258W; -. DR PeptideAtlas; P27472; -. DR TopDownProteomics; P27472; -. DR EnsemblFungi; YLR258W_mRNA; YLR258W; YLR258W. DR GeneID; 850962; -. DR KEGG; sce:YLR258W; -. DR AGR; SGD:S000004248; -. DR SGD; S000004248; GSY2. DR VEuPathDB; FungiDB:YLR258W; -. DR eggNOG; KOG3742; Eukaryota. DR GeneTree; ENSGT00390000018612; -. DR HOGENOM; CLU_015910_1_0_1; -. DR InParanoid; P27472; -. DR OMA; RMHKSNV; -. DR OrthoDB; 9432at2759; -. DR BioCyc; YEAST:YLR258W-MONOMER; -. DR Reactome; R-SCE-3322077; Glycogen synthesis. DR SABIO-RK; P27472; -. DR UniPathway; UPA00164; -. DR BioGRID-ORCS; 850962; 7 hits in 10 CRISPR screens. DR EvolutionaryTrace; P27472; -. DR PRO; PR:P27472; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; P27472; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:SGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0140678; F:molecular function inhibitor activity; EXP:DisProt. DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:SGD. DR CDD; cd03793; GT3_GSY2-like; 1. DR DisProt; DP02097; -. DR Gene3D; 6.10.260.10; -; 1. 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 3D-structure; Allosteric enzyme; Direct protein sequencing; KW Glycogen biosynthesis; Glycosyltransferase; Phosphoprotein; KW Reference proteome; Transferase. FT CHAIN 1..705 FT /note="Glycogen [starch] synthase isoform 2" FT /id="PRO_0000194774" FT REGION 686..705 FT /note="Disordered" 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 467 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15665377, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 655 FT /note="Phosphoserine; by PHO85" FT /evidence="ECO:0000269|PubMed:9584169, FT ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:18407956" FT MOD_RES 661 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000255" FT MOD_RES 663 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000255" FT MOD_RES 668 FT /note="Phosphothreonine; by PHO85" FT /evidence="ECO:0000269|PubMed:9584169" FT CONFLICT 248 FT /note="S -> P (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 535 FT /note="A -> S (in Ref. 1; AAA88716)" FT /evidence="ECO:0000305" FT CONFLICT 622 FT /note="F -> FF (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 4..14 FT /evidence="ECO:0007829|PDB:3NB0" FT TURN 15..18 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 23..39 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:3NB0" FT TURN 51..53 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 54..57 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:4KQM" FT HELIX 74..84 FT /evidence="ECO:0007829|PDB:3NB0" FT TURN 85..87 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 90..97 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 102..106 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 109..114 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 115..126 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 135..157 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 160..169 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 175..181 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 187..194 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 196..201 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 209..212 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 218..224 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 228..240 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 241..248 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 249..258 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 259..261 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 264..266 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 273..276 FT /evidence="ECO:0007829|PDB:3NCH" FT HELIX 281..300 FT /evidence="ECO:0007829|PDB:3NB0" FT TURN 301..303 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 312..320 FT /evidence="ECO:0007829|PDB:3NB0" FT TURN 323..327 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 328..344 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 350..356 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 361..364 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 366..399 FT /evidence="ECO:0007829|PDB:3NB0" FT TURN 400..404 FT /evidence="ECO:0007829|PDB:4KQ2" FT STRAND 407..409 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 413..416 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 419..432 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 442..447 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 450..452 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 454..462 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 471..476 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 486..488 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 492..498 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 500..503 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 507..511 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 513..520 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 525..528 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 532..538 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 543..548 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 551..554 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 557..559 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 561..576 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 580..592 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 593..597 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 599..617 FT /evidence="ECO:0007829|PDB:3NB0" FT HELIX 619..624 FT /evidence="ECO:0007829|PDB:3NB0" FT STRAND 626..628 FT /evidence="ECO:0007829|PDB:5SUL" FT HELIX 635..638 FT /evidence="ECO:0007829|PDB:3NB0" SQ SEQUENCE 705 AA; 80079 MW; 4670D8328CEDB0D2 CRC64; MSRDLQNHLL FETATEVANR VGGIYSVLKS KAPITVAQYK DHYHLIGPLN KATYQNEVDI LDWKKPEAFS DEMRPVQHAL QTMESRGVHF VYGRWLIEGA PKVILFDLDS VRGYSNEWKG DLWSLVGIPS PENDFETNDA ILLGYTVAWF LGEVAHLDSQ HAIVAHFHEW LAGVALPLCR KRRIDVVTIF TTHATLLGRY LCASGSFDFY NCLESVDVDH EAGRFGIYHR YCIERAAAHS ADVFTTVSQI TAFEAEHLLK RKPDGILPNG LNVIKFQAFH EFQNLHALKK EKINDFVRGH FHGCFDFDLD NTLYFFIAGR YEYKNKGADM FIEALARLNY RLKVSGSKKT VVAFIVMPAK NNSFTVEALK GQAEVRALEN TVHEVTTSIG KRIFDHAIRY PHNGLTTELP TDLGELLKSS DKVMLKRRIL ALRRPEGQLP PIVTHNMVDD ANDLILNKIR QVQLFNSPSD RVKMIFHPEF LNANNPILGL DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGVPSITTNV SGFGAYMEDL IETNQAKDYG IYIVDRRFKA PDESVEQLVD YMEEFVKKTR RQRINQRNRT ERLSDLLDWK RMGLEYVKAR QLALRRGYPD QFRELVGEEL NDSNMDALAG GKKLKVARPL SVPGSPRDLR SNSTVYMTPG DLGTLQEVNN ADDYFSLGVN PAADDDDDGP YADDS //