GYS2_YEAST
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 03-AUG-2022, entry version 194.
DE RecName: Full=Glycogen [starch] synthase isoform 2;
DE EC=2.4.1.11;
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 -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate, and
CC phosphorylation by a cAMP-dependent kinase.
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
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; 104.
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; P27472; -.
DR PRIDE; P27472; -.
DR TopDownProteomics; P27472; -.
DR EnsemblFungi; YLR258W_mRNA; YLR258W; YLR258W.
DR GeneID; 850962; -.
DR KEGG; sce:YLR258W; -.
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; WEACGVG; -.
DR BioCyc; YEAST:YLR258W-MON; -.
DR Reactome; R-SCE-3322077; Glycogen synthesis.
DR UniPathway; UPA00164; -.
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:0005978; P:glycogen biosynthetic process; IMP:SGD.
DR DisProt; DP02097; -.
DR InterPro; IPR008631; Glycogen_synth.
DR PANTHER; PTHR10176; PTHR10176; 1.
DR Pfam; PF05693; Glycogen_syn; 1.
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
