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Database: UniProt/SWISS-PROT
Entry: GYS1_YEAST
LinkDB: GYS1_YEAST
Original site: GYS1_YEAST 
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   12-SEP-2018, entry version 176.
DE   RecName: Full=Glycogen [starch] synthase isoform 1;
DE            EC=2.4.1.11;
GN   Name=GSY1; OrderedLocusNames=YFR015C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE OF 2-17;
RP   52-62; 86-105; 377-391; 593-600; 602-608 AND 660-669, AND CLEAVAGE OF
RP   INITIATOR METHIONINE.
RC   STRAIN=YPH52;
RX   PubMed=2123485;
RA   Farkas I., Hardy T.A., Depaoli-Roach A.A., Roach P.J.;
RT   "Isolation of the GSY1 gene encoding yeast glycogen synthase and
RT   evidence 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.,
RA   Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K.,
RA   Yamazaki M., Tashiro H., Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from
RT   Saccharomyces 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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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.,
RA   Dephoure N., 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
RP   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.,
RA   Mann M., Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone
RT   signaling 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
RT   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
RT   phosphoproteome 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
RT   insights 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
CC       synthesis of glycogen.
CC   -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + ((1->4)-alpha-D-
CC       glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
CC   -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate,
CC       and phosphorylation by a cAMP-dependent kinase.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- DEVELOPMENTAL STAGE: Activity increases just before cells entry in
CC       the stationary phase.
CC   -!- INDUCTION: Synthesized in response to growth limitation.
CC   -!- MISCELLANEOUS: Present with 6300 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000305}.
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   ProteinModelPortal; P23337; -.
DR   SMR; P23337; -.
DR   BioGrid; 31167; 79.
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; P23337; -.
DR   PRIDE; P23337; -.
DR   EnsemblFungi; BAA09254; BAA09254; BAA09254.
DR   EnsemblFungi; YFR015C; YFR015C; YFR015C.
DR   GeneID; 850569; -.
DR   KEGG; sce:YFR015C; -.
DR   EuPathDB; FungiDB:YFR015C; -.
DR   SGD; S000001911; GSY1.
DR   GeneTree; ENSGT00920000150586; -.
DR   HOGENOM; HOG000160890; -.
DR   InParanoid; P23337; -.
DR   KO; K00693; -.
DR   OMA; KVYFGRW; -.
DR   OrthoDB; EOG092C0XGC; -.
DR   BioCyc; YEAST:YFR015C-MONOMER; -.
DR   UniPathway; UPA00164; -.
DR   PRO; PR:P23337; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:SGD.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IMP:SGD.
DR   CDD; cd03793; GT1_Glycogen_synthase_GSY2_lik; 1.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176; PTHR10176; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Complete proteome; Direct protein sequencing;
KW   Glycogen biosynthesis; Glycosyltransferase; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:2123485}.
FT   CHAIN         2    708       Glycogen [starch] synthase isoform 1.
FT                                /FTId=PRO_0000194773.
FT   BINDING      20     20       UDP-glucose. {ECO:0000250}.
FT   MOD_RES     159    159       Phosphoserine. {ECO:0000255}.
FT   MOD_RES     363    363       Phosphoserine. {ECO:0000255}.
FT   MOD_RES     560    560       Phosphoserine. {ECO:0000255}.
FT   MOD_RES     651    651       Phosphoserine.
FT                                {ECO:0000244|PubMed:17287358,
FT                                ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES     655    655       Phosphoserine.
FT                                {ECO:0000244|PubMed:15665377,
FT                                ECO:0000244|PubMed:17287358,
FT                                ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES     660    660       Phosphoserine; by PKA. {ECO:0000255}.
FT   MOD_RES     662    662       Phosphoserine; by PKA. {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
//
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