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Glycogen [starch] synthase isoform 2 (EC 2.4.1.11)

 GYS2_YEAST              Reviewed;         705 AA.
P27472; D6VYQ5;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 170.
RecName: Full=Glycogen [starch] synthase isoform 2;
EC=2.4.1.11;
Name=GSY2; OrderedLocusNames=YLR258W; ORFNames=L8479.8;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 52-62; 378-391;
593-600; 602-608 AND 661-670, AND PROBABLE CLEAVAGE OF INITIATOR
METHIONINE.
STRAIN=YPH52;
PubMed=1908457;
Farkast I., Hardy T.A., Roach P.J., Goebl M.G.;
"Two glycogen synthase isoforms in Saccharomyces cerevisiae are coded
by distinct genes that are differentially controlled.";
J. Biol. Chem. 266:15602-15607(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PROTEIN SEQUENCE OF 96-99; 236-253; 549-556; 593-600 AND 617-623.
PubMed=2114092; DOI=10.1042/bj2680401;
Carabaza A., Arino J., Fox J.W., Villar-Palasi C., Guinovart J.J.;
"Purification, characterization and partial amino acid sequence of
glycogen synthase from Saccharomyces cerevisiae.";
Biochem. J. 268:401-407(1990).
[5]
PHOSPHORYLATION AT SER-655 AND THR-668.
PubMed=9584169; DOI=10.1128/MCB.18.6.3289;
Huang D., Moffat J., Wilson W.A., Moore L., Cheng C., Roach P.J.,
Andrews B.J.;
"Cyclin partners determine Pho85 protein kinase substrate specificity
in vitro and in vivo: control of glycogen biosynthesis by Pcl8 and
Pcl10.";
Mol. Cell. Biol. 18:3289-3299(1998).
[6]
INTERACTION WITH PCL10.
PubMed=10490639; DOI=10.1128/MCB.19.10.7020;
Wilson W.A., Mahrenholz A.M., Roach P.J.;
"Substrate targeting of the yeast cyclin-dependent kinase Pho85p by
the cyclin Pcl10p.";
Mol. Cell. Biol. 19:7020-7030(1999).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467; SER-651 AND
SER-655, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
reducing end of alpha-1,4-glucan. Is believed to regulate the
synthesis of glycogen.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + ((1->4)-alpha-D-
glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
-!- ENZYME REGULATION: Allosteric activation by glucose-6-phosphate,
and phosphorylation by a cAMP-dependent kinase.
-!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
-!- SUBUNIT: Interacts with PCL10. {ECO:0000269|PubMed:10490639}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-8036, EBI-8036;
-!- PTM: Phosphorylated by the cyclin-CDK PCL10-PHO85. Phosphorylation
causes inactivation of enzyme. {ECO:0000269|PubMed:9584169}.
-!- MISCELLANEOUS: Present with 14600 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M65206; AAA88716.1; -; Genomic_DNA.
EMBL; U17244; AAB67378.1; -; Genomic_DNA.
EMBL; BK006945; DAA09571.1; -; Genomic_DNA.
PIR; S51396; S51396.
RefSeq; NP_013359.1; NM_001182145.1.
PDB; 3NAZ; X-ray; 3.00 A; A/B/C/D=1-705.
PDB; 3NB0; X-ray; 2.41 A; A/B/C/D=1-705.
PDB; 3NCH; X-ray; 2.88 A; A/B/C/D=1-705.
PDB; 3O3C; X-ray; 3.51 A; A/B/C/D=1-705.
PDB; 3RSZ; X-ray; 3.01 A; A/B/C/D=1-705.
PDB; 3RT1; X-ray; 2.80 A; A/B/C/D=1-705.
PDB; 4KQ2; X-ray; 2.95 A; A/B/C/D=1-705.
PDB; 4KQM; X-ray; 2.77 A; A/B/C/D=1-705.
PDB; 5SUK; X-ray; 2.88 A; A/B/C/D=1-705.
PDB; 5SUL; X-ray; 3.30 A; A/B=1-705.
PDB; 5UW0; X-ray; 2.73 A; A/B/C/D=1-700.
PDB; 5UW1; X-ray; 3.26 A; A/B/C/D=1-700.
PDB; 5UW4; X-ray; 2.98 A; A/B/C/D=1-700.
PDB; 5UX7; X-ray; 2.69 A; A/B/C/D=1-700.
PDB; 5VNC; X-ray; 2.98 A; A/B/C/D=1-700.
PDBsum; 3NAZ; -.
PDBsum; 3NB0; -.
PDBsum; 3NCH; -.
PDBsum; 3O3C; -.
PDBsum; 3RSZ; -.
PDBsum; 3RT1; -.
PDBsum; 4KQ2; -.
PDBsum; 4KQM; -.
PDBsum; 5SUK; -.
PDBsum; 5SUL; -.
PDBsum; 5UW0; -.
PDBsum; 5UW1; -.
PDBsum; 5UW4; -.
PDBsum; 5UX7; -.
PDBsum; 5VNC; -.
ProteinModelPortal; P27472; -.
SMR; P27472; -.
BioGrid; 31526; 99.
DIP; DIP-1255N; -.
IntAct; P27472; 26.
MINT; P27472; -.
STRING; 4932.YLR258W; -.
CAZy; GT3; Glycosyltransferase Family 3.
iPTMnet; P27472; -.
MaxQB; P27472; -.
PaxDb; P27472; -.
PRIDE; P27472; -.
TopDownProteomics; P27472; -.
EnsemblFungi; YLR258W; YLR258W; YLR258W.
GeneID; 850962; -.
KEGG; sce:YLR258W; -.
EuPathDB; FungiDB:YLR258W; -.
SGD; S000004248; GSY2.
GeneTree; ENSGT00390000018612; -.
HOGENOM; HOG000160890; -.
InParanoid; P27472; -.
KO; K00693; -.
OMA; TADEWGD; -.
OrthoDB; EOG092C0XGC; -.
BioCyc; YEAST:YLR258W-MONOMER; -.
UniPathway; UPA00164; -.
EvolutionaryTrace; P27472; -.
PRO; PR:P27472; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005978; P:glycogen biosynthetic process; IMP:SGD.
CDD; cd03793; GT1_Glycogen_synthase_GSY2_lik; 1.
InterPro; IPR008631; Glycogen_synth.
PANTHER; PTHR10176; PTHR10176; 1.
Pfam; PF05693; Glycogen_syn; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Complete proteome;
Direct protein sequencing; Glycogen biosynthesis; Glycosyltransferase;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 705 Glycogen [starch] synthase isoform 2.
/FTId=PRO_0000194774.
BINDING 20 20 UDP-glucose. {ECO:0000250}.
MOD_RES 159 159 Phosphoserine. {ECO:0000255}.
MOD_RES 363 363 Phosphoserine. {ECO:0000255}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 655 655 Phosphoserine; by PHO85.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:18407956,
ECO:0000269|PubMed:9584169}.
MOD_RES 661 661 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 663 663 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 668 668 Phosphothreonine; by PHO85.
{ECO:0000269|PubMed:9584169}.
CONFLICT 248 248 S -> P (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 535 535 A -> S (in Ref. 1; AAA88716).
{ECO:0000305}.
CONFLICT 622 622 F -> FF (in Ref. 4; AA sequence).
{ECO:0000305}.
STRAND 4 14 {ECO:0000244|PDB:3NB0}.
TURN 15 18 {ECO:0000244|PDB:3NB0}.
HELIX 23 39 {ECO:0000244|PDB:3NB0}.
HELIX 40 42 {ECO:0000244|PDB:3NB0}.
STRAND 43 48 {ECO:0000244|PDB:3NB0}.
TURN 51 53 {ECO:0000244|PDB:3NB0}.
HELIX 54 57 {ECO:0000244|PDB:3NB0}.
STRAND 58 60 {ECO:0000244|PDB:3NB0}.
STRAND 63 65 {ECO:0000244|PDB:3NB0}.
HELIX 66 68 {ECO:0000244|PDB:3NB0}.
HELIX 71 73 {ECO:0000244|PDB:4KQM}.
HELIX 74 84 {ECO:0000244|PDB:3NB0}.
TURN 85 87 {ECO:0000244|PDB:3NB0}.
STRAND 90 97 {ECO:0000244|PDB:3NB0}.
STRAND 102 106 {ECO:0000244|PDB:3NB0}.
HELIX 109 114 {ECO:0000244|PDB:3NB0}.
HELIX 115 126 {ECO:0000244|PDB:3NB0}.
HELIX 135 157 {ECO:0000244|PDB:3NB0}.
STRAND 160 169 {ECO:0000244|PDB:3NB0}.
HELIX 170 172 {ECO:0000244|PDB:3NB0}.
HELIX 175 181 {ECO:0000244|PDB:3NB0}.
STRAND 187 194 {ECO:0000244|PDB:3NB0}.
HELIX 196 201 {ECO:0000244|PDB:3NB0}.
STRAND 203 205 {ECO:0000244|PDB:3NB0}.
HELIX 209 212 {ECO:0000244|PDB:3NB0}.
HELIX 213 215 {ECO:0000244|PDB:3NB0}.
HELIX 218 224 {ECO:0000244|PDB:3NB0}.
HELIX 228 240 {ECO:0000244|PDB:3NB0}.
STRAND 241 248 {ECO:0000244|PDB:3NB0}.
HELIX 249 258 {ECO:0000244|PDB:3NB0}.
STRAND 259 261 {ECO:0000244|PDB:3NB0}.
STRAND 264 266 {ECO:0000244|PDB:3NB0}.
HELIX 273 276 {ECO:0000244|PDB:3NCH}.
HELIX 281 300 {ECO:0000244|PDB:3NB0}.
TURN 301 303 {ECO:0000244|PDB:3NB0}.
HELIX 309 311 {ECO:0000244|PDB:3NB0}.
STRAND 312 320 {ECO:0000244|PDB:3NB0}.
TURN 323 327 {ECO:0000244|PDB:3NB0}.
HELIX 328 344 {ECO:0000244|PDB:3NB0}.
STRAND 350 356 {ECO:0000244|PDB:3NB0}.
STRAND 361 364 {ECO:0000244|PDB:3NB0}.
HELIX 366 399 {ECO:0000244|PDB:3NB0}.
TURN 400 404 {ECO:0000244|PDB:4KQ2}.
STRAND 407 409 {ECO:0000244|PDB:3NB0}.
HELIX 413 416 {ECO:0000244|PDB:3NB0}.
HELIX 419 432 {ECO:0000244|PDB:3NB0}.
STRAND 442 447 {ECO:0000244|PDB:3NB0}.
HELIX 450 452 {ECO:0000244|PDB:3NB0}.
HELIX 454 462 {ECO:0000244|PDB:3NB0}.
STRAND 471 476 {ECO:0000244|PDB:3NB0}.
STRAND 486 488 {ECO:0000244|PDB:3NB0}.
HELIX 492 498 {ECO:0000244|PDB:3NB0}.
STRAND 500 503 {ECO:0000244|PDB:3NB0}.
STRAND 507 511 {ECO:0000244|PDB:3NB0}.
HELIX 513 520 {ECO:0000244|PDB:3NB0}.
STRAND 525 528 {ECO:0000244|PDB:3NB0}.
HELIX 532 538 {ECO:0000244|PDB:3NB0}.
HELIX 543 548 {ECO:0000244|PDB:3NB0}.
STRAND 551 554 {ECO:0000244|PDB:3NB0}.
STRAND 557 559 {ECO:0000244|PDB:3NB0}.
HELIX 561 576 {ECO:0000244|PDB:3NB0}.
HELIX 580 592 {ECO:0000244|PDB:3NB0}.
HELIX 593 597 {ECO:0000244|PDB:3NB0}.
HELIX 599 617 {ECO:0000244|PDB:3NB0}.
HELIX 619 624 {ECO:0000244|PDB:3NB0}.
STRAND 626 628 {ECO:0000244|PDB:5SUL}.
HELIX 635 638 {ECO:0000244|PDB:3NB0}.
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


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