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P27472

- GYS2_YEAST

UniProt

P27472 - GYS2_YEAST

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Protein
Glycogen [starch] synthase isoform 2
Gene
GSY2, YLR258W, L8479.8
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

UDP-glucose ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).

Enzyme regulationi

Allosteric activation by glucose-6-phosphate, and phosphorylation by a cAMP-dependent kinase.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201UDP-glucose By similarity

GO - Molecular functioni

  1. glycogen (starch) synthase activity Source: SGD

GO - Biological processi

  1. glycogen biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

BioCyciYEAST:YLR258W-MONOMER.
UniPathwayiUPA00164.

Protein family/group databases

CAZyiGT3. Glycosyltransferase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen [starch] synthase isoform 2 (EC:2.4.1.11)
Gene namesi
Name:GSY2
Ordered Locus Names:YLR258W
ORF Names:L8479.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

SGDiS000004248. GSY2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 705705Glycogen [starch] synthase isoform 2
PRO_0000194774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei159 – 1591Phosphoserine Reviewed prediction
Modified residuei363 – 3631Phosphoserine Reviewed prediction
Modified residuei467 – 4671Phosphoserine1 Publication
Modified residuei651 – 6511Phosphoserine4 Publications
Modified residuei655 – 6551Phosphoserine; by PHO854 Publications
Modified residuei661 – 6611Phosphoserine; by PKA Reviewed prediction
Modified residuei663 – 6631Phosphoserine; by PKA Reviewed prediction
Modified residuei668 – 6681Phosphothreonine; by PHO851 Publication

Post-translational modificationi

Phosphorylated by the cyclin-CDK PCL10-PHO85. Phosphorylation causes inactivation of enzyme.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP27472.
PaxDbiP27472.
PeptideAtlasiP27472.

Expressioni

Gene expression databases

GenevestigatoriP27472.

Interactioni

Subunit structurei

Interacts with PCL10.1 Publication

Protein-protein interaction databases

BioGridi31526. 71 interactions.
DIPiDIP-1255N.
IntActiP27472. 22 interactions.
MINTiMINT-387549.
STRINGi4932.YLR258W.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1411
Turni15 – 184
Helixi23 – 3917
Helixi40 – 423
Beta strandi43 – 486
Turni51 – 533
Helixi54 – 574
Beta strandi58 – 603
Beta strandi63 – 653
Helixi66 – 683
Helixi71 – 733
Helixi74 – 8411
Turni85 – 873
Beta strandi90 – 978
Beta strandi102 – 1065
Helixi109 – 1146
Helixi115 – 12612
Helixi135 – 15723
Beta strandi160 – 16910
Helixi170 – 1723
Helixi175 – 1817
Beta strandi187 – 1948
Helixi196 – 2016
Beta strandi203 – 2053
Helixi209 – 2124
Helixi213 – 2153
Helixi218 – 2247
Helixi228 – 24013
Beta strandi241 – 2488
Helixi249 – 25810
Beta strandi259 – 2613
Beta strandi264 – 2663
Helixi273 – 2764
Helixi281 – 30020
Turni301 – 3033
Helixi309 – 3113
Beta strandi312 – 3209
Turni323 – 3275
Helixi328 – 34417
Beta strandi350 – 3567
Beta strandi361 – 3644
Helixi366 – 39934
Turni400 – 4045
Beta strandi407 – 4093
Helixi413 – 4164
Helixi419 – 43214
Beta strandi442 – 4476
Helixi450 – 4523
Helixi454 – 4629
Beta strandi471 – 4766
Beta strandi486 – 4883
Helixi492 – 4987
Beta strandi500 – 5034
Beta strandi507 – 5115
Helixi513 – 5208
Beta strandi525 – 5284
Helixi532 – 5387
Helixi543 – 5486
Beta strandi551 – 5544
Beta strandi557 – 5593
Helixi561 – 57616
Helixi580 – 59213
Helixi593 – 5975
Helixi599 – 61719
Helixi619 – 6246
Helixi635 – 6384

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NAZX-ray3.00A/B/C/D1-705[»]
3NB0X-ray2.41A/B/C/D1-705[»]
3NCHX-ray2.88A/B/C/D1-705[»]
3O3CX-ray3.51A/B/C/D1-705[»]
3RSZX-ray3.01A/B/C/D1-705[»]
3RT1X-ray2.80A/B/C/D1-705[»]
4KQ2X-ray2.95A/B/C/D1-705[»]
4KQMX-ray2.77A/B/C/D1-705[»]
ProteinModelPortaliP27472.
SMRiP27472. Positions 2-647.

Miscellaneous databases

EvolutionaryTraceiP27472.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0438.
HOGENOMiHOG000160890.
KOiK00693.
OMAiFKAPDES.
OrthoDBiEOG7QK0MF.

Family and domain databases

InterProiIPR008631. Glycogen_synth.
[Graphical view]
PANTHERiPTHR10176. PTHR10176. 1 hit.
PfamiPF05693. Glycogen_syn. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27472-1 [UniParc]FASTAAdd to Basket

« Hide

MSRDLQNHLL FETATEVANR VGGIYSVLKS KAPITVAQYK DHYHLIGPLN    50
KATYQNEVDI LDWKKPEAFS DEMRPVQHAL QTMESRGVHF VYGRWLIEGA 100
PKVILFDLDS VRGYSNEWKG DLWSLVGIPS PENDFETNDA ILLGYTVAWF 150
LGEVAHLDSQ HAIVAHFHEW LAGVALPLCR KRRIDVVTIF TTHATLLGRY 200
LCASGSFDFY NCLESVDVDH EAGRFGIYHR YCIERAAAHS ADVFTTVSQI 250
TAFEAEHLLK RKPDGILPNG LNVIKFQAFH EFQNLHALKK EKINDFVRGH 300
FHGCFDFDLD NTLYFFIAGR YEYKNKGADM FIEALARLNY RLKVSGSKKT 350
VVAFIVMPAK NNSFTVEALK GQAEVRALEN TVHEVTTSIG KRIFDHAIRY 400
PHNGLTTELP TDLGELLKSS DKVMLKRRIL ALRRPEGQLP PIVTHNMVDD 450
ANDLILNKIR QVQLFNSPSD RVKMIFHPEF LNANNPILGL DYDEFVRGCH 500
LGVFPSYYEP WGYTPAECTV MGVPSITTNV SGFGAYMEDL IETNQAKDYG 550
IYIVDRRFKA PDESVEQLVD YMEEFVKKTR RQRINQRNRT ERLSDLLDWK 600
RMGLEYVKAR QLALRRGYPD QFRELVGEEL NDSNMDALAG GKKLKVARPL 650
SVPGSPRDLR SNSTVYMTPG DLGTLQEVNN ADDYFSLGVN PAADDDDDGP 700
YADDS 705
Length:705
Mass (Da):80,079
Last modified:January 23, 2007 - v3
Checksum:i4670D8328CEDB0D2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481S → P AA sequence 1 Publication
Sequence conflicti535 – 5351A → S in AAA88716. 1 Publication
Sequence conflicti622 – 6221F → FF AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M65206 Genomic DNA. Translation: AAA88716.1.
U17244 Genomic DNA. Translation: AAB67378.1.
BK006945 Genomic DNA. Translation: DAA09571.1.
PIRiS51396.
RefSeqiNP_013359.1. NM_001182145.1.

Genome annotation databases

EnsemblFungiiYLR258W; YLR258W; YLR258W.
GeneIDi850962.
KEGGisce:YLR258W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M65206 Genomic DNA. Translation: AAA88716.1 .
U17244 Genomic DNA. Translation: AAB67378.1 .
BK006945 Genomic DNA. Translation: DAA09571.1 .
PIRi S51396.
RefSeqi NP_013359.1. NM_001182145.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NAZ X-ray 3.00 A/B/C/D 1-705 [» ]
3NB0 X-ray 2.41 A/B/C/D 1-705 [» ]
3NCH X-ray 2.88 A/B/C/D 1-705 [» ]
3O3C X-ray 3.51 A/B/C/D 1-705 [» ]
3RSZ X-ray 3.01 A/B/C/D 1-705 [» ]
3RT1 X-ray 2.80 A/B/C/D 1-705 [» ]
4KQ2 X-ray 2.95 A/B/C/D 1-705 [» ]
4KQM X-ray 2.77 A/B/C/D 1-705 [» ]
ProteinModelPortali P27472.
SMRi P27472. Positions 2-647.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31526. 71 interactions.
DIPi DIP-1255N.
IntActi P27472. 22 interactions.
MINTi MINT-387549.
STRINGi 4932.YLR258W.

Protein family/group databases

CAZyi GT3. Glycosyltransferase Family 3.

Proteomic databases

MaxQBi P27472.
PaxDbi P27472.
PeptideAtlasi P27472.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR258W ; YLR258W ; YLR258W .
GeneIDi 850962.
KEGGi sce:YLR258W.

Organism-specific databases

SGDi S000004248. GSY2.

Phylogenomic databases

eggNOGi COG0438.
HOGENOMi HOG000160890.
KOi K00693.
OMAi FKAPDES.
OrthoDBi EOG7QK0MF.

Enzyme and pathway databases

UniPathwayi UPA00164 .
BioCyci YEAST:YLR258W-MONOMER.

Miscellaneous databases

EvolutionaryTracei P27472.
NextBioi 967445.

Gene expression databases

Genevestigatori P27472.

Family and domain databases

InterProi IPR008631. Glycogen_synth.
[Graphical view ]
PANTHERi PTHR10176. PTHR10176. 1 hit.
Pfami PF05693. Glycogen_syn. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Two glycogen synthase isoforms in Saccharomyces cerevisiae are coded by distinct genes that are differentially controlled."
    Farkast I., Hardy T.A., Roach P.J., Goebl M.G.
    J. Biol. Chem. 266:15602-15607(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 52-62; 378-391; 593-600; 602-608 AND 661-670, PROBABLE CLEAVAGE OF INITIATOR METHIONINE.
    Strain: YPH52.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    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.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Purification, characterization and partial amino acid sequence of glycogen synthase from Saccharomyces cerevisiae."
    Carabaza A., Arino J., Fox J.W., Villar-Palasi C., Guinovart J.J.
    Biochem. J. 268:401-407(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 96-99; 236-253; 549-556; 593-600 AND 617-623.
  5. "Cyclin partners determine Pho85 protein kinase substrate specificity in vitro and in vivo: control of glycogen biosynthesis by Pcl8 and Pcl10."
    Huang D., Moffat J., Wilson W.A., Moore L., Cheng C., Roach P.J., Andrews B.J.
    Mol. Cell. Biol. 18:3289-3299(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-655 AND THR-668.
  6. "Substrate targeting of the yeast cyclin-dependent kinase Pho85p by the cyclin Pcl10p."
    Wilson W.A., Mahrenholz A.M., Roach P.J.
    Mol. Cell. Biol. 19:7020-7030(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCL10.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467; SER-651 AND SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGYS2_YEAST
AccessioniPrimary (citable) accession number: P27472
Secondary accession number(s): D6VYQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 14600 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

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