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P27472 (GYS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen [starch] synthase isoform 2

EC=2.4.1.11
Gene names
Name:GSY2
Ordered Locus Names:YLR258W
ORF Names:L8479.8
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length705 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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-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 structure

Interacts with PCL10. Ref.6

Post-translational modification

Phosphorylated by the cyclin-CDK PCL10-PHO85. Phosphorylation causes inactivation of enzyme. Ref.5

Miscellaneous

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

Sequence similarities

Belongs to the glycosyltransferase 3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 705705Glycogen [starch] synthase isoform 2
PRO_0000194774

Sites

Binding site201UDP-glucose By similarity

Amino acid modifications

Modified residue1591Phosphoserine Potential
Modified residue3631Phosphoserine Potential
Modified residue4671Phosphoserine Ref.10
Modified residue6511Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11
Modified residue6551Phosphoserine; by PHO85 Ref.5 Ref.8 Ref.9 Ref.10
Modified residue6611Phosphoserine; by PKA Potential
Modified residue6631Phosphoserine; by PKA Potential
Modified residue6681Phosphothreonine; by PHO85 Ref.5

Experimental info

Sequence conflict2481S → P AA sequence Ref.4
Sequence conflict5351A → S in AAA88716. Ref.1
Sequence conflict6221F → FF AA sequence Ref.4

Secondary structure

.................................................................................................................. 705
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27472 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4670D8328CEDB0D2

FASTA70580,079
        10         20         30         40         50         60 
MSRDLQNHLL FETATEVANR VGGIYSVLKS KAPITVAQYK DHYHLIGPLN KATYQNEVDI 

        70         80         90        100        110        120 
LDWKKPEAFS DEMRPVQHAL QTMESRGVHF VYGRWLIEGA PKVILFDLDS VRGYSNEWKG 

       130        140        150        160        170        180 
DLWSLVGIPS PENDFETNDA ILLGYTVAWF LGEVAHLDSQ HAIVAHFHEW LAGVALPLCR 

       190        200        210        220        230        240 
KRRIDVVTIF TTHATLLGRY LCASGSFDFY NCLESVDVDH EAGRFGIYHR YCIERAAAHS 

       250        260        270        280        290        300 
ADVFTTVSQI TAFEAEHLLK RKPDGILPNG LNVIKFQAFH EFQNLHALKK EKINDFVRGH 

       310        320        330        340        350        360 
FHGCFDFDLD NTLYFFIAGR YEYKNKGADM FIEALARLNY RLKVSGSKKT VVAFIVMPAK 

       370        380        390        400        410        420 
NNSFTVEALK GQAEVRALEN TVHEVTTSIG KRIFDHAIRY PHNGLTTELP TDLGELLKSS 

       430        440        450        460        470        480 
DKVMLKRRIL ALRRPEGQLP PIVTHNMVDD ANDLILNKIR QVQLFNSPSD RVKMIFHPEF 

       490        500        510        520        530        540 
LNANNPILGL DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGVPSITTNV SGFGAYMEDL 

       550        560        570        580        590        600 
IETNQAKDYG IYIVDRRFKA PDESVEQLVD YMEEFVKKTR RQRINQRNRT ERLSDLLDWK 

       610        620        630        640        650        660 
RMGLEYVKAR QLALRRGYPD QFRELVGEEL NDSNMDALAG GKKLKVARPL SVPGSPRDLR 

       670        680        690        700 
SNSTVYMTPG DLGTLQEVNN ADDYFSLGVN PAADDDDDGP YADDS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M65206 Genomic DNA. Translation: AAA88716.1.
U17244 Genomic DNA. Translation: AAB67378.1.
BK006945 Genomic DNA. Translation: DAA09571.1.
PIRS51396.
RefSeqNP_013359.1. NM_001182145.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP27472.
SMRP27472. Positions 2-647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31526. 71 interactions.
DIPDIP-1255N.
IntActP27472. 22 interactions.
MINTMINT-387549.
STRING4932.YLR258W.

Protein family/group databases

CAZyGT3. Glycosyltransferase Family 3.

Proteomic databases

PaxDbP27472.
PeptideAtlasP27472.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR258W; YLR258W; YLR258W.
GeneID850962.
KEGGsce:YLR258W.

Organism-specific databases

SGDS000004248. GSY2.

Phylogenomic databases

eggNOGCOG0438.
HOGENOMHOG000160890.
KOK00693.
OMAQITAFEA.
OrthoDBEOG7QK0MF.

Enzyme and pathway databases

BioCycYEAST:YLR258W-MONOMER.
UniPathwayUPA00164.

Gene expression databases

GenevestigatorP27472.

Family and domain databases

InterProIPR008631. Glycogen_synth.
[Graphical view]
PANTHERPTHR10176. PTHR10176. 1 hit.
PfamPF05693. Glycogen_syn. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP27472.
NextBio967445.

Entry information

Entry nameGYS2_YEAST
AccessionPrimary (citable) accession number: P27472
Secondary accession number(s): D6VYQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways