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P27472

- GYS2_YEAST

UniProt

P27472 - GYS2_YEAST

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Protein

Glycogen [starch] synthase isoform 2

Gene

GSY2

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-alpha-D-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-glucoseBy 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.
ReactomeiREACT_191292. Glycogen synthesis.
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 2PRO_0000194774Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

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

Structurei

Secondary structure

1
705
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1411Combined sources
Turni15 – 184Combined sources
Helixi23 – 3917Combined sources
Helixi40 – 423Combined sources
Beta strandi43 – 486Combined sources
Turni51 – 533Combined sources
Helixi54 – 574Combined sources
Beta strandi58 – 603Combined sources
Beta strandi63 – 653Combined sources
Helixi66 – 683Combined sources
Helixi71 – 733Combined sources
Helixi74 – 8411Combined sources
Turni85 – 873Combined sources
Beta strandi90 – 978Combined sources
Beta strandi102 – 1065Combined sources
Helixi109 – 1146Combined sources
Helixi115 – 12612Combined sources
Helixi135 – 15723Combined sources
Beta strandi160 – 16910Combined sources
Helixi170 – 1723Combined sources
Helixi175 – 1817Combined sources
Beta strandi187 – 1948Combined sources
Helixi196 – 2016Combined sources
Beta strandi203 – 2053Combined sources
Helixi209 – 2124Combined sources
Helixi213 – 2153Combined sources
Helixi218 – 2247Combined sources
Helixi228 – 24013Combined sources
Beta strandi241 – 2488Combined sources
Helixi249 – 25810Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi264 – 2663Combined sources
Helixi273 – 2764Combined sources
Helixi281 – 30020Combined sources
Turni301 – 3033Combined sources
Helixi309 – 3113Combined sources
Beta strandi312 – 3209Combined sources
Turni323 – 3275Combined sources
Helixi328 – 34417Combined sources
Beta strandi350 – 3567Combined sources
Beta strandi361 – 3644Combined sources
Helixi366 – 39934Combined sources
Turni400 – 4045Combined sources
Beta strandi407 – 4093Combined sources
Helixi413 – 4164Combined sources
Helixi419 – 43214Combined sources
Beta strandi442 – 4476Combined sources
Helixi450 – 4523Combined sources
Helixi454 – 4629Combined sources
Beta strandi471 – 4766Combined sources
Beta strandi486 – 4883Combined sources
Helixi492 – 4987Combined sources
Beta strandi500 – 5034Combined sources
Beta strandi507 – 5115Combined sources
Helixi513 – 5208Combined sources
Beta strandi525 – 5284Combined sources
Helixi532 – 5387Combined sources
Helixi543 – 5486Combined sources
Beta strandi551 – 5544Combined sources
Beta strandi557 – 5593Combined sources
Helixi561 – 57616Combined sources
Helixi580 – 59213Combined sources
Helixi593 – 5975Combined sources
Helixi599 – 61719Combined sources
Helixi619 – 6246Combined sources
Helixi635 – 6384Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27472.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 3 family.Curated

Phylogenomic databases

eggNOGiCOG0438.
HOGENOMiHOG000160890.
InParanoidiP27472.
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

        10         20         30         40         50
MSRDLQNHLL FETATEVANR VGGIYSVLKS KAPITVAQYK DHYHLIGPLN
60 70 80 90 100
KATYQNEVDI LDWKKPEAFS DEMRPVQHAL QTMESRGVHF VYGRWLIEGA
110 120 130 140 150
PKVILFDLDS VRGYSNEWKG DLWSLVGIPS PENDFETNDA ILLGYTVAWF
160 170 180 190 200
LGEVAHLDSQ HAIVAHFHEW LAGVALPLCR KRRIDVVTIF TTHATLLGRY
210 220 230 240 250
LCASGSFDFY NCLESVDVDH EAGRFGIYHR YCIERAAAHS ADVFTTVSQI
260 270 280 290 300
TAFEAEHLLK RKPDGILPNG LNVIKFQAFH EFQNLHALKK EKINDFVRGH
310 320 330 340 350
FHGCFDFDLD NTLYFFIAGR YEYKNKGADM FIEALARLNY RLKVSGSKKT
360 370 380 390 400
VVAFIVMPAK NNSFTVEALK GQAEVRALEN TVHEVTTSIG KRIFDHAIRY
410 420 430 440 450
PHNGLTTELP TDLGELLKSS DKVMLKRRIL ALRRPEGQLP PIVTHNMVDD
460 470 480 490 500
ANDLILNKIR QVQLFNSPSD RVKMIFHPEF LNANNPILGL DYDEFVRGCH
510 520 530 540 550
LGVFPSYYEP WGYTPAECTV MGVPSITTNV SGFGAYMEDL IETNQAKDYG
560 570 580 590 600
IYIVDRRFKA PDESVEQLVD YMEEFVKKTR RQRINQRNRT ERLSDLLDWK
610 620 630 640 650
RMGLEYVKAR QLALRRGYPD QFRELVGEEL NDSNMDALAG GKKLKVARPL
660 670 680 690 700
SVPGSPRDLR SNSTVYMTPG DLGTLQEVNN ADDYFSLGVN PAADDDDDGP

YADDS
Length:705
Mass (Da):80,079
Last modified:January 23, 2007 - v3
Checksum:i4670D8328CEDB0D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481S → P AA sequence (PubMed:2114092)Curated
Sequence conflicti535 – 5351A → S in AAA88716. (PubMed:1908457)Curated
Sequence conflicti622 – 6221F → FF AA sequence (PubMed:2114092)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 72 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.
InParanoidi P27472.
KOi K00693.
OMAi FKAPDES.
OrthoDBi EOG7QK0MF.

Enzyme and pathway databases

UniPathwayi UPA00164 .
BioCyci YEAST:YLR258W-MONOMER.
Reactomei REACT_191292. Glycogen synthesis.

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: November 26, 2014
This is version 133 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.1 Publication

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