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P27472

- GYS2_YEAST

UniProt

P27472 - GYS2_YEAST

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
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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. 71 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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27472.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 3 family.Curated

    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

    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:
    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

    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: October 1, 2014
    This is version 131 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