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P06738

- PHSG_YEAST

UniProt

P06738 - PHSG_YEAST

Protein

Glycogen phosphorylase

Gene

GPH1

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 146 (01 Oct 2014)
      Sequence version 4 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.

    Enzyme regulationi

    Activated by phosphorylation of Thr-31.

    GO - Molecular functioni

    1. glycogen phosphorylase activity Source: SGD
    2. protein binding Source: IntAct
    3. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. glycogen catabolic process Source: SGD

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen metabolism

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13684.
    YEAST:YPR160W-MONOMER.

    Protein family/group databases

    CAZyiGT35. Glycosyltransferase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycogen phosphorylase (EC:2.4.1.1)
    Gene namesi
    Name:GPH1
    Ordered Locus Names:YPR160W
    ORF Names:P9584.1
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    SGDiS000006364. GPH1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 902901Glycogen phosphorylasePRO_0000188545Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311Phosphothreonine6 Publications
    Modified residuei333 – 3331Phosphoserine2 Publications
    Modified residuei751 – 7511N6-(pyridoxal phosphate)lysine

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP06738.
    PaxDbiP06738.
    PeptideAtlasiP06738.

    Expressioni

    Gene expression databases

    GenevestigatoriP06738.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRP40P332032EBI-13389,EBI-701
    RSP5P399402EBI-13389,EBI-16219

    Protein-protein interaction databases

    BioGridi36333. 91 interactions.
    DIPiDIP-2648N.
    IntActiP06738. 12 interactions.
    MINTiMINT-426238.
    STRINGi4932.YPR160W.

    Structurei

    Secondary structure

    1
    902
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi35 – 4410
    Helixi47 – 559
    Helixi64 – 7613
    Helixi83 – 853
    Helixi88 – 11730
    Beta strandi121 – 1255
    Helixi134 – 1407
    Helixi158 – 16811
    Helixi172 – 1765
    Helixi188 – 20215
    Beta strandi207 – 2126
    Beta strandi220 – 2245
    Beta strandi227 – 2315
    Turni235 – 2384
    Beta strandi244 – 25613
    Beta strandi258 – 2603
    Beta strandi273 – 2753
    Beta strandi277 – 29014
    Beta strandi297 – 30812
    Helixi313 – 3175
    Helixi321 – 3244
    Helixi326 – 33611
    Beta strandi337 – 3393
    Helixi345 – 37228
    Helixi377 – 3793
    Helixi380 – 3834
    Beta strandi384 – 3918
    Turni392 – 3943
    Helixi395 – 40612
    Helixi412 – 42211
    Beta strandi423 – 4275
    Helixi432 – 4343
    Beta strandi437 – 4393
    Helixi440 – 4467
    Helixi448 – 46821
    Helixi474 – 4796
    Beta strandi481 – 4833
    Beta strandi486 – 4883
    Beta strandi490 – 4923
    Helixi493 – 5008
    Beta strandi501 – 5088
    Helixi509 – 5179
    Turni518 – 5203
    Helixi521 – 5277
    Helixi529 – 5313
    Beta strandi532 – 5343
    Helixi541 – 5444
    Turni545 – 5484
    Helixi550 – 55910
    Helixi566 – 5683
    Helixi571 – 58212
    Helixi585 – 60723
    Turni608 – 6114
    Helixi620 – 6223
    Beta strandi624 – 6307
    Helixi634 – 6363
    Helixi638 – 65720
    Helixi662 – 6687
    Beta strandi672 – 6776
    Helixi685 – 70117
    Helixi705 – 7073
    Beta strandi710 – 7167
    Helixi721 – 7277
    Helixi728 – 7303
    Beta strandi732 – 7365
    Helixi747 – 7537
    Turni754 – 7563
    Beta strandi758 – 7636
    Helixi766 – 7749
    Helixi776 – 7783
    Beta strandi779 – 7835
    Helixi786 – 79813
    Helixi805 – 8139
    Turni824 – 8274
    Helixi828 – 8369
    Turni838 – 8414
    Helixi843 – 86321
    Helixi865 – 87915
    Helixi880 – 8823
    Helixi884 – 89411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YGPX-ray2.80A/B24-902[»]
    ProteinModelPortaliP06738.
    SMRiP06738. Positions 27-901.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06738.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycogen phosphorylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0058.
    GeneTreeiENSGT00390000016886.
    HOGENOMiHOG000278444.
    KOiK00688.
    OMAiMDQISSG.
    OrthoDBiEOG7FJH7X.

    Family and domain databases

    InterProiIPR011833. Glycg_phsphrylas.
    IPR000811. Glyco_trans_35.
    [Graphical view]
    PANTHERiPTHR11468. PTHR11468. 1 hit.
    PfamiPF00343. Phosphorylase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000460. Pprylas_GlgP. 1 hit.
    TIGRFAMsiTIGR02093. P_ylase. 1 hit.
    PROSITEiPS00102. PHOSPHORYLASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P06738-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPASTSTTN DMITEEPTSP HQIPRLTRRL TGFLPQEIKS IDTMIPLKSR    50
    ALWNKHQVKK FNKAEDFQDR FIDHVETTLA RSLYNCDDMA AYEAASMSIR 100
    DNLVIDWNKT QQKFTTRDPK RVYYLSLEFL MGRALDNALI NMKIEDPEDP 150
    AASKGKPREM IKGALDDLGF KLEDVLDQEP DAGLGNGGLG RLAACFVDSM 200
    ATEGIPAWGY GLRYEYGIFA QKIIDGYQVE TPDYWLNSGN PWEIERNEVQ 250
    IPVTFYGYVD RPEGGKTTLS ASQWIGGERV LAVAYDFPVP GFKTSNVNNL 300
    RLWQARPTTE FDFAKFNNGD YKNSVAQQQR AESITAVLYP NDNFAQGKEL 350
    RLKQQYFWCA ASLHDILRRF KKSKRPWTEF PDQVAIQLND THPTLAIVEL 400
    QRVLVDLEKL DWHEAWDIVT KTFAYTNHTV MQEALEKWPV GLFGHLLPRH 450
    LEIIYDINWF FLQDVAKKFP KDVDLLSRIS IIEENSPERQ IRMAFLAIVG 500
    SHKVNGVAEL HSELIKTTIF KDFVKFYGPS KFVNVTNGIT PRRWLKQANP 550
    SLAKLISETL NDPTEEYLLD MAKLTQLGKY VEDKEFLKKW NQVKLNNKIR 600
    LVDLIKKEND GVDIINREYL DDTLFDMQVK RIHEYKRQQL NVFGIIYRYL 650
    AMKNMLKNGA SIEEVAKKYP RKVSIFGGKS APGYYMAKLI IKLINCVADI 700
    VNNDESIEHL LKVVFVADYN VSKAEIIIPA SDLSEHISTA GTEASGTSNM 750
    KFVMNGGLII GTVDGANVEI TREIGEDNVF LFGNLSENVE ELRYNHQYHP 800
    QDLPSSLDSV LSYIESGQFS PENPNEFKPL VDSIKYHGDY YLVSDDFESY 850
    LATHELVDQE FHNQRSEWLK KSVLSVANVG FFSSDRCIEE YSDTIWNVEP 900
    VT 902
    Length:902
    Mass (Da):103,275
    Last modified:October 5, 2010 - v4
    Checksum:iF5B6098D69ABAE43
    GO

    Sequence cautioni

    The sequence CAA28273.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti167 – 1682DL → EG in CAA28273. (PubMed:3537803)Curated
    Sequence conflicti167 – 1682DL → EG in AAB59313. (PubMed:7871892)Curated
    Sequence conflicti326 – 3261A → P in CAA28273. (PubMed:3537803)Curated
    Sequence conflicti326 – 3261A → P in AAB59313. (PubMed:7871892)Curated
    Sequence conflicti440 – 4412VG → RR in CAA28273. (PubMed:3537803)Curated
    Sequence conflicti440 – 4412VG → RR in AAB59313. (PubMed:7871892)Curated
    Sequence conflicti508 – 5081A → V in CAA28273. (PubMed:3537803)Curated
    Sequence conflicti508 – 5081A → V in AAB59313. (PubMed:7871892)Curated
    Sequence conflicti524 – 5241V → I in CAA28273. (PubMed:3537803)Curated
    Sequence conflicti524 – 5241V → I in AAB59313. (PubMed:7871892)Curated
    Sequence conflicti578 – 5781G → E in CAA28273. (PubMed:3537803)Curated
    Sequence conflicti578 – 5781G → E in AAB59313. (PubMed:7871892)Curated
    Sequence conflicti876 – 8761V → L in CAA28273. (PubMed:3537803)Curated
    Sequence conflicti876 – 8761V → L in AAB59313. (PubMed:7871892)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04604 Genomic DNA. Translation: CAA28273.1. Different initiation.
    L33835 Genomic DNA. Translation: AAB59313.1.
    U28371 Genomic DNA. Translation: AAB68057.1.
    BK006949 Genomic DNA. Translation: DAA11577.1.
    PIRiS61144.
    RefSeqiNP_015486.1. NM_001184257.1.

    Genome annotation databases

    EnsemblFungiiYPR160W; YPR160W; YPR160W.
    GeneIDi856289.
    KEGGisce:YPR160W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04604 Genomic DNA. Translation: CAA28273.1 . Different initiation.
    L33835 Genomic DNA. Translation: AAB59313.1 .
    U28371 Genomic DNA. Translation: AAB68057.1 .
    BK006949 Genomic DNA. Translation: DAA11577.1 .
    PIRi S61144.
    RefSeqi NP_015486.1. NM_001184257.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YGP X-ray 2.80 A/B 24-902 [» ]
    ProteinModelPortali P06738.
    SMRi P06738. Positions 27-901.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36333. 91 interactions.
    DIPi DIP-2648N.
    IntActi P06738. 12 interactions.
    MINTi MINT-426238.
    STRINGi 4932.YPR160W.

    Protein family/group databases

    CAZyi GT35. Glycosyltransferase Family 35.

    Proteomic databases

    MaxQBi P06738.
    PaxDbi P06738.
    PeptideAtlasi P06738.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPR160W ; YPR160W ; YPR160W .
    GeneIDi 856289.
    KEGGi sce:YPR160W.

    Organism-specific databases

    SGDi S000006364. GPH1.

    Phylogenomic databases

    eggNOGi COG0058.
    GeneTreei ENSGT00390000016886.
    HOGENOMi HOG000278444.
    KOi K00688.
    OMAi MDQISSG.
    OrthoDBi EOG7FJH7X.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-13684.
    YEAST:YPR160W-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P06738.
    NextBioi 981626.

    Gene expression databases

    Genevestigatori P06738.

    Family and domain databases

    InterProi IPR011833. Glycg_phsphrylas.
    IPR000811. Glyco_trans_35.
    [Graphical view ]
    PANTHERi PTHR11468. PTHR11468. 1 hit.
    Pfami PF00343. Phosphorylase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000460. Pprylas_GlgP. 1 hit.
    TIGRFAMsi TIGR02093. P_ylase. 1 hit.
    PROSITEi PS00102. PHOSPHORYLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Convergent and divergent evolution of regulatory sites in eukaryotic phosphorylases."
      Hwang P.K., Fletterick R.J.
      Nature 324:80-84(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "DNA sequence analysis of a 10.4 kbp region on the right arm of yeast chromosome XVI positions GPH1 and SGV1 adjacent to KRE6, and identifies two novel tRNA genes."
      Roemer T.D., Fortin N., Bussey H.
      Yeast 10:1527-1530(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Purification and crystallization of glycogen phosphorylase from Saccharomyces cerevisiae."
      Rath V.L., Hwang P.K., Fletterick R.J.
      J. Mol. Biol. 225:1027-1034(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10, PHOSPHORYLATION AT THR-31.
    6. "Amino acid sequence of two functional sites in yeast glycogen phosphorylase."
      Lerch K., Fischer E.H.
      Biochemistry 14:2009-2014(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-37 AND 737-754, PHOSPHORYLATION AT THR-31, PYRIDOXAL PHOSPHATE AT LYS-751.
    7. "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 THR-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    8. "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 THR-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    9. "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 THR-31 AND SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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 THR-31 AND SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "A protein phosphorylation switch at the conserved allosteric site in GP."
      Lin K., Rath V.L., Dai S.C., Fletterick R.J., Hwang P.K.
      Science 273:1539-1542(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 14-901.
    13. "Purification and properties of phosphorylase from baker's yeast."
      Becker J.U., Wingender-Drissen R., Schiltz E.
      Arch. Biochem. Biophys. 225:667-678(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.

    Entry informationi

    Entry nameiPHSG_YEAST
    AccessioniPrimary (citable) accession number: P06738
    Secondary accession number(s): D6W4G1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 146 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3