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P53043

- PPT1_YEAST

UniProt

P53043 - PPT1_YEAST

Protein

Serine/threonine-protein phosphatase T

Gene

PPT1

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 140 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90 (HSC82 and HSP82). Dephosphorylation positively regulates the Hsp90 chaperone machinery.1 Publication

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    Stimulated by arachidonic acid and other unsaturated fatty acids, and by arachidoyl coenzyme A.1 Publication

    Kineticsi

    1. KM=34 mM for p-nitrophenylphosphate1 Publication

    pH dependencei

    Optimum pH is 7.8.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi249 – 2491Manganese 1By similarity
    Metal bindingi251 – 2511Manganese 1By similarity
    Metal bindingi278 – 2781Manganese 1By similarity
    Metal bindingi278 – 2781Manganese 2By similarity
    Metal bindingi310 – 3101Manganese 2By similarity
    Active sitei311 – 3111Proton donorBy similarity
    Metal bindingi359 – 3591Manganese 2By similarity
    Metal bindingi434 – 4341Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein serine/threonine phosphatase activity Source: SGD

    GO - Biological processi

    1. protein dephosphorylation Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30830-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase T (EC:3.1.3.16)
    Short name:
    PPT
    Gene namesi
    Name:PPT1
    Ordered Locus Names:YGR123C
    ORF Names:G6347
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR123c.
    SGDiS000003355. PPT1.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi311 – 3111H → A: Loss of phosphatase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 513513Serine/threonine-protein phosphatase TPRO_0000058898Add
    BLAST

    Proteomic databases

    MaxQBiP53043.
    PaxDbiP53043.
    PeptideAtlasiP53043.

    Expressioni

    Inductioni

    Expression peaks in early log phase and decreases dramatically during the stationary phase (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriP53043.

    Interactioni

    Subunit structurei

    Interacts (via TPR repeats) with HSP82 (via C-terminal MEEVD pentapeptide).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSC82P151083EBI-13796,EBI-8666
    HSP82P028298EBI-13796,EBI-8659

    Protein-protein interaction databases

    BioGridi33370. 29 interactions.
    DIPiDIP-1525N.
    IntActiP53043. 10 interactions.
    MINTiMINT-406578.
    STRINGi4932.YGR123C.

    Structurei

    Secondary structure

    1
    513
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi192 – 20110
    Helixi203 – 2053
    Helixi211 – 22616
    Beta strandi230 – 2345
    Beta strandi237 – 2393
    Beta strandi243 – 2475
    Helixi254 – 26411
    Beta strandi271 – 2755
    Beta strandi280 – 2834
    Helixi286 – 29914
    Turni301 – 3033
    Beta strandi304 – 3063
    Helixi314 – 3207
    Helixi322 – 3298
    Helixi332 – 34211
    Beta strandi347 – 3515
    Turni352 – 3543
    Beta strandi355 – 3573
    Helixi370 – 3745
    Beta strandi384 – 3863
    Helixi387 – 3937
    Beta strandi398 – 4047
    Beta strandi411 – 4133
    Helixi415 – 42410
    Beta strandi428 – 4325
    Beta strandi439 – 4446
    Helixi445 – 4473
    Beta strandi449 – 4524
    Helixi458 – 4603
    Beta strandi465 – 4717
    Turni480 – 4823
    Beta strandi488 – 4936
    Turni503 – 5064

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ICFX-ray2.30A/B179-513[»]
    ProteinModelPortaliP53043.
    SMRiP53043. Positions 11-508.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53043.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati12 – 4534TPR 1Add
    BLAST
    Repeati46 – 7934TPR 2Add
    BLAST
    Repeati80 – 11334TPR 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni188 – 513326CatalyticAdd
    BLAST

    Domaini

    The TPR repeats mediate protein-protein interactions with substrate proteins, but also autoinhibit PPT1 phosphatase activity.

    Sequence similaritiesi

    Contains 3 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000063173.
    HOGENOMiHOG000172698.
    KOiK04460.
    OMAiFKLLYPN.
    OrthoDBiEOG7Z3FDD.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR013235. PPP_dom.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    IPR011236. Ser/Thr_PPase_5.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR11668:SF12. PTHR11668:SF12. 1 hit.
    PfamiPF00149. Metallophos. 1 hit.
    PF08321. PPP5. 1 hit.
    PF00515. TPR_1. 1 hit.
    PF07719. TPR_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF033096. PPPtase_5. 1 hit.
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P53043-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPTAADRA KALERKNEGN VFVKEKHFLK AIEKYTEAID LDSTQSIYFS    50
    NRAFAHFKVD NFQSALNDCD EAIKLDPKNI KAYHRRALSC MALLEFKKAR 100
    KDLNVLLKAK PNDPAATKAL LTCDRFIREE RFRKAIGGAE NEAKISLCQT 150
    LNLSSFDANA DLANYEGPKL EFEQLYDDKN AFKGAKIKNM SQEFISKMVN 200
    DLFLKGKYLP KKYVAAIISH ADTLFRQEPS MVELENNSTP DVKISVCGDT 250
    HGQFYDVLNL FRKFGKVGPK HTYLFNGDFV DRGSWSCEVA LLFYCLKILH 300
    PNNFFLNRGN HESDNMNKIY GFEDECKYKY SQRIFNMFAQ SFESLPLATL 350
    INNDYLVMHG GLPSDPSATL SDFKNIDRFA QPPRDGAFME LLWADPQEAN 400
    GMGPSQRGLG HAFGPDITDR FLRNNKLRKI FRSHELRMGG VQFEQKGKLM 450
    TVFSAPNYCD SQGNLGGVIH VVPGHGILQA GRNDDQNLII ETFEAVEHPD 500
    IKPMAYSNGG FGL 513
    Length:513
    Mass (Da):57,995
    Last modified:October 1, 1996 - v1
    Checksum:i6966DA22340A5793
    GO

    Sequence cautioni

    The sequence CAA61596.1 differs from that shown. Reason: Frameshift at position 381.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89417 Genomic DNA. Translation: CAA61596.1. Frameshift.
    X83099 Genomic DNA. Translation: CAA58158.1.
    Z72908 Genomic DNA. Translation: CAA97134.1.
    AY558095 Genomic DNA. Translation: AAS56421.1.
    S39959 Genomic DNA. Translation: AAB22462.1.
    BK006941 Genomic DNA. Translation: DAA08216.1.
    PIRiS52571.
    RefSeqiNP_011639.3. NM_001181252.3.

    Genome annotation databases

    EnsemblFungiiYGR123C; YGR123C; YGR123C.
    GeneIDi853023.
    KEGGisce:YGR123C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89417 Genomic DNA. Translation: CAA61596.1 . Frameshift.
    X83099 Genomic DNA. Translation: CAA58158.1 .
    Z72908 Genomic DNA. Translation: CAA97134.1 .
    AY558095 Genomic DNA. Translation: AAS56421.1 .
    S39959 Genomic DNA. Translation: AAB22462.1 .
    BK006941 Genomic DNA. Translation: DAA08216.1 .
    PIRi S52571.
    RefSeqi NP_011639.3. NM_001181252.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ICF X-ray 2.30 A/B 179-513 [» ]
    ProteinModelPortali P53043.
    SMRi P53043. Positions 11-508.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33370. 29 interactions.
    DIPi DIP-1525N.
    IntActi P53043. 10 interactions.
    MINTi MINT-406578.
    STRINGi 4932.YGR123C.

    Proteomic databases

    MaxQBi P53043.
    PaxDbi P53043.
    PeptideAtlasi P53043.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR123C ; YGR123C ; YGR123C .
    GeneIDi 853023.
    KEGGi sce:YGR123C.

    Organism-specific databases

    CYGDi YGR123c.
    SGDi S000003355. PPT1.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00530000063173.
    HOGENOMi HOG000172698.
    KOi K04460.
    OMAi FKLLYPN.
    OrthoDBi EOG7Z3FDD.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30830-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P53043.
    NextBioi 972897.
    PROi P53043.

    Gene expression databases

    Genevestigatori P53043.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR013235. PPP_dom.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    IPR011236. Ser/Thr_PPase_5.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view ]
    PANTHERi PTHR11668:SF12. PTHR11668:SF12. 1 hit.
    Pfami PF00149. Metallophos. 1 hit.
    PF08321. PPP5. 1 hit.
    PF00515. TPR_1. 1 hit.
    PF07719. TPR_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF033096. PPPtase_5. 1 hit.
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus."
      Chen M.X., McPartlin A.E., Brown L., Chen Y.H., Barker H.M., Cohen P.T.W.
      EMBO J. 13:4278-4290(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "An 18.3 kb DNA fragment from yeast chromosome VII carries four unknown open reading frames, the gene for an Asn synthase, remnants of Ty and three tRNA genes."
      van Dyck L., Tettelin H., Purnelle B., Goffeau A.
      Yeast 13:171-176(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Polymerase chain reactions using Saccharomyces, Drosophila and human DNA predict a large family of protein serine/threonine phosphatases."
      Chen M.X., Chen Y.H., Cohen P.T.W.
      FEBS Lett. 306:54-58(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-277.
    7. "Characterization of Saccharomyces cerevisiae protein Ser/Thr phosphatase T1 and comparison to its mammalian homolog PP5."
      Jeong J.-Y., Johns J., Sinclair C., Park J.-M., Rossie S.
      BMC Cell Biol. 4:3-3(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, ENZYME REGULATION, SUBCELLULAR LOCATION, INDUCTION.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90."
      Wandinger S.K., Suhre M.H., Wegele H., Buchner J.
      EMBO J. 25:367-376(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSP82, MUTAGENESIS OF HIS-311.
    11. "Expression, purification and refolding of the phosphatase domain of protein phosphatase 1 (Ppt1) from Saccharomyces cerevisiae."
      Suhre M.H., Wegele H., Wandinger S.K.
      Int. J. Biol. Macromol. 39:23-28(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    12. "Structure of protein serine/threonine phosphatase from Saccharomyces cerevisiae with similarity to human phosphatase PP5."
      Midwest center for structural genomics (MCSG)
      Submitted (JUL-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 179-513.

    Entry informationi

    Entry nameiPPT1_YEAST
    AccessioniPrimary (citable) accession number: P53043
    Secondary accession number(s): D6VUQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 6990 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3