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Protein

Serine/threonine-protein phosphatase T

Gene

PPT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mn2+By similarityNote: 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

    • metal ion binding Source: UniProtKB-KW
    • protein serine/threonine phosphatase activity Source: SGD

    GO - Biological processi

    • protein dephosphorylation Source: SGD
    Complete GO annotation...

    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 Componenti: Chromosome VII

    Organism-specific databases

    CYGDiYGR123c.
    EuPathDBiFungiDB:YGR123C.
    SGDiS000003355. PPT1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: SGD
    • nucleus Source: SGD
    Complete GO annotation...

    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

    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. 30 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 – 20110Combined sources
    Helixi203 – 2053Combined sources
    Helixi211 – 22616Combined sources
    Beta strandi230 – 2345Combined sources
    Beta strandi237 – 2393Combined sources
    Beta strandi243 – 2475Combined sources
    Helixi254 – 26411Combined sources
    Beta strandi271 – 2755Combined sources
    Beta strandi280 – 2834Combined sources
    Helixi286 – 29914Combined sources
    Turni301 – 3033Combined sources
    Beta strandi304 – 3063Combined sources
    Helixi314 – 3207Combined sources
    Helixi322 – 3298Combined sources
    Helixi332 – 34211Combined sources
    Beta strandi347 – 3515Combined sources
    Turni352 – 3543Combined sources
    Beta strandi355 – 3573Combined sources
    Helixi370 – 3745Combined sources
    Beta strandi384 – 3863Combined sources
    Helixi387 – 3937Combined sources
    Beta strandi398 – 4047Combined sources
    Beta strandi411 – 4133Combined sources
    Helixi415 – 42410Combined sources
    Beta strandi428 – 4325Combined sources
    Beta strandi439 – 4446Combined sources
    Helixi445 – 4473Combined sources
    Beta strandi449 – 4524Combined sources
    Helixi458 – 4603Combined sources
    Beta strandi465 – 4717Combined sources
    Turni480 – 4823Combined sources
    Beta strandi488 – 4936Combined sources
    Turni503 – 5064Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    InParanoidiP53043.
    KOiK04460.
    OMAiYGYAIAD.
    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_dom.
    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]
    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

            10         20         30         40         50
    MSTPTAADRA KALERKNEGN VFVKEKHFLK AIEKYTEAID LDSTQSIYFS
    60 70 80 90 100
    NRAFAHFKVD NFQSALNDCD EAIKLDPKNI KAYHRRALSC MALLEFKKAR
    110 120 130 140 150
    KDLNVLLKAK PNDPAATKAL LTCDRFIREE RFRKAIGGAE NEAKISLCQT
    160 170 180 190 200
    LNLSSFDANA DLANYEGPKL EFEQLYDDKN AFKGAKIKNM SQEFISKMVN
    210 220 230 240 250
    DLFLKGKYLP KKYVAAIISH ADTLFRQEPS MVELENNSTP DVKISVCGDT
    260 270 280 290 300
    HGQFYDVLNL FRKFGKVGPK HTYLFNGDFV DRGSWSCEVA LLFYCLKILH
    310 320 330 340 350
    PNNFFLNRGN HESDNMNKIY GFEDECKYKY SQRIFNMFAQ SFESLPLATL
    360 370 380 390 400
    INNDYLVMHG GLPSDPSATL SDFKNIDRFA QPPRDGAFME LLWADPQEAN
    410 420 430 440 450
    GMGPSQRGLG HAFGPDITDR FLRNNKLRKI FRSHELRMGG VQFEQKGKLM
    460 470 480 490 500
    TVFSAPNYCD SQGNLGGVIH VVPGHGILQA GRNDDQNLII ETFEAVEHPD
    510
    IKPMAYSNGG FGL
    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. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi33370. 30 interactions.
    DIPiDIP-1525N.
    IntActiP53043. 10 interactions.
    MINTiMINT-406578.
    STRINGi4932.YGR123C.

    Proteomic databases

    MaxQBiP53043.
    PaxDbiP53043.
    PeptideAtlasiP53043.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CYGDiYGR123c.
    EuPathDBiFungiDB:YGR123C.
    SGDiS000003355. PPT1.

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000063173.
    HOGENOMiHOG000172698.
    InParanoidiP53043.
    KOiK04460.
    OMAiYGYAIAD.
    OrthoDBiEOG7Z3FDD.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30830-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP53043.
    NextBioi972897.
    PROiP53043.

    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_dom.
    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]
    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 146 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.