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P40454

- PTPA1_YEAST

UniProt

P40454 - PTPA1_YEAST

Protein

Serine/threonine-protein phosphatase 2A activator 1

Gene

RRD1

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 124 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for TAP42-associated PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg2+ by dissociating the inactive form from the complex. Involved in the regulation of cell cycle progression, mitotic spindle formation, bud morphogenesis and DNA repair.6 Publications

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    GO - Molecular functioni

    1. peptidyl-prolyl cis-trans isomerase activity Source: SGD
    2. phosphatase activator activity Source: InterPro
    3. protein binding Source: IntAct
    4. protein phosphatase type 2A regulator activity Source: SGD

    GO - Biological processi

    1. DNA repair Source: SGD
    2. G1/S transition of mitotic cell cycle Source: SGD
    3. mitotic spindle organization in nucleus Source: SGD
    4. protein folding Source: UniProtKB-KW
    5. protein peptidyl-prolyl isomerization Source: GOC
    6. regulation of catalytic activity Source: GOC
    7. regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD
    8. response to osmotic stress Source: SGD

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31402-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A activator 1 (EC:5.2.1.8)
    Alternative name(s):
    Peptidyl-prolyl cis-trans isomerase PTPA-1
    Short name:
    PPIase PTPA-1
    Short name:
    Rotamase PTPA-1
    Phosphotyrosyl phosphatase activator 1
    Gene namesi
    Name:RRD1
    Synonyms:NCS1, YPA1
    Ordered Locus Names:YIL153W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IX

    Organism-specific databases

    CYGDiYIL153w.
    SGDiS000001415. RRD1.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi205 – 2051D → G: Abolishes PPIase activity and fails to activate PP2A phosphatases. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393Serine/threonine-protein phosphatase 2A activator 1PRO_0000202955Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei341 – 3411Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP40454.
    PaxDbiP40454.
    PeptideAtlasiP40454.

    Expressioni

    Gene expression databases

    GenevestigatoriP40454.

    Interactioni

    Subunit structurei

    Interacts with the phosphatase PP2A-like catalytic subunits PPG1, PPH3 and SIT4. Forms a ternary complex with SIT4-TAP42.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PSY2P401643EBI-25278,EBI-29107
    SIT4P206044EBI-25278,EBI-13707

    Protein-protein interaction databases

    BioGridi34839. 128 interactions.
    DIPiDIP-5663N.
    IntActiP40454. 20 interactions.
    MINTiMINT-520859.
    STRINGi4932.YIL153W.

    Structurei

    Secondary structure

    1
    393
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni8 – 103
    Helixi23 – 286
    Helixi29 – 313
    Helixi33 – 4917
    Helixi65 – 7915
    Helixi97 – 11620
    Helixi119 – 1246
    Helixi125 – 1339
    Turni139 – 1413
    Helixi146 – 16116
    Helixi170 – 19021
    Helixi200 – 2023
    Beta strandi205 – 2073
    Helixi210 – 2189
    Beta strandi220 – 2223
    Helixi223 – 2253
    Beta strandi226 – 2283
    Helixi230 – 2345
    Helixi236 – 2427
    Turni243 – 2453
    Helixi247 – 25812
    Helixi263 – 2664
    Helixi268 – 2747
    Helixi280 – 29415
    Turni295 – 2973
    Helixi299 – 3024
    Beta strandi309 – 3124

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IXOX-ray2.60A/B1-317[»]
    2IXPX-ray2.80A/B/C/D1-317[»]
    ProteinModelPortaliP40454.
    SMRiP40454. Positions 2-317.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40454.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PTPA-type PPIase family.Curated

    Phylogenomic databases

    eggNOGiCOG5057.
    GeneTreeiENSGT00390000011500.
    HOGENOMiHOG000205736.
    KOiK17605.
    OMAiSEYHEVV.
    OrthoDBiEOG76HQD0.

    Family and domain databases

    InterProiIPR004327. Phstyr_phstse_ac.
    [Graphical view]
    PANTHERiPTHR10012. PTHR10012. 1 hit.
    PfamiPF03095. PTPA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016325. Phstyr_phstse_ac. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P40454-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLDRVDWPH ATFSTPVKRI FDTQTTLDFQ SSLAIHRIKY HLHKYTTLIS    50
    HCSDPDPHAT ASSIAMVNGL MGVLDKLAHL IDETPPLPGP RRYGNLACRE 100
    WHHKLDERLP QWLQEMLPSE YHEVVPELQY YLGNSFGSST RLDYGTGHEL 150
    SFMATVAALD MLGMFPHMRG ADVFLLFNKY YTIMRRLILT YTLEPAGSHG 200
    VWGLDDHFHL VYILGSSQWQ LLDAQAPLQP REILDKSLVR EYKDTNFYCQ 250
    GINFINEVKM GPFEEHSPIL YDIAVTVPRW SKVCKGLLKM YSVEVLKKFP 300
    VVQHFWFGTG FFPWVNIQNG TDLPVFEEKE EESIEQANAG SPGREQTSTR 350
    FPTSTSMPPP GVPPSGNNIN YLLSHQNQSH RNQTSFSRDR LRR 393
    Length:393
    Mass (Da):45,082
    Last modified:February 1, 1995 - v1
    Checksum:i22F52B3359739B6E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38059 Genomic DNA. Translation: CAA86125.1.
    BK006942 Genomic DNA. Translation: DAA08400.1.
    PIRiS48381.
    RefSeqiNP_012113.1. NM_001179501.1.

    Genome annotation databases

    EnsemblFungiiYIL153W; YIL153W; YIL153W.
    GeneIDi854653.
    KEGGisce:YIL153W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38059 Genomic DNA. Translation: CAA86125.1 .
    BK006942 Genomic DNA. Translation: DAA08400.1 .
    PIRi S48381.
    RefSeqi NP_012113.1. NM_001179501.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IXO X-ray 2.60 A/B 1-317 [» ]
    2IXP X-ray 2.80 A/B/C/D 1-317 [» ]
    ProteinModelPortali P40454.
    SMRi P40454. Positions 2-317.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34839. 128 interactions.
    DIPi DIP-5663N.
    IntActi P40454. 20 interactions.
    MINTi MINT-520859.
    STRINGi 4932.YIL153W.

    Proteomic databases

    MaxQBi P40454.
    PaxDbi P40454.
    PeptideAtlasi P40454.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YIL153W ; YIL153W ; YIL153W .
    GeneIDi 854653.
    KEGGi sce:YIL153W.

    Organism-specific databases

    CYGDi YIL153w.
    SGDi S000001415. RRD1.

    Phylogenomic databases

    eggNOGi COG5057.
    GeneTreei ENSGT00390000011500.
    HOGENOMi HOG000205736.
    KOi K17605.
    OMAi SEYHEVV.
    OrthoDBi EOG76HQD0.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31402-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P40454.
    NextBioi 977208.
    PROi P40454.

    Gene expression databases

    Genevestigatori P40454.

    Family and domain databases

    InterProi IPR004327. Phstyr_phstse_ac.
    [Graphical view ]
    PANTHERi PTHR10012. PTHR10012. 1 hit.
    Pfami PF03095. PTPA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016325. Phstyr_phstse_ac. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "The Saccharomyces cerevisiae phosphotyrosyl phosphatase activator proteins are required for a subset of the functions disrupted by protein phosphatase 2A mutations."
      Van Hoof C., Janssens V., De Baere I., Stark M.J.R., de Winde J.H., Winderickx J., Thevelein J.M., Merlevede W., Goris J.
      Exp. Cell Res. 264:372-387(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "The phosphotyrosyl phosphatase activator, Ncs1p (Rrd1p), functions with Cla4p to regulate the G(2)/M transition in Saccharomyces cerevisiae."
      Mitchell D.A., Sprague G.F. Jr.
      Mol. Cell. Biol. 21:488-500(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SIT4.
    5. "A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo."
      Fellner T., Lackner D.H., Hombauer H., Piribauer P., Mudrak I., Zaragoza K., Juno C., Ogris E.
      Genes Dev. 17:2138-2150(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "The yeast phosphotyrosyl phosphatase activator protein, yPtpa1/Rrd1, interacts with Sit4 phosphatase to mediate resistance to 4-nitroquinoline-1-oxide and UVA."
      Douville J., David J., Fortier P.K., Ramotar D.
      Curr. Genet. 46:72-81(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SIT4.
    9. "Specific interactions of PP2A and PP2A-like phosphatases with the yeast PTPA homologues, Ypa1 and Ypa2."
      Van Hoof C., Martens E., Longin S., Jordens J., Stevens I., Janssens V., Goris J.
      Biochem. J. 386:93-102(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPG1; PPH3 AND SIT4.
    10. "The yeast phosphotyrosyl phosphatase activator is part of the Tap42-phosphatase complexes."
      Zheng Y., Jiang Y.
      Mol. Biol. Cell 16:2119-2127(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SIT4 AND TAP42.
    11. "The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/trans-isomerase."
      Jordens J., Janssens V., Longin S., Stevens I., Martens E., Bultynck G., Engelborghs Y., Lescrinier E., Waelkens E., Goris J., Van Hoof C.
      J. Biol. Chem. 281:6349-6357(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-205.
    12. "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-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPTPA1_YEAST
    AccessioniPrimary (citable) accession number: P40454
    Secondary accession number(s): D6VVD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 124 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 4590 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 IX
      Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

    External Data

    Dasty 3