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P23595

- PP2A2_YEAST

UniProt

P23595 - PP2A2_YEAST

Protein

Serine/threonine-protein phosphatase PP2A-2 catalytic subunit

Gene

PPH22

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 142 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Exact function not known, phosphatase 2A performs an essential cellular function.

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi125 – 1251Manganese 1By similarity
    Metal bindingi127 – 1271Manganese 1By similarity
    Metal bindingi153 – 1531Manganese 1By similarity
    Metal bindingi153 – 1531Manganese 2By similarity
    Metal bindingi185 – 1851Manganese 2By similarity
    Active sitei186 – 1861Proton donorBy similarity
    Metal bindingi235 – 2351Manganese 2By similarity
    Metal bindingi309 – 3091Manganese 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. actin filament organization Source: SGD
    2. budding cell bud growth Source: SGD
    3. G1/S transition of mitotic cell cycle Source: SGD
    4. mitotic spindle assembly checkpoint Source: SGD
    5. protein dephosphorylation Source: SGD
    6. regulation of translation Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29573-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP2A-2 catalytic subunit (EC:3.1.3.16)
    Gene namesi
    Name:PPH22
    Synonyms:SIS4
    Ordered Locus Names:YDL188C
    ORF Names:D1271
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL188c.
    SGDiS000002347. PPH22.

    Subcellular locationi

    GO - Cellular componenti

    1. condensed nuclear chromosome, centromeric region Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Serine/threonine-protein phosphatase PP2A-2 catalytic subunitPRO_0000058874Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381Phosphoserine1 Publication
    Modified residuei43 – 431Phosphothreonine3 Publications
    Modified residuei377 – 3771Leucine methyl ester2 Publications

    Post-translational modificationi

    Reversibly methyl esterified on Leu-377 by leucine carboxyl methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1 (PPE1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization.2 Publications

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP23595.
    PaxDbiP23595.

    Expressioni

    Gene expression databases

    GenevestigatoriP23595.

    Interactioni

    Subunit structurei

    Inactivated in a complex with phosphatase methylesterase PPE1 (PP2Ai). Interacts with phosphatase 2A activator RRD2, which can reactivate PP2Ai by dissociating the catalytic subunit from the complex. Interacts with TAP42.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HMT1P380743EBI-12752,EBI-8394
    TAP42Q043724EBI-12752,EBI-18926
    TIP41Q121993EBI-12752,EBI-38123

    Protein-protein interaction databases

    BioGridi31857. 98 interactions.
    DIPiDIP-2283N.
    IntActiP23595. 28 interactions.
    MINTiMINT-499723.
    STRINGi4932.YDL188C.

    Structurei

    3D structure databases

    ProteinModelPortaliP23595.
    SMRiP23595. Positions 43-360.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-2A subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00550000074618.
    HOGENOMiHOG000172696.
    KOiK04382.
    OMAiSVPVTIC.
    OrthoDBiEOG7FFN29.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23595-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDMEIDDPMH GSDEDQLSPT LDEDMNSDDG KNNTKARSND EDTDEELEDF    50
    NFKPGSSGIA DHKSSKPLKL TNTNINQLDQ WIEHLSKCEP LSEDDVARLC 100
    KMAVDVLQFE ENVKPINVPV TICGDVHGQF HDLLELFKIG GPCPDTNYLF 150
    MGDYVDRGYY SVETVSYLVA MKVRYPHRIT ILRGNHESRQ ITQVYGFYDE 200
    CLRKYGSANV WKMFTDLFDY FPVTALVDNK IFCLHGGLSP MIETIDQVRD 250
    LNRIQEVPHE GPMCDLLWSD PDDRGGWGIS PRGAGFTFGQ DISEQFNHTN 300
    DLSLIARAHQ LVMEGYSWSH QQNVVTIFSA PNYCYRCGNQ AAIMEVDENH 350
    NRQFLQYDPS VRPGEPTVTR KTPDYFL 377
    Length:377
    Mass (Da):43,047
    Last modified:November 1, 1991 - v1
    Checksum:i549D3C6F1E2EB335
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56262 Genomic DNA. Translation: CAA39703.1.
    M60317 Genomic DNA. Translation: AAB04032.1.
    X58857 Genomic DNA. Translation: CAA41659.1.
    X83276 Genomic DNA. Translation: CAA58259.1.
    Z74236 Genomic DNA. Translation: CAA98765.1.
    BK006938 Genomic DNA. Translation: DAA11675.1.
    PIRiB41525. PABY22.
    RefSeqiNP_010093.1. NM_001180248.1.

    Genome annotation databases

    EnsemblFungiiYDL188C; YDL188C; YDL188C.
    GeneIDi851339.
    KEGGisce:YDL188C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56262 Genomic DNA. Translation: CAA39703.1 .
    M60317 Genomic DNA. Translation: AAB04032.1 .
    X58857 Genomic DNA. Translation: CAA41659.1 .
    X83276 Genomic DNA. Translation: CAA58259.1 .
    Z74236 Genomic DNA. Translation: CAA98765.1 .
    BK006938 Genomic DNA. Translation: DAA11675.1 .
    PIRi B41525. PABY22.
    RefSeqi NP_010093.1. NM_001180248.1.

    3D structure databases

    ProteinModelPortali P23595.
    SMRi P23595. Positions 43-360.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31857. 98 interactions.
    DIPi DIP-2283N.
    IntActi P23595. 28 interactions.
    MINTi MINT-499723.
    STRINGi 4932.YDL188C.

    Proteomic databases

    MaxQBi P23595.
    PaxDbi P23595.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL188C ; YDL188C ; YDL188C .
    GeneIDi 851339.
    KEGGi sce:YDL188C.

    Organism-specific databases

    CYGDi YDL188c.
    SGDi S000002347. PPH22.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00550000074618.
    HOGENOMi HOG000172696.
    KOi K04382.
    OMAi SVPVTIC.
    OrthoDBi EOG7FFN29.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29573-MONOMER.

    Miscellaneous databases

    NextBioi 968414.

    Gene expression databases

    Genevestigatori P23595.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Saccharomyces cerevisiae protein phosphatase 2A performs an essential cellular function and is encoded by two genes."
      Sneddon A.A., Cohen P.T.W., Stark M.J.R.
      EMBO J. 9:4339-4346(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: LL20.
    2. "The SIT4 protein phosphatase functions in late G1 for progression into S phase."
      Sutton A., Immanuel D., Arndt K.T.
      Mol. Cell. Biol. 11:2133-2148(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth and bud morphogenesis."
      Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.
      Mol. Cell. Biol. 11:4876-4884(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 208353 / W303-1A.
    4. "New open reading frames, one of which is similar to the nifV gene of Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of Saccharomyces cerevisiae."
      Verhasselt P., Voet M., Volckaert G.
      Yeast 11:961-966(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo."
      Wu J., Tolstykh T., Lee J., Boyd K., Stock J.B., Broach J.R.
      EMBO J. 19:5672-5681(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LEU-377 BY PPM1, DEMETHYLATION BY PPE1.
    8. "Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast."
      Kalhor H.R., Luk K., Ramos A., Zobel-Thropp P., Clarke S.
      Arch. Biochem. Biophys. 395:239-245(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LEU-377 BY PPM1.
    9. "Interaction with Tap42 is required for the essential function of Sit4 and type 2A phosphatases."
      Wang H., Wang X., Jiang Y.
      Mol. Biol. Cell 14:4342-4351(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAP42.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "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 PPE1 AND RRD2.
    12. "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-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    13. "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-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-38 AND THR-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPP2A2_YEAST
    AccessioniPrimary (citable) accession number: P23595
    Secondary accession number(s): D6VRG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 142 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 4110 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3