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P23635

- PP2A1_SCHPO

UniProt

P23635 - PP2A1_SCHPO

Protein

Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit

Gene

ppa1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Essential role in cell cycle control. PP2A may be involved in controlling the entry into mitosis, possibly acting as an inhibitor.

    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 bindingi57 – 571Manganese 1By similarity
    Metal bindingi59 – 591Manganese 1By similarity
    Metal bindingi85 – 851Manganese 1By similarity
    Metal bindingi85 – 851Manganese 2By similarity
    Metal bindingi117 – 1171Manganese 2By similarity
    Active sitei118 – 1181Proton donorBy similarity
    Metal bindingi167 – 1671Manganese 2By similarity
    Metal bindingi241 – 2411Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoprotein phosphatase activity Source: UniProtKB-KW

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW
    2. protein dephosphorylation Source: PomBase
    3. regulation of cytoplasmic translation Source: PomBase
    4. signal transduction Source: PomBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit (EC:3.1.3.16)
    Gene namesi
    Name:ppa1
    ORF Names:SPAC823.15
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC823.15.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: PomBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunitPRO_0000058871Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei309 – 3091Leucine methyl esterBy similarity

    Keywords - PTMi

    Methylation

    Proteomic databases

    MaxQBiP23635.

    Interactioni

    Protein-protein interaction databases

    BioGridi278531. 12 interactions.
    MINTiMINT-4687784.
    STRINGi4896.SPAC823.15-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP23635.
    SMRiP23635. Positions 9-309.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172696.
    KOiK04382.
    OMAiNSHTFIQ.
    PhylomeDBiP23635.

    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.

    P23635-1 [UniParc]FASTAAdd to Basket

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    MSVSGKIGEV DRWIEQLSRC EPLSEEDVIQ MCDLAKEVLS VESNVQSVRC    50
    PVTVCGDIHG QFHDLMELFN IGGPSPDTNY LFMGDYVDRG YHSVETVSLL 100
    IAFKIRYPQR ITILRGNHES RQITQVYGFY DECLRKYGNA NVWQYFTDLF 150
    DYLPLTALIE DRIFCLHGGL SPSIDTLDHV RILDRVQEVP HEGPICDLLW 200
    SDPDDRPGWG ISPRGAGYTF GPDIAEAFNH NNGLDLIARA HQLVMEGYNW 250
    TTNHNVVTIF SAPNYCYRCG NQAAIMGIDD HINYAFIQYD TAPRKEELHV 300
    TRRTPDYFL 309
    Length:309
    Mass (Da):35,291
    Last modified:November 1, 1991 - v1
    Checksum:i0F47604E5F740B0C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58518 Genomic DNA. Translation: AAA63578.1.
    CU329670 Genomic DNA. Translation: CAB90160.1.
    PIRiA36076.
    RefSeqiNP_593842.1. NM_001019271.2.

    Genome annotation databases

    EnsemblFungiiSPAC823.15.1; SPAC823.15.1:pep; SPAC823.15.
    GeneIDi2542052.
    KEGGispo:SPAC823.15.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58518 Genomic DNA. Translation: AAA63578.1 .
    CU329670 Genomic DNA. Translation: CAB90160.1 .
    PIRi A36076.
    RefSeqi NP_593842.1. NM_001019271.2.

    3D structure databases

    ProteinModelPortali P23635.
    SMRi P23635. Positions 9-309.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 278531. 12 interactions.
    MINTi MINT-4687784.
    STRINGi 4896.SPAC823.15-1.

    Proteomic databases

    MaxQBi P23635.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC823.15.1 ; SPAC823.15.1:pep ; SPAC823.15 .
    GeneIDi 2542052.
    KEGGi spo:SPAC823.15.

    Organism-specific databases

    PomBasei SPAC823.15.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172696.
    KOi K04382.
    OMAi NSHTFIQ.
    PhylomeDBi P23635.

    Miscellaneous databases

    NextBioi 20803127.

    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. "Distinct, essential roles of type 1 and 2A protein phosphatases in the control of the fission yeast cell division cycle."
      Kinoshita N., Ohkura H., Yanagida M.
      Cell 63:405-415(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 972 / HM123.
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.

    Entry informationi

    Entry nameiPP2A1_SCHPO
    AccessioniPrimary (citable) accession number: P23635
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3