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O15757

- PP1_DICDI

UniProt

O15757 - PP1_DICDI

Protein

Serine/threonine-protein phosphatase PP1

Gene

pppB

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Protein phosphatase activity in vitro.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

    Inhibited by okadaic acid, tautomycin and calyculin A. Inhibited by phosphatase inhibitor 2 (dpiA).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi60 – 601Manganese 1By similarity
    Metal bindingi62 – 621Manganese 1By similarity
    Metal bindingi88 – 881Manganese 1By similarity
    Metal bindingi88 – 881Manganese 2By similarity
    Metal bindingi120 – 1201Manganese 2By similarity
    Active sitei121 – 1211Proton donorBy similarity
    Metal bindingi169 – 1691Manganese 2By similarity
    Metal bindingi244 – 2441Manganese 2By similarity

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1 (EC:3.1.3.16)
    Alternative name(s):
    DdPP1c
    Gene namesi
    Name:pppB
    ORF Names:DDB_G0275619
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 2, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0275619. pppB.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi269 – 2691F → C: Five-fold increase in phosphatase activity, decreased binding efficiency to dpiA and reduced sensitivity to dpiA inhibition. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 321321Serine/threonine-protein phosphatase PP1PRO_0000328376Add
    BLAST

    Proteomic databases

    PRIDEiO15757.

    Expressioni

    Developmental stagei

    Expressed throughout development.1 Publication

    Interactioni

    Subunit structurei

    Interacts with dpiA.1 Publication

    Protein-protein interaction databases

    STRINGi44689.DDB_0185058.

    Structurei

    3D structure databases

    ProteinModelPortaliO15757.
    SMRiO15757. Positions 2-298.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    KOiK06269.
    OMAiGSKPGQQ.
    PhylomeDBiO15757.

    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.

    O15757-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEIDLDSIIT RLLEPRTTKP GKLVDLAEEE IRYLTVQATE IFINQPILLE    50
    LEAPIKICGD IHGQYYDLLR LFEYGGFPPQ SNYLFLGDYV DRGKQSLETI 100
    CLLLAYKIKY PENFFILRGN HECASINRIY GFYDECKRRY NSKLWKAFTD 150
    CFNCLPVAAI IDEKIFCMHG GLSPDLKNMD QIRRITRPTV VPDFGLLCDL 200
    LWADPDKNIQ GWEDNDRGVS YTFGADVVES FLKKHDLDLV CRAHQVVEDG 250
    YEFFAKRQLV TLFSAPNYFG EFDNAGAMMG VDETLMCSFQ ILKPADKKKL 300
    TNDSNGRPLT PPRNKQQKPK K 321
    Length:321
    Mass (Da):36,939
    Last modified:January 1, 1998 - v1
    Checksum:i571EECA8BE113BA4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF020537 mRNA. Translation: AAB71415.1.
    AAFI02000013 Genomic DNA. Translation: EAL69560.1.
    RefSeqiXP_643639.1. XM_638547.1.

    Genome annotation databases

    EnsemblProtistsiDDB0185058; DDB0185058; DDB_G0275619.
    GeneIDi8620226.
    KEGGiddi:DDB_G0275619.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF020537 mRNA. Translation: AAB71415.1 .
    AAFI02000013 Genomic DNA. Translation: EAL69560.1 .
    RefSeqi XP_643639.1. XM_638547.1.

    3D structure databases

    ProteinModelPortali O15757.
    SMRi O15757. Positions 2-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0185058.

    Proteomic databases

    PRIDEi O15757.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0185058 ; DDB0185058 ; DDB_G0275619 .
    GeneIDi 8620226.
    KEGGi ddi:DDB_G0275619.

    Organism-specific databases

    dictyBasei DDB_G0275619. pppB.

    Phylogenomic databases

    eggNOGi COG0639.
    KOi K06269.
    OMAi GSKPGQQ.
    PhylomeDBi O15757.

    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. "Dictyostelium discoideum protein phosphatase-1 catalytic subunit exhibits distinct biochemical properties."
      Andrioli L.P.M., Zaini P.A., Viviani W., da Silva A.M.
      Biochem. J. 373:703-711(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF PHE-269.
      Strain: AX4.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    3. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    4. "Identification and domain mapping of Dictyostelium discoideum type-1 protein phosphatase inhibitor-2."
      Sousa-Canavez J.M., Beton D., Gonzalez-Kristeller D.C., da Silva A.M.
      Biochimie 89:692-701(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH DPIA, MUTAGENESIS OF PHE-269.
      Strain: AX4.

    Entry informationi

    Entry nameiPP1_DICDI
    AccessioniPrimary (citable) accession number: O15757
    Secondary accession number(s): Q552P2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3