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P48461

- PP11_DROME

UniProt

P48461 - PP11_DROME

Protein

Serine/threonine-protein phosphatase alpha-1 isoform

Gene

Pp1alpha-96A

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    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 bindingi62 – 621Manganese 1By similarity
    Metal bindingi64 – 641Manganese 1By similarity
    Metal bindingi90 – 901Manganese 1By similarity
    Metal bindingi90 – 901Manganese 2By similarity
    Metal bindingi122 – 1221Manganese 2By similarity
    Active sitei123 – 1231Proton donorBy similarity
    Metal bindingi171 – 1711Manganese 2By similarity
    Metal bindingi246 – 2461Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein serine/threonine phosphatase activity Source: FlyBase

    GO - Biological processi

    1. defense response to Gram-negative bacterium Source: FlyBase
    2. positive regulation of innate immune response Source: FlyBase
    3. protein dephosphorylation Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    SignaLinkiP48461.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase alpha-1 isoform (EC:3.1.3.16)
    Gene namesi
    Name:Pp1alpha-96A
    Synonyms:Pp1-96A
    ORF Names:CG6593
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0003134. Pp1alpha-96A.

    Subcellular locationi

    GO - Cellular componenti

    1. protein phosphatase type 1 complex Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 327327Serine/threonine-protein phosphatase alpha-1 isoformPRO_0000058791Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei315 – 3151Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP48461.
    PRIDEiP48461.

    Expressioni

    Gene expression databases

    BgeeiP48461.

    Interactioni

    Subunit structurei

    Interacts with Nop17l.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NiPp1Q9V7W93EBI-91997,EBI-108894
    Nop17lQ0E9G34EBI-91997,EBI-150380

    Protein-protein interaction databases

    BioGridi67848. 14 interactions.
    DIPiDIP-19812N.
    IntActiP48461. 24 interactions.
    MINTiMINT-190817.

    Structurei

    3D structure databases

    ProteinModelPortaliP48461.
    SMRiP48461. Positions 5-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000062911.
    InParanoidiP48461.
    KOiK06269.
    OMAiPRGANSK.
    OrthoDBiEOG7TJ3K3.
    PhylomeDBiP48461.

    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.

    P48461-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDIMNIDSI ISRLLEVRGA RPGKNVQLSE SEIRSLCLKS REIFLSQPIL    50
    LELEAPLKIC GDIHGQYYDL LRLFEYGGFP PESNYLFLGD YVDRGKQSLE 100
    TICLLLAYKI KYAENFFLLR GNHECASINR IYGFYDECKR RYTIKLWKTF 150
    TDCFNCLPVA AIVDEKIFCC HGGLSPDLSS MEQIRRIMRP TDVPDQGLLC 200
    DLLWSDPDKD TMGWGENDRG VSFTFGAEVV GKFLQKHEFD LICRAHQVVE 250
    DGYEFFAKRQ LVTLFSAPNY CGEFDNAGAM MSVDDTLMCS FQILKPADKR 300
    RFVYPNFGSS GRPLTPPRGA NNKNKKK 327
    Length:327
    Mass (Da):37,370
    Last modified:February 1, 1996 - v1
    Checksum:i372390FBBB3CA8F0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56438 mRNA. Translation: CAA39820.1.
    AE014297 Genomic DNA. Translation: AAF56306.1.
    BT016110 mRNA. Translation: AAV36995.1.
    PIRiS13827.
    RefSeqiNP_001262919.1. NM_001275990.1.
    NP_524484.1. NM_079760.3.
    UniGeneiDm.2362.

    Genome annotation databases

    EnsemblMetazoaiFBtr0084642; FBpp0084026; FBgn0003134.
    GeneIDi42922.
    KEGGidme:Dmel_CG6593.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56438 mRNA. Translation: CAA39820.1 .
    AE014297 Genomic DNA. Translation: AAF56306.1 .
    BT016110 mRNA. Translation: AAV36995.1 .
    PIRi S13827.
    RefSeqi NP_001262919.1. NM_001275990.1.
    NP_524484.1. NM_079760.3.
    UniGenei Dm.2362.

    3D structure databases

    ProteinModelPortali P48461.
    SMRi P48461. Positions 5-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67848. 14 interactions.
    DIPi DIP-19812N.
    IntActi P48461. 24 interactions.
    MINTi MINT-190817.

    Proteomic databases

    PaxDbi P48461.
    PRIDEi P48461.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0084642 ; FBpp0084026 ; FBgn0003134 .
    GeneIDi 42922.
    KEGGi dme:Dmel_CG6593.

    Organism-specific databases

    CTDi 42922.
    FlyBasei FBgn0003134. Pp1alpha-96A.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00530000062911.
    InParanoidi P48461.
    KOi K06269.
    OMAi PRGANSK.
    OrthoDBi EOG7TJ3K3.
    PhylomeDBi P48461.

    Enzyme and pathway databases

    SignaLinki P48461.

    Miscellaneous databases

    ChiTaRSi Pp1alpha-96A. drosophila.
    GenomeRNAii 42922.
    NextBioi 831285.

    Gene expression databases

    Bgeei P48461.

    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. "Drosophila contains three genes that encode distinct isoforms of protein phosphatase 1."
      Dombradi V., Axton J.M., Brewis N.D., da Cruz e Silva E.F., Alphey L., Cohen P.T.W.
      Eur. J. Biochem. 194:739-745(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryo.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. "Towards a comprehensive analysis of the protein phosphatase 1 interactome in Drosophila."
      Bennett D., Lyulcheva E., Alphey L.
      J. Mol. Biol. 364:196-212(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOP17L.
    6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiPP11_DROME
    AccessioniPrimary (citable) accession number: P48461
    Secondary accession number(s): Q5U0Y2, Q9VC69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3