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Q27889

- PP2B2_DROME

UniProt

Q27889 - PP2B2_DROME

Protein

Serine/threonine-protein phosphatase 2B catalytic subunit 2

Gene

Pp2B-14D

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.2 Publications

    Catalytic activityi

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

    Cofactori

    Binds 1 Fe3+ ion per subunit.By similarity
    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi156 – 1561IronBy similarity
    Metal bindingi158 – 1581IronBy similarity
    Metal bindingi184 – 1841IronBy similarity
    Metal bindingi184 – 1841ZincBy similarity
    Metal bindingi216 – 2161ZincBy similarity
    Active sitei217 – 2171Proton donorBy similarity
    Metal bindingi265 – 2651ZincBy similarity
    Metal bindingi347 – 3471ZincBy similarity

    GO - Molecular functioni

    1. calcium-dependent protein serine/threonine phosphatase activity Source: FlyBase
    2. calmodulin binding Source: FlyBase
    3. calmodulin-dependent protein phosphatase activity Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. protein serine/threonine phosphatase activity Source: FlyBase

    GO - Biological processi

    1. female meiotic division Source: FlyBase
    2. meiotic nuclear division Source: FlyBase
    3. protein dephosphorylation Source: FlyBase
    4. sleep Source: FlyBase
    5. wing disc development Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Calcium, Calmodulin-binding, Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_184321. Ca2+ pathway.
    REACT_203584. FCERI mediated Ca+2 mobilization.
    REACT_213958. DARPP-32 events.
    SignaLinkiQ27889.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2B catalytic subunit 2 (EC:3.1.3.16)
    Alternative name(s):
    Calmodulin-dependent calcineurin A2 subunit
    Gene namesi
    Name:Pp2B-14D
    ORF Names:CG9842
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0011826. Pp2B-14D.

    Subcellular locationi

    GO - Cellular componenti

    1. calcineurin complex Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 570570Serine/threonine-protein phosphatase 2B catalytic subunit 2PRO_0000058831Add
    BLAST

    Proteomic databases

    PaxDbiQ27889.
    PRIDEiQ27889.

    Expressioni

    Tissue specificityi

    Expressed in CNS and PNS.1 Publication

    Developmental stagei

    Expressed both maternally and zygotically in embryos, larvae and adults.2 Publications

    Gene expression databases

    BgeeiQ27889.

    Interactioni

    Subunit structurei

    Interacts with sra in a complex that contains CanA-14F.2 Publications

    Protein-protein interaction databases

    BioGridi58962. 33 interactions.
    DIPiDIP-17529N.
    IntActiQ27889. 10 interactions.
    MINTiMINT-809182.

    Structurei

    3D structure databases

    ProteinModelPortaliQ27889.
    SMRiQ27889. Positions 86-479.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi36 – 405Poly-Asn

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000063087.
    InParanoidiQ27889.
    KOiK04348.
    OMAiMFWSPED.
    OrthoDBiEOG7BZVSC.
    PhylomeDBiQ27889.

    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.

    Q27889-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSNNQSSSV AQAATSARTV SAGSAEATDA NSTASNNNNN SSSTAAAGNN    50
    SDNSSPTTGT GTGASTGKLH GGHTAVNTKE RVVDSVPFPP SHKLTLAEVF 100
    DQRTGKPNHE LLKQHFILEG RIEEAPALKI IQDGAALLRQ EKTMIDIEAP 150
    VTVCGDIHGQ FYDLMKLFEV GGSPASTKYL FLGDYVDRGY FSIECVLYLW 200
    SLKITYPQTL FLLRGNHECR HLTEYFTFKQ ECKIKYSERV YDACMDAFDC 250
    LPLAALMNQQ FLCVHGGLSP EIHELEDIRR LDRFKEPPAF GPMCDLLWSD 300
    PLEDFGNEKN SDFYTHNSVR GCSYFYSYAA CCDFLQNNNL LSIIRAHEAQ 350
    DAGYRMYRKS QTTGFPSLIT IFSAPNYLDV YNNKAAVLKY ENNVMNIRQF 400
    NCSPHPYWLP NFMDVFTWSL PFVGEKVTEM LVNVLNICSD DELMTEESEE 450
    PLSDDEAALR KEVIRNKIRA IGKMARVFSV LREESESVLQ LKGLTPTGAL 500
    PLGALSGGKQ SLKNAMQGFS PNHKITSFAE AKGLDAVNER MPPRRDQPPT 550
    PSEDPNQHSQ QGGKNGAGHG 570
    Length:570
    Mass (Da):63,101
    Last modified:August 30, 2005 - v2
    Checksum:i4A5429A620C0C275
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111Missing(PubMed:8849894)Curated
    Sequence conflicti133 – 1331D → E in CAA54807. (PubMed:8313960)Curated
    Sequence conflicti175 – 1751A → Q in CAA54807. (PubMed:8313960)Curated
    Sequence conflicti175 – 1751A → Q in AAB29893. (PubMed:8849894)Curated
    Sequence conflicti323 – 33311SYFYSYAACCD → CY in CAA54807. (PubMed:8313960)CuratedAdd
    BLAST
    Sequence conflicti407 – 4071Y → I in CAA54807. (PubMed:8313960)Curated
    Sequence conflicti459 – 4591L → V in CAA54807. (PubMed:8313960)Curated
    Sequence conflicti491 – 4911Missing in CAA54807. (PubMed:8313960)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77768 mRNA. Translation: CAA54807.1.
    S68806 mRNA. Translation: AAB29893.1.
    AE014298 Genomic DNA. Translation: AAF48622.1.
    BT010083 mRNA. Translation: AAQ22552.1.
    PIRiS41743.
    S70551.
    RefSeqiNP_001245715.1. NM_001258786.2.
    NP_001245716.1. NM_001258787.1.
    NP_523373.2. NM_078649.3.
    UniGeneiDm.33340.

    Genome annotation databases

    EnsemblMetazoaiFBtr0074294; FBpp0074069; FBgn0011826.
    FBtr0305593; FBpp0294044; FBgn0011826.
    FBtr0309793; FBpp0301546; FBgn0011826.
    GeneIDi32624.
    KEGGidme:Dmel_CG9842.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77768 mRNA. Translation: CAA54807.1 .
    S68806 mRNA. Translation: AAB29893.1 .
    AE014298 Genomic DNA. Translation: AAF48622.1 .
    BT010083 mRNA. Translation: AAQ22552.1 .
    PIRi S41743.
    S70551.
    RefSeqi NP_001245715.1. NM_001258786.2.
    NP_001245716.1. NM_001258787.1.
    NP_523373.2. NM_078649.3.
    UniGenei Dm.33340.

    3D structure databases

    ProteinModelPortali Q27889.
    SMRi Q27889. Positions 86-479.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58962. 33 interactions.
    DIPi DIP-17529N.
    IntActi Q27889. 10 interactions.
    MINTi MINT-809182.

    Proteomic databases

    PaxDbi Q27889.
    PRIDEi Q27889.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0074294 ; FBpp0074069 ; FBgn0011826 .
    FBtr0305593 ; FBpp0294044 ; FBgn0011826 .
    FBtr0309793 ; FBpp0301546 ; FBgn0011826 .
    GeneIDi 32624.
    KEGGi dme:Dmel_CG9842.

    Organism-specific databases

    CTDi 32624.
    FlyBasei FBgn0011826. Pp2B-14D.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00530000063087.
    InParanoidi Q27889.
    KOi K04348.
    OMAi MFWSPED.
    OrthoDBi EOG7BZVSC.
    PhylomeDBi Q27889.

    Enzyme and pathway databases

    Reactomei REACT_184321. Ca2+ pathway.
    REACT_203584. FCERI mediated Ca+2 mobilization.
    REACT_213958. DARPP-32 events.
    SignaLinki Q27889.

    Miscellaneous databases

    ChiTaRSi Pp2B-14D. drosophila.
    GenomeRNAii 32624.
    NextBioi 779520.

    Gene expression databases

    Bgeei Q27889.

    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. "Identification of a cDNA encoding a Drosophila calcium/calmodulin regulated protein phosphatase, which has its most abundant expression in the early embryo."
      Brown L., Chen M.X., Cohen P.T.W.
      FEBS Lett. 339:124-128(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
      Strain: Oregon-R.
      Tissue: Eye imaginal disk.
    2. "Molecular characterization of neurally expressing genes in the para sodium channel gene cluster of Drosophila."
      Hong C.-S., Ganetzky B.
      Genetics 142:879-892(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    6. "The calcineurin regulator sra plays an essential role in female meiosis in Drosophila."
      Takeo S., Tsuda M., Akahori S., Matsuo T., Aigaki T.
      Curr. Biol. 16:1435-1440(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SRA.
    7. "Shaggy/glycogen synthase kinase 3beta and phosphorylation of Sarah/regulator of calcineurin are essential for completion of Drosophila female meiosis."
      Takeo S., Swanson S.K., Nandanan K., Nakai Y., Aigaki T., Washburn M.P., Florens L., Hawley R.S.
      Proc. Natl. Acad. Sci. U.S.A. 109:6382-6389(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRA.

    Entry informationi

    Entry nameiPP2B2_DROME
    AccessioniPrimary (citable) accession number: Q27889
    Secondary accession number(s): Q26248, Q9VXF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 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