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P48462

- PP1B_DROME

UniProt

P48462 - PP1B_DROME

Protein

Serine/threonine-protein phosphatase beta isoform

Gene

flw

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 130 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Required for cell adhesion in non-muscle tissues and in maintenance of muscle attachment. Vital for larval development.1 Publication

    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 bindingi63 – 631Manganese 1By similarity
    Metal bindingi65 – 651Manganese 1By similarity
    Metal bindingi91 – 911Manganese 1By similarity
    Metal bindingi91 – 911Manganese 2By similarity
    Metal bindingi123 – 1231Manganese 2By similarity
    Active sitei124 – 1241Proton donorBy similarity
    Metal bindingi172 – 1721Manganese 2By similarity
    Metal bindingi247 – 2471Manganese 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. chromosome segregation Source: FlyBase
    3. female germline ring canal formation Source: FlyBase
    4. imaginal disc-derived wing morphogenesis Source: FlyBase
    5. mesoderm development Source: FlyBase
    6. negative regulation of JNK cascade Source: FlyBase
    7. oocyte nucleus migration involved in oocyte dorsal/ventral axis specification Source: FlyBase
    8. ovarian nurse cell to oocyte transport Source: FlyBase
    9. protein dephosphorylation Source: FlyBase
    10. regulation of actomyosin contractile ring contraction Source: FlyBase
    11. striated muscle tissue development Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_184294. Regulation of PLK1 Activity at G2/M Transition.
    SignaLinkiP48462.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase beta isoform (EC:3.1.3.16)
    Alternative name(s):
    Protein flap wing
    Gene namesi
    Name:flw
    Synonyms:PP1-9C, PP1-BETA-9C
    ORF Names:CG2096
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0000711. flw.

    Subcellular locationi

    GO - Cellular componenti

    1. protein phosphatase type 1 complex Source: FlyBase

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi133 – 1331Y → F: Semi lethal, adult escapers exhibit muscle and wing mutant phenotype; allele flw-6. 1 Publication
    Mutagenesisi284 – 2841V → A: Muscle and wing mutant phenotype; allele flw-1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 330330Serine/threonine-protein phosphatase beta isoformPRO_0000058794Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei315 – 3151Phosphothreonine1 Publication
    Modified residuei316 – 3161Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP48462.
    PRIDEiP48462.

    Expressioni

    Gene expression databases

    BgeeiP48462.

    Interactioni

    Subunit structurei

    Interacts with Nop17l.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Nop17lQ0E9G33EBI-869621,EBI-150380

    Protein-protein interaction databases

    BioGridi68952. 26 interactions.
    IntActiP48462. 28 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP48462.
    SMRiP48462. Positions 1-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000062911.
    HOGENOMiHOG000263972.
    InParanoidiP48462.
    KOiK06269.
    OrthoDBiEOG7TJ3K3.
    PhylomeDBiP48462.

    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.

    P48462-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDFDLNVDS LIQRLLEMRS CRTGKQVQMT EAEVRGLCLK SREIFLQQPI    50
    LLELEAPLII CGDIHGQYTD LLRLFEYGGF PPAANYLFLG DYVDRGKQSL 100
    ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRYNVKLWKT 150
    FTDCFNCLPV AAIIDEKIFC CHGGLSPDLQ GMEQIRRLMR PTDVPDTGLL 200
    CDLLWSDPDK DVQGWGENDR GVSFTFGVDV VSKFLNRHEL DLICRAHQVV 250
    EDGYEFFARR QLVTLFSAPN YCGEFDNAGG MMTVDDTLMC SFQILKPSEK 300
    KAKYLYSGMN SSRPTTPQRS APMLATNKKK 330
    Length:330
    Mass (Da):37,740
    Last modified:February 1, 1996 - v1
    Checksum:i9233DFC06EAE17AD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56439 mRNA. Translation: CAA39821.1.
    AJ249214, AJ249215 Genomic DNA. Translation: CAB59732.1.
    AE014298 Genomic DNA. Translation: AAF46583.2.
    PIRiS13828.
    RefSeqiNP_001259407.1. NM_001272478.1.
    NP_524738.1. NM_079999.3.
    UniGeneiDm.7222.

    Genome annotation databases

    EnsemblMetazoaiFBtr0071447; FBpp0071382; FBgn0000711.
    FBtr0333305; FBpp0305497; FBgn0000711.
    GeneIDi44289.
    KEGGidme:Dmel_CG2096.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56439 mRNA. Translation: CAA39821.1 .
    AJ249214 , AJ249215 Genomic DNA. Translation: CAB59732.1 .
    AE014298 Genomic DNA. Translation: AAF46583.2 .
    PIRi S13828.
    RefSeqi NP_001259407.1. NM_001272478.1.
    NP_524738.1. NM_079999.3.
    UniGenei Dm.7222.

    3D structure databases

    ProteinModelPortali P48462.
    SMRi P48462. Positions 1-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68952. 26 interactions.
    IntActi P48462. 28 interactions.

    Proteomic databases

    PaxDbi P48462.
    PRIDEi P48462.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0071447 ; FBpp0071382 ; FBgn0000711 .
    FBtr0333305 ; FBpp0305497 ; FBgn0000711 .
    GeneIDi 44289.
    KEGGi dme:Dmel_CG2096.

    Organism-specific databases

    CTDi 44289.
    FlyBasei FBgn0000711. flw.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00530000062911.
    HOGENOMi HOG000263972.
    InParanoidi P48462.
    KOi K06269.
    OrthoDBi EOG7TJ3K3.
    PhylomeDBi P48462.

    Enzyme and pathway databases

    Reactomei REACT_184294. Regulation of PLK1 Activity at G2/M Transition.
    SignaLinki P48462.

    Miscellaneous databases

    ChiTaRSi flw. drosophila.
    GenomeRNAii 44289.
    NextBioi 837117.
    PROi P48462.

    Gene expression databases

    Bgeei P48462.

    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. "Protein phosphatase 1beta is required for the maintenance of muscle attachments."
      Raghavan S., Williams I., Aslam H., Thomas D., Szoor B., Morgan G., Gross S., Turner J., Fernandes J., VijayRaghavan K., Alphey L.
      Curr. Biol. 10:269-272(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF TYR-133 AND VAL-284.
    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. "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 AND THR-316, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiPP1B_DROME
    AccessioniPrimary (citable) accession number: P48462
    Secondary accession number(s): Q9W2V5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 130 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