Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P23696

- PP2A_DROME

UniProt

P23696 - PP2A_DROME

Protein

Serine/threonine-protein phosphatase PP2A

Gene

mts

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 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. phosphatase regulator activity Source: FlyBase
    3. protein serine/threonine phosphatase activity Source: FlyBase

    GO - Biological processi

    1. actin filament organization Source: FlyBase
    2. asymmetric neuroblast division Source: FlyBase
    3. autophagy Source: FlyBase
    4. canonical Wnt signaling pathway Source: FlyBase
    5. cell adhesion Source: FlyBase
    6. centriole replication Source: FlyBase
    7. centrosome cycle Source: FlyBase
    8. centrosome duplication Source: FlyBase
    9. centrosome organization Source: FlyBase
    10. chromosome segregation Source: FlyBase
    11. establishment of epithelial cell polarity Source: FlyBase
    12. microtubule cytoskeleton organization Source: FlyBase
    13. mitotic cell cycle Source: FlyBase
    14. mitotic nuclear division Source: FlyBase
    15. negative regulation of neuroblast proliferation Source: FlyBase
    16. oogenesis Source: FlyBase
    17. phagocytosis Source: FlyBase
    18. positive regulation of smoothened signaling pathway Source: FlyBase
    19. protein dephosphorylation Source: FlyBase
    20. R7 cell fate commitment Source: FlyBase
    21. regulation of catalytic activity Source: GOC
    22. regulation of cell shape Source: FlyBase
    23. response to light stimulus Source: FlyBase
    24. spindle assembly Source: FlyBase
    25. spindle organization Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_180232. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_180238. Spry regulation of FGF signaling.
    REACT_180845. Cyclin D associated events in G1.
    REACT_184313. Initiation of Nuclear Envelope Reformation.
    REACT_184356. MASTL Facilitates Mitotic Progression.
    REACT_205322. PP2A-mediated dephosphorylation of key metabolic factors.
    REACT_206319. Glycolysis.
    REACT_220429. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_221837. Integration of energy metabolism.
    SignaLinkiP23696.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP2A (EC:3.1.3.16)
    Alternative name(s):
    Protein microtubule star
    Gene namesi
    Name:mts
    Synonyms:PP2A, Pp2A-28D
    ORF Names:CG7109
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0004177. mts.

    Subcellular locationi

    GO - Cellular componenti

    1. centriole Source: FlyBase
    2. cytoplasm Source: FlyBase
    3. protein phosphatase type 2A complex Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309Serine/threonine-protein phosphatase PP2APRO_0000058850Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1 (PPME1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization By similarity.By similarity

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiP23696.
    PRIDEiP23696.

    Expressioni

    Gene expression databases

    BgeeiP23696.

    Interactioni

    Protein-protein interaction databases

    BioGridi70018. 59 interactions.
    DIPiDIP-17814N.
    IntActiP23696. 5 interactions.
    MINTiMINT-333628.
    STRINGi7227.FBpp0079148.

    Structurei

    3D structure databases

    ProteinModelPortaliP23696.
    SMRiP23696. Positions 7-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00550000074618.
    InParanoidiP23696.
    KOiK04382.
    OMAiQVKTLCD.
    OrthoDBiEOG74N5H2.
    PhylomeDBiP23696.

    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.

    P23696-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEDKATTKDL DQWIEQLNEC NQLTETQVRT LCDKAKEILS KESNVQEVKC    50
    PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL 100
    VALKVRYRER ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF 150
    DYLPLTALVD GQIFCLHGGL SPSIDSLDHI RALDRLQEVP HEGPMCDLLW 200
    SDPDDRGGWG ISPRGAGYTF GQDISETFNN TNGLTLVSRA HQLVMEGYNW 250
    CHDRNVVTIF SAPNYCYRCG NQAALMELDD SLKFSFLQFD PAPRRGEPHV 300
    TRRTPDYFL 309
    Length:309
    Mass (Da):35,469
    Last modified:November 1, 1991 - v1
    Checksum:i6F1E2486A514FBAF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55199 mRNA. Translation: CAA38984.1.
    X78577 mRNA. Translation: CAA55315.1.
    AE014134 Genomic DNA. Translation: AAF52567.2.
    AY058571 mRNA. Translation: AAL13800.1.
    PIRiS12961.
    RefSeqiNP_476805.1. NM_057457.3.
    UniGeneiDm.4245.

    Genome annotation databases

    EnsemblMetazoaiFBtr0079525; FBpp0079148; FBgn0004177.
    GeneIDi45959.
    KEGGidme:Dmel_CG7109.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55199 mRNA. Translation: CAA38984.1 .
    X78577 mRNA. Translation: CAA55315.1 .
    AE014134 Genomic DNA. Translation: AAF52567.2 .
    AY058571 mRNA. Translation: AAL13800.1 .
    PIRi S12961.
    RefSeqi NP_476805.1. NM_057457.3.
    UniGenei Dm.4245.

    3D structure databases

    ProteinModelPortali P23696.
    SMRi P23696. Positions 7-293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 70018. 59 interactions.
    DIPi DIP-17814N.
    IntActi P23696. 5 interactions.
    MINTi MINT-333628.
    STRINGi 7227.FBpp0079148.

    Proteomic databases

    PaxDbi P23696.
    PRIDEi P23696.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0079525 ; FBpp0079148 ; FBgn0004177 .
    GeneIDi 45959.
    KEGGi dme:Dmel_CG7109.

    Organism-specific databases

    CTDi 45959.
    FlyBasei FBgn0004177. mts.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00550000074618.
    InParanoidi P23696.
    KOi K04382.
    OMAi QVKTLCD.
    OrthoDBi EOG74N5H2.
    PhylomeDBi P23696.

    Enzyme and pathway databases

    Reactomei REACT_180232. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_180238. Spry regulation of FGF signaling.
    REACT_180845. Cyclin D associated events in G1.
    REACT_184313. Initiation of Nuclear Envelope Reformation.
    REACT_184356. MASTL Facilitates Mitotic Progression.
    REACT_205322. PP2A-mediated dephosphorylation of key metabolic factors.
    REACT_206319. Glycolysis.
    REACT_220429. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_221837. Integration of energy metabolism.
    SignaLinki P23696.

    Miscellaneous databases

    ChiTaRSi mts. drosophila.
    GenomeRNAii 45959.
    NextBioi 838521.

    Gene expression databases

    Bgeei P23696.

    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. "The structure of protein phosphatase 2A is as highly conserved as that of protein phosphatase 1."
      Orgad S., Brewis N.D., Alphey L., Axton J.M., Dudai Y., Cohen P.T.W.
      FEBS Lett. 275:44-48(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.

    Entry informationi

    Entry nameiPP2A_DROME
    AccessioniPrimary (citable) accession number: P23696
    Secondary accession number(s): Q9VLW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 134 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