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P20483

- MPIP_DROME

UniProt

P20483 - MPIP_DROME

Protein

M-phase inducer phosphatase

Gene

stg

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 133 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    This protein functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It may directly dephosphorylate p34(cdc2) and activate the p34(cdc2) kinase activity.

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei379 – 3791By similarity

    GO - Molecular functioni

    1. protein tyrosine/serine/threonine phosphatase activity Source: FlyBase
    2. protein tyrosine phosphatase activity Source: FlyBase

    GO - Biological processi

    1. cell proliferation Source: FlyBase
    2. cellular process Source: FlyBase
    3. centriole replication Source: FlyBase
    4. G2/M transition of mitotic cell cycle Source: FlyBase
    5. gastrulation Source: FlyBase
    6. Golgi organization Source: FlyBase
    7. lateral inhibition Source: FlyBase
    8. mesoderm development Source: FlyBase
    9. mitotic cell cycle Source: FlyBase
    10. mitotic nuclear division Source: UniProtKB-KW
    11. negative regulation of cell size Source: FlyBase
    12. negative regulation of mitotic cell cycle Source: FlyBase
    13. open tracheal system development Source: FlyBase
    14. peptidyl-tyrosine dephosphorylation Source: GOC
    15. peripheral nervous system development Source: FlyBase
    16. positive regulation of cell proliferation Source: FlyBase
    17. positive regulation of mitotic cell cycle Source: FlyBase
    18. positive regulation of mitotic cell cycle, embryonic Source: FlyBase
    19. protein dephosphorylation Source: FlyBase
    20. regulation of cell diameter Source: FlyBase
    21. regulation of mitotic cell cycle Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_180658. G0 and Early G1.
    REACT_208929. Polo-like kinase mediated events.
    REACT_218568. Activation of ATR in response to replication stress.
    REACT_222733. E2F-enabled inhibition of pre-replication complex formation.
    REACT_222970. p53-Independent DNA Damage Response.
    REACT_225636. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
    REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    M-phase inducer phosphatase (EC:3.1.3.48)
    Alternative name(s):
    Cdc25-like protein
    Protein string
    Gene namesi
    Name:stg
    Synonyms:cdc25
    ORF Names:CG1395
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0003525. stg.

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome Source: FlyBase
    2. nucleus Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 479479M-phase inducer phosphatasePRO_0000198658Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei455 – 4551Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP20483.

    Expressioni

    Gene expression databases

    BgeeiP20483.

    Interactioni

    Protein-protein interaction databases

    BioGridi68333. 22 interactions.
    DIPiDIP-19931N.
    IntActiP20483. 2 interactions.
    MINTiMINT-848308.
    STRINGi7227.FBpp0084766.

    Structurei

    3D structure databases

    ProteinModelPortaliP20483.
    SMRiP20483. Positions 277-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini316 – 432117RhodanesePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MPI phosphatase family.Curated
    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5105.
    GeneTreeiENSGT00390000018747.
    HOGENOMiHOG000263899.
    InParanoidiP20483.
    KOiK16723.
    OMAiYMELFEM.
    OrthoDBiEOG757D02.
    PhylomeDBiP20483.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    InterProiIPR000751. MPI_Phosphatase.
    IPR001763. Rhodanese-like_dom.
    [Graphical view]
    PfamiPF00581. Rhodanese. 1 hit.
    [Graphical view]
    PRINTSiPR00716. MPIPHPHTASE.
    SMARTiSM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52821. SSF52821. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P20483-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLWETIVEEN NCSMDCNISN NTSSSSSINK MSGSRRARRS LELMSMDQEE    50
    LSFYDDDVVP QDQQRSASPE LMGLLSPEGS PQRFQIVRQP KILPAMGVSS 100
    DHTPARSFRI FNSLSSTCSM ESSMDDEYME LFEMESQSQQ TALGFPSGLN 150
    SLISGQIKEQ PAAKSPAGLS MRRPSVRRCL SMTESNTNST TTPPPKTPET 200
    ARDCFKRPEP PASANCSPIQ SKRHRCAAVE KENCPAPSPL SQVTISHPPP 250
    LRKCMSLNDA EIMSALARSE NRNEPELIGD FSKAYALPLM EGRHRDLKSI 300
    SSETVARLLK GEFSDKVASY RIIDCRYPYE FEGGHIEGAK NLYTTEQILD 350
    EFLTVQQTEL QQQQNAESGH KRNIIIFHCE FSSERGPKMS RFLRNLDRER 400
    NTNAYPALHY PEIYLLHNGY KEFFESHVEL CEPHAYRTML DPAYNEAYRH 450
    FRAKSKSWNG DGLGGATGRL KKSRSRLML 479
    Length:479
    Mass (Da):54,095
    Last modified:December 1, 2000 - v2
    Checksum:i68483F3A285962CC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti228 – 2281A → T in AAA28916. (PubMed:2702688)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24909 mRNA. Translation: AAA28916.1.
    X57495 mRNA. Translation: CAA40732.1.
    AE014297 Genomic DNA. Translation: AAF56885.1.
    AY069704 mRNA. Translation: AAL39849.1.
    PIRiA32290.
    RefSeqiNP_001263066.1. NM_001276137.1.
    NP_524547.1. NM_079823.3.
    UniGeneiDm.3208.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085397; FBpp0084766; FBgn0003525.
    GeneIDi43466.
    KEGGidme:Dmel_CG1395.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24909 mRNA. Translation: AAA28916.1 .
    X57495 mRNA. Translation: CAA40732.1 .
    AE014297 Genomic DNA. Translation: AAF56885.1 .
    AY069704 mRNA. Translation: AAL39849.1 .
    PIRi A32290.
    RefSeqi NP_001263066.1. NM_001276137.1.
    NP_524547.1. NM_079823.3.
    UniGenei Dm.3208.

    3D structure databases

    ProteinModelPortali P20483.
    SMRi P20483. Positions 277-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68333. 22 interactions.
    DIPi DIP-19931N.
    IntActi P20483. 2 interactions.
    MINTi MINT-848308.
    STRINGi 7227.FBpp0084766.

    Proteomic databases

    PRIDEi P20483.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085397 ; FBpp0084766 ; FBgn0003525 .
    GeneIDi 43466.
    KEGGi dme:Dmel_CG1395.

    Organism-specific databases

    CTDi 43466.
    FlyBasei FBgn0003525. stg.

    Phylogenomic databases

    eggNOGi COG5105.
    GeneTreei ENSGT00390000018747.
    HOGENOMi HOG000263899.
    InParanoidi P20483.
    KOi K16723.
    OMAi YMELFEM.
    OrthoDBi EOG757D02.
    PhylomeDBi P20483.

    Enzyme and pathway databases

    Reactomei REACT_180658. G0 and Early G1.
    REACT_208929. Polo-like kinase mediated events.
    REACT_218568. Activation of ATR in response to replication stress.
    REACT_222733. E2F-enabled inhibition of pre-replication complex formation.
    REACT_222970. p53-Independent DNA Damage Response.
    REACT_225636. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
    REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

    Miscellaneous databases

    ChiTaRSi C6orf15. drosophila.
    GenomeRNAii 43466.
    NextBioi 834076.

    Gene expression databases

    Bgeei P20483.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    InterProi IPR000751. MPI_Phosphatase.
    IPR001763. Rhodanese-like_dom.
    [Graphical view ]
    Pfami PF00581. Rhodanese. 1 hit.
    [Graphical view ]
    PRINTSi PR00716. MPIPHPHTASE.
    SMARTi SM00450. RHOD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52821. SSF52821. 1 hit.
    PROSITEi PS50206. RHODANESE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genetic control of cell division patterns in the Drosophila embryo."
      Edgar B.A., O'Farrell P.H.
      Cell 57:177-187(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complementation of fission yeast cdc2ts and cdc25ts mutants identifies two cell cycle genes from Drosophila: a cdc2 homologue and string."
      Jimenez J., Alphey L., Nurse P., Glover D.M.
      EMBO J. 9:3565-3571(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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. "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 SER-455, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiMPIP_DROME
    AccessioniPrimary (citable) accession number: P20483
    Secondary accession number(s): Q9VAL9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 133 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