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P48966

- MPIP2_RAT

UniProt

P48966 - MPIP2_RAT

Protein

M-phase inducer phosphatase 2

Gene

Cdc25b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Directly dephosphorylates CDK1 and stimulates its kinase activity By similarity.By similarity

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Enzyme regulationi

    Stimulated by B-type cyclins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei481 – 4811By similarity

    GO - Molecular functioni

    1. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. mitotic nuclear division Source: RGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    M-phase inducer phosphatase 2 (EC:3.1.3.48)
    Alternative name(s):
    Dual specificity phosphatase Cdc25B
    Gene namesi
    Name:Cdc25b
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621500. Cdc25b.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB-KW
    3. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 574574M-phase inducer phosphatase 2PRO_0000198646Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei166 – 1661Phosphoserine; by MELKBy similarity
    Modified residuei246 – 2461PhosphoserineBy similarity
    Modified residuei319 – 3191Phosphoserine; by MAPKAPK2 and MELK; alternateBy similarity
    Modified residuei319 – 3191Phosphoserine; by MELK and MAPK14; alternateBy similarity
    Modified residuei349 – 3491Phosphoserine; by AURKABy similarity
    Modified residuei370 – 3701Phosphoserine; by BRSK1 and MAPK14By similarity

    Post-translational modificationi

    Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-349 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-166 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-319 and Ser-370 by MAPK14 is required for binding to 14-3-3 proteins By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP48966.
    PRIDEiP48966.

    PTM databases

    PhosphoSiteiP48966.

    Expressioni

    Gene expression databases

    GenevestigatoriP48966.

    Interactioni

    Subunit structurei

    Interacts with MAPK14 and 14-3-3 proteins.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000028864.

    Structurei

    3D structure databases

    ProteinModelPortaliP48966.
    SMRiP48966. Positions 381-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini425 – 532108RhodanesePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5105.
    HOGENOMiHOG000082672.
    HOVERGENiHBG052501.
    KOiK05866.
    PhylomeDBiP48966.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    InterProiIPR000751. MPI_Phosphatase.
    IPR001763. Rhodanese-like_dom.
    [Graphical view]
    PfamiPF06617. M-inducer_phosp. 1 hit.
    PF00581. 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.

    P48966-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEVPPQKSAP GSALSTARVL GGIQRPRHLS GFGFGSDGLL GSPERAASSS    50
    PVTTLTQTMY NLAGLGSETP KTQVGSLSFQ NRLTDLSLSR RTSECSLSSE 100
    SSESSDAGLC MDSPSPMDPQ TAERTFEQAI QAASRVIQKM QFTIKASVFA 150
    SEAAGHSPVL QNITNSQALD SWEKDEAGYR AASSPGEDKE NDGYIFKMPQ 200
    KLPHSSSARA LAEWASRREA FTQRPSSAPD LMCLTTDGKM DVEEASPVAQ 250
    SSSLTPVERA CEEDDGFVDI LESDLKDDDM VPAGMENLIS APLVKKLDKE 300
    EEQDLIMFSK CQRLFRSPSM PCSVIRPILK RLERPHDRDV PVLSKRRKSG 350
    TPLEEQQLEE PKARVFRSKS LCHEIESILD SDHRGLIGDY SKAFLLQTVD 400
    GKHQDLKYIS PETMVALLTG KFSNIVEKFV IVDCRYPYEY EGGHIKNAVN 450
    LPLEPDAETF LLKHPITPCN LDKRIILIFH CEFSSERGPR MCRFIRERDR 500
    AANDYPSLYY PEMYILKGGY KEFFPQHPNF CEPQDYRPMN HAAFRDELRN 550
    FRLKTRSWAG ERSTTQLCSR LQDQ 574
    Length:574
    Mass (Da):64,287
    Last modified:February 1, 1996 - v1
    Checksum:i9367CE203B15FAAD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16237 mRNA. Translation: BAA03762.1.
    RefSeqiNP_598256.1. NM_133572.1.
    UniGeneiRn.11312.

    Genome annotation databases

    GeneIDi171103.
    KEGGirno:171103.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16237 mRNA. Translation: BAA03762.1 .
    RefSeqi NP_598256.1. NM_133572.1.
    UniGenei Rn.11312.

    3D structure databases

    ProteinModelPortali P48966.
    SMRi P48966. Positions 381-558.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000028864.

    PTM databases

    PhosphoSitei P48966.

    Proteomic databases

    PaxDbi P48966.
    PRIDEi P48966.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 171103.
    KEGGi rno:171103.

    Organism-specific databases

    CTDi 994.
    RGDi 621500. Cdc25b.

    Phylogenomic databases

    eggNOGi COG5105.
    HOGENOMi HOG000082672.
    HOVERGENi HBG052501.
    KOi K05866.
    PhylomeDBi P48966.

    Miscellaneous databases

    NextBioi 621786.
    PROi P48966.

    Gene expression databases

    Genevestigatori P48966.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    InterProi IPR000751. MPI_Phosphatase.
    IPR001763. Rhodanese-like_dom.
    [Graphical view ]
    Pfami PF06617. M-inducer_phosp. 1 hit.
    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. "Cdc25A is a novel phosphatase functioning early in the cell cycle."
      Jinno S., Suto K., Nagata A., Igarashi M., Kanaoka Y., Nojima H., Okayama H.
      EMBO J. 13:1549-1556(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: NRK49F.

    Entry informationi

    Entry nameiMPIP2_RAT
    AccessioniPrimary (citable) accession number: P48966
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3