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P48965

- MPIP1_RAT

UniProt

P48965 - MPIP1_RAT

Protein

M-phase inducer phosphatase 1

Gene

Cdc25a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (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. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro By similarity. Phosphorylation by PIM1 leads to an increase in phosphatase activity.By similarity

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Enzyme regulationi

    Stimulated by B-type cyclins. Stimulated by PIM1-mediated phosphorylation By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei432 – 4321By similarity

    GO - Molecular functioni

    1. phosphoprotein phosphatase activity Source: RGD
    2. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. G1/S transition of mitotic cell cycle Source: RGD
    2. mitotic nuclear division Source: UniProtKB-KW
    3. response to radiation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    M-phase inducer phosphatase 1 (EC:3.1.3.48)
    Alternative name(s):
    Dual specificity phosphatase Cdc25A
    Gene namesi
    Name:Cdc25a
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621498. Cdc25a.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. nucleus Source: RGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 525525M-phase inducer phosphatase 1PRO_0000198643Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 761Phosphoserine; by CHEK1By similarity
    Modified residuei79 – 791Phosphoserine; by NEK11By similarity
    Modified residuei82 – 821Phosphoserine; by NEK11By similarity
    Modified residuei88 – 881Phosphoserine; by NEK11By similarity
    Modified residuei124 – 1241Phosphoserine; by CHEK1 and CHEK2By similarity
    Modified residuei178 – 1781Phosphoserine; by CHEK1By similarity
    Modified residuei283 – 2831Phosphoserine; by CHEK1 and CHEK2By similarity
    Modified residuei296 – 2961Phosphoserine; by CHEK1 and CHEK2By similarity
    Modified residuei508 – 5081Phosphothreonine; by CHEK1By similarity
    Modified residuei514 – 5141Phosphoserine; by PLK3By similarity
    Modified residuei520 – 5201Phosphoserine; by PLK3By similarity

    Post-translational modificationi

    Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-283, Ser-296 and Thr-508 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-283, and Ser-296 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-508 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-283 and Ser-296 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation at Ser-79, Ser-82 and Ser-88 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation By similarity.By similarity
    Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP48965.

    PTM databases

    PhosphoSiteiP48965.

    Expressioni

    Gene expression databases

    GenevestigatoriP48965.

    Interactioni

    Subunit structurei

    Interacts with CCNB1/cyclin B1. Interacts with YWHAE/14-3-3 epsilon when phosphorylated. Interacts with CUL1 specifically when CUL1 is neddylated and active. Interacts with BTRC/BTRCP1 and FBXW11/BTRCP2. Interactions with CUL1, BTRC and FBXW11 are enhanced upon DNA damage. Interacts with CHEK2; mediates CDC25A phosphorylation and degradation in response to infrared-induced DNA damages By similarity. Interacts with PIM1.By similarity1 Publication

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000028141.

    Structurei

    3D structure databases

    ProteinModelPortaliP48965.
    SMRiP48965. Positions 338-497.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini377 – 483107RhodanesePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi74 – 8411PhosphodegronAdd
    BLAST
    Motifi141 – 1433KEN box

    Domaini

    The phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-79 and Ser-82 appear to be essential for this interaction By similarity.By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5105.
    HOGENOMiHOG000082672.
    HOVERGENiHBG052501.
    InParanoidiP48965.
    KOiK06645.
    PhylomeDBiP48965.

    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.

    P48965-1 [UniParc]FASTAAdd to Basket

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    MELGPEPPHR RRLLFTCSPT PAPQPTGKVQ FGASRAGGLS PVTNLTVTMD    50
    QLEGLGSDYE KPMDVRNSSS LQRMGSSEST DSGFCLDSPG PLDSKENLEI 100
    SLRRINCLPQ KLLGCSPALK RSHSDSLDHD IFQLIDQDEN KENEAFEFKK 150
    PIRPASRGCL NAHVHEESKD PFTHRQNSAP ARMLSSNESD ISESGNFSPL 200
    FTPQSPVKAS LSDEDDGFID LLDGENLKND EETPSCMSSL WTAPLVMRRP 250
    TNLADRCGLF DSPSPCSSTS SCSTRAVKRA DRSHEESPRG TKRRKSSEAS 300
    PVKADVPEPT QLPHQSLSLT SFPKGTIENI FHSDPRDLIG DFSKGYLFHT 350
    VSGKHQDLKY ISPEIMASVL NGKFANLIKE FVIIDCRYPY EYEGGHIKGA 400
    VNLHMEEEVE EFLLKKPIVP ADGKRVIVVF HCEFSSERGP RMCRYVRERD 450
    RLGNEYPKLH YPELYVLKGG YKEFFLKCQS HCEPPSYRPM HHEDFKEDLK 500
    KFRTKSRTWA GEKSKREMYS RLKKL 525
    Length:525
    Mass (Da):59,218
    Last modified:February 1, 1996 - v1
    Checksum:iA60EC0AF46D63A9C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16236 mRNA. Translation: BAA03761.1.
    RefSeqiNP_598255.1. NM_133571.1.
    UniGeneiRn.11390.

    Genome annotation databases

    GeneIDi171102.
    KEGGirno:171102.
    UCSCiRGD:621498. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16236 mRNA. Translation: BAA03761.1 .
    RefSeqi NP_598255.1. NM_133571.1.
    UniGenei Rn.11390.

    3D structure databases

    ProteinModelPortali P48965.
    SMRi P48965. Positions 338-497.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000028141.

    PTM databases

    PhosphoSitei P48965.

    Proteomic databases

    PRIDEi P48965.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 171102.
    KEGGi rno:171102.
    UCSCi RGD:621498. rat.

    Organism-specific databases

    CTDi 993.
    RGDi 621498. Cdc25a.

    Phylogenomic databases

    eggNOGi COG5105.
    HOGENOMi HOG000082672.
    HOVERGENi HBG052501.
    InParanoidi P48965.
    KOi K06645.
    PhylomeDBi P48965.

    Miscellaneous databases

    NextBioi 621782.
    PROi P48965.

    Gene expression databases

    Genevestigatori P48965.

    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.
    2. "Physical and functional interactions between Pim-1 kinase and Cdc25A phosphatase. Implications for the Pim-1-mediated activation of the c-Myc signaling pathway."
      Mochizuki T., Kitanaka C., Noguchi K., Muramatsu T., Asai A., Kuchino Y.
      J. Biol. Chem. 274:18659-18666(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIM1, PHOSPHORYLATION.

    Entry informationi

    Entry nameiMPIP1_RAT
    AccessioniPrimary (citable) accession number: P48965
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 95 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