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P48964

- MPIP1_MOUSE

UniProt

P48964 - MPIP1_MOUSE

Protein

M-phase inducer phosphatase 1

Gene

Cdc25a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (18 Sep 2013)
      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.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 sitei421 – 4211By similarity

    GO - Molecular functioni

    1. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular response to UV Source: Ensembl
    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

    Enzyme and pathway databases

    ReactomeiREACT_199110. G0 and Early G1.
    REACT_204269. E2F-enabled inhibition of pre-replication complex formation.
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_209377. Cyclin B2 mediated events.
    REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

    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
    Synonyms:Cdc25m3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:103198. Cdc25a.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleus Source: MGI

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 514514M-phase inducer phosphatase 1PRO_0000198642Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751Phosphoserine; by CHEK1By similarity
    Modified residuei78 – 781Phosphoserine; by NEK11By similarity
    Modified residuei81 – 811Phosphoserine; by NEK11By similarity
    Modified residuei87 – 871Phosphoserine; by NEK11By similarity
    Modified residuei123 – 1231Phosphoserine; by CHEK1 and CHEK2By similarity
    Modified residuei172 – 1721Phosphoserine; by CHEK1By similarity
    Modified residuei271 – 2711Phosphoserine; by CHEK1 and CHEK2By similarity
    Modified residuei284 – 2841Phosphoserine; by CHEK1 and CHEK2By similarity
    Modified residuei497 – 4971Phosphothreonine; by CHEK1By similarity
    Modified residuei503 – 5031Phosphoserine; by PLK3By similarity
    Modified residuei509 – 5091Phosphoserine; by PLK3By similarity

    Post-translational modificationi

    Phosphorylated by CHEK1 on Ser-75, Ser-123, Ser-172, Ser-271, Ser-284 and Thr-497 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-123, Ser-271, and Ser-284 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-172 and Thr-497 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-75, Ser-123, Ser-172, Ser-271 and Ser-284 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-75 by CHEK1 primes it for subsequent phosphorylation at Ser-75, Ser-81 and Ser-87 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

    PRIDEiP48964.

    PTM databases

    PhosphoSiteiP48964.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in most developing tissue. High levels in the testis and lower levels in the ovary, particularly in germ cells. Lower levels also in kidney, liver, heart and muscle.1 Publication

    Developmental stagei

    First detected at the blastocyst stage.1 Publication

    Gene expression databases

    CleanExiMM_CDC25A.
    GenevestigatoriP48964.

    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 PIM1. Interacts with CHEK2; mediates CDC25A phosphorylation and degradation in response to infrared-induced DNA damages By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP48964.
    SMRiP48964. Positions 327-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini366 – 472107RhodanesePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi73 – 8311PhosphodegronAdd
    BLAST
    Motifi140 – 1423KEN box

    Domaini

    The phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-78 and Ser-81 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.
    GeneTreeiENSGT00390000018747.
    HOVERGENiHBG052501.
    KOiK06645.
    OMAiNLTVTMD.
    OrthoDBiEOG7288R1.
    PhylomeDBiP48964.
    TreeFamiTF101056.

    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.

    P48964-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELGPEPPHR RRLFFACSPT PAPQPTGKML FGASAAGGLS PVTNLTVTMD    50
    QLEGLGSDCE KMEVRNNSSL QRMGSSESTD SGFCLDSPGP LDSKENLEIS 100
    LTRINSLPQK LLGCSPALKR SHSDSLDHDT FHLIDQDENK ENEAFEFKKP 150
    IRPASRHIYE ESKDPFTHRQ NSAPARMLSS NESESGNFSP LFIPQSPVKA 200
    TLSDEDDGFI DLLDGENMKN DEETPSCMAS LWTAPLVMRR PANLADRCGL 250
    FDSPSPCGSS TRAVLKRADR SHEEPPRGTK RRKSVPSPVK AKADVPEPAQ 300
    LPSQSLSLMS SPKGTIENIL DSDPRDLIGD FSKGYLFNTV SGKHQDLKYI 350
    SPEIMASVLN GKFAGLIKEF VIIDCRYPYE YEGGHIKGAV NLHMEEEVED 400
    FLLKNPIVPT DGKRVIVVFH CEFSSERGPR MCRYVRERDR LGNEYPKLHY 450
    PELYVLKGGY KEFFLKCQSH CEPPSYRPMH HEDFKEDLKK FRTKSRTWAG 500
    EKSKREMYSR LKKL 514
    Length:514
    Mass (Da):57,806
    Last modified:September 18, 2013 - v2
    Checksum:i7D7AD1CB4C39ACF6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61E → S in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti9 – 102HR → P in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti23 – 231P → S in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti128 – 1281H → Q in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti138 – 1381E → K in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti147 – 16014FKKPI…RHIYE → PKKQYDLHLSSHLQ in AAA85580. (PubMed:7635051)CuratedAdd
    BLAST
    Sequence conflicti165 – 1684PFTH → LYTQ in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti174 – 1763PAR → QLG in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti193 – 1931I → T in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti218 – 2181M → L in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti226 – 2294SCMA → TSMV in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti248 – 2481C → LR in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti365 – 3651G → S in AAA85580. (PubMed:7635051)Curated
    Sequence conflicti503 – 5031S → R in AAA85580. (PubMed:7635051)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27323 mRNA. Translation: AAA85580.1.
    CT573087 Genomic DNA. No translation available.
    CCDSiCCDS23559.1.
    RefSeqiNP_031684.3. NM_007658.3.
    UniGeneiMm.307103.

    Genome annotation databases

    EnsembliENSMUST00000094324; ENSMUSP00000091882; ENSMUSG00000032477.
    GeneIDi12530.
    KEGGimmu:12530.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27323 mRNA. Translation: AAA85580.1 .
    CT573087 Genomic DNA. No translation available.
    CCDSi CCDS23559.1.
    RefSeqi NP_031684.3. NM_007658.3.
    UniGenei Mm.307103.

    3D structure databases

    ProteinModelPortali P48964.
    SMRi P48964. Positions 327-486.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P48964.

    Proteomic databases

    PRIDEi P48964.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000094324 ; ENSMUSP00000091882 ; ENSMUSG00000032477 .
    GeneIDi 12530.
    KEGGi mmu:12530.

    Organism-specific databases

    CTDi 993.
    MGIi MGI:103198. Cdc25a.

    Phylogenomic databases

    eggNOGi COG5105.
    GeneTreei ENSGT00390000018747.
    HOVERGENi HBG052501.
    KOi K06645.
    OMAi NLTVTMD.
    OrthoDBi EOG7288R1.
    PhylomeDBi P48964.
    TreeFami TF101056.

    Enzyme and pathway databases

    Reactomei REACT_199110. G0 and Early G1.
    REACT_204269. E2F-enabled inhibition of pre-replication complex formation.
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_209377. Cyclin B2 mediated events.
    REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

    Miscellaneous databases

    NextBioi 281558.
    PROi P48964.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_CDC25A.
    Genevestigatori P48964.

    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. "Two CDC25 homologues are differentially expressed during mouse development."
      Wickramasinghe D., Becker S., Ernst M.K., Resnick J.L., Centanni J.M., Tessarollo L., Grabel L.B., Donovan P.J.
      Development 121:2047-2056(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.

    Entry informationi

    Entry nameiMPIP1_MOUSE
    AccessioniPrimary (citable) accession number: P48964
    Secondary accession number(s): E9PVD0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: September 18, 2013
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3