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P30304

- MPIP1_HUMAN

UniProt

P30304 - MPIP1_HUMAN

Protein

M-phase inducer phosphatase 1

Gene

CDC25A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      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.

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei431 – 4311

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein kinase binding Source: UniProtKB
    3. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. cellular response to UV Source: UniProtKB
    3. DNA replication Source: Reactome
    4. G1/S transition of mitotic cell cycle Source: Reactome
    5. G2/M transition of mitotic cell cycle Source: Reactome
    6. mitotic cell cycle Source: Reactome
    7. mitotic nuclear division Source: UniProtKB-KW
    8. regulation of cell cycle Source: Reactome
    9. regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
    10. response to radiation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    BRENDAi3.1.3.48. 2681.
    ReactomeiREACT_1006. Polo-like kinase mediated events.
    REACT_111214. G0 and Early G1.
    REACT_1321. E2F-enabled inhibition of pre-replication complex formation.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_2101. Cyclin B2 mediated events.
    REACT_2160. p53-Independent DNA Damage Response.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_683. G1/S-Specific Transcription.
    REACT_9029. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:1725. CDC25A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi76 – 761S → A: Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation. 3 Publications
    Mutagenesisi79 – 791S → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. 2 Publications
    Mutagenesisi81 – 811D → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. 2 Publications
    Mutagenesisi82 – 821S → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. 2 Publications
    Mutagenesisi124 – 1241S → A: Abrogates phosphorylation by CHEK2 and infrared-induced degradation. Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-178; A-279 and A-293. 5 Publications
    Mutagenesisi141 – 1433KEN → AAA: Prevents ubiquitination and subsequent degradation by the APC/C ubiquitin ligase complex. 1 Publication
    Mutagenesisi178 – 1781S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-279 and A-293. Abrogates 14-3-3 protein binding. 4 Publications
    Mutagenesisi279 – 2791S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293. 2 Publications
    Mutagenesisi293 – 2931S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279. 2 Publications
    Mutagenesisi431 – 4311C → S: Abolishes phosphatase activity. 3 Publications
    Mutagenesisi507 – 5071T → A: Abrogates 14-3-3 protein binding; increases binding to cyclin B1. 2 Publications
    Mutagenesisi513 – 5131S → A: Increased stability following IR treatment. 2 Publications
    Mutagenesisi513 – 5131S → D: Mimicks phosphorylation state, leading to promote degradation following IR treatment. 2 Publications
    Mutagenesisi514 – 5141K → L: Abrogates binding to CCNB1; when associated with L-520. 2 Publications
    Mutagenesisi519 – 5191S → A: Increased stability following IR treatment. 2 Publications
    Mutagenesisi519 – 5191S → D: Mimicks phosphorylation state, leading to promote degradation following IR treatment. 2 Publications
    Mutagenesisi520 – 5201R → L: Abrogates binding to CCNB1; when associated with L-514. 2 Publications

    Organism-specific databases

    PharmGKBiPA26259.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 524524M-phase inducer phosphatase 1PRO_0000198641Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 761Phosphoserine; by CHEK13 Publications
    Modified residuei79 – 791Phosphoserine; by NEK112 Publications
    Modified residuei82 – 821Phosphoserine; by NEK113 Publications
    Modified residuei88 – 881Phosphoserine; by NEK113 Publications
    Modified residuei124 – 1241Phosphoserine; by CHEK1 and CHEK26 Publications
    Modified residuei178 – 1781Phosphoserine; by CHEK14 Publications
    Modified residuei279 – 2791Phosphoserine; by CHEK1 and CHEK22 Publications
    Modified residuei293 – 2931Phosphoserine; by CHEK1 and CHEK22 Publications
    Modified residuei507 – 5071Phosphothreonine; by CHEK12 Publications
    Modified residuei513 – 5131Phosphoserine; by PLK32 Publications
    Modified residuei519 – 5191Phosphoserine; by PLK32 Publications

    Post-translational modificationi

    Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-279, Ser-293 and Thr-507 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-279, and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-507 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-279 and Ser-293 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.11 Publications
    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.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP30304.
    PRIDEiP30304.

    PTM databases

    PhosphoSiteiP30304.

    Expressioni

    Gene expression databases

    ArrayExpressiP30304.
    BgeeiP30304.
    CleanExiHS_CDC25A.
    GenevestigatoriP30304.

    Organism-specific databases

    HPAiHPA005855.

    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.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAF1P040494EBI-747671,EBI-365996
    YWHABP319468EBI-747671,EBI-359815
    YWHAZP631042EBI-747671,EBI-347088

    Protein-protein interaction databases

    BioGridi107428. 51 interactions.
    DIPiDIP-166N.
    IntActiP30304. 35 interactions.
    MINTiMINT-124723.
    STRINGi9606.ENSP00000303706.

    Structurei

    Secondary structure

    1
    524
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi341 – 3444
    Helixi362 – 3698
    Turni370 – 3767
    Beta strandi377 – 3848
    Helixi388 – 3925
    Helixi405 – 4117
    Turni412 – 4143
    Beta strandi423 – 4308
    Beta strandi432 – 4365
    Helixi437 – 45115
    Beta strandi463 – 4664
    Helixi469 – 4779
    Helixi478 – 4803
    Beta strandi481 – 4844

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C25X-ray2.30A337-496[»]
    ProteinModelPortaliP30304.
    SMRiP30304. Positions 337-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30304.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini376 – 482107RhodanesePROSITE-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.1 Publication

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5105.
    HOGENOMiHOG000082672.
    HOVERGENiHBG052501.
    InParanoidiP30304.
    KOiK06645.
    OMAiNLTVTMD.
    OrthoDBiEOG7288R1.
    PhylomeDBiP30304.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30304-1) [UniParc]FASTAAdd to Basket

    Also known as: CDC25A1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MELGPEPPHR RRLLFACSPP PASQPVVKAL FGASAAGGLS PVTNLTVTMD    50
    QLQGLGSDYE QPLEVKNNSN LQRMGSSEST DSGFCLDSPG PLDSKENLEN 100
    PMRRIHSLPQ KLLGCSPALK RSHSDSLDHD IFQLIDPDEN KENEAFEFKK 150
    PVRPVSRGCL HSHGLQEGKD LFTQRQNSAP ARMLSSNERD SSEPGNFIPL 200
    FTPQSPVTAT LSDEDDGFVD LLDGENLKNE EETPSCMASL WTAPLVMRTT 250
    NLDNRCKLFD SPSLCSSSTR SVLKRPERSQ EESPPGSTKR RKSMSGASPK 300
    ESTNPEKAHE TLHQSLSLAS SPKGTIENIL DNDPRDLIGD FSKGYLFHTV 350
    AGKHQDLKYI SPEIMASVLN GKFANLIKEF VIIDCRYPYE YEGGHIKGAV 400
    NLHMEEEVED FLLKKPIVPT DGKRVIVVFH CEFSSERGPR MCRYVRERDR 450
    LGNEYPKLHY PELYVLKGGY KEFFMKCQSY CEPPSYRPMH HEDFKEDLKK 500
    FRTKSRTWAG EKSKREMYSR LKKL 524
    Length:524
    Mass (Da):59,087
    Last modified:July 19, 2004 - v2
    Checksum:iB2F6B792D4E6122B
    GO
    Isoform 2 (identifier: P30304-2) [UniParc]FASTAAdd to Basket

    Also known as: CDC25A2

    The sequence of this isoform differs from the canonical sequence as follows:
         144-183: Missing.

    Show »
    Length:484
    Mass (Da):54,551
    Checksum:iAE6326F34B704D4B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 105EPPHR → SPAP in AAA58415. (PubMed:1836978)Curated
    Sequence conflicti180 – 1812PA → QL in AAA58415. (PubMed:1836978)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881S → F.1 Publication
    Corresponds to variant rs3731499 [ dbSNP | Ensembl ].
    VAR_020932
    Natural varianti182 – 1821R → G.1 Publication
    Corresponds to variant rs6771386 [ dbSNP | Ensembl ].
    VAR_023532
    Natural varianti182 – 1821R → W.
    Corresponds to variant rs6771386 [ dbSNP | Ensembl ].
    VAR_023533

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei144 – 18340Missing in isoform 2. 2 PublicationsVSP_000860Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81933 mRNA. Translation: AAA58415.1.
    AY137580 mRNA. Translation: AAN11305.1.
    AF527417 Genomic DNA. Translation: AAM77917.1.
    BC007401 mRNA. Translation: AAH07401.1.
    BC018642 mRNA. Translation: AAH18642.1.
    AF277722 mRNA. Translation: AAG41884.1.
    CCDSiCCDS2760.1. [P30304-1]
    CCDS2761.1. [P30304-2]
    PIRiA41648.
    RefSeqiNP_001780.2. NM_001789.2. [P30304-1]
    NP_963861.1. NM_201567.1. [P30304-2]
    UniGeneiHs.437705.

    Genome annotation databases

    EnsembliENST00000302506; ENSP00000303706; ENSG00000164045. [P30304-1]
    ENST00000351231; ENSP00000343166; ENSG00000164045. [P30304-2]
    GeneIDi993.
    KEGGihsa:993.
    UCSCiuc003csh.1. human. [P30304-1]
    uc003csi.1. human. [P30304-2]

    Polymorphism databases

    DMDMi50403734.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81933 mRNA. Translation: AAA58415.1 .
    AY137580 mRNA. Translation: AAN11305.1 .
    AF527417 Genomic DNA. Translation: AAM77917.1 .
    BC007401 mRNA. Translation: AAH07401.1 .
    BC018642 mRNA. Translation: AAH18642.1 .
    AF277722 mRNA. Translation: AAG41884.1 .
    CCDSi CCDS2760.1. [P30304-1 ]
    CCDS2761.1. [P30304-2 ]
    PIRi A41648.
    RefSeqi NP_001780.2. NM_001789.2. [P30304-1 ]
    NP_963861.1. NM_201567.1. [P30304-2 ]
    UniGenei Hs.437705.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C25 X-ray 2.30 A 337-496 [» ]
    ProteinModelPortali P30304.
    SMRi P30304. Positions 337-496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107428. 51 interactions.
    DIPi DIP-166N.
    IntActi P30304. 35 interactions.
    MINTi MINT-124723.
    STRINGi 9606.ENSP00000303706.

    Chemistry

    BindingDBi P30304.
    ChEMBLi CHEMBL3775.

    PTM databases

    PhosphoSitei P30304.

    Polymorphism databases

    DMDMi 50403734.

    Proteomic databases

    PaxDbi P30304.
    PRIDEi P30304.

    Protocols and materials databases

    DNASUi 993.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302506 ; ENSP00000303706 ; ENSG00000164045 . [P30304-1 ]
    ENST00000351231 ; ENSP00000343166 ; ENSG00000164045 . [P30304-2 ]
    GeneIDi 993.
    KEGGi hsa:993.
    UCSCi uc003csh.1. human. [P30304-1 ]
    uc003csi.1. human. [P30304-2 ]

    Organism-specific databases

    CTDi 993.
    GeneCardsi GC03M048173.
    HGNCi HGNC:1725. CDC25A.
    HPAi HPA005855.
    MIMi 116947. gene.
    neXtProti NX_P30304.
    PharmGKBi PA26259.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5105.
    HOGENOMi HOG000082672.
    HOVERGENi HBG052501.
    InParanoidi P30304.
    KOi K06645.
    OMAi NLTVTMD.
    OrthoDBi EOG7288R1.
    PhylomeDBi P30304.
    TreeFami TF101056.

    Enzyme and pathway databases

    BRENDAi 3.1.3.48. 2681.
    Reactomei REACT_1006. Polo-like kinase mediated events.
    REACT_111214. G0 and Early G1.
    REACT_1321. E2F-enabled inhibition of pre-replication complex formation.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_2101. Cyclin B2 mediated events.
    REACT_2160. p53-Independent DNA Damage Response.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_683. G1/S-Specific Transcription.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.

    Miscellaneous databases

    EvolutionaryTracei P30304.
    GeneWikii CDC25A.
    GenomeRNAii 993.
    NextBioi 4164.
    PROi P30304.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30304.
    Bgeei P30304.
    CleanExi HS_CDC25A.
    Genevestigatori P30304.

    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. "Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins."
      Galaktionov K.I., Beach D.
      Cell 67:1181-1194(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-182.
    2. Varmeh-Ziaie S., Manfredi J.J.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. NIEHS SNPs program
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-88.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lymph.
    5. "Alternative splicing in the regulatory region of the human phosphatases CDC25A and CDC25C."
      Wegener S., Hampe W., Herrmann D., Schaller H.C.
      Eur. J. Cell Biol. 79:810-815(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-234 (ISOFORM 2).
    6. "The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis."
      Falck J., Mailand N., Syljuaasen R.G., Bartek J., Lukas J.
      Nature 410:842-847(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHEK2, PHOSPHORYLATION AT SER-124 BY CHEK2, MUTAGENESIS OF SER-124.
    7. Cited for: UBIQUITINATION BY THE APC/C UBIQUITIN LIGASE COMPLEX, DOMAIN KEN BOX MOTIF, MUTAGENESIS OF 141-LYS--ASN-143.
    8. "Disruption of the checkpoint kinase 1/cell division cycle 25A pathway abrogates ionizing radiation-induced S and G2 checkpoints."
      Zhao H., Watkins J.L., Piwnica-Worms H.
      Proc. Natl. Acad. Sci. U.S.A. 99:14795-14800(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-124, MUTAGENESIS OF SER-124.
    9. "Chk1 regulates the S phase checkpoint by coupling the physiological turnover and ionizing radiation-induced accelerated proteolysis of Cdc25A."
      Soerensen C.S., Syljuaesen R.G., Falck J., Schroeder T., Roennstrand L., Khanna K.K., Zhou B.-B., Bartek J., Lukas J.
      Cancer Cell 3:247-258(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-124; SER-178; SER-279 AND SER-293, MUTAGENESIS OF SER-124; SER-178; SER-279 AND SER-293.
    10. "SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase."
      Jin J., Shirogane T., Xu L., Nalepa G., Qin J., Elledge S.J., Harper J.W.
      Genes Dev. 17:3062-3074(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BTRC; CUL1 AND FBXW11, PHOSPHODEGRON MOTIF, PHOSPHORYLATION AT SER-76 AND SER-124, UBIQUITINATION, MUTAGENESIS OF SER-76; SER-79; ASP-81 AND SER-82.
    11. "Chk1 mediates S and G2 arrests through Cdc25A degradation in response to DNA-damaging agents."
      Xiao Z., Chen Z., Gunasekera A.H., Sowin T.J., Rosenberg S.H., Fesik S., Zhang H.
      J. Biol. Chem. 278:21767-21773(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, MUTAGENESIS OF CYS-431.
    12. "Phosphorylation at serine 75 is required for UV-mediated degradation of human Cdc25A phosphatase at the S-phase checkpoint."
      Hassepass I., Voit R., Hoffmann I.
      J. Biol. Chem. 278:29824-29829(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-76; SER-124 AND SER-178, MUTAGENESIS OF SER-76; SER-124 AND SER-178.
    13. "Chk1 kinase negatively regulates mitotic function of Cdc25A phosphatase through 14-3-3 binding."
      Chen M.-S., Ryan C.E., Piwnica-Worms H.
      Mol. Cell. Biol. 23:7488-7497(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCNB1 AND YWHAE, PHOSPHORYLATION AT SER-178 AND THR-507, MUTAGENESIS OF SER-178; CYS-431; THR-507; LYS-514 AND ARG-520.
    14. "The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and activates the G2/M specific phosphatase Cdc25C."
      Bachmann M., Kosan C., Xing P.X., Montenarh M., Hoffmann I., Moroy T.
      Int. J. Biochem. Cell Biol. 38:430-443(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIM1.
    15. "NEK11 regulates CDC25A degradation and the IR-induced G2/M checkpoint."
      Melixetian M., Klein D.K., Soerensen C.S., Helin K.
      Nat. Cell Biol. 11:1247-1253(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-79; SER-82 AND SER-88.
    16. "NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling."
      Soerensen C.S., Melixetian M., Klein D.K., Helin K.
      Cell Cycle 9:450-455(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-82 AND SER-88.
    17. "Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A."
      Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L., French D.M., Dixit V.M.
      Nat. Cell Biol. 12:400-406(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEUBIQUITINATION BY USP17L2.
    18. "Absence of polo-like kinase 3 in mice stabilizes Cdc25A after DNA damage but is not sufficient to produce tumors."
      Myer D.L., Robbins S.B., Yin M., Boivin G.P., Liu Y., Greis K.D., Bahassi el M., Stambrook P.J.
      Mutat. Res. 714:1-10(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-513 AND SER-519 BY PLK3, UBIQUITINATION, MUTAGENESIS OF SER-513 AND SER-519.
    19. "Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A."
      Fauman E.B., Cogswell J.P., Lovejoy B., Rocque W.J., Holmes W., Montana V.G., Piwnica-Worms H., Rink M.J., Saper M.A.
      Cell 93:617-625(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 336-496.

    Entry informationi

    Entry nameiMPIP1_HUMAN
    AccessioniPrimary (citable) accession number: P30304
    Secondary accession number(s): Q8IZH5, Q96IL3, Q9H2F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3