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P30307

- MPIP3_HUMAN

UniProt

P30307 - MPIP3_HUMAN

Protein

M-phase inducer phosphatase 3

Gene

CDC25C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity.1 Publication

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei377 – 3771By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein kinase binding Source: UniProtKB
    3. protein tyrosine phosphatase activity Source: UniProtKB
    4. WW domain binding Source: BHF-UCL

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. DNA replication Source: Reactome
    3. G2/M transition of mitotic cell cycle Source: UniProtKB
    4. mitotic cell cycle Source: Reactome
    5. mitotic nuclear division Source: UniProtKB-KW
    6. peptidyl-tyrosine dephosphorylation Source: GOC
    7. regulation of cell cycle Source: Reactome
    8. regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
    9. regulation of mitosis Source: ProtInc
    10. spermatogenesis Source: Ensembl
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Host-virus interaction, Mitosis

    Enzyme and pathway databases

    BRENDAi3.1.3.48. 2681.
    ReactomeiREACT_1006. Polo-like kinase mediated events.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_2101. Cyclin B2 mediated events.
    REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
    REACT_6769. Activation of ATR in response to replication stress.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    M-phase inducer phosphatase 3 (EC:3.1.3.48)
    Alternative name(s):
    Dual specificity phosphatase Cdc25C
    Gene namesi
    Name:CDC25C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:1727. CDC25C.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi129 – 1291S → V: Loss of phosphorylation. Severely impairs PLK1-binding. 1 Publication
    Mutagenesisi130 – 1301T → A: Loss of phosphorylation. Severely impairs PLK1-binding. 1 Publication
    Mutagenesisi191 – 1911S → A: Facilitates nuclear exclusion. 1 Publication
    Mutagenesisi191 – 1911S → D: Mimicks phosphorylation state, leading to enhanced accumulation in the nucleus. 1 Publication
    Mutagenesisi352 – 3521E → K: Partial loss of HIV-1 Vpr binding. 1 Publication
    Mutagenesisi359 – 3591K → E: No effect on HIV-1 Vpr binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA100.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 473472M-phase inducer phosphatase 3PRO_0000198647Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei38 – 381Phosphoserine1 Publication
    Modified residuei48 – 481Phosphothreonine2 Publications
    Modified residuei57 – 571Phosphoserine1 Publication
    Modified residuei61 – 611Phosphoserine2 Publications
    Modified residuei64 – 641Phosphoserine3 Publications
    Modified residuei67 – 671Phosphothreonine3 Publications
    Modified residuei122 – 1221Phosphoserine; by CDK11 Publication
    Modified residuei129 – 1291Phosphoserine
    Modified residuei130 – 1301Phosphothreonine; by CDK11 Publication
    Modified residuei168 – 1681Phosphoserine2 Publications
    Modified residuei191 – 1911Phosphoserine; by PLK31 Publication
    Modified residuei198 – 1981Phosphoserine; by PLK31 Publication
    Modified residuei214 – 2141Phosphoserine; by CDK11 Publication
    Modified residuei216 – 2161Phosphoserine; by CHEK1, CHEK2, BRSK1 and MAPK143 Publications
    Modified residuei472 – 4721Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by CHEK1 and MAPK14 at Ser-216. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-191 promotes nuclear translocation. Ser-198 is a minor phosphorylation site. Was initially reported to be phosphorylated by PLK3 at Ser-216 (PubMed:10557092). However, such phosphorylation by PLK3 was not confirmed by other groups. Phosphorylation at Thr-48, Thr-67, Ser-122, Thr-130, Ser-168 and Ser-214 occurs at G2 and G2-M transition and is probably catalyzed by CDK1. Ser-168 phosphorylation levels are lower than those at the other 5 CDK1 sites. Phosphorylation by CDK1 leads to increased activity.11 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP30307.
    PaxDbiP30307.
    PRIDEiP30307.

    PTM databases

    PhosphoSiteiP30307.

    Expressioni

    Developmental stagei

    Expressed predominantly in G2 phase.

    Gene expression databases

    ArrayExpressiP30307.
    BgeeiP30307.
    CleanExiHS_CDC25C.
    GenevestigatoriP30307.

    Organism-specific databases

    HPAiCAB003800.

    Interactioni

    Subunit structurei

    Interacts with HIV-1 Vpr, thereby inactivating CDC25C phosphatase activity. Interacts with MAPK14 and 14-3-3 proteins. When phosphorylated on Ser-129 and/or Thr-130, interacts with PLK1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDK1P064932EBI-974439,EBI-444308
    CHEK1O147572EBI-974439,EBI-974488
    LZTS1Q9Y2502EBI-974439,EBI-1216080

    Protein-protein interaction databases

    BioGridi107430. 32 interactions.
    DIPiDIP-24183N.
    IntActiP30307. 7 interactions.
    MINTiMINT-86355.
    STRINGi9606.ENSP00000321656.

    Structurei

    Secondary structure

    1
    473
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi127 – 1293
    Beta strandi286 – 2894
    Beta strandi300 – 3056
    Helixi307 – 3148
    Turni315 – 3217
    Beta strandi322 – 3298
    Helixi333 – 3375
    Beta strandi339 – 3413
    Helixi350 – 3578
    Beta strandi369 – 3768
    Helixi384 – 39714
    Beta strandi409 – 4124
    Helixi415 – 4195
    Turni420 – 4223
    Helixi424 – 4263
    Beta strandi427 – 4304
    Beta strandi438 – 4403

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OJXX-ray2.85E126-134[»]
    3BZIX-ray2.10E126-134[»]
    3OP3X-ray2.63A270-462[»]
    ProteinModelPortaliP30307.
    SMRiP30307. Positions 280-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30307.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini321 – 428108RhodanesePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni334 – 37946HIV-1 Vpr binding siteAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5105.
    HOVERGENiHBG052501.
    InParanoidiP30307.
    KOiK05867.
    OMAiTVSLCDI.
    OrthoDBiEOG7288R1.
    PhylomeDBiP30307.
    TreeFamiTF101056.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    InterProiIPR000751. MPI_Phosphatase.
    IPR001763. Rhodanese-like_dom.
    [Graphical view]
    PfamiPF06617. M-inducer_phosp. 2 hits.
    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 (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30307-1) [UniParc]FASTAAdd to Basket

    Also known as: CDC25C1

    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

    MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV    50
    GKFLGDSANL SILSGGTPKR CLDLSNLSSG EITATQLTTS ADLDETGHLD 100
    SSGLQEVHLA GMNHDQHLMK CSPAQLLCST PNGLDRGHRK RDAMCSSSAN 150
    KENDNGNLVD SEMKYLGSPI TTVPKLDKNP NLGEDQAEEI SDELMEFSLK 200
    DQEAKVSRSG LYRSPSMPEN LNRPRLKQVE KFKDNTIPDK VKKKYFSGQG 250
    KLRKGLCLKK TVSLCDITIT QMLEEDSNQG HLIGDFSKVC ALPTVSGKHQ 300
    DLKYVNPETV AALLSGKFQG LIEKFYVIDC RYPYEYLGGH IQGALNLYSQ 350
    EELFNFFLKK PIVPLDTQKR IIIVFHCEFS SERGPRMCRC LREEDRSLNQ 400
    YPALYYPELY ILKGGYRDFF PEYMELCEPQ SYCPMHHQDH KTELLRCRSQ 450
    SKVQEGERQL REQIALLVKD MSP 473
    Length:473
    Mass (Da):53,365
    Last modified:October 17, 2006 - v2
    Checksum:i0658A1F1B9B8996A
    GO
    Isoform 2 (identifier: P30307-2) [UniParc]FASTAAdd to Basket

    Also known as: CDC25C2

    The sequence of this isoform differs from the canonical sequence as follows:
         124-153: Missing.

    Show »
    Length:443
    Mass (Da):50,122
    Checksum:i11480DF49B3F04DD
    GO
    Isoform 3 (identifier: P30307-5)

    Also known as: CDC25C3

    Sequence is not available
    Length:
    Mass (Da):
    Isoform 4 (identifier: P30307-3) [UniParc]FASTAAdd to Basket

    Also known as: CDC25C4

    The sequence of this isoform differs from the canonical sequence as follows:
         66-123: GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSP → SPGFFRTSGSAFSWD

    Note: Contains a phosphoserine at position 61.

    Show »
    Length:430
    Mass (Da):48,851
    Checksum:iF2DDF9DB1653BCEE
    GO
    Isoform 5 (identifier: P30307-4) [UniParc]FASTAAdd to Basket

    Also known as: CDC25C5, Cdc25Cdm

    The sequence of this isoform differs from the canonical sequence as follows:
         66-123: GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSP → SPGFFRTSGSAFSWD
         124-153: Missing.

    Note: Contains a phosphoserine at position 61.

    Show »
    Length:400
    Mass (Da):45,608
    Checksum:i212EA5FD75672289
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141S → N.
    Corresponds to variant rs11567959 [ dbSNP | Ensembl ].
    VAR_027922
    Natural varianti70 – 701R → C.3 Publications
    Corresponds to variant rs3734166 [ dbSNP | Ensembl ].
    VAR_027923
    Natural varianti78 – 781S → N.
    Corresponds to variant rs11567962 [ dbSNP | Ensembl ].
    VAR_027924
    Natural varianti297 – 2971G → R.
    Corresponds to variant rs11567997 [ dbSNP | Ensembl ].
    VAR_020146

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei66 – 12358GTPKR…MKCSP → SPGFFRTSGSAFSWD in isoform 4 and isoform 5. 2 PublicationsVSP_000863Add
    BLAST
    Alternative sequencei124 – 15330Missing in isoform 2 and isoform 5. 2 PublicationsVSP_000864Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34065 mRNA. Translation: AAA35666.1.
    AJ304504 mRNA. Translation: CAC19192.1.
    AY497474 Genomic DNA. Translation: AAR32098.1.
    CH471062 Genomic DNA. Translation: EAW62145.1.
    CH471062 Genomic DNA. Translation: EAW62149.1.
    BC019089 mRNA. Translation: AAH19089.1.
    AF277723 mRNA. Translation: AAG41885.1.
    AF277725 mRNA. Translation: AAG41887.1.
    AF277726 mRNA. Translation: AAG41888.1.
    AF312681 mRNA. Translation: AAL26835.1.
    CCDSiCCDS4202.1. [P30307-1]
    CCDS4203.1. [P30307-4]
    PIRiI59168. A38874.
    RefSeqiNP_001274511.1. NM_001287582.1. [P30307-1]
    NP_001781.2. NM_001790.4. [P30307-1]
    NP_073720.1. NM_022809.3. [P30307-4]
    UniGeneiHs.656.

    Genome annotation databases

    EnsembliENST00000323760; ENSP00000321656; ENSG00000158402. [P30307-1]
    ENST00000348983; ENSP00000345205; ENSG00000158402. [P30307-4]
    ENST00000415130; ENSP00000392631; ENSG00000158402. [P30307-4]
    ENST00000513970; ENSP00000424795; ENSG00000158402. [P30307-1]
    ENST00000514555; ENSP00000425470; ENSG00000158402. [P30307-2]
    GeneIDi995.
    KEGGihsa:995.
    UCSCiuc003lcp.1. human. [P30307-1]
    uc003lcq.1. human. [P30307-4]

    Polymorphism databases

    DMDMi116242631.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34065 mRNA. Translation: AAA35666.1 .
    AJ304504 mRNA. Translation: CAC19192.1 .
    AY497474 Genomic DNA. Translation: AAR32098.1 .
    CH471062 Genomic DNA. Translation: EAW62145.1 .
    CH471062 Genomic DNA. Translation: EAW62149.1 .
    BC019089 mRNA. Translation: AAH19089.1 .
    AF277723 mRNA. Translation: AAG41885.1 .
    AF277725 mRNA. Translation: AAG41887.1 .
    AF277726 mRNA. Translation: AAG41888.1 .
    AF312681 mRNA. Translation: AAL26835.1 .
    CCDSi CCDS4202.1. [P30307-1 ]
    CCDS4203.1. [P30307-4 ]
    PIRi I59168. A38874.
    RefSeqi NP_001274511.1. NM_001287582.1. [P30307-1 ]
    NP_001781.2. NM_001790.4. [P30307-1 ]
    NP_073720.1. NM_022809.3. [P30307-4 ]
    UniGenei Hs.656.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OJX X-ray 2.85 E 126-134 [» ]
    3BZI X-ray 2.10 E 126-134 [» ]
    3OP3 X-ray 2.63 A 270-462 [» ]
    ProteinModelPortali P30307.
    SMRi P30307. Positions 280-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107430. 32 interactions.
    DIPi DIP-24183N.
    IntActi P30307. 7 interactions.
    MINTi MINT-86355.
    STRINGi 9606.ENSP00000321656.

    Chemistry

    BindingDBi P30307.
    ChEMBLi CHEMBL2378.

    PTM databases

    PhosphoSitei P30307.

    Polymorphism databases

    DMDMi 116242631.

    Proteomic databases

    MaxQBi P30307.
    PaxDbi P30307.
    PRIDEi P30307.

    Protocols and materials databases

    DNASUi 995.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323760 ; ENSP00000321656 ; ENSG00000158402 . [P30307-1 ]
    ENST00000348983 ; ENSP00000345205 ; ENSG00000158402 . [P30307-4 ]
    ENST00000415130 ; ENSP00000392631 ; ENSG00000158402 . [P30307-4 ]
    ENST00000513970 ; ENSP00000424795 ; ENSG00000158402 . [P30307-1 ]
    ENST00000514555 ; ENSP00000425470 ; ENSG00000158402 . [P30307-2 ]
    GeneIDi 995.
    KEGGi hsa:995.
    UCSCi uc003lcp.1. human. [P30307-1 ]
    uc003lcq.1. human. [P30307-4 ]

    Organism-specific databases

    CTDi 995.
    GeneCardsi GC05M137620.
    HGNCi HGNC:1727. CDC25C.
    HPAi CAB003800.
    MIMi 157680. gene.
    neXtProti NX_P30307.
    PharmGKBi PA100.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5105.
    HOVERGENi HBG052501.
    InParanoidi P30307.
    KOi K05867.
    OMAi TVSLCDI.
    OrthoDBi EOG7288R1.
    PhylomeDBi P30307.
    TreeFami TF101056.

    Enzyme and pathway databases

    BRENDAi 3.1.3.48. 2681.
    Reactomei REACT_1006. Polo-like kinase mediated events.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_2101. Cyclin B2 mediated events.
    REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
    REACT_6769. Activation of ATR in response to replication stress.

    Miscellaneous databases

    ChiTaRSi CDC25C. human.
    EvolutionaryTracei P30307.
    GeneWikii CDC25C.
    GenomeRNAii 995.
    NextBioi 4178.
    PROi P30307.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30307.
    Bgeei P30307.
    CleanExi HS_CDC25C.
    Genevestigatori P30307.

    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. 2 hits.
    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. "Human homolog of fission yeast cdc25 mitotic inducer is predominantly expressed in G2."
      Sadhu K., Reed B.I., Richardson H., Russell P.
      Proc. Natl. Acad. Sci. U.S.A. 87:5139-5143(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-70.
    2. "An additional transcript of the cdc25C gene from A431 cells encodes a functional protein."
      Bureik M., Rief N., Drescher R., Jungbluth A., Montenarh M., Wagner P.
      Int. J. Oncol. 17:1251-1258(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    3. NIEHS SNPs program
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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), VARIANT CYS-70.
      Tissue: Skin.
    6. "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 32-210 (ISOFORMS 2; 4 AND 5), VARIANT CYS-70.
    7. "Differential expression of cdc25 cell-cycle-activating phosphatases in human colorectal carcinoma."
      Hernandez S., Bessa X., Bea S., Hernandez L., Nadal A., Mallofre C., Muntane J., Castells A., Fernandez P.L., Cardesa A., Campo E.
      Lab. Invest. 81:465-473(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
      Tissue: Colon carcinoma.
    8. "Activation of p34cdc2 protein kinase by microinjection of human cdc25C into mammalian cells. Requirement for prior phosphorylation of cdc25C by p34cdc2 on sites phosphorylated at mitosis."
      Strausfeld U., Fernandez A., Capony J.P., Girard F., Lautredou N., Derancourt J., Labbe J.C., Lamb N.J.
      J. Biol. Chem. 269:5989-6000(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-48; THR-67; SER-122; THR-130; SER-168 AND SER-214.
    9. "The physical association and phosphorylation of Cdc25C protein phosphatase by Prk."
      Ouyang B., Li W., Pan H., Meadows J., Hoffmann I., Dai W.
      Oncogene 18:6029-6036(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PLK3.
    10. "The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase."
      Roshak A.K., Capper E.A., Imburgia C., Fornwald J., Scott G., Marshall L.A.
      Cell. Signal. 12:405-411(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PLK1.
    11. "Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase."
      Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V., Potapova O., Appella E., Fornace A.J. Jr.
      Nature 411:102-107(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-216, INTERACTION WITH MAPK14 AND 14-3-3 PROTEINS.
    12. "Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates."
      Elia A.E., Cantley L.C., Yaffe M.B.
      Science 299:1228-1231(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLK1, MUTAGENESIS OF SER-129 AND THR-130.
    13. "Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function."
      Lu R., Niida H., Nakanishi M.
      J. Biol. Chem. 279:31164-31170(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-216.
      Tissue: Testis.
    14. "Cdc25C phosphorylation on serine 191 by Plk3 promotes its nuclear translocation."
      Bahassi el M., Hennigan R.F., Myer D.L., Stambrook P.J.
      Oncogene 23:2658-2663(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-191 AND SER-198, MUTAGENESIS OF SER-191.
    15. "The human immunodeficiency virus Vpr protein binds Cdc25C: implications for G2 arrest."
      Goh W.C., Manel N., Emerman M.
      Virology 318:337-349(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 VPR, MUTAGENESIS OF GLU-352 AND LYS-359.
    16. "MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M transition and S phase progression in response to UV irradiation."
      Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., Yaffe M.B.
      Mol. Cell 17:37-48(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-216 BY MAPKAPK2.
    17. "Human Plk4 phosphorylates Cdc25C."
      Bonni S., Ganuelas M.L., Petrinac S., Hudson J.W.
      Cell Cycle 7:545-547(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PLK4.
    18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-168 AND SER-472, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; THR-48; SER-57; SER-61; SER-64 AND THR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-64 AND THR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMPIP3_HUMAN
    AccessioniPrimary (citable) accession number: P30307
    Secondary accession number(s): D3DQB8
    , Q96PL3, Q9H168, Q9H2E8, Q9H2E9, Q9H2F1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 153 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 5
      Human chromosome 5: 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