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P30305

- MPIP2_HUMAN

UniProt

P30305 - MPIP2_HUMAN

Protein

M-phase inducer phosphatase 2

Gene

CDC25B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (27 May 2002)
      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. The three isoforms seem to have a different level of activity.1 Publication

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Enzyme regulationi

    Stimulated by B-type cyclins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei487 – 4871

    GO - Molecular functioni

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

    GO - Biological processi

    1. female meiosis I Source: Ensembl
    2. G2/M transition of mitotic cell cycle Source: UniProtKB
    3. mitotic cell cycle Source: UniProtKB
    4. mitotic nuclear division Source: ProtInc
    5. oocyte maturation Source: Ensembl
    6. peptidyl-tyrosine dephosphorylation Source: GOC
    7. positive regulation of cell proliferation Source: ProtInc
    8. positive regulation of cytokinesis Source: UniProtKB
    9. positive regulation of mitotic cell cycle Source: UniProtKB
    10. positive regulation of protein kinase activity Source: Ensembl
    11. protein phosphorylation 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_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_2101. Cyclin B2 mediated events.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.

    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
    Synonyms:CDC25HU2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:1726. CDC25B.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA
    6. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26260.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 580580M-phase inducer phosphatase 2PRO_0000198644Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei169 – 1691Phosphoserine; by MELK1 Publication
    Modified residuei249 – 2491Phosphoserine1 Publication
    Modified residuei323 – 3231Phosphoserine; by MELK and MAPK143 Publications
    Modified residuei353 – 3531Phosphoserine; by AURKA1 Publication
    Modified residuei375 – 3751Phosphoserine; by BRSK1 and MAPK142 Publications

    Post-translational modificationi

    Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-353 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-169 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-323 and Ser-375 by MAPK14 is required for binding to 14-3-3 proteins.9 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP30305.
    PaxDbiP30305.
    PRIDEiP30305.

    PTM databases

    PhosphoSiteiP30305.

    Expressioni

    Gene expression databases

    ArrayExpressiP30305.
    BgeeiP30305.
    CleanExiHS_CDC25B.
    GenevestigatoriP30305.

    Organism-specific databases

    HPAiCAB002663.
    HPA038892.
    HPA038893.

    Interactioni

    Subunit structurei

    Interacts with MAPK14 and 14-3-3 proteins.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YWHABP319464EBI-1051746,EBI-359815
    YWHAHQ049173EBI-1051746,EBI-306940
    YWHAZP631044EBI-1051746,EBI-347088

    Protein-protein interaction databases

    BioGridi107429. 30 interactions.
    DIPiDIP-323N.
    IntActiP30305. 8 interactions.
    MINTiMINT-124404.
    STRINGi9606.ENSP00000245960.

    Structurei

    Secondary structure

    1
    580
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi396 – 3994
    Helixi417 – 4248
    Turni425 – 4317
    Beta strandi432 – 4398
    Helixi443 – 4475
    Helixi460 – 4689
    Turni469 – 4713
    Beta strandi480 – 4867
    Beta strandi488 – 4925
    Helixi493 – 50715
    Beta strandi519 – 5224
    Helixi525 – 5295
    Turni530 – 5323
    Helixi534 – 5363
    Beta strandi537 – 5404
    Helixi548 – 5503
    Helixi551 – 5588

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CWRX-ray2.10A370-580[»]
    1CWSX-ray2.00A370-580[»]
    1CWTX-ray2.30A388-565[»]
    1QB0X-ray1.91A370-580[»]
    1YM9X-ray2.00A391-564[»]
    1YMDX-ray1.70A391-564[»]
    1YMKX-ray1.70A391-564[»]
    1YMLX-ray1.70A391-564[»]
    1YS0X-ray2.00A391-564[»]
    2A2KX-ray1.52A391-564[»]
    2IFDX-ray2.00A391-564[»]
    2IFVX-ray1.60A391-564[»]
    2UZQX-ray2.38A/B/C/D/E/F391-580[»]
    3FQTX-ray1.80C38-46[»]
    3FQUX-ray1.80C38-46[»]
    ProteinModelPortaliP30305.
    SMRiP30305. Positions 388-564.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30305.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini431 – 538108RhodanesePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5105.
    HOVERGENiHBG052501.
    InParanoidiP30305.
    KOiK05866.
    OMAiTPKSQVG.
    OrthoDBiEOG7288R1.
    PhylomeDBiP30305.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 3 (identifier: P30305-1) [UniParc]FASTAAdd to Basket

    Also known as: CDC25B3

    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

    MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS    50
    PVTTLTQTMH DLAGLGSETP KSQVGTLLFR SRSRLTHLSL SRRASESSLS 100
    SESSESSDAG LCMDSPSPMD PHMAEQTFEQ AIQAASRIIR NEQFAIRRFQ 150
    SMPVRLLGHS PVLRNITNSQ APDGRRKSEA GSGAASSSGE DKENDGFVFK 200
    MPWKPTHPSS THALAEWASR REAFAQRPSS APDLMCLSPD RKMEVEELSP 250
    LALGRFSLTP AEGDTEEDDG FVDILESDLK DDDAVPPGME SLISAPLVKT 300
    LEKEEEKDLV MYSKCQRLFR SPSMPCSVIR PILKRLERPQ DRDTPVQNKR 350
    RRSVTPPEEQ QEAEEPKARV LRSKSLCHDE IENLLDSDHR ELIGDYSKAF 400
    LLQTVDGKHQ DLKYISPETM VALLTGKFSN IVDKFVIVDC RYPYEYEGGH 450
    IKTAVNLPLE RDAESFLLKS PIAPCSLDKR VILIFHCEFS SERGPRMCRF 500
    IRERDRAVND YPSLYYPEMY ILKGGYKEFF PQHPNFCEPQ DYRPMNHEAF 550
    KDELKTFRLK TRSWAGERSR RELCSRLQDQ 580
    Length:580
    Mass (Da):64,987
    Last modified:May 27, 2002 - v2
    Checksum:iEDE24B0E84AC1BE3
    GO
    Isoform 1 (identifier: P30305-2) [UniParc]FASTAAdd to Basket

    Also known as: CDC25B1

    The sequence of this isoform differs from the canonical sequence as follows:
         68-81: Missing.

    Show »
    Length:566
    Mass (Da):63,443
    Checksum:i7C54E3E799ECDA50
    GO
    Isoform 2 (identifier: P30305-3) [UniParc]FASTAAdd to Basket

    Also known as: CDC25B2

    The sequence of this isoform differs from the canonical sequence as follows:
         154-194: Missing.

    Show »
    Length:539
    Mass (Da):60,756
    Checksum:iCDA92929F8183BE9
    GO
    Isoform 4 (identifier: P30305-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         68-81: Missing.
         194-194: N → NVRFWKAGVGALREEEGACWGGSLACEDPPLPSWLQ

    Note: No experimental confirmation available.

    Show »
    Length:601
    Mass (Da):67,241
    Checksum:i8E32AEC15A3845D7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti575 – 5751S → D in AAB21139. (PubMed:1662986)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti548 – 5481E → K.1 Publication
    Corresponds to variant rs11570019 [ dbSNP | Ensembl ].
    VAR_020933

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei68 – 8114Missing in isoform 1 and isoform 4. 2 PublicationsVSP_000861Add
    BLAST
    Alternative sequencei154 – 19441Missing in isoform 2. 1 PublicationVSP_000862Add
    BLAST
    Alternative sequencei194 – 1941N → NVRFWKAGVGALREEEGACW GGSLACEDPPLPSWLQ in isoform 4. CuratedVSP_012587

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81934 mRNA. Translation: AAA58416.1.
    S78187 mRNA. Translation: AAB21139.1.
    X96436 Genomic DNA. Translation: CAA65303.1.
    Z68092 mRNA. Translation: CAA92108.1.
    AY494082 Genomic DNA. Translation: AAR26469.1.
    AL109804 Genomic DNA. Translation: CAC17548.1.
    AL109804 Genomic DNA. Translation: CAC17549.1.
    AL109804 Genomic DNA. Translation: CAI18847.1.
    CH471133 Genomic DNA. Translation: EAX10491.1.
    CH471133 Genomic DNA. Translation: EAX10492.1.
    CH471133 Genomic DNA. Translation: EAX10493.1.
    CH471133 Genomic DNA. Translation: EAX10494.1.
    CH471133 Genomic DNA. Translation: EAX10496.1.
    CH471133 Genomic DNA. Translation: EAX10497.1.
    CH471133 Genomic DNA. Translation: EAX10498.1.
    CH471133 Genomic DNA. Translation: EAX10499.1.
    BC006395 mRNA. Translation: AAH06395.1.
    BC009953 mRNA. Translation: AAH09953.1.
    BC051711 mRNA. Translation: AAH51711.1.
    AF036233 Genomic DNA. Translation: AAB94622.1.
    AF036233 Genomic DNA. Translation: AAB94624.1.
    CCDSiCCDS13065.1. [P30305-2]
    CCDS13066.1. [P30305-3]
    CCDS13067.1. [P30305-1]
    PIRiB41648.
    RefSeqiNP_001274448.1. NM_001287519.1.
    NP_001274453.1. NM_001287524.1.
    NP_004349.1. NM_004358.4. [P30305-2]
    NP_068658.1. NM_021872.3. [P30305-3]
    NP_068659.1. NM_021873.3. [P30305-1]
    UniGeneiHs.153752.

    Genome annotation databases

    EnsembliENST00000245960; ENSP00000245960; ENSG00000101224. [P30305-1]
    ENST00000340833; ENSP00000339170; ENSG00000101224. [P30305-3]
    ENST00000439880; ENSP00000405972; ENSG00000101224. [P30305-2]
    GeneIDi994.
    KEGGihsa:994.
    UCSCiuc002wjl.3. human. [P30305-1]
    uc002wjo.3. human. [P30305-2]
    uc002wjp.3. human. [P30305-3]

    Polymorphism databases

    DMDMi21264471.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81934 mRNA. Translation: AAA58416.1 .
    S78187 mRNA. Translation: AAB21139.1 .
    X96436 Genomic DNA. Translation: CAA65303.1 .
    Z68092 mRNA. Translation: CAA92108.1 .
    AY494082 Genomic DNA. Translation: AAR26469.1 .
    AL109804 Genomic DNA. Translation: CAC17548.1 .
    AL109804 Genomic DNA. Translation: CAC17549.1 .
    AL109804 Genomic DNA. Translation: CAI18847.1 .
    CH471133 Genomic DNA. Translation: EAX10491.1 .
    CH471133 Genomic DNA. Translation: EAX10492.1 .
    CH471133 Genomic DNA. Translation: EAX10493.1 .
    CH471133 Genomic DNA. Translation: EAX10494.1 .
    CH471133 Genomic DNA. Translation: EAX10496.1 .
    CH471133 Genomic DNA. Translation: EAX10497.1 .
    CH471133 Genomic DNA. Translation: EAX10498.1 .
    CH471133 Genomic DNA. Translation: EAX10499.1 .
    BC006395 mRNA. Translation: AAH06395.1 .
    BC009953 mRNA. Translation: AAH09953.1 .
    BC051711 mRNA. Translation: AAH51711.1 .
    AF036233 Genomic DNA. Translation: AAB94622.1 .
    AF036233 Genomic DNA. Translation: AAB94624.1 .
    CCDSi CCDS13065.1. [P30305-2 ]
    CCDS13066.1. [P30305-3 ]
    CCDS13067.1. [P30305-1 ]
    PIRi B41648.
    RefSeqi NP_001274448.1. NM_001287519.1.
    NP_001274453.1. NM_001287524.1.
    NP_004349.1. NM_004358.4. [P30305-2 ]
    NP_068658.1. NM_021872.3. [P30305-3 ]
    NP_068659.1. NM_021873.3. [P30305-1 ]
    UniGenei Hs.153752.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CWR X-ray 2.10 A 370-580 [» ]
    1CWS X-ray 2.00 A 370-580 [» ]
    1CWT X-ray 2.30 A 388-565 [» ]
    1QB0 X-ray 1.91 A 370-580 [» ]
    1YM9 X-ray 2.00 A 391-564 [» ]
    1YMD X-ray 1.70 A 391-564 [» ]
    1YMK X-ray 1.70 A 391-564 [» ]
    1YML X-ray 1.70 A 391-564 [» ]
    1YS0 X-ray 2.00 A 391-564 [» ]
    2A2K X-ray 1.52 A 391-564 [» ]
    2IFD X-ray 2.00 A 391-564 [» ]
    2IFV X-ray 1.60 A 391-564 [» ]
    2UZQ X-ray 2.38 A/B/C/D/E/F 391-580 [» ]
    3FQT X-ray 1.80 C 38-46 [» ]
    3FQU X-ray 1.80 C 38-46 [» ]
    ProteinModelPortali P30305.
    SMRi P30305. Positions 388-564.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107429. 30 interactions.
    DIPi DIP-323N.
    IntActi P30305. 8 interactions.
    MINTi MINT-124404.
    STRINGi 9606.ENSP00000245960.

    Chemistry

    BindingDBi P30305.
    ChEMBLi CHEMBL4804.

    PTM databases

    PhosphoSitei P30305.

    Polymorphism databases

    DMDMi 21264471.

    Proteomic databases

    MaxQBi P30305.
    PaxDbi P30305.
    PRIDEi P30305.

    Protocols and materials databases

    DNASUi 994.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000245960 ; ENSP00000245960 ; ENSG00000101224 . [P30305-1 ]
    ENST00000340833 ; ENSP00000339170 ; ENSG00000101224 . [P30305-3 ]
    ENST00000439880 ; ENSP00000405972 ; ENSG00000101224 . [P30305-2 ]
    GeneIDi 994.
    KEGGi hsa:994.
    UCSCi uc002wjl.3. human. [P30305-1 ]
    uc002wjo.3. human. [P30305-2 ]
    uc002wjp.3. human. [P30305-3 ]

    Organism-specific databases

    CTDi 994.
    GeneCardsi GC20P003771.
    HGNCi HGNC:1726. CDC25B.
    HPAi CAB002663.
    HPA038892.
    HPA038893.
    MIMi 116949. gene.
    neXtProti NX_P30305.
    PharmGKBi PA26260.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5105.
    HOVERGENi HBG052501.
    InParanoidi P30305.
    KOi K05866.
    OMAi TPKSQVG.
    OrthoDBi EOG7288R1.
    PhylomeDBi P30305.
    TreeFami TF101056.

    Enzyme and pathway databases

    BRENDAi 3.1.3.48. 2681.
    Reactomei REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_2101. Cyclin B2 mediated events.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.

    Miscellaneous databases

    EvolutionaryTracei P30305.
    GeneWikii CDC25B.
    GenomeRNAii 994.
    NextBioi 4170.
    PROi P30305.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30305.
    Bgeei P30305.
    CleanExi HS_CDC25B.
    Genevestigatori P30305.

    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).
    2. "An additional homolog of the fission yeast cdc25+ gene occurs in humans and is highly expressed in some cancer cells."
      Nagata A., Igarashi M., Jinno S., Suto K., Okayama H.
      New Biol. 3:959-968(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Alternative splicing of the human CDC25B tyrosine phosphatase. Possible implications for growth control?"
      Baldin V., Cans C., Superti-Furga G., Docommun B.
      Oncogene 14:2485-2495(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3).
    4. NIEHS SNPs program
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-548.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 3).
      Tissue: Brain.
    8. "Alternative splicing of cdc25B."
      McCormack A.K., DeSouza C.C.P.C., Tonks I.D., Clark J.M., Forrest A.R.R., Hayward N.K., Ellem K.A.O., Gabrielli B.G.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-352 (ISOFORMS 2 AND 3).
    9. "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-323 AND SER-375, INTERACTION WITH MAPK14 AND 14-3-3 PROTEINS.
    10. "Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a potential role for pEg3 in cell cycle regulation."
      Davezac N., Baldin V., Blot J., Ducommun B., Tassan J.P.
      Oncogene 21:7630-7641(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-323.
    11. "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-375.
      Tissue: Testis.
    12. Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-353 BY AURKA.
    13. "Centrosome-associated Chk1 prevents premature activation of cyclin-B-Cdk1 kinase."
      Kraemer A., Mailand N., Lukas C., Syljuaesen R.G., Wilkinson C.J., Nigg E.A., Bartek J., Lukas J.
      Nat. Cell Biol. 6:884-891(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY CHEK1.
    14. "CDC25B phosphorylated by pEg3 localizes to the centrosome and the spindle poles at mitosis."
      Mirey G., Chartrain I., Froment C., Quaranta M., Bouche J.P., Monsarrat B., Tassan J.P., Ducommun B.
      Cell Cycle 4:806-811(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-169, SUBCELLULAR LOCATION.
    15. "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-323 BY MAPKAPK2.
    16. "Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis."
      Schmidt A., Durgan J., Magalhaes A., Hall A.
      EMBO J. 26:1624-1636(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle."
      Reynolds R.A., Yem A.W., Wolfe C.L., Deibel M.R. Jr., Chidester C.G., Watenpaugh K.D.
      J. Mol. Biol. 293:559-568(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 370-580.

    Entry informationi

    Entry nameiMPIP2_HUMAN
    AccessioniPrimary (citable) accession number: P30305
    Secondary accession number(s): D3DVY1
    , D3DVY2, D3DVY3, D3DVY4, O43551, Q13971, Q5JX77, Q6RSS1, Q9BRA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: May 27, 2002
    Last modified: October 1, 2014
    This is version 159 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 20
      Human chromosome 20: 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