MPIP2_HUMAN
ID MPIP2_HUMAN Reviewed; 580 AA.
AC P30305; D3DVY1; D3DVY2; D3DVY3; D3DVY4; O43551; Q13971; Q5JX77; Q6RSS1;
AC Q9BRA6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=M-phase inducer phosphatase 2;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity phosphatase Cdc25B;
GN Name=CDC25B; Synonyms=CDC25HU2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1836978; DOI=10.1016/0092-8674(91)90294-9;
RA Galaktionov K.I., Beach D.;
RT "Specific activation of cdc25 tyrosine phosphatases by B-type cyclins:
RT evidence for multiple roles of mitotic cyclins.";
RL Cell 67:1181-1194(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1662986;
RA Nagata A., Igarashi M., Jinno S., Suto K., Okayama H.;
RT "An additional homolog of the fission yeast cdc25+ gene occurs in humans
RT and is highly expressed in some cancer cells.";
RL New Biol. 3:959-968(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3).
RX PubMed=9188863; DOI=10.1038/sj.onc.1201063;
RA Baldin V., Cans C., Superti-Furga G., Docommun B.;
RT "Alternative splicing of the human CDC25B tyrosine phosphatase. Possible
RT implications for growth control?";
RL Oncogene 14:2485-2495(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-548.
RG NIEHS SNPs program;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-352 (ISOFORMS 2 AND 3).
RA McCormack A.K., DeSouza C.C.P.C., Tonks I.D., Clark J.M., Forrest A.R.R.,
RA Hayward N.K., Ellem K.A.O., Gabrielli B.G.;
RT "Alternative splicing of cdc25B.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PHOSPHORYLATION AT SER-323 AND SER-375, AND INTERACTION WITH MAPK14 AND
RP 14-3-3 PROTEINS.
RX PubMed=11333986; DOI=10.1038/35075107;
RA Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V.,
RA Potapova O., Appella E., Fornace A.J. Jr.;
RT "Initiation of a G2/M checkpoint after ultraviolet radiation requires p38
RT kinase.";
RL Nature 411:102-107(2001).
RN [10]
RP PHOSPHORYLATION AT SER-323.
RX PubMed=12400006; DOI=10.1038/sj.onc.1205870;
RA Davezac N., Baldin V., Blot J., Ducommun B., Tassan J.P.;
RT "Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a
RT potential role for pEg3 in cell cycle regulation.";
RL Oncogene 21:7630-7641(2002).
RN [11]
RP PHOSPHORYLATION AT SER-375.
RC TISSUE=Testis;
RX PubMed=15150265; DOI=10.1074/jbc.m404728200;
RA Lu R., Niida H., Nakanishi M.;
RT "Human SAD1 kinase is involved in UV-induced DNA damage checkpoint
RT function.";
RL J. Biol. Chem. 279:31164-31170(2004).
RN [12]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-353 BY AURKA.
RX PubMed=15128871; DOI=10.1242/jcs.01108;
RA Dutertre S., Cazales M., Quaranta M., Froment C., Trabut V., Dozier C.,
RA Mirey G., Bouche J.P., Theis-Febvre N., Schmitt E., Monsarrat B.,
RA Prigent C., Ducommun B.;
RT "Phosphorylation of CDC25B by Aurora-A at the centrosome contributes to the
RT G2-M transition.";
RL J. Cell Sci. 117:2523-2531(2004).
RN [13]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY CHEK1.
RX PubMed=15311285; DOI=10.1038/ncb1165;
RA Kraemer A., Mailand N., Lukas C., Syljuaesen R.G., Wilkinson C.J.,
RA Nigg E.A., Bartek J., Lukas J.;
RT "Centrosome-associated Chk1 prevents premature activation of cyclin-B-Cdk1
RT kinase.";
RL Nat. Cell Biol. 6:884-891(2004).
RN [14]
RP PHOSPHORYLATION AT SER-169, AND SUBCELLULAR LOCATION.
RX PubMed=15908796; DOI=10.4161/cc.4.6.1716;
RA Mirey G., Chartrain I., Froment C., Quaranta M., Bouche J.P., Monsarrat B.,
RA Tassan J.P., Ducommun B.;
RT "CDC25B phosphorylated by pEg3 localizes to the centrosome and the spindle
RT poles at mitosis.";
RL Cell Cycle 4:806-811(2005).
RN [15]
RP PHOSPHORYLATION AT SER-323 BY MAPKAPK2.
RX PubMed=15629715; DOI=10.1016/j.molcel.2004.11.021;
RA Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., Yaffe M.B.;
RT "MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M
RT transition and S phase progression in response to UV irradiation.";
RL Mol. Cell 17:37-48(2005).
RN [16]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=17332740; DOI=10.1038/sj.emboj.7601637;
RA Schmidt A., Durgan J., Magalhaes A., Hall A.;
RT "Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from
RT cytokinesis.";
RL EMBO J. 26:1624-1636(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; SER-323; SER-353;
RP SER-375; SER-470 AND SER-563, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 370-580.
RX PubMed=10543950; DOI=10.1006/jmbi.1999.3168;
RA Reynolds R.A., Yem A.W., Wolfe C.L., Deibel M.R. Jr., Chidester C.G.,
RA Watenpaugh K.D.;
RT "Crystal structure of the catalytic subunit of Cdc25B required for G2/M
RT phase transition of the cell cycle.";
RL J. Mol. Biol. 293:559-568(1999).
CC -!- FUNCTION: Tyrosine protein phosphatase which functions as a dosage-
CC dependent inducer of mitotic progression. Required for G2/M phases of
CC the cell cycle progression and abscission during cytokinesis in a ECT2-
CC dependent manner. Directly dephosphorylates CDK1 and stimulates its
CC kinase activity. The three isoforms seem to have a different level of
CC activity. {ECO:0000269|PubMed:17332740}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- ACTIVITY REGULATION: Stimulated by B-type cyclins.
CC -!- SUBUNIT: Interacts with MAPK14 and 14-3-3 proteins.
CC {ECO:0000269|PubMed:11333986}.
CC -!- INTERACTION:
CC P30305; P61289: PSME3; NbExp=3; IntAct=EBI-1051746, EBI-355546;
CC P30305; P31946: YWHAB; NbExp=5; IntAct=EBI-1051746, EBI-359815;
CC P30305; P61981: YWHAG; NbExp=3; IntAct=EBI-1051746, EBI-359832;
CC P30305; Q04917: YWHAH; NbExp=5; IntAct=EBI-1051746, EBI-306940;
CC P30305; P63104: YWHAZ; NbExp=7; IntAct=EBI-1051746, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:15128871,
CC ECO:0000269|PubMed:15311285, ECO:0000269|PubMed:15908796}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:15908796}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3; Synonyms=CDC25B3;
CC IsoId=P30305-1; Sequence=Displayed;
CC Name=1; Synonyms=CDC25B1;
CC IsoId=P30305-2; Sequence=VSP_000861;
CC Name=2; Synonyms=CDC25B2;
CC IsoId=P30305-3; Sequence=VSP_000862;
CC Name=4;
CC IsoId=P30305-4; Sequence=VSP_000861, VSP_012587;
CC -!- PTM: Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which
CC inhibits the activity of this protein. Phosphorylation at Ser-353 by
CC AURKA might locally participate in the control of the onset of mitosis.
CC Phosphorylation by MELK at Ser-169 promotes localization to the
CC centrosome and the spindle poles during mitosis. Phosphorylation at
CC Ser-323 and Ser-375 by MAPK14 is required for binding to 14-3-3
CC proteins. {ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:12400006,
CC ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15150265,
CC ECO:0000269|PubMed:15311285, ECO:0000269|PubMed:15629715,
CC ECO:0000269|PubMed:15908796, ECO:0000269|PubMed:17332740}.
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc25b/";
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DR EMBL; M81934; AAA58416.1; -; mRNA.
DR EMBL; S78187; AAB21139.1; -; mRNA.
DR EMBL; X96436; CAA65303.1; -; Genomic_DNA.
DR EMBL; Z68092; CAA92108.1; -; mRNA.
DR EMBL; AY494082; AAR26469.1; -; Genomic_DNA.
DR EMBL; AL109804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10491.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10492.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10493.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10494.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10496.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10497.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10498.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10499.1; -; Genomic_DNA.
DR EMBL; BC006395; AAH06395.1; -; mRNA.
DR EMBL; BC009953; AAH09953.1; -; mRNA.
DR EMBL; BC051711; AAH51711.1; -; mRNA.
DR EMBL; AF036233; AAB94622.1; -; Genomic_DNA.
DR EMBL; AF036233; AAB94624.1; -; Genomic_DNA.
DR CCDS; CCDS13065.1; -. [P30305-2]
DR CCDS; CCDS13066.1; -. [P30305-3]
DR CCDS; CCDS13067.1; -. [P30305-1]
DR PIR; B41648; B41648.
DR RefSeq; NP_001274448.1; NM_001287519.1.
DR RefSeq; NP_001274453.1; NM_001287524.1.
DR RefSeq; NP_004349.1; NM_004358.4. [P30305-2]
DR RefSeq; NP_068658.1; NM_021872.3. [P30305-3]
DR RefSeq; NP_068659.1; NM_021873.3. [P30305-1]
DR PDB; 1CWR; X-ray; 2.10 A; A=370-580.
DR PDB; 1CWS; X-ray; 2.00 A; A=370-580.
DR PDB; 1CWT; X-ray; 2.30 A; A=388-565.
DR PDB; 1QB0; X-ray; 1.91 A; A=370-580.
DR PDB; 1YM9; X-ray; 2.00 A; A=391-564.
DR PDB; 1YMD; X-ray; 1.70 A; A=391-564.
DR PDB; 1YMK; X-ray; 1.70 A; A=391-564.
DR PDB; 1YML; X-ray; 1.70 A; A=391-564.
DR PDB; 1YS0; X-ray; 2.00 A; A=391-564.
DR PDB; 2A2K; X-ray; 1.52 A; A=391-564.
DR PDB; 2IFD; X-ray; 2.00 A; A=391-564.
DR PDB; 2IFV; X-ray; 1.60 A; A=391-564.
DR PDB; 2UZQ; X-ray; 2.38 A; A/B/C/D/E/F=391-580.
DR PDB; 3FQT; X-ray; 1.80 A; C=38-46.
DR PDB; 3FQU; X-ray; 1.80 A; C=38-46.
DR PDB; 4WH7; X-ray; 1.62 A; A=386-565.
DR PDB; 4WH9; X-ray; 1.50 A; A=386-565.
DR PDBsum; 1CWR; -.
DR PDBsum; 1CWS; -.
DR PDBsum; 1CWT; -.
DR PDBsum; 1QB0; -.
DR PDBsum; 1YM9; -.
DR PDBsum; 1YMD; -.
DR PDBsum; 1YMK; -.
DR PDBsum; 1YML; -.
DR PDBsum; 1YS0; -.
DR PDBsum; 2A2K; -.
DR PDBsum; 2IFD; -.
DR PDBsum; 2IFV; -.
DR PDBsum; 2UZQ; -.
DR PDBsum; 3FQT; -.
DR PDBsum; 3FQU; -.
DR PDBsum; 4WH7; -.
DR PDBsum; 4WH9; -.
DR AlphaFoldDB; P30305; -.
DR SMR; P30305; -.
DR BioGRID; 107429; 128.
DR DIP; DIP-323N; -.
DR ELM; P30305; -.
DR IntAct; P30305; 19.
DR MINT; P30305; -.
DR STRING; 9606.ENSP00000245960; -.
DR BindingDB; P30305; -.
DR ChEMBL; CHEMBL4804; -.
DR DrugBank; DB03661; L-cysteic acid.
DR DrugCentral; P30305; -.
DR DEPOD; CDC25B; -.
DR iPTMnet; P30305; -.
DR PhosphoSitePlus; P30305; -.
DR BioMuta; CDC25B; -.
DR DMDM; 21264471; -.
DR CPTAC; CPTAC-1253; -.
DR CPTAC; CPTAC-1254; -.
DR EPD; P30305; -.
DR jPOST; P30305; -.
DR MassIVE; P30305; -.
DR MaxQB; P30305; -.
DR PaxDb; P30305; -.
DR PeptideAtlas; P30305; -.
DR PRIDE; P30305; -.
DR ProteomicsDB; 54654; -. [P30305-1]
DR ProteomicsDB; 54655; -. [P30305-2]
DR ProteomicsDB; 54656; -. [P30305-3]
DR ProteomicsDB; 54657; -. [P30305-4]
DR Antibodypedia; 3625; 976 antibodies from 40 providers.
DR CPTC; P30305; 2 antibodies.
DR DNASU; 994; -.
DR Ensembl; ENST00000245960.10; ENSP00000245960.5; ENSG00000101224.18. [P30305-1]
DR Ensembl; ENST00000340833.4; ENSP00000339170.4; ENSG00000101224.18. [P30305-3]
DR Ensembl; ENST00000439880.6; ENSP00000405972.2; ENSG00000101224.18. [P30305-2]
DR GeneID; 994; -.
DR KEGG; hsa:994; -.
DR MANE-Select; ENST00000245960.10; ENSP00000245960.5; NM_021873.4; NP_068659.1.
DR UCSC; uc002wjn.5; human. [P30305-1]
DR CTD; 994; -.
DR DisGeNET; 994; -.
DR GeneCards; CDC25B; -.
DR HGNC; HGNC:1726; CDC25B.
DR HPA; ENSG00000101224; Low tissue specificity.
DR MIM; 116949; gene.
DR neXtProt; NX_P30305; -.
DR OpenTargets; ENSG00000101224; -.
DR PharmGKB; PA26260; -.
DR VEuPathDB; HostDB:ENSG00000101224; -.
DR eggNOG; KOG3772; Eukaryota.
DR GeneTree; ENSGT00940000158524; -.
DR InParanoid; P30305; -.
DR OMA; MHSKCRR; -.
DR PhylomeDB; P30305; -.
DR TreeFam; TF101056; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P30305; -.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
DR SignaLink; P30305; -.
DR SIGNOR; P30305; -.
DR BioGRID-ORCS; 994; 151 hits in 1089 CRISPR screens.
DR ChiTaRS; CDC25B; human.
DR EvolutionaryTrace; P30305; -.
DR GeneWiki; CDC25B; -.
DR GenomeRNAi; 994; -.
DR Pharos; P30305; Tchem.
DR PRO; PR:P30305; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P30305; protein.
DR Bgee; ENSG00000101224; Expressed in granulocyte and 191 other tissues.
DR ExpressionAtlas; P30305; baseline and differential.
DR Genevisible; P30305; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:Reactome.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007144; P:female meiosis I; IEA:Ensembl.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0110032; P:positive regulation of G2/MI transition of meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR CDD; cd01530; Cdc25; 1.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR000751; MPI_Phosphatase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF06617; M-inducer_phosp; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00716; MPIPHPHTASE.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Hydrolase; Mitosis; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..580
FT /note="M-phase inducer phosphatase 2"
FT /id="PRO_0000198644"
FT DOMAIN 431..538
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 487
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48966"
FT MOD_RES 169
FT /note="Phosphoserine; by MELK"
FT /evidence="ECO:0000269|PubMed:15908796"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Phosphoserine; by MELK and MAPK14"
FT /evidence="ECO:0000269|PubMed:11333986,
FT ECO:0000269|PubMed:12400006, ECO:0000269|PubMed:15629715,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 353
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000269|PubMed:15128871,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 375
FT /note="Phosphoserine; by BRSK1 and MAPK14"
FT /evidence="ECO:0000269|PubMed:11333986,
FT ECO:0000269|PubMed:15150265, ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 68..81
FT /note="Missing (in isoform 1 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:1662986,
FT ECO:0000303|PubMed:1836978"
FT /id="VSP_000861"
FT VAR_SEQ 154..194
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9188863"
FT /id="VSP_000862"
FT VAR_SEQ 194
FT /note="N -> NVRFWKAGVGALREEEGACWGGSLACEDPPLPSWLQ (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_012587"
FT VARIANT 548
FT /note="E -> K (in dbSNP:rs11570019)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020933"
FT CONFLICT 575
FT /note="S -> D (in Ref. 2; AAB21139)"
FT /evidence="ECO:0000305"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:4WH9"
FT HELIX 417..424
FT /evidence="ECO:0007829|PDB:4WH9"
FT TURN 425..431
FT /evidence="ECO:0007829|PDB:4WH9"
FT STRAND 432..439
FT /evidence="ECO:0007829|PDB:4WH9"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:4WH9"
FT HELIX 460..468
FT /evidence="ECO:0007829|PDB:4WH9"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:4WH9"
FT STRAND 479..486
FT /evidence="ECO:0007829|PDB:4WH9"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:4WH9"
FT HELIX 493..508
FT /evidence="ECO:0007829|PDB:4WH9"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:4WH9"
FT HELIX 525..532
FT /evidence="ECO:0007829|PDB:4WH9"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:4WH9"
FT STRAND 537..540
FT /evidence="ECO:0007829|PDB:4WH9"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:2A2K"
FT HELIX 551..558
FT /evidence="ECO:0007829|PDB:4WH9"
SQ SEQUENCE 580 AA; 64987 MW; EDE24B0E84AC1BE3 CRC64;
MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS PVTTLTQTMH
DLAGLGSETP KSQVGTLLFR SRSRLTHLSL SRRASESSLS SESSESSDAG LCMDSPSPMD
PHMAEQTFEQ AIQAASRIIR NEQFAIRRFQ SMPVRLLGHS PVLRNITNSQ APDGRRKSEA
GSGAASSSGE DKENDGFVFK MPWKPTHPSS THALAEWASR REAFAQRPSS APDLMCLSPD
RKMEVEELSP LALGRFSLTP AEGDTEEDDG FVDILESDLK DDDAVPPGME SLISAPLVKT
LEKEEEKDLV MYSKCQRLFR SPSMPCSVIR PILKRLERPQ DRDTPVQNKR RRSVTPPEEQ
QEAEEPKARV LRSKSLCHDE IENLLDSDHR ELIGDYSKAF LLQTVDGKHQ DLKYISPETM
VALLTGKFSN IVDKFVIVDC RYPYEYEGGH IKTAVNLPLE RDAESFLLKS PIAPCSLDKR
VILIFHCEFS SERGPRMCRF IRERDRAVND YPSLYYPEMY ILKGGYKEFF PQHPNFCEPQ
DYRPMNHEAF KDELKTFRLK TRSWAGERSR RELCSRLQDQ
