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 27-MAR-2024, entry version 225. DE RecName: Full=M-phase inducer phosphatase 2; DE EC=3.1.3.48 {ECO:0000305|PubMed:20360007}; 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), FUNCTION, AND ACTIVITY REGULATION. 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 FUNCTION. RX PubMed=20360007; DOI=10.1074/jbc.m109.096552; RA Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.; RT "Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B at RT the G2/M transition."; RL J. Biol. Chem. 285:16978-16990(2010). RN [20] 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 [21] 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 [22] 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 (PubMed:1836978, CC PubMed:20360007). Directly dephosphorylates CDK1 and stimulates its CC kinase activity (PubMed:20360007). Required for G2/M phases of the cell CC cycle progression and abscission during cytokinesis in a ECT2-dependent CC manner (PubMed:17332740). The three isoforms seem to have a different CC level of activity (PubMed:1836978). {ECO:0000269|PubMed:17332740, CC ECO:0000269|PubMed:1836978, ECO:0000269|PubMed:20360007}. 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 Evidence={ECO:0000305|PubMed:20360007}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685; CC Evidence={ECO:0000305|PubMed:20360007}; CC -!- ACTIVITY REGULATION: Stimulated by B-type cyclins. CC {ECO:0000269|PubMed:1836978}. 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; P31947: SFN; NbExp=2; IntAct=EBI-1051746, EBI-476295; CC P30305; P31946: YWHAB; NbExp=5; IntAct=EBI-1051746, EBI-359815; CC P30305; P62258: YWHAE; NbExp=4; IntAct=EBI-1051746, EBI-356498; CC P30305; P61981: YWHAG; NbExp=4; IntAct=EBI-1051746, EBI-359832; CC P30305; Q04917: YWHAH; NbExp=6; 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 131. 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 GlyGen; P30305; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P30305; -. DR PhosphoSitePlus; P30305; -. DR BioMuta; CDC25B; -. DR DMDM; 21264471; -. DR CPTAC; CPTAC-1253; -. DR CPTAC; CPTAC-1254; -. DR CPTAC; CPTAC-5903; -. DR CPTAC; CPTAC-5904; -. DR CPTAC; CPTAC-5905; -. DR EPD; P30305; -. DR jPOST; P30305; -. DR MassIVE; P30305; -. DR MaxQB; P30305; -. DR PaxDb; 9606-ENSP00000245960; -. DR PeptideAtlas; P30305; -. DR ProteomicsDB; 54654; -. [P30305-1] DR ProteomicsDB; 54655; -. [P30305-2] DR ProteomicsDB; 54656; -. [P30305-3] DR ProteomicsDB; 54657; -. [P30305-4] DR Pumba; P30305; -. DR Antibodypedia; 3625; 1094 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 AGR; HGNC:1726; -. 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 OrthoDB; 12481at2759; -. 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; 156 hits in 1183 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 193 other cell types or tissues. DR ExpressionAtlas; P30305; baseline and differential. 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; IDA:UniProtKB. 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; IDA:UniProtKB. 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:0006468; P:protein phosphorylation; IDA:UniProtKB. DR CDD; cd01530; Cdc25; 1. DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1. DR InterPro; IPR000751; MPI_Phosphatase. DR InterPro; IPR001763; Rhodanese-like_dom. DR InterPro; IPR036873; Rhodanese-like_dom_sf. DR PANTHER; PTHR10828:SF48; M-PHASE INDUCER PHOSPHATASE 2; 1. DR PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1. DR Pfam; PF06617; M-inducer_phosp; 1. DR Pfam; PF00581; Rhodanese; 1. DR PRINTS; PR00716; MPIPHPHTASE. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1. DR PROSITE; PS50206; RHODANESE_3; 1. DR Genevisible; P30305; HS. 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 //