MPIP3_HUMAN
ID MPIP3_HUMAN Reviewed; 473 AA.
AC P30307; D3DQB8; Q96PL3; Q9H168; Q9H2E8; Q9H2E9; Q9H2F1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=M-phase inducer phosphatase 3;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity phosphatase Cdc25C;
GN Name=CDC25C;
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), AND VARIANT CYS-70.
RX PubMed=2195549; DOI=10.1073/pnas.87.13.5139;
RA Sadhu K., Reed B.I., Richardson H., Russell P.;
RT "Human homolog of fission yeast cdc25 mitotic inducer is predominantly
RT expressed in G2.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5139-5143(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX PubMed=11078813; DOI=10.3892/ijo.17.6.1251;
RA Bureik M., Rief N., Drescher R., Jungbluth A., Montenarh M., Wagner P.;
RT "An additional transcript of the cdc25C gene from A431 cells encodes a
RT functional protein.";
RL Int. J. Oncol. 17:1251-1258(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT CYS-70.
RC TISSUE=Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-210 (ISOFORMS 2; 4 AND 5), AND VARIANT
RP CYS-70.
RX PubMed=11139144; DOI=10.1078/0171-9335-00115;
RA Wegener S., Hampe W., Herrmann D., Schaller H.C.;
RT "Alternative splicing in the regulatory region of the human phosphatases
RT CDC25A and CDC25C.";
RL Eur. J. Cell Biol. 79:810-815(2000).
RN [7]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC TISSUE=Colon carcinoma;
RX PubMed=11304565; DOI=10.1038/labinvest.3780254;
RA Hernandez S., Bessa X., Bea S., Hernandez L., Nadal A., Mallofre C.,
RA Muntane J., Castells A., Fernandez P.L., Cardesa A., Campo E.;
RT "Differential expression of cdc25 cell-cycle-activating phosphatases in
RT human colorectal carcinoma.";
RL Lab. Invest. 81:465-473(2001).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-48; THR-67;
RP SER-122; THR-130; SER-168 AND SER-214.
RX PubMed=8119945; DOI=10.1016/s0021-9258(17)37560-9;
RA Strausfeld U., Fernandez A., Capony J.P., Girard F., Lautredou N.,
RA Derancourt J., Labbe J.C., Lamb N.J.;
RT "Activation of p34cdc2 protein kinase by microinjection of human cdc25C
RT into mammalian cells. Requirement for prior phosphorylation of cdc25C by
RT p34cdc2 on sites phosphorylated at mitosis.";
RL J. Biol. Chem. 269:5989-6000(1994).
RN [9]
RP PHOSPHORYLATION BY PLK3.
RX PubMed=10557092; DOI=10.1038/sj.onc.1202983;
RA Ouyang B., Li W., Pan H., Meadows J., Hoffmann I., Dai W.;
RT "The physical association and phosphorylation of Cdc25C protein phosphatase
RT by Prk.";
RL Oncogene 18:6029-6036(1999).
RN [10]
RP PHOSPHORYLATION BY PLK1.
RX PubMed=11202906; DOI=10.1016/s0898-6568(00)00080-2;
RA Roshak A.K., Capper E.A., Imburgia C., Fornwald J., Scott G.,
RA Marshall L.A.;
RT "The human polo-like kinase, PLK, regulates cdc2/cyclin B through
RT phosphorylation and activation of the cdc25C phosphatase.";
RL Cell. Signal. 12:405-411(2000).
RN [11]
RP PHOSPHORYLATION AT SER-216, AND INTERACTION WITH MAPK14 AND 14-3-3
RP 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 [12]
RP INTERACTION WITH PLK1, PHOSPHORYLATION AT SER-129 AND THR-130, AND
RP MUTAGENESIS OF SER-129 AND THR-130.
RX PubMed=12595692; DOI=10.1126/science.1079079;
RA Elia A.E., Cantley L.C., Yaffe M.B.;
RT "Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic
RT substrates.";
RL Science 299:1228-1231(2003).
RN [13]
RP PHOSPHORYLATION AT SER-216.
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 [14]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-191 AND SER-198, AND
RP MUTAGENESIS OF SER-191.
RX PubMed=14968113; DOI=10.1038/sj.onc.1207425;
RA Bahassi el M., Hennigan R.F., Myer D.L., Stambrook P.J.;
RT "Cdc25C phosphorylation on serine 191 by Plk3 promotes its nuclear
RT translocation.";
RL Oncogene 23:2658-2663(2004).
RN [15]
RP INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION), AND MUTAGENESIS OF
RP GLU-352 AND LYS-359.
RX PubMed=14972559; DOI=10.1016/j.virol.2003.10.007;
RA Goh W.C., Manel N., Emerman M.;
RT "The human immunodeficiency virus Vpr protein binds Cdc25C: implications
RT for G2 arrest.";
RL Virology 318:337-349(2004).
RN [16]
RP PHOSPHORYLATION AT SER-216 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 [17]
RP PHOSPHORYLATION BY PLK4.
RX PubMed=18239451; DOI=10.4161/cc.7.4.5387;
RA Bonni S., Ganuelas M.L., Petrinac S., Hudson J.W.;
RT "Human Plk4 phosphorylates Cdc25C.";
RL Cell Cycle 7:545-547(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-168 AND SER-472,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 (ISOFORMS 4 AND 5), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; THR-48; SER-57; SER-61;
RP SER-64 AND THR-67, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-64 AND THR-67, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-38 AND SER-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Functions as a dosage-dependent inducer in mitotic control.
CC Tyrosine protein phosphatase required for progression of the cell
CC cycle. When phosphorylated, highly effective in activating G2 cells
CC into prophase. Directly dephosphorylates CDK1 and activates its kinase
CC activity. {ECO:0000269|PubMed:8119945}.
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 -!- SUBUNIT: Interacts with MAPK14 and 14-3-3 proteins. When phosphorylated
CC on Ser-129 and/or Thr-130, interacts with PLK1.
CC {ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:12595692}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr; this
CC interaction inactivates CDC25C phosphatase activity.
CC {ECO:0000269|PubMed:14972559}.
CC -!- INTERACTION:
CC P30307; P06493: CDK1; NbExp=3; IntAct=EBI-974439, EBI-444308;
CC P30307; O14757: CHEK1; NbExp=2; IntAct=EBI-974439, EBI-974488;
CC P30307; Q9Y250: LZTS1; NbExp=2; IntAct=EBI-974439, EBI-1216080;
CC P30307; P53350: PLK1; NbExp=5; IntAct=EBI-974439, EBI-476768;
CC P30307; P31946: YWHAB; NbExp=5; IntAct=EBI-974439, EBI-359815;
CC P30307; P63104: YWHAZ; NbExp=2; IntAct=EBI-974439, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14968113,
CC ECO:0000269|PubMed:8119945}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=CDC25C1;
CC IsoId=P30307-1; Sequence=Displayed;
CC Name=2; Synonyms=CDC25C2;
CC IsoId=P30307-2; Sequence=VSP_000864;
CC Name=3; Synonyms=CDC25C3;
CC IsoId=P30307-5; Sequence=Not described;
CC Name=4; Synonyms=CDC25C4;
CC IsoId=P30307-3; Sequence=VSP_000863;
CC Name=5; Synonyms=CDC25C5, Cdc25Cdm;
CC IsoId=P30307-4; Sequence=VSP_000863, VSP_000864;
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly in G2 phase.
CC -!- PTM: Phosphorylated by CHEK1 and MAPK14 at Ser-216. This
CC phosphorylation creates a binding site for 14-3-3 protein and inhibits
CC the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1,
CC leading to activate the phosphatase activity. Phosphorylation by PLK3
CC at Ser-191 promotes nuclear translocation. Ser-198 is a minor
CC phosphorylation site. Was initially reported to be phosphorylated by
CC PLK3 at Ser-216 (PubMed:10557092). However, such phosphorylation by
CC PLK3 was not confirmed by other groups. Phosphorylation at Thr-48, Thr-
CC 67, Ser-122, Thr-130, Ser-168 and Ser-214 occurs at G2 and G2-M
CC transition and is probably catalyzed by CDK1. Ser-168 phosphorylation
CC levels are lower than those at the other 5 CDK1 sites. Phosphorylation
CC by CDK1 leads to increased activity. {ECO:0000269|PubMed:10557092,
CC ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:11333986,
CC ECO:0000269|PubMed:14968113, ECO:0000269|PubMed:15150265,
CC ECO:0000269|PubMed:15629715, ECO:0000269|PubMed:18239451,
CC ECO:0000269|PubMed:8119945}.
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc25c/";
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; M34065; AAA35666.1; -; mRNA.
DR EMBL; AJ304504; CAC19192.1; -; mRNA.
DR EMBL; AY497474; AAR32098.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62145.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62149.1; -; Genomic_DNA.
DR EMBL; BC019089; AAH19089.1; -; mRNA.
DR EMBL; AF277723; AAG41885.1; -; mRNA.
DR EMBL; AF277725; AAG41887.1; -; mRNA.
DR EMBL; AF277726; AAG41888.1; -; mRNA.
DR EMBL; AF312681; AAL26835.1; -; mRNA.
DR CCDS; CCDS4202.1; -. [P30307-1]
DR CCDS; CCDS4203.1; -. [P30307-4]
DR PIR; I59168; A38874.
DR RefSeq; NP_001274511.1; NM_001287582.1. [P30307-1]
DR RefSeq; NP_001305027.1; NM_001318098.1.
DR RefSeq; NP_001781.2; NM_001790.4. [P30307-1]
DR RefSeq; NP_073720.1; NM_022809.3. [P30307-4]
DR RefSeq; XP_011542064.1; XM_011543762.1. [P30307-4]
DR PDB; 2OJX; X-ray; 2.85 A; E=126-134.
DR PDB; 3BZI; X-ray; 2.10 A; E=126-134.
DR PDB; 3OP3; X-ray; 2.63 A; A=270-462.
DR PDB; 5M35; X-ray; 2.38 A; C/D=207-244.
DR PDB; 5M36; X-ray; 2.45 A; C/D=207-244.
DR PDB; 5M37; X-ray; 2.35 A; C/D=207-226.
DR PDBsum; 2OJX; -.
DR PDBsum; 3BZI; -.
DR PDBsum; 3OP3; -.
DR PDBsum; 5M35; -.
DR PDBsum; 5M36; -.
DR PDBsum; 5M37; -.
DR AlphaFoldDB; P30307; -.
DR SMR; P30307; -.
DR BioGRID; 107430; 144.
DR DIP; DIP-24183N; -.
DR IntAct; P30307; 27.
DR MINT; P30307; -.
DR STRING; 9606.ENSP00000321656; -.
DR BindingDB; P30307; -.
DR ChEMBL; CHEMBL2378; -.
DR DrugCentral; P30307; -.
DR DEPOD; CDC25C; -.
DR iPTMnet; P30307; -.
DR PhosphoSitePlus; P30307; -.
DR BioMuta; CDC25C; -.
DR DMDM; 116242631; -.
DR EPD; P30307; -.
DR jPOST; P30307; -.
DR MassIVE; P30307; -.
DR MaxQB; P30307; -.
DR PaxDb; P30307; -.
DR PeptideAtlas; P30307; -.
DR PRIDE; P30307; -.
DR ProteomicsDB; 54658; -. [P30307-1]
DR ProteomicsDB; 54659; -. [P30307-2]
DR ProteomicsDB; 54660; -. [P30307-3]
DR ProteomicsDB; 54661; -. [P30307-4]
DR Antibodypedia; 3534; 1127 antibodies from 44 providers.
DR CPTC; P30307; 1 antibody.
DR DNASU; 995; -.
DR Ensembl; ENST00000323760.11; ENSP00000321656.6; ENSG00000158402.21. [P30307-1]
DR Ensembl; ENST00000415130.6; ENSP00000392631.2; ENSG00000158402.21. [P30307-4]
DR Ensembl; ENST00000513970.5; ENSP00000424795.1; ENSG00000158402.21. [P30307-1]
DR Ensembl; ENST00000514555.5; ENSP00000425470.1; ENSG00000158402.21. [P30307-2]
DR GeneID; 995; -.
DR KEGG; hsa:995; -.
DR MANE-Select; ENST00000323760.11; ENSP00000321656.6; NM_001790.5; NP_001781.2.
DR UCSC; uc003lcp.3; human. [P30307-1]
DR CTD; 995; -.
DR DisGeNET; 995; -.
DR GeneCards; CDC25C; -.
DR HGNC; HGNC:1727; CDC25C.
DR HPA; ENSG00000158402; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MIM; 157680; gene.
DR neXtProt; NX_P30307; -.
DR OpenTargets; ENSG00000158402; -.
DR PharmGKB; PA100; -.
DR VEuPathDB; HostDB:ENSG00000158402; -.
DR eggNOG; KOG3772; Eukaryota.
DR GeneTree; ENSGT00940000161460; -.
DR HOGENOM; CLU_014464_4_0_1; -.
DR InParanoid; P30307; -.
DR OMA; MHHQDHQ; -.
DR OrthoDB; 1423329at2759; -.
DR PhylomeDB; P30307; -.
DR TreeFam; TF101056; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P30307; -.
DR Reactome; R-HSA-156711; Polo-like kinase mediated events.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
DR SignaLink; P30307; -.
DR SIGNOR; P30307; -.
DR BioGRID-ORCS; 995; 17 hits in 1094 CRISPR screens.
DR ChiTaRS; CDC25C; human.
DR EvolutionaryTrace; P30307; -.
DR GeneWiki; CDC25C; -.
DR GenomeRNAi; 995; -.
DR Pharos; P30307; Tchem.
DR PRO; PR:P30307; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P30307; protein.
DR Bgee; ENSG00000158402; Expressed in ventricular zone and 118 other tissues.
DR ExpressionAtlas; P30307; baseline and differential.
DR Genevisible; P30307; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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:0050699; F:WW domain binding; IPI:BHF-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; TAS:ProtInc.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IGI: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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd01530; Cdc25; 1.
DR DisProt; DP02126; -.
DR Gene3D; 3.40.250.10; -; 1.
DR IDEAL; IID00198; -.
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; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Host-virus interaction; Hydrolase; Mitosis; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..473
FT /note="M-phase inducer phosphatase 3"
FT /id="PRO_0000198647"
FT DOMAIN 321..428
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..379
FT /note="HIV-1 Vpr binding site"
FT ACT_SITE 377
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:8119945,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231"
FT MOD_RES 67
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:8119945,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 122
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000305|PubMed:8119945"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12595692"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12595692"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8119945,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 191
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000269|PubMed:14968113"
FT MOD_RES 198
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000269|PubMed:14968113"
FT MOD_RES 214
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000305|PubMed:8119945"
FT MOD_RES 216
FT /note="Phosphoserine; by CHEK1, CHEK2, BRSK1 and MAPK14"
FT /evidence="ECO:0000269|PubMed:11333986,
FT ECO:0000269|PubMed:15150265, ECO:0000269|PubMed:15629715,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 66..123
FT /note="GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQH
FT LMKCSP -> SPGFFRTSGSAFSWD (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11078813,
FT ECO:0000303|PubMed:11139144"
FT /id="VSP_000863"
FT VAR_SEQ 124..153
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11078813,
FT ECO:0000303|PubMed:11139144"
FT /id="VSP_000864"
FT VARIANT 14
FT /note="S -> N (in dbSNP:rs11567959)"
FT /id="VAR_027922"
FT VARIANT 70
FT /note="R -> C (in dbSNP:rs3734166)"
FT /evidence="ECO:0000269|PubMed:11139144,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2195549"
FT /id="VAR_027923"
FT VARIANT 78
FT /note="S -> N (in dbSNP:rs11567962)"
FT /id="VAR_027924"
FT VARIANT 297
FT /note="G -> R (in dbSNP:rs11567997)"
FT /id="VAR_020146"
FT MUTAGEN 129
FT /note="S->V: Loss of phosphorylation. Severely impairs
FT PLK1-binding."
FT /evidence="ECO:0000269|PubMed:12595692"
FT MUTAGEN 130
FT /note="T->A: Loss of phosphorylation. Severely impairs
FT PLK1-binding."
FT /evidence="ECO:0000269|PubMed:12595692"
FT MUTAGEN 191
FT /note="S->A: Facilitates nuclear exclusion."
FT /evidence="ECO:0000269|PubMed:14968113"
FT MUTAGEN 191
FT /note="S->D: Mimicks phosphorylation state, leading to
FT enhanced accumulation in the nucleus."
FT /evidence="ECO:0000269|PubMed:14968113"
FT MUTAGEN 352
FT /note="E->K: Partial loss of HIV-1 Vpr binding."
FT /evidence="ECO:0000269|PubMed:14972559"
FT MUTAGEN 359
FT /note="K->E: No effect on HIV-1 Vpr binding."
FT /evidence="ECO:0000269|PubMed:14972559"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3BZI"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:3OP3"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:3OP3"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:3OP3"
FT TURN 315..321
FT /evidence="ECO:0007829|PDB:3OP3"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:3OP3"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:3OP3"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:3OP3"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:3OP3"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:3OP3"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:3OP3"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:3OP3"
FT HELIX 415..419
FT /evidence="ECO:0007829|PDB:3OP3"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:3OP3"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:3OP3"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:3OP3"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:3OP3"
FT MOD_RES P30307-3:61
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES P30307-4:61
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 53365 MW; 0658A1F1B9B8996A CRC64;
MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV GKFLGDSANL
SILSGGTPKR CLDLSNLSSG EITATQLTTS ADLDETGHLD SSGLQEVHLA GMNHDQHLMK
CSPAQLLCST PNGLDRGHRK RDAMCSSSAN KENDNGNLVD SEMKYLGSPI TTVPKLDKNP
NLGEDQAEEI SDELMEFSLK DQEAKVSRSG LYRSPSMPEN LNRPRLKQVE KFKDNTIPDK
VKKKYFSGQG KLRKGLCLKK TVSLCDITIT QMLEEDSNQG HLIGDFSKVC ALPTVSGKHQ
DLKYVNPETV AALLSGKFQG LIEKFYVIDC RYPYEYLGGH IQGALNLYSQ EELFNFFLKK
PIVPLDTQKR IIIVFHCEFS SERGPRMCRC LREEDRSLNQ YPALYYPELY ILKGGYRDFF
PEYMELCEPQ SYCPMHHQDH KTELLRCRSQ SKVQEGERQL REQIALLVKD MSP
