ID   MPIP2_MOUSE             Reviewed;         576 AA.
AC   P30306; Q99LP3;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=M-phase inducer phosphatase 2;
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:P30305};
DE   AltName: Full=Dual specificity phosphatase Cdc25B;
GN   Name=Cdc25b; Synonyms=Cdc25m2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=1313771; DOI=10.1101/gad.6.4.578;
RA   Kakizuka A., Sebastian B., Borgmeyer U., Hermans-Borgmeyer I., Bolado J.,
RA   Hunter T., Hoekstra M.F., Evans R.M.;
RT   "A mouse cdc25 homolog is differentially and developmentally expressed.";
RL   Genes Dev. 6:578-590(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-576.
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Tyrosine protein phosphatase which functions as a dosage-
CC       dependent inducer of mitotic progression. Directly dephosphorylates
CC       CDK1 and stimulates its kinase activity. Required for G2/M phases of
CC       the cell cycle progression and abscission during cytokinesis in a ECT2-
CC       dependent manner. The three isoforms seem to have a different level of
CC       activity. {ECO:0000250|UniProtKB:P30305}.
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:0000250|UniProtKB:P30305};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC         Evidence={ECO:0000250|UniProtKB:P30305};
CC   -!- ACTIVITY REGULATION: Stimulated by B-type cyclins.
CC       {ECO:0000250|UniProtKB:P30305}.
CC   -!- SUBUNIT: Interacts with MAPK14 and 14-3-3 proteins.
CC       {ECO:0000250|UniProtKB:P30305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:P30305}. Cytoplasm,
CC       cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P30305}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in spleen, lung, heart,
CC       brain, intestine, and muscle. {ECO:0000269|PubMed:1313771}.
CC   -!- DEVELOPMENTAL STAGE: Detected at the one-cell stage followed by a
CC       decrease in signal intensity at the two-cell stage. Detectable at
CC       higher level in the four-cell stage and expressed through the eight-
CC       cell, 16-cell and morula stages. Maximal expression at the blastocyst
CC       stage. {ECO:0000269|PubMed:1313771}.
CC   -!- PTM: Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which
CC       inhibits the activity of this protein. Phosphorylation at Ser-351 by
CC       AURKA might locally participate in the control of the onset of mitosis.
CC       Phosphorylation by MELK at Ser-167 promotes localization to the
CC       centrosome and the spindle poles during mitosis. Phosphorylation at
CC       Ser-321 and Ser-372 by MAPK14 is required for binding to 14-3-3
CC       proteins (By similarity). {ECO:0000250|UniProtKB:P30305}.
CC   -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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; S93521; AAB22026.1; -; mRNA.
DR   EMBL; BC002287; AAH02287.1; -; mRNA.
DR   CCDS; CCDS16758.1; -.
DR   PIR; A42236; A42236.
DR   RefSeq; NP_075606.1; NM_023117.4.
DR   AlphaFoldDB; P30306; -.
DR   SMR; P30306; -.
DR   BioGRID; 198622; 5.
DR   IntAct; P30306; 3.
DR   MINT; P30306; -.
DR   STRING; 10090.ENSMUSP00000028804; -.
DR   BindingDB; P30306; -.
DR   ChEMBL; CHEMBL2723; -.
DR   iPTMnet; P30306; -.
DR   PhosphoSitePlus; P30306; -.
DR   EPD; P30306; -.
DR   jPOST; P30306; -.
DR   PaxDb; 10090-ENSMUSP00000028804; -.
DR   ProteomicsDB; 252608; -.
DR   Antibodypedia; 3625; 1094 antibodies from 40 providers.
DR   DNASU; 12531; -.
DR   Ensembl; ENSMUST00000028804.15; ENSMUSP00000028804.9; ENSMUSG00000027330.17.
DR   GeneID; 12531; -.
DR   KEGG; mmu:12531; -.
DR   UCSC; uc008mky.3; mouse.
DR   AGR; MGI:99701; -.
DR   CTD; 994; -.
DR   MGI; MGI:99701; Cdc25b.
DR   VEuPathDB; HostDB:ENSMUSG00000027330; -.
DR   eggNOG; KOG3772; Eukaryota.
DR   GeneTree; ENSGT00940000158524; -.
DR   InParanoid; P30306; -.
DR   OMA; MHSKCRR; -.
DR   OrthoDB; 12481at2759; -.
DR   PhylomeDB; P30306; -.
DR   TreeFam; TF101056; -.
DR   Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   BioGRID-ORCS; 12531; 2 hits in 80 CRISPR screens.
DR   ChiTaRS; Cdc25b; mouse.
DR   PRO; PR:P30306; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P30306; Protein.
DR   Bgee; ENSMUSG00000027330; Expressed in fetal liver hematopoietic progenitor cell and 188 other cell types or tissues.
DR   ExpressionAtlas; P30306; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
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; IMP:MGI.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0001556; P:oocyte maturation; IMP:MGI.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISS: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; ISO:MGI.
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; P30306; MM.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Hydrolase; Mitosis;
KW   Phosphoprotein; Protein phosphatase; Reference proteome.
FT   CHAIN           1..576
FT                   /note="M-phase inducer phosphatase 2"
FT                   /id="PRO_0000198645"
FT   DOMAIN          427..534
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          90..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        483
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48966"
FT   MOD_RES         167
FT                   /note="Phosphoserine; by MELK"
FT                   /evidence="ECO:0000250|UniProtKB:P30305"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30305"
FT   MOD_RES         321
FT                   /note="Phosphoserine; by MELK and MAPK14"
FT                   /evidence="ECO:0000250|UniProtKB:P30305"
FT   MOD_RES         351
FT                   /note="Phosphoserine; by AURKA"
FT                   /evidence="ECO:0000250|UniProtKB:P30305"
FT   MOD_RES         372
FT                   /note="Phosphoserine; by BRSK1 and MAPK14"
FT                   /evidence="ECO:0000250|UniProtKB:P30305"
FT   MOD_RES         559
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30305"
FT   CONFLICT        532
FT                   /note="F -> L (in Ref. 2; AAH02287)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   576 AA;  65490 MW;  5086B676581CD570 CRC64;
     MEVPLQKSAP GSALSPARVL GGIQRPRHLS VFEFESDGFL GSPEPTASSS PVTTLTQTMH
     NLAGLGSEPP KAQVGSLSFQ NRLADLSLSR RTSECSLSSE SSESSDAGLC MDSPSPVDPQ
     MAERTFEQAI QAASRVIQNE QFTIKRFRSL PVRLLEHSPV LQSITNSRAL DSWRKTEAGY
     RAAANSPGED KENDGYIFKM PQELPHSSSA QALAEWVSRR QAFTQRPSSA PDLMCLTTEW
     KMEVEELSPV AQSSSLTPVE RASEEDDGFV DILESDLKDD EKVPAGMENL ISAPLVKKLD
     KEEEQDLIMF SKCQRLFRSP SMPCSVIRPI LKRLERPQDR DVPVQSKRRK SVTPLEEQQL
     EEPKARVFRS KSLCHEIENI LDSDHRGLIG DYSKAFLLQT VDGKHQDLKY ISPETMVALL
     TGKFSNIVEK FVIVDCRYPY EYEGGHIKNA VNLPLERDAE TFLLQRPIMP CSLDKRIILI
     FHCEFSSERG PRMCRFIRER DRAANDYPSL YYPEMYILKG GYKEFFPQHP NFCEPQDYRP
     MNHEAFRDEL RNFRLKTRSW AGERSRRELC SRLQDQ
//