ID MPIP2_RAT Reviewed; 574 AA. AC P48966; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 146. 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; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=NRK49F; RX PubMed=8156993; DOI=10.1002/j.1460-2075.1994.tb06417.x; RA Jinno S., Suto K., Nagata A., Igarashi M., Kanaoka Y., Nojima H., RA Okayama H.; RT "Cdc25A is a novel phosphatase functioning early in the cell cycle."; RL EMBO J. 13:1549-1556(1994). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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 -!- PTM: Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which CC inhibits the activity of this protein. Phosphorylation at Ser-349 by CC AURKA might locally participate in the control of the onset of mitosis. CC Phosphorylation by MELK at Ser-166 promotes localization to the CC centrosome and the spindle poles during mitosis. Phosphorylation at CC Ser-319 and Ser-370 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; D16237; BAA03762.1; -; mRNA. DR RefSeq; NP_598256.1; NM_133572.1. DR AlphaFoldDB; P48966; -. DR SMR; P48966; -. DR BioGRID; 251111; 2. DR STRING; 10116.ENSRNOP00000051129; -. DR iPTMnet; P48966; -. DR PhosphoSitePlus; P48966; -. DR PaxDb; 10116-ENSRNOP00000051129; -. DR GeneID; 171103; -. DR KEGG; rno:171103; -. DR AGR; RGD:621500; -. DR CTD; 994; -. DR RGD; 621500; Cdc25b. DR eggNOG; KOG3772; Eukaryota. DR InParanoid; P48966; -. DR OrthoDB; 12481at2759; -. DR PhylomeDB; P48966; -. DR Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition. DR Reactome; R-RNO-69656; Cyclin A:Cdk2-associated events at S phase entry. DR PRO; PR:P48966; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. 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:RGD. 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; ISO:RGD. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0001556; P:oocyte maturation; ISO:RGD. DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:RGD. 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:RGD. 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. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Hydrolase; Mitosis; KW Phosphoprotein; Protein phosphatase; Reference proteome. FT CHAIN 1..574 FT /note="M-phase inducer phosphatase 2" FT /id="PRO_0000198646" FT DOMAIN 425..532 FT /note="Rhodanese" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173" FT REGION 31..51 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 90..110 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 339..359 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 481 FT /evidence="ECO:0000250|UniProtKB:P30304" FT MOD_RES 42 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 166 FT /note="Phosphoserine; by MELK" FT /evidence="ECO:0000250|UniProtKB:P30305" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30305" FT MOD_RES 319 FT /note="Phosphoserine; by MAPKAPK2 and MELK" FT /evidence="ECO:0000250|UniProtKB:P30305" FT MOD_RES 319 FT /note="Phosphoserine; by MELK and MAPK14" FT /evidence="ECO:0000250|UniProtKB:P30305" FT MOD_RES 349 FT /note="Phosphoserine; by AURKA" FT /evidence="ECO:0000250|UniProtKB:P30305" FT MOD_RES 370 FT /note="Phosphoserine; by BRSK1 and MAPK14" FT /evidence="ECO:0000250|UniProtKB:P30305" FT MOD_RES 557 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30305" SQ SEQUENCE 574 AA; 64287 MW; 9367CE203B15FAAD CRC64; MEVPPQKSAP GSALSTARVL GGIQRPRHLS GFGFGSDGLL GSPERAASSS PVTTLTQTMY NLAGLGSETP KTQVGSLSFQ NRLTDLSLSR RTSECSLSSE SSESSDAGLC MDSPSPMDPQ TAERTFEQAI QAASRVIQKM QFTIKASVFA SEAAGHSPVL QNITNSQALD SWEKDEAGYR AASSPGEDKE NDGYIFKMPQ KLPHSSSARA LAEWASRREA FTQRPSSAPD LMCLTTDGKM DVEEASPVAQ SSSLTPVERA CEEDDGFVDI LESDLKDDDM VPAGMENLIS APLVKKLDKE EEQDLIMFSK CQRLFRSPSM PCSVIRPILK RLERPHDRDV PVLSKRRKSG TPLEEQQLEE PKARVFRSKS LCHEIESILD SDHRGLIGDY SKAFLLQTVD GKHQDLKYIS PETMVALLTG KFSNIVEKFV IVDCRYPYEY EGGHIKNAVN LPLEPDAETF LLKHPITPCN LDKRIILIFH CEFSSERGPR MCRFIRERDR AANDYPSLYY PEMYILKGGY KEFFPQHPNF CEPQDYRPMN HAAFRDELRN FRLKTRSWAG ERSTTQLCSR LQDQ //