MPIP2_MOUSE
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 03-AUG-2022, entry version 171.
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=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].
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. 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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
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.
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.
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}.
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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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; P30306; -.
DR PRIDE; P30306; -.
DR ProteomicsDB; 252608; -.
DR Antibodypedia; 3625; 976 antibodies from 40 providers.
DR DNASU; 12531; -.
DR Ensembl; ENSMUST00000028804; ENSMUSP00000028804; ENSMUSG00000027330.
DR GeneID; 12531; -.
DR KEGG; mmu:12531; -.
DR UCSC; uc008mky.3; mouse.
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; 1423329at2759; -.
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; 1 hit in 75 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 185 other tissues.
DR ExpressionAtlas; P30306; baseline and differential.
DR Genevisible; P30306; MM.
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: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:0000278; P:mitotic cell cycle; ISO:MGI.
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; 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; ISO:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
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 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"
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
