MPIP_YEAST
ID MPIP_YEAST Reviewed; 554 AA.
AC P23748; D6VZL1;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=M-phase inducer phosphatase;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:P30303};
DE AltName: Full=Mitosis initiation protein MIH1;
DE AltName: Full=Mitotic inducer homolog;
GN Name=MIH1; OrderedLocusNames=YMR036C {ECO:0000312|SGD:S000004639};
GN ORFNames=YM9532.01C, YM9973.10C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2649252; DOI=10.1016/0092-8674(89)90967-7;
RA Russell P., Moreno S., Reed S.I.;
RT "Conservation of mitotic controls in fission and budding yeasts.";
RL Cell 57:295-303(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Terminates the cell cycle delay. Reverses the CDC28
CC phosphorylation catalyzed by SWE1.
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:P30303};
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; J04846; AAA57223.1; -; Genomic_DNA.
DR EMBL; Z48502; CAA88402.1; -; Genomic_DNA.
DR EMBL; Z49213; CAA89152.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09935.1; -; Genomic_DNA.
DR PIR; A32386; A32386.
DR RefSeq; NP_013750.1; NM_001182533.1.
DR AlphaFoldDB; P23748; -.
DR SMR; P23748; -.
DR BioGRID; 35208; 161.
DR DIP; DIP-2713N; -.
DR IntAct; P23748; 21.
DR MINT; P23748; -.
DR STRING; 4932.YMR036C; -.
DR iPTMnet; P23748; -.
DR PaxDb; P23748; -.
DR PRIDE; P23748; -.
DR EnsemblFungi; YMR036C_mRNA; YMR036C; YMR036C.
DR GeneID; 855052; -.
DR KEGG; sce:YMR036C; -.
DR SGD; S000004639; MIH1.
DR VEuPathDB; FungiDB:YMR036C; -.
DR eggNOG; KOG3772; Eukaryota.
DR GeneTree; ENSGT00940000166659; -.
DR HOGENOM; CLU_036651_0_0_1; -.
DR InParanoid; P23748; -.
DR OMA; GTEDECA; -.
DR BioCyc; YEAST:G3O-32741-MON; -.
DR Reactome; R-SCE-156711; Polo-like kinase mediated events.
DR Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SCE-5625740; RHO GTPases activate PKNs.
DR Reactome; R-SCE-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-SCE-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-SCE-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SCE-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-SCE-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR PRO; PR:P23748; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P23748; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
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; IMP:SGD.
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; 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; Hydrolase; Mitosis; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..554
FT /note="M-phase inducer phosphatase"
FT /id="PRO_0000198662"
FT DOMAIN 261..373
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 72..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /evidence="ECO:0000250"
FT CONFLICT 238..239
FT /note="ND -> MT (in Ref. 1; AAA57223)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..248
FT /note="FPRISPET -> SLEFLQKR (in Ref. 1; AAA57223)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..367
FT /note="FDN -> LT (in Ref. 1; AAA57223)"
FT /evidence="ECO:0000305"
FT CONFLICT 475..554
FT /note="ILSKSSMSSNSNLSTSHMLLMDGLDTPSYFSFEDERGNHQQVSGDEEQDGDF
FT TFVGSDREDLPRPARRSLFPSLETEDKK -> S (in Ref. 1; AAA57223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 63358 MW; DBD85D02CF48CA6F CRC64;
MNNIFHGTED ECANEDVLSF QKISLKSPFG KKKNIFRNVQ TFFKSKSKHS NVDDDLINKE
NLAFDKSPLL TNHRSKEIDG PSPNIKQLGH RDELDENENE NDDIVLSMHF ASQTLQSPTR
NSSRRSLTNN RDNDLLSRIK YPGSPQRSSS FSRSRSLSRK PSMNSSSNSS RRVQRQDGKI
PRSSRKSSQK FSNITQNTLN FTSASSSPLA PNSVGVKCFE SCLAKTQIPY YYDDRNSNDF
FPRISPETLK NILQNNMCES FYNSCRIIDC RFEYEYTGGH IINSVNIHSR DELEYEFIHK
VLHSDTSNNN TLPTLLIIHC EFSSHRGPSL ASHLRNCDRI INQDHYPKLF YPDILILDGG
YKAVFDNFPE LCYPRQYVGM NSQENLLNCE QEMDKFRRES KRFATKNNSF RKLASPSNPN
FFYRDSHQSS TTMASSALSF RFEPPPKLSL NHRRVSSGSS LNSSESTGDE NFFPILSKSS
MSSNSNLSTS HMLLMDGLDT PSYFSFEDER GNHQQVSGDE EQDGDFTFVG SDREDLPRPA
RRSLFPSLET EDKK
