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M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B)

 MPIP2_HUMAN             Reviewed;         580 AA.
P30305; D3DVY1; D3DVY2; D3DVY3; D3DVY4; O43551; Q13971; Q5JX77;
Q6RSS1; Q9BRA6;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
27-MAY-2002, sequence version 2.
12-SEP-2018, entry version 193.
RecName: Full=M-phase inducer phosphatase 2;
EC=3.1.3.48;
AltName: Full=Dual specificity phosphatase Cdc25B;
Name=CDC25B; Synonyms=CDC25HU2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1836978; DOI=10.1016/0092-8674(91)90294-9;
Galaktionov K.I., Beach D.;
"Specific activation of cdc25 tyrosine phosphatases by B-type cyclins:
evidence for multiple roles of mitotic cyclins.";
Cell 67:1181-1194(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1662986;
Nagata A., Igarashi M., Jinno S., Suto K., Okayama H.;
"An additional homolog of the fission yeast cdc25+ gene occurs in
humans and is highly expressed in some cancer cells.";
New Biol. 3:959-968(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3).
PubMed=9188863; DOI=10.1038/sj.onc.1201063;
Baldin V., Cans C., Superti-Furga G., Docommun B.;
"Alternative splicing of the human CDC25B tyrosine phosphatase.
Possible implications for growth control?";
Oncogene 14:2485-2495(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-548.
NIEHS SNPs program;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-352 (ISOFORMS 2 AND 3).
McCormack A.K., DeSouza C.C.P.C., Tonks I.D., Clark J.M.,
Forrest A.R.R., Hayward N.K., Ellem K.A.O., Gabrielli B.G.;
"Alternative splicing of cdc25B.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[9]
PHOSPHORYLATION AT SER-323 AND SER-375, AND INTERACTION WITH MAPK14
AND 14-3-3 PROTEINS.
PubMed=11333986; DOI=10.1038/35075107;
Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V.,
Potapova O., Appella E., Fornace A.J. Jr.;
"Initiation of a G2/M checkpoint after ultraviolet radiation requires
p38 kinase.";
Nature 411:102-107(2001).
[10]
PHOSPHORYLATION AT SER-323.
PubMed=12400006; DOI=10.1038/sj.onc.1205870;
Davezac N., Baldin V., Blot J., Ducommun B., Tassan J.P.;
"Human pEg3 kinase associates with and phosphorylates CDC25B
phosphatase: a potential role for pEg3 in cell cycle regulation.";
Oncogene 21:7630-7641(2002).
[11]
PHOSPHORYLATION AT SER-375.
TISSUE=Testis;
PubMed=15150265; DOI=10.1074/jbc.M404728200;
Lu R., Niida H., Nakanishi M.;
"Human SAD1 kinase is involved in UV-induced DNA damage checkpoint
function.";
J. Biol. Chem. 279:31164-31170(2004).
[12]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-353 BY AURKA.
PubMed=15128871; DOI=10.1242/jcs.01108;
Dutertre S., Cazales M., Quaranta M., Froment C., Trabut V.,
Dozier C., Mirey G., Bouche J.P., Theis-Febvre N., Schmitt E.,
Monsarrat B., Prigent C., Ducommun B.;
"Phosphorylation of CDC25B by Aurora-A at the centrosome contributes
to the G2-M transition.";
J. Cell Sci. 117:2523-2531(2004).
[13]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY CHEK1.
PubMed=15311285; DOI=10.1038/ncb1165;
Kraemer A., Mailand N., Lukas C., Syljuaesen R.G., Wilkinson C.J.,
Nigg E.A., Bartek J., Lukas J.;
"Centrosome-associated Chk1 prevents premature activation of cyclin-B-
Cdk1 kinase.";
Nat. Cell Biol. 6:884-891(2004).
[14]
PHOSPHORYLATION AT SER-169, AND SUBCELLULAR LOCATION.
PubMed=15908796; DOI=10.4161/cc.4.6.1716;
Mirey G., Chartrain I., Froment C., Quaranta M., Bouche J.P.,
Monsarrat B., Tassan J.P., Ducommun B.;
"CDC25B phosphorylated by pEg3 localizes to the centrosome and the
spindle poles at mitosis.";
Cell Cycle 4:806-811(2005).
[15]
PHOSPHORYLATION AT SER-323 BY MAPKAPK2.
PubMed=15629715; DOI=10.1016/j.molcel.2004.11.021;
Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., Yaffe M.B.;
"MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the
G2/M transition and S phase progression in response to UV
irradiation.";
Mol. Cell 17:37-48(2005).
[16]
FUNCTION, AND PHOSPHORYLATION.
PubMed=17332740; DOI=10.1038/sj.emboj.7601637;
Schmidt A., Durgan J., Magalhaes A., Hall A.;
"Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit
from cytokinesis.";
EMBO J. 26:1624-1636(2007).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; SER-323; SER-353;
SER-375; SER-470 AND SER-563, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 370-580.
PubMed=10543950; DOI=10.1006/jmbi.1999.3168;
Reynolds R.A., Yem A.W., Wolfe C.L., Deibel M.R. Jr., Chidester C.G.,
Watenpaugh K.D.;
"Crystal structure of the catalytic subunit of Cdc25B required for
G2/M phase transition of the cell cycle.";
J. Mol. Biol. 293:559-568(1999).
-!- FUNCTION: Tyrosine protein phosphatase which functions as a
dosage-dependent inducer of mitotic progression. Required for G2/M
phases of the cell cycle progression and abscission during
cytokinesis in a ECT2-dependent manner. Directly dephosphorylates
CDK1 and stimulates its kinase activity. The three isoforms seem
to have a different level of activity.
{ECO:0000269|PubMed:17332740}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate.
-!- ACTIVITY REGULATION: Stimulated by B-type cyclins.
-!- SUBUNIT: Interacts with MAPK14 and 14-3-3 proteins.
{ECO:0000269|PubMed:11333986}.
-!- INTERACTION:
P31946:YWHAB; NbExp=5; IntAct=EBI-1051746, EBI-359815;
Q04917:YWHAH; NbExp=4; IntAct=EBI-1051746, EBI-306940;
P63104:YWHAZ; NbExp=5; IntAct=EBI-1051746, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:15128871,
ECO:0000269|PubMed:15311285, ECO:0000269|PubMed:15908796}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:15908796}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=3; Synonyms=CDC25B3;
IsoId=P30305-1; Sequence=Displayed;
Name=1; Synonyms=CDC25B1;
IsoId=P30305-2; Sequence=VSP_000861;
Name=2; Synonyms=CDC25B2;
IsoId=P30305-3; Sequence=VSP_000862;
Name=4;
IsoId=P30305-4; Sequence=VSP_000861, VSP_012587;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1,
which inhibits the activity of this protein. Phosphorylation at
Ser-353 by AURKA might locally participate in the control of the
onset of mitosis. Phosphorylation by MELK at Ser-169 promotes
localization to the centrosome and the spindle poles during
mitosis. Phosphorylation at Ser-323 and Ser-375 by MAPK14 is
required for binding to 14-3-3 proteins.
{ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:12400006,
ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15150265,
ECO:0000269|PubMed:15311285, ECO:0000269|PubMed:15629715,
ECO:0000269|PubMed:15908796, ECO:0000269|PubMed:17332740}.
-!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc25b/";
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EMBL; M81934; AAA58416.1; -; mRNA.
EMBL; S78187; AAB21139.1; -; mRNA.
EMBL; X96436; CAA65303.1; -; Genomic_DNA.
EMBL; Z68092; CAA92108.1; -; mRNA.
EMBL; AY494082; AAR26469.1; -; Genomic_DNA.
EMBL; AL109804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471133; EAX10491.1; -; Genomic_DNA.
EMBL; CH471133; EAX10492.1; -; Genomic_DNA.
EMBL; CH471133; EAX10493.1; -; Genomic_DNA.
EMBL; CH471133; EAX10494.1; -; Genomic_DNA.
EMBL; CH471133; EAX10496.1; -; Genomic_DNA.
EMBL; CH471133; EAX10497.1; -; Genomic_DNA.
EMBL; CH471133; EAX10498.1; -; Genomic_DNA.
EMBL; CH471133; EAX10499.1; -; Genomic_DNA.
EMBL; BC006395; AAH06395.1; -; mRNA.
EMBL; BC009953; AAH09953.1; -; mRNA.
EMBL; BC051711; AAH51711.1; -; mRNA.
EMBL; AF036233; AAB94622.1; -; Genomic_DNA.
EMBL; AF036233; AAB94624.1; -; Genomic_DNA.
CCDS; CCDS13065.1; -. [P30305-2]
CCDS; CCDS13066.1; -. [P30305-3]
CCDS; CCDS13067.1; -. [P30305-1]
PIR; B41648; B41648.
RefSeq; NP_001274448.1; NM_001287519.1.
RefSeq; NP_001274453.1; NM_001287524.1.
RefSeq; NP_004349.1; NM_004358.4. [P30305-2]
RefSeq; NP_068658.1; NM_021872.3. [P30305-3]
RefSeq; NP_068659.1; NM_021873.3. [P30305-1]
UniGene; Hs.153752; -.
PDB; 1CWR; X-ray; 2.10 A; A=370-580.
PDB; 1CWS; X-ray; 2.00 A; A=370-580.
PDB; 1CWT; X-ray; 2.30 A; A=388-565.
PDB; 1QB0; X-ray; 1.91 A; A=370-580.
PDB; 1YM9; X-ray; 2.00 A; A=391-564.
PDB; 1YMD; X-ray; 1.70 A; A=391-564.
PDB; 1YMK; X-ray; 1.70 A; A=391-564.
PDB; 1YML; X-ray; 1.70 A; A=391-564.
PDB; 1YS0; X-ray; 2.00 A; A=391-564.
PDB; 2A2K; X-ray; 1.52 A; A=391-564.
PDB; 2IFD; X-ray; 2.00 A; A=391-564.
PDB; 2IFV; X-ray; 1.60 A; A=391-564.
PDB; 2UZQ; X-ray; 2.38 A; A/B/C/D/E/F=391-580.
PDB; 3FQT; X-ray; 1.80 A; C=38-46.
PDB; 3FQU; X-ray; 1.80 A; C=38-46.
PDB; 4WH7; X-ray; 1.62 A; A=386-565.
PDB; 4WH9; X-ray; 1.50 A; A=386-565.
PDBsum; 1CWR; -.
PDBsum; 1CWS; -.
PDBsum; 1CWT; -.
PDBsum; 1QB0; -.
PDBsum; 1YM9; -.
PDBsum; 1YMD; -.
PDBsum; 1YMK; -.
PDBsum; 1YML; -.
PDBsum; 1YS0; -.
PDBsum; 2A2K; -.
PDBsum; 2IFD; -.
PDBsum; 2IFV; -.
PDBsum; 2UZQ; -.
PDBsum; 3FQT; -.
PDBsum; 3FQU; -.
PDBsum; 4WH7; -.
PDBsum; 4WH9; -.
ProteinModelPortal; P30305; -.
SMR; P30305; -.
BioGrid; 107429; 100.
DIP; DIP-323N; -.
ELM; P30305; -.
IntAct; P30305; 16.
MINT; P30305; -.
STRING; 9606.ENSP00000245960; -.
BindingDB; P30305; -.
ChEMBL; CHEMBL4804; -.
DrugBank; DB03661; Cysteinesulfonic Acid.
DEPOD; P30305; -.
iPTMnet; P30305; -.
PhosphoSitePlus; P30305; -.
DMDM; 21264471; -.
EPD; P30305; -.
MaxQB; P30305; -.
PaxDb; P30305; -.
PeptideAtlas; P30305; -.
PRIDE; P30305; -.
ProteomicsDB; 54654; -.
ProteomicsDB; 54655; -. [P30305-2]
ProteomicsDB; 54656; -. [P30305-3]
ProteomicsDB; 54657; -. [P30305-4]
DNASU; 994; -.
Ensembl; ENST00000245960; ENSP00000245960; ENSG00000101224. [P30305-1]
Ensembl; ENST00000340833; ENSP00000339170; ENSG00000101224. [P30305-3]
Ensembl; ENST00000439880; ENSP00000405972; ENSG00000101224. [P30305-2]
GeneID; 994; -.
KEGG; hsa:994; -.
UCSC; uc002wjn.5; human. [P30305-1]
CTD; 994; -.
DisGeNET; 994; -.
EuPathDB; HostDB:ENSG00000101224.17; -.
GeneCards; CDC25B; -.
HGNC; HGNC:1726; CDC25B.
HPA; HPA038892; -.
HPA; HPA038893; -.
HPA; HPA075215; -.
MIM; 116949; gene.
neXtProt; NX_P30305; -.
OpenTargets; ENSG00000101224; -.
PharmGKB; PA26260; -.
eggNOG; KOG3772; Eukaryota.
eggNOG; COG5105; LUCA.
GeneTree; ENSGT00390000018747; -.
HOVERGEN; HBG052501; -.
InParanoid; P30305; -.
KO; K05866; -.
OMA; THALAEW; -.
OrthoDB; EOG091G0H0D; -.
PhylomeDB; P30305; -.
TreeFam; TF101056; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
SIGNOR; P30305; -.
ChiTaRS; CDC25B; human.
EvolutionaryTrace; P30305; -.
GeneWiki; CDC25B; -.
GenomeRNAi; 994; -.
PRO; PR:P30305; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101224; Expressed in 220 organ(s), highest expression level in right hemisphere of cerebellum.
CleanEx; HS_CDC25B; -.
ExpressionAtlas; P30305; baseline and differential.
Genevisible; P30305; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:Reactome.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007144; P:female meiosis I; IEA:Ensembl.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; TAS:UniProtKB.
GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
CDD; cd01530; Cdc25; 1.
Gene3D; 3.40.250.10; -; 1.
InterPro; IPR000751; MPI_Phosphatase.
InterPro; IPR001763; Rhodanese-like_dom.
InterPro; IPR036873; Rhodanese-like_dom_sf.
Pfam; PF06617; M-inducer_phosp; 1.
Pfam; PF00581; Rhodanese; 1.
PRINTS; PR00716; MPIPHPHTASE.
SMART; SM00450; RHOD; 1.
SUPFAM; SSF52821; SSF52821; 1.
PROSITE; PS50206; RHODANESE_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Mitosis;
Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome.
CHAIN 1 580 M-phase inducer phosphatase 2.
/FTId=PRO_0000198644.
DOMAIN 431 538 Rhodanese. {ECO:0000255|PROSITE-
ProRule:PRU00173}.
ACT_SITE 487 487
MOD_RES 42 42 Phosphoserine.
{ECO:0000250|UniProtKB:P48966}.
MOD_RES 169 169 Phosphoserine; by MELK.
{ECO:0000269|PubMed:15908796}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 323 323 Phosphoserine; by MELK and MAPK14.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11333986,
ECO:0000269|PubMed:12400006,
ECO:0000269|PubMed:15629715}.
MOD_RES 353 353 Phosphoserine; by AURKA.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15128871}.
MOD_RES 375 375 Phosphoserine; by BRSK1 and MAPK14.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11333986,
ECO:0000269|PubMed:15150265}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 563 563 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 68 81 Missing (in isoform 1 and isoform 4).
{ECO:0000303|PubMed:1662986,
ECO:0000303|PubMed:1836978}.
/FTId=VSP_000861.
VAR_SEQ 154 194 Missing (in isoform 2).
{ECO:0000303|PubMed:9188863}.
/FTId=VSP_000862.
VAR_SEQ 194 194 N -> NVRFWKAGVGALREEEGACWGGSLACEDPPLPSWLQ
(in isoform 4). {ECO:0000305}.
/FTId=VSP_012587.
VARIANT 548 548 E -> K (in dbSNP:rs11570019).
{ECO:0000269|Ref.4}.
/FTId=VAR_020933.
CONFLICT 575 575 S -> D (in Ref. 2; AAB21139).
{ECO:0000305}.
STRAND 396 399 {ECO:0000244|PDB:4WH9}.
HELIX 417 424 {ECO:0000244|PDB:4WH9}.
TURN 425 431 {ECO:0000244|PDB:4WH9}.
STRAND 432 439 {ECO:0000244|PDB:4WH9}.
HELIX 443 447 {ECO:0000244|PDB:4WH9}.
HELIX 460 468 {ECO:0000244|PDB:4WH9}.
TURN 469 471 {ECO:0000244|PDB:4WH9}.
STRAND 479 486 {ECO:0000244|PDB:4WH9}.
STRAND 488 492 {ECO:0000244|PDB:4WH9}.
HELIX 493 508 {ECO:0000244|PDB:4WH9}.
STRAND 519 522 {ECO:0000244|PDB:4WH9}.
HELIX 525 532 {ECO:0000244|PDB:4WH9}.
HELIX 534 536 {ECO:0000244|PDB:4WH9}.
STRAND 537 540 {ECO:0000244|PDB:4WH9}.
HELIX 548 550 {ECO:0000244|PDB:2A2K}.
HELIX 551 558 {ECO:0000244|PDB:4WH9}.
SEQUENCE 580 AA; 64987 MW; EDE24B0E84AC1BE3 CRC64;
MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS PVTTLTQTMH
DLAGLGSETP KSQVGTLLFR SRSRLTHLSL SRRASESSLS SESSESSDAG LCMDSPSPMD
PHMAEQTFEQ AIQAASRIIR NEQFAIRRFQ SMPVRLLGHS PVLRNITNSQ APDGRRKSEA
GSGAASSSGE DKENDGFVFK MPWKPTHPSS THALAEWASR REAFAQRPSS APDLMCLSPD
RKMEVEELSP LALGRFSLTP AEGDTEEDDG FVDILESDLK DDDAVPPGME SLISAPLVKT
LEKEEEKDLV MYSKCQRLFR SPSMPCSVIR PILKRLERPQ DRDTPVQNKR RRSVTPPEEQ
QEAEEPKARV LRSKSLCHDE IENLLDSDHR ELIGDYSKAF LLQTVDGKHQ DLKYISPETM
VALLTGKFSN IVDKFVIVDC RYPYEYEGGH IKTAVNLPLE RDAESFLLKS PIAPCSLDKR
VILIFHCEFS SERGPRMCRF IRERDRAVND YPSLYYPEMY ILKGGYKEFF PQHPNFCEPQ
DYRPMNHEAF KDELKTFRLK TRSWAGERSR RELCSRLQDQ


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