Human protein: IPI00216430 * 54551 Da * CDC25A Isoform 2 of M-phase inducer phosphatase 1 - Liebel-Lab @ KIT
Bioinformatic Harvester logo 

>CDC25A Isoform 2 of M-phase inducer phosphatase 1 - Length: 484 AS 
MELGPEPPHRRRLLFACSPPPASQPVVKALFGASAAGGLSPVTNLTVTMDQLQGLGSDYEQPLEVKNNSNLQRMGSSEST
DSGFCLDSPGPLDSKENLENPMRRIHSLPQKLLGCSPALKRSHSDSLDHDIFQLIDPDENKENLSSNERDSSEPGNFIPL
FTPQSPVTATLSDEDDGFVDLLDGENLKNEEETPSCMASLWTAPLVMRTTNLDNRCKLFDSPSLCSSSTRSVLKRPERSQ
EESPPGSTKRRKSMSGASPKESTNPEKAHETLHQSLSLASSPKGTIENILDNDPRDLIGDFSKGYLFHTVAGKHQDLKYI
SPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSERGPR
MCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPMHHEDFKEDLKKFRTKSRTWAGEKSKREMYSR
LKKL
Linkouts to other data resources: BioCompare * Entrez * PolyMeta * GeneCard * imaGenes * GenomeBrowser * Google Scholar * Mitocheck
AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
Diseaselink to OMIM


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
ACTIVATE: SMART analysis
NameBeginEndE-value
low complexity2940-
Pfam:M-inducer_phosp862891.10e-97
RHOD3264395.65e-26

These features and domains are not shown in the diagram, either because their scores are less significant than the required threshold, or because they overlap with some other source of annotation:

NameBeginEndE-valueReason
Pfam:Rhodanese3294366.10e-39overlap


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
General information
Entry name MPIP1_HUMAN
Accession number P30304, Q8IZH5, Q96IL3, Q9H2F2
Integrated 01-APR-1993, UniProtKB/Swiss-Prot.
Sequence update 19-JUL-2004, sequence version 2
Annotation update 25-NOV-2008, entry version 84
UniSave P30304, Q8IZH5, Q96IL3, Q9H2F2
UniRef100 UniRef100_P30304, UniRef100_P30304-2
UniParc UPI000006ED4E, UPI0000074110
Description and origin of the Protein
Description Recommended
Full=M-phase inducer phosphatase 1;
EC=3.1.3.48;
Synonym
Full=Dual specificity phosphatase Cdc25A;
Gene name(s) CDC25A
Organism source Homo sapiens (Human).
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
NCBI TaxID 9606
References
[1] Galaktionov,K.I., Beach,D.,
Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins.
(1991) Cell 67:1181-1194
Position NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-182.
Medline 92103683
DOI 10.1016/0092-8674(91)90294-9;
PubMed
1836978 Subscription requiredClick to get it from ScienceDirect CiteXplore
[2] Varmeh-Ziaie,S., Manfredi,J.J.,
Submitted JUL-2002 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE (ISOFORM 2).
[3] Rieder,M.J., Livingston,R.J., Braun,A.C., Montoya,M.A., Chung,M.-W., Miyamoto,K.E., Nguyen,C.P., Nguyen,D.A., Poel,C.L., Robertson,P.D., Schackwitz,W.S., Sherwood,J.K., Witrak,L.A., Nickerson,D.A.,
NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).
Submitted JUL-2002 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-88.
[4]
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
(2004) Genome Res. 14:2121-2127
Position NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Comments TISSUE=Lymph;
DOI 10.1101/gr.2596504;
PubMed
15489334 Free after 6 monthsClick to get it from www.genome.org Free after 6 monthsClick to get it from www.genome.org FreeClick to get it from www.genome.org Subscription requiredClick to get it from DOI Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[5] Wegener,S., Hampe,W., Herrmann,D., Schaller,H.C.,
Alternative splicing in the regulatory region of the human phosphatases CDC25A and CDC25C.
(2000) Eur. J. Cell Biol. 79:810-815
Position NUCLEOTIDE SEQUENCE OF 37-234 (ISOFORM 2).
Medline 21020092
DOI 10.1078/0171-9335-00115;
PubMed
11139144 Subscription requiredClick to get it from ScienceDirect CiteXplore
[6] Zhao,H., Watkins,J.L., Piwnica-Worms,H.,
Disruption of the checkpoint kinase 1/cell division cycle 25A pathway abrogates ionizing radiation-induced S and G2 checkpoints.
(2002) Proc. Natl. Acad. Sci. U.S.A. 99:14795-14800
Position PHOSPHORYLATION AT SER-124, AND MUTAGENESIS OF SER-124.
DOI 10.1073/pnas.182557299;
PubMed
12399544 Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral Free after 6 monthsClick to get it from www.pnas.org Free after 6 monthsClick to get it from www.pnas.org Free after 6 monthsClick to get it from www.pnas.org Subscription requiredClick to get it from www.pnas.org CiteXplore
[7] Soerensen,C.S., Syljuaesen,R.G., Falck,J., Schroeder,T., Roennstrand,L., Khanna,K.K., Zhou,B.-B., Bartek,J., Lukas,J.,
Chk1 regulates the S phase checkpoint by coupling the physiological turnover and ionizing radiation-induced accelerated proteolysis of Cdc25A.
(2003) Cancer Cell 3:247-258
Position PHOSPHORYLATION AT SER-124; SER-178; SER-279 AND SER-293, AND MUTAGENESIS OF SER-124; SER-178; SER-279 AND SER-293.
DOI 10.1016/S1535-6108(03)00048-5;
PubMed
12676583 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from ScienceDirect CiteXplore
[8] Jin,J., Shirogane,T., Xu,L., Nalepa,G., Qin,J., Elledge,S.J., Harper,J.W.,
SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase.
(2003) Genes Dev. 17:3062-3074
Position INTERACTION WITH BTRC; CUL1 AND FBXW11, PHOSPHODEGRON MOTIF, PHOSPHORYLATION AT SER-76 AND SER-124, UBIQUITINATION, AND MUTAGENESIS OF SER-76; SER-79; ASP-81 AND SER-82.
DOI 10.1101/gad.1157503;
PubMed
14681206 Free after 12 monthsClick to get it from www.genesdev.org Free after 12 monthsClick to get it from www.genesdev.org FreeClick to get it from www.genesdev.org Subscription requiredClick to get it from DOI Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[9] Xiao,Z., Chen,Z., Gunasekera,A.H., Sowin,T.J., Rosenberg,S.H., Fesik,S., Zhang,H.,
Chk1 mediates S and G2 arrests through Cdc25A degradation in response to DNA-damaging agents.
(2003) J. Biol. Chem. 278:21767-21773
Position PHOSPHORYLATION, AND MUTAGENESIS OF CYS-431.
DOI 10.1074/jbc.M300229200;
PubMed
12676925 Open AccessClick to get it from intl.jbc.org Open AccessClick to get it from intl.jbc.org Open AccessClick to get it from intl.jbc.org Subscription requiredClick to get it from DOI Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[10] Hassepass,I., Voit,R., Hoffmann,I.,
Phosphorylation at serine 75 is required for UV-mediated degradation of human Cdc25A phosphatase at the S-phase checkpoint.
(2003) J. Biol. Chem. 278:29824-29829
Position PHOSPHORYLATION AT SER-76; SER-124 AND SER-178, AND MUTAGENESIS OF SER-76; SER-124 AND SER-178.
DOI 10.1074/jbc.M302704200;
PubMed
12759351 Open AccessClick to get it from intl.jbc.org Open AccessClick to get it from intl.jbc.org Open AccessClick to get it from intl.jbc.org Subscription requiredClick to get it from DOI Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[11] Chen,M.-S., Ryan,C.E., Piwnica-Worms,H.,
Chk1 kinase negatively regulates mitotic function of Cdc25A phosphatase through 14-3-3 binding.
(2003) Mol. Cell. Biol. 23:7488-7497
Position INTERACTION WITH CCNB1 AND YWHAE, PHOSPHORYLATION AT SER-178 AND THR-507, AND MUTAGENESIS OF SER-178; CYS-431; THR-507; LYS-514 AND ARG-520.
DOI 10.1128/MCB.23.21.7488-7497.2003;
PubMed
14559997 Free after 4 monthsClick to get it from mcb.asm.org Free after 4 monthsClick to get it from mcb.asm.org FreeClick to get it from mcb.asm.org Subscription requiredClick to get it from asm.org Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[12] Fauman,E.B., Cogswell,J.P., Lovejoy,B., Rocque,W.J., Holmes,W., Montana,V.G., Piwnica-Worms,H., Rink,M.J., Saper,M.A.,
Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A.
(1998) Cell 93:617-625
Position X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 336-496.
Medline 98265972
DOI 10.1016/S0092-8674(00)81190-3;
PubMed
9604936 Subscription requiredClick to get it from www.cell.com Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from ScienceDirect CiteXplore
Comments
FUNCTION Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDC2 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro.
CATALYTIC ACTIVITY Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
ENZYME REGULATION Stimulated by B-type cyclins.
SUBUNIT Interacts with CCNB1/cyclin B1. Interacts with YWHAE/14- 3-3 epsilon when phosphorylated. Interacts with CUL1 specifically when CUL1 is neddylated and active. Interacts with BTRC/BTRCP1 and FBXW11/BTRCP2. Interactions with CUL1, BTRC and FBXW11 are enhanced upon DNA damage.
INTERACTION
O14757:CHEK1 NbExp=1 IntAct=EBI-747671, EBI-974488
P49137:MAPKAPK2 NbExp=1 IntAct=EBI-747671, EBI-993299
ALTERNATIVE PRODUCTS Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=CDC25A1;
IsoId=P30304-1; Sequence=Displayed;
Name=2; Synonyms=CDC25A2;
IsoId=P30304-2; Sequence=VSP_000860;
DOMAIN The phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-79 and Ser-82 appear to be essential for this interaction.
PTM Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-279, Ser-293 and Thr-507 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-279, and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-507 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser- 178, Ser-279 and Ser-293 may also promote ubiquitin-dependent proteolysis of CDC25A.
PTM Ubiquitinated. Association with the F-box proteins BTRC and FBXW11 targets the protein for ubiquitination by CUL1 and proteolysis by the ubiquitin-dependent proteasome pathway.
SIMILARITY Belongs to the MPI phosphatase family.
SIMILARITY Contains 1 rhodanese domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms Distributed under the Creative Commons Attribution-NoDerivs License
Database cross-references
EMBL
M81933; AAA58415.1; -; mRNA.
AY137580; AAN11305.1; -; mRNA.
AF527417; AAM77917.1; -; Genomic_DNA.
BC007401; AAH07401.1; -; mRNA.
BC018642; AAH18642.1; -; mRNA.
AF277722; AAG41884.1; -; mRNA.
PIR
A41648; A41648.
RefSeq
NP_001780.2; -.
NP_963861.1; -.
UniGene
Hs.437705; -.
PDB
1C25; X-ray; 2.30 A; A=337-496.
PDBsum
1C25; -.
DIP
DIP:166N; -.
IntAct
P30304; -.
PhosphoSite
P30304; -.
Ensembl
ENSG00000164045; Homo sapiens.
GeneID
993; -.
KEGG
hsa:993; -.
H-InvDB
HIX0003280; -.
HGNC
HGNC:1725; CDC25A.
HPA
CAB002674; -.
HPA005855; -.
MIM
116947; gene.
PharmGKB
PA26259; -.
HOGENOM
P30304; -.
HOVERGEN
P30304; -.
Reactome
REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_9013; Activation of Cdc25A by c-myc.
NextBio
4164; -.
ArrayExpress
P30304; -.
CleanEx
HS_CDC25A; -.
GermOnline
ENSG00000164045; Homo sapiens.
GO
GO:0005794; C:Golgi apparatus; IDA:HPA.
GO:0005654; C:nucleoplasm; EXP:Reactome.
GO:0005515; F:protein binding; IPI:IntAct.
GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0008283; P:cell proliferation; TAS:UniProtKB.
GO:0006260; P:DNA replication; EXP:Reactome.
GO:0007067; P:mitosis; IEA:UniProtKB-KW.
GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro.
GO:0000079; P:regulation of cyclin-dependent protein kina...; TAS:UniProtKB.
InterPro
IPR000751; MPI_Phosphatase.
IPR001763; Rhodanese-like.
Gene3D
G3DSA:3.40.250.10; Rhodanese-like; 1.
PANTHER
PTHR10828; MPI_Phosphatase; 1.
Pfam
PF06617; M-inducer_phosp; 1.
PF00581; Rhodanese; 1.
PRINTS
PR00716; MPIPHPHTASE.
SMART
SM00450; RHOD; 1.
PROSITE
PS50206; RHODANESE_3; 1.
Protein Existence
1: Evidence at protein level;
Keywords
3D-structure; Alternative splicing; Cell cycle; Cell division; Hydrolase; Mitosis; Phosphoprotein; Polymorphism; Protein phosphatase; Ubl conjugation;
CHAIN: 1 524, M-phase inducer phosphatase 1. /FTId=PRO_0000198641. DOMAIN: 376 482, Rhodanese. MOTIF: 74 84, Phosphodegron. ACT_SITE: 431 431, MOD_RES: 76 76, Phosphoserine; by CHK1. MOD_RES: 124 124, Phosphoserine; by CHK1 and CHK2. MOD_RES: 178 178, Phosphoserine; by CHK1. MOD_RES: 279 279, Phosphoserine; by CHK1 and CHK2. MOD_RES: 293 293, Phosphoserine; by CHK1 and CHK2. MOD_RES: 507 507, Phosphothreonine; by CHK1. VAR_SEQ: 144 183, Missing (in isoform 2). /FTId=VSP_000860. VARIANT: 88 88, S -> F (in dbSNP:rs3731499). /FTId=VAR_020932. VARIANT: 182 182, R -> G (in dbSNP:rs6771386). /FTId=VAR_023532. VARIANT: 182 182, R -> W (in dbSNP:rs6771386). /FTId=VAR_023533. MUTAGEN: 76 76, S->A: Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation. MUTAGEN: 79 79, S->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. MUTAGEN: 81 81, D->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. MUTAGEN: 82 82, S->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. MUTAGEN: 124 124, S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-178; A-279 and A-293. MUTAGEN: 178 178, S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-279 and A-293. Abrogates 14-3-3 protein binding. MUTAGEN: 279 279, S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293. MUTAGEN: 293 293, S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279. MUTAGEN: 431 431, C->S: Abolishes phosphatase activity. MUTAGEN: 507 507, T->A: Abrogates 14-3-3 protein binding; increases binding to cyclin B1. MUTAGEN: 514 514, K->L: Abrogates binding to CCNB1; when associated with L-520. MUTAGEN: 520 520, R->L: Abrogates binding to CCNB1; when associated with L-514. CONFLICT: 6 10, EPPHR -> SPAP (in Ref. 1; AAA58415). CONFLICT: 180 181, PA -> QL (in Ref. 1). STRAND: 341 344, STRAND: 377 384, STRAND: 423 430, STRAND: 432 436, STRAND: 463 466, STRAND: 481 484, HELIX: 362 369, HELIX: 388 392, HELIX: 405 411, HELIX: 437 451, HELIX: 469 477, HELIX: 478 480, TURN: 370 376, TURN: 412 414, CHAIN: 1 524, M-phase inducer phosphatase 1. /FTId=PRO_0000198641. DOMAIN: 376 482, Rhodanese. MOTIF: 74 84, Phosphodegron. ACT_SITE: 431 431, MOD_RES: 76 76, Phosphoserine; by CHK1. MOD_RES: 124 124, Phosphoserine; by CHK1 and CHK2. MOD_RES: 178 178, Phosphoserine; by CHK1. MOD_RES: 279 279, Phosphoserine; by CHK1 and CHK2. MOD_RES: 293 293, Phosphoserine; by CHK1 and CHK2. MOD_RES: 507 507, Phosphothreonine; by CHK1. VAR_SEQ: 144 183, Missing (in isoform 2). /FTId=VSP_000860. VARIANT: 88 88, S -> F (in dbSNP:rs3731499). /FTId=VAR_020932. VARIANT: 182 182, R -> G (in dbSNP:rs6771386). /FTId=VAR_023532. VARIANT: 182 182, R -> W (in dbSNP:rs6771386). /FTId=VAR_023533. MUTAGEN: 76 76, S->A: Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation. MUTAGEN: 79 79, S->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. MUTAGEN: 81 81, D->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. MUTAGEN: 82 82, S->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. MUTAGEN: 124 124, S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-178; A-279 and A-293. MUTAGEN: 178 178, S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-279 and A-293. Abrogates 14-3-3 protein binding. MUTAGEN: 279 279, S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293. MUTAGEN: 293 293, S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279. MUTAGEN: 431 431, C->S: Abolishes phosphatase activity. MUTAGEN: 507 507, T->A: Abrogates 14-3-3 protein binding; increases binding to cyclin B1. MUTAGEN: 514 514, K->L: Abrogates binding to CCNB1; when associated with L-520. MUTAGEN: 520 520, R->L: Abrogates binding to CCNB1; when associated with L-514. CONFLICT: 6 10, EPPHR -> SPAP (in Ref. 1; AAA58415). CONFLICT: 180 181, PA -> QL (in Ref. 1). STRAND: 341 344, HELIX: 362 369, TURN: 370 376, STRAND: 377 384, HELIX: 388 392, HELIX: 405 411, TURN: 412 414, STRAND: 423 430, STRAND: 432 436, HELIX: 437 451, STRAND: 463 466, HELIX: 469 477, HELIX: 478 480, STRAND: 481 484,
Key Begin End Length Description RESID
  CHAIN 1 524 524 M-phase inducer phosphatase 1. /FTId=PRO_0000198641.
  DOMAIN 376 482 107 Rhodanese.
  MOTIF 74 84 11 Phosphodegron.
  ACT_SITE 431 431 1 RESID:AA0005; RESID:AA0171; RESID:AA0269
  MOD_RES 76 76 1 Phosphoserine; by CHK1.
  MOD_RES 124 124 1 Phosphoserine; by CHK1 and CHK2.
  MOD_RES 178 178 1 Phosphoserine; by CHK1.
  MOD_RES 279 279 1 Phosphoserine; by CHK1 and CHK2.
  MOD_RES 293 293 1 Phosphoserine; by CHK1 and CHK2.
  MOD_RES 507 507 1 Phosphothreonine; by CHK1.
  VAR_SEQ 144 183 40 Missing (in isoform 2). /FTId=VSP_000860.
  VARIANT 88 88 1 S -> F (in dbSNP:rs3731499). /FTId=VAR_020932.
  VARIANT 182 182 1 R -> G (in dbSNP:rs6771386). /FTId=VAR_023532.
  VARIANT 182 182 1 R -> W (in dbSNP:rs6771386). /FTId=VAR_023533.
  MUTAGEN 76 76 1 S->A: Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation.
  MUTAGEN 79 79 1 S->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination.
  MUTAGEN 81 81 1 D->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination.
  MUTAGEN 82 82 1 S->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination.
  MUTAGEN 124 124 1 S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-178; A-279 and A-293.
  MUTAGEN 178 178 1 S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-279 and A-293. Abrogates 14-3-3 protein binding.
  MUTAGEN 279 279 1 S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293.
  MUTAGEN 293 293 1 S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279.
  MUTAGEN 431 431 1 C->S: Abolishes phosphatase activity.
  MUTAGEN 507 507 1 T->A: Abrogates 14-3-3 protein binding; increases binding to cyclin B1.
  MUTAGEN 514 514 1 K->L: Abrogates binding to CCNB1; when associated with L-520.
  MUTAGEN 520 520 1 R->L: Abrogates binding to CCNB1; when associated with L-514.
  CONFLICT 6 10 5 EPPHR -> SPAP (in Ref. 1; AAA58415).
  CONFLICT 180 181 2 PA -> QL (in Ref. 1).
  STRAND 341 344 4
  HELIX 362 369 8
  TURN 370 376 7
  STRAND 377 384 8
  HELIX 388 392 5
  HELIX 405 411 7
  TURN 412 414 3
  STRAND 423 430 8
  STRAND 432 436 5
  HELIX 437 451 15
  STRAND 463 466 4
  HELIX 469 477 9
  HELIX 478 480 3
  STRAND 481 484 4


IPI crosslinks:
SP P30304-2 IPI00216430 ENSP00000343166; REVIEWED:NP_963861; 1725,CDC25A; 993,CDC25A; UPI0000074110 Hs.437705; CCDS2761.1; GI:42490760; OTTHUMP00000164817;OTTHUMP00000171145;
IPI gene crosslinks:
3 48173674 48204805 -1 3p21 ENSG00000164045 1725,CDC25A 993,CDC25A IPI00220981;IPI00216430;IPI00794445; P30304-1;P30304-2; A8K3D9; ENSP00000303706;ENSP00000343166; REVIEWED:NP_001780;REVIEWED:NP_963861; HIT000033191; Hs.437705; CCDS2760.1;CCDS2761.1; GI:42490758;GI:42490760; OTTHUMG00000133535;OTTHUMG00000136216; OTTHUMP00000164816;OTTHUMP00000164817;OTTHUMP00000171145;OTTHUMP00000171146;OTTHUMP00000171147;