Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

M-phase inducer phosphatase 1 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25A)

 MPIP1_HUMAN             Reviewed;         524 AA.
P30304; Q8IZH5; Q96IL3; Q9H2F2;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 2.
28-MAR-2018, entry version 177.
RecName: Full=M-phase inducer phosphatase 1;
EC=3.1.3.48;
AltName: Full=Dual specificity phosphatase Cdc25A;
Name=CDC25A;
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), AND VARIANT GLY-182.
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 2).
Varmeh-Ziaie S., Manfredi J.J.;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-88.
NIEHS SNPs program;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 37-234 (ISOFORM 2).
PubMed=11139144; DOI=10.1078/0171-9335-00115;
Wegener S., Hampe W., Herrmann D., Schaller H.C.;
"Alternative splicing in the regulatory region of the human
phosphatases CDC25A and CDC25C.";
Eur. J. Cell Biol. 79:810-815(2000).
[6]
INTERACTION WITH CHEK2, PHOSPHORYLATION AT SER-124 BY CHEK2, AND
MUTAGENESIS OF SER-124.
PubMed=11298456; DOI=10.1038/35071124;
Falck J., Mailand N., Syljuaasen R.G., Bartek J., Lukas J.;
"The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant
DNA synthesis.";
Nature 410:842-847(2001).
[7]
UBIQUITINATION BY THE APC/C UBIQUITIN LIGASE COMPLEX, DOMAIN KEN BOX
MOTIF, AND MUTAGENESIS OF 141-LYS--ASN-143.
PubMed=12234927; DOI=10.1093/emboj/cdf491;
Donzelli M., Squatrito M., Ganoth D., Hershko A., Pagano M.,
Draetta G.F.;
"Dual mode of degradation of Cdc25 A phosphatase.";
EMBO J. 21:4875-4884(2002).
[8]
PHOSPHORYLATION AT SER-124, AND MUTAGENESIS OF SER-124.
PubMed=12399544; DOI=10.1073/pnas.182557299;
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.";
Proc. Natl. Acad. Sci. U.S.A. 99:14795-14800(2002).
[9]
PHOSPHORYLATION AT SER-124; SER-178; SER-279 AND SER-293, AND
MUTAGENESIS OF SER-124; SER-178; SER-279 AND SER-293.
PubMed=12676583; DOI=10.1016/S1535-6108(03)00048-5;
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.";
Cancer Cell 3:247-258(2003).
[10]
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.
PubMed=14681206; DOI=10.1101/gad.1157503;
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.";
Genes Dev. 17:3062-3074(2003).
[11]
PHOSPHORYLATION, AND MUTAGENESIS OF CYS-431.
PubMed=12676925; DOI=10.1074/jbc.M300229200;
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.";
J. Biol. Chem. 278:21767-21773(2003).
[12]
PHOSPHORYLATION AT SER-76; SER-124 AND SER-178, AND MUTAGENESIS OF
SER-76; SER-124 AND SER-178.
PubMed=12759351; DOI=10.1074/jbc.M302704200;
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.";
J. Biol. Chem. 278:29824-29829(2003).
[13]
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.
PubMed=14559997; DOI=10.1128/MCB.23.21.7488-7497.2003;
Chen M.-S., Ryan C.E., Piwnica-Worms H.;
"Chk1 kinase negatively regulates mitotic function of Cdc25A
phosphatase through 14-3-3 binding.";
Mol. Cell. Biol. 23:7488-7497(2003).
[14]
INTERACTION WITH PIM1.
PubMed=16356754; DOI=10.1016/j.biocel.2005.10.010;
Bachmann M., Kosan C., Xing P.X., Montenarh M., Hoffmann I., Moroy T.;
"The oncogenic serine/threonine kinase Pim-1 directly phosphorylates
and activates the G2/M specific phosphatase Cdc25C.";
Int. J. Biochem. Cell Biol. 38:430-443(2006).
[15]
PHOSPHORYLATION AT SER-79; SER-82 AND SER-88.
PubMed=19734889; DOI=10.1038/ncb1969;
Melixetian M., Klein D.K., Soerensen C.S., Helin K.;
"NEK11 regulates CDC25A degradation and the IR-induced G2/M
checkpoint.";
Nat. Cell Biol. 11:1247-1253(2009).
[16]
PHOSPHORYLATION AT SER-82 AND SER-88.
PubMed=20090422; DOI=10.4161/cc.9.3.10513;
Soerensen C.S., Melixetian M., Klein D.K., Helin K.;
"NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling.";
Cell Cycle 9:450-455(2010).
[17]
DEUBIQUITINATION BY USP17L2.
PubMed=20228808; DOI=10.1038/ncb2041;
Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L.,
French D.M., Dixit V.M.;
"Ubiquitin hydrolase Dub3 promotes oncogenic transformation by
stabilizing Cdc25A.";
Nat. Cell Biol. 12:400-406(2010).
[18]
PHOSPHORYLATION AT SER-513 AND SER-519 BY PLK3, UBIQUITINATION, AND
MUTAGENESIS OF SER-513 AND SER-519.
PubMed=21376736; DOI=10.1016/j.mrfmmm.2011.02.006;
Myer D.L., Robbins S.B., Yin M., Boivin G.P., Liu Y., Greis K.D.,
Bahassi el M., Stambrook P.J.;
"Absence of polo-like kinase 3 in mice stabilizes Cdc25A after DNA
damage but is not sufficient to produce tumors.";
Mutat. Res. 714:1-10(2011).
[19]
INTERACTION WITH HSP90AB1.
PubMed=22843495; DOI=10.1093/hmg/dds303;
Giessrigl B., Krieger S., Rosner M., Huttary N., Saiko P., Alami M.,
Messaoudi S., Peyrat J.F., Maciuk A., Gollinger M., Kopf S.,
Kazlauskas E., Mazal P., Szekeres T., Hengstschlaeger M., Matulis D.,
Jaeger W., Krupitza G.;
"Hsp90 stabilizes Cdc25A and counteracts heat shock-mediated Cdc25A
degradation and cell-cycle attenuation in pancreatic carcinoma
cells.";
Hum. Mol. Genet. 21:4615-4627(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-321, 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 (2.3 ANGSTROMS) OF 336-496.
PubMed=9604936; DOI=10.1016/S0092-8674(00)81190-3;
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.";
Cell 93:617-625(1998).
-!- FUNCTION: Tyrosine protein phosphatase which functions as a
dosage-dependent inducer of mitotic progression. Directly
dephosphorylates CDK1 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. Stimulated by
PIM1-mediated phosphorylation.
-!- 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. Interacts with PIM1. Interacts with
CHEK2; mediates CDC25A phosphorylation and degradation in response
to infrared-induced DNA damages. Interacts with HSP90AB1; prevents
heat shock-mediated CDC25A degradation and contributes to cell
cycle progression (PubMed:22843495). {ECO:0000269|PubMed:11298456,
ECO:0000269|PubMed:14559997, ECO:0000269|PubMed:14681206,
ECO:0000269|PubMed:16356754, ECO:0000269|PubMed:22843495}.
-!- INTERACTION:
Q9Y297:BTRC; NbExp=4; IntAct=EBI-747671, EBI-307461;
O96017:CHEK2; NbExp=2; IntAct=EBI-747671, EBI-1180783;
Q9UKB1:FBXW11; NbExp=4; IntAct=EBI-747671, EBI-355189;
P04049:RAF1; NbExp=4; IntAct=EBI-747671, EBI-365996;
P31946:YWHAB; NbExp=10; IntAct=EBI-747671, EBI-359815;
P62258:YWHAE; NbExp=5; IntAct=EBI-747671, EBI-356498;
P27348:YWHAQ; NbExp=3; IntAct=EBI-747671, EBI-359854;
P63104:YWHAZ; NbExp=2; IntAct=EBI-747671, EBI-347088;
-!- 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.
{ECO:0000269|PubMed:12234927}.
-!- 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 by the SCF complex. Phosphorylation of
CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation
at Ser-79, Ser-82 and Ser-88 by NEK11. Phosphorylation by NEK11 is
required for BTRC-mediated polyubiquitination and degradation.
Phosphorylation by PIM1 leads to an increase in phosphatase
activity. Phosphorylated by PLK3 following DNA damage, leading to
promote its ubiquitination and degradation.
{ECO:0000269|PubMed:11298456, ECO:0000269|PubMed:12399544,
ECO:0000269|PubMed:12676583, ECO:0000269|PubMed:12676925,
ECO:0000269|PubMed:12759351, ECO:0000269|PubMed:14559997,
ECO:0000269|PubMed:14681206, ECO:0000269|PubMed:19734889,
ECO:0000269|PubMed:20090422, ECO:0000269|PubMed:20228808,
ECO:0000269|PubMed:21376736}.
-!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome
(APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1
phase leading to its degradation by the proteasome. Ubiquitinated
by a SCF complex containing BTRC and FBXW11 during S phase leading
to its degradation by the proteasome. Deubiquitination by
USP17L2/DUB3 leads to its stabilization.
{ECO:0000269|PubMed:20228808}.
-!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CDC25AID40004ch3p21.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc25a/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M81933; AAA58415.1; -; mRNA.
EMBL; AY137580; AAN11305.1; -; mRNA.
EMBL; AF527417; AAM77917.1; -; Genomic_DNA.
EMBL; BC007401; AAH07401.1; -; mRNA.
EMBL; BC018642; AAH18642.1; -; mRNA.
EMBL; AF277722; AAG41884.1; -; mRNA.
CCDS; CCDS2760.1; -. [P30304-1]
CCDS; CCDS2761.1; -. [P30304-2]
PIR; A41648; A41648.
RefSeq; NP_001780.2; NM_001789.2. [P30304-1]
RefSeq; NP_963861.1; NM_201567.1. [P30304-2]
RefSeq; XP_011532618.1; XM_011534316.1. [P30304-1]
UniGene; Hs.437705; -.
PDB; 1C25; X-ray; 2.30 A; A=337-496.
PDBsum; 1C25; -.
ProteinModelPortal; P30304; -.
SMR; P30304; -.
BioGrid; 107428; 76.
DIP; DIP-166N; -.
ELM; P30304; -.
IntAct; P30304; 44.
MINT; P30304; -.
STRING; 9606.ENSP00000303706; -.
BindingDB; P30304; -.
ChEMBL; CHEMBL3775; -.
DEPOD; P30304; -.
iPTMnet; P30304; -.
PhosphoSitePlus; P30304; -.
BioMuta; CDC25A; -.
DMDM; 50403734; -.
EPD; P30304; -.
MaxQB; P30304; -.
PaxDb; P30304; -.
PeptideAtlas; P30304; -.
PRIDE; P30304; -.
DNASU; 993; -.
Ensembl; ENST00000302506; ENSP00000303706; ENSG00000164045. [P30304-1]
Ensembl; ENST00000351231; ENSP00000343166; ENSG00000164045. [P30304-2]
GeneID; 993; -.
KEGG; hsa:993; -.
UCSC; uc003csh.2; human. [P30304-1]
CTD; 993; -.
DisGeNET; 993; -.
EuPathDB; HostDB:ENSG00000164045.11; -.
GeneCards; CDC25A; -.
HGNC; HGNC:1725; CDC25A.
HPA; HPA005855; -.
MIM; 116947; gene.
neXtProt; NX_P30304; -.
OpenTargets; ENSG00000164045; -.
PharmGKB; PA26259; -.
eggNOG; KOG3772; Eukaryota.
eggNOG; COG5105; LUCA.
GeneTree; ENSGT00390000018747; -.
HOGENOM; HOG000082672; -.
HOVERGEN; HBG052501; -.
InParanoid; P30304; -.
KO; K06645; -.
OMA; RGCLHSH; -.
OrthoDB; EOG091G0H0D; -.
PhylomeDB; P30304; -.
TreeFam; TF101056; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-156711; Polo-like kinase mediated events.
Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
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; P30304; -.
ChiTaRS; CDC25A; human.
EvolutionaryTrace; P30304; -.
GeneWiki; CDC25A; -.
GenomeRNAi; 993; -.
PRO; PR:P30304; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000164045; -.
CleanEx; HS_CDC25A; -.
ExpressionAtlas; P30304; baseline and differential.
Genevisible; P30304; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0051087; F:chaperone binding; IPI: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; IEA:UniProtKB-EC.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051726; P:regulation of cell cycle; TAS:Reactome.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:UniProtKB.
GO; GO:0009314; P:response to radiation; 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; Hydrolase; Mitosis; Phosphoprotein; Polymorphism;
Protein phosphatase; Reference proteome; Ubl conjugation.
CHAIN 1 524 M-phase inducer phosphatase 1.
/FTId=PRO_0000198641.
DOMAIN 376 482 Rhodanese. {ECO:0000255|PROSITE-
ProRule:PRU00173}.
MOTIF 74 84 Phosphodegron.
MOTIF 141 143 KEN box.
ACT_SITE 431 431
MOD_RES 76 76 Phosphoserine; by CHEK1.
{ECO:0000269|PubMed:12759351,
ECO:0000269|PubMed:14681206}.
MOD_RES 79 79 Phosphoserine; by NEK11.
{ECO:0000269|PubMed:19734889}.
MOD_RES 82 82 Phosphoserine; by NEK11.
{ECO:0000269|PubMed:19734889,
ECO:0000269|PubMed:20090422}.
MOD_RES 88 88 Phosphoserine; by NEK11.
{ECO:0000269|PubMed:19734889,
ECO:0000269|PubMed:20090422}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 124 124 Phosphoserine; by CHEK1 and CHEK2.
{ECO:0000269|PubMed:11298456,
ECO:0000269|PubMed:12399544,
ECO:0000269|PubMed:12676583,
ECO:0000269|PubMed:12759351,
ECO:0000269|PubMed:14681206}.
MOD_RES 178 178 Phosphoserine; by CHEK1.
{ECO:0000269|PubMed:12676583,
ECO:0000269|PubMed:12759351,
ECO:0000269|PubMed:14559997}.
MOD_RES 279 279 Phosphoserine; by CHEK1 and CHEK2.
{ECO:0000269|PubMed:12676583}.
MOD_RES 293 293 Phosphoserine; by CHEK1 and CHEK2.
{ECO:0000269|PubMed:12676583}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 507 507 Phosphothreonine; by CHEK1.
{ECO:0000269|PubMed:14559997}.
MOD_RES 513 513 Phosphoserine; by PLK3.
{ECO:0000269|PubMed:21376736}.
MOD_RES 519 519 Phosphoserine; by PLK3.
{ECO:0000269|PubMed:21376736}.
VAR_SEQ 144 183 Missing (in isoform 2).
{ECO:0000303|PubMed:11139144,
ECO:0000303|Ref.2}.
/FTId=VSP_000860.
VARIANT 88 88 S -> F (in dbSNP:rs3731499).
{ECO:0000269|Ref.3}.
/FTId=VAR_020932.
VARIANT 182 182 R -> G (in dbSNP:rs6771386).
{ECO:0000269|PubMed:1836978}.
/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.
{ECO:0000269|PubMed:12759351,
ECO:0000269|PubMed:14681206}.
MUTAGEN 79 79 S->A: Abrogates interactions with BTRC
and FBXW11 and prevents ubiquitination.
{ECO:0000269|PubMed:14681206}.
MUTAGEN 81 81 D->A: Abrogates interactions with BTRC
and FBXW11 and prevents ubiquitination.
{ECO:0000269|PubMed:14681206}.
MUTAGEN 82 82 S->A: Abrogates interactions with BTRC
and FBXW11 and prevents ubiquitination.
{ECO:0000269|PubMed:14681206}.
MUTAGEN 124 124 S->A: Abrogates phosphorylation by CHEK2
and infrared-induced degradation.
Increases basal stability and impairs
CHEK1-dependent degradation following
checkpoint activation; when associated
with A-178; A-279 and A-293.
{ECO:0000269|PubMed:11298456,
ECO:0000269|PubMed:12399544,
ECO:0000269|PubMed:12676583,
ECO:0000269|PubMed:12759351}.
MUTAGEN 141 143 KEN->AAA: Prevents ubiquitination and
subsequent degradation by the APC/C
ubiquitin ligase complex.
{ECO:0000269|PubMed:12234927}.
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.
{ECO:0000269|PubMed:12676583,
ECO:0000269|PubMed:12759351,
ECO:0000269|PubMed:14559997}.
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.
{ECO:0000269|PubMed:12676583}.
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.
{ECO:0000269|PubMed:12676583}.
MUTAGEN 431 431 C->S: Abolishes phosphatase activity.
{ECO:0000269|PubMed:12676925,
ECO:0000269|PubMed:14559997}.
MUTAGEN 507 507 T->A: Abrogates 14-3-3 protein binding;
increases binding to cyclin B1.
{ECO:0000269|PubMed:14559997}.
MUTAGEN 513 513 S->A: Increased stability following IR
treatment. {ECO:0000269|PubMed:21376736}.
MUTAGEN 513 513 S->D: Mimicks phosphorylation state,
leading to promote degradation following
IR treatment.
{ECO:0000269|PubMed:21376736}.
MUTAGEN 514 514 K->L: Abrogates binding to CCNB1; when
associated with L-520.
{ECO:0000269|PubMed:14559997}.
MUTAGEN 519 519 S->A: Increased stability following IR
treatment. {ECO:0000269|PubMed:21376736}.
MUTAGEN 519 519 S->D: Mimicks phosphorylation state,
leading to promote degradation following
IR treatment.
{ECO:0000269|PubMed:21376736}.
MUTAGEN 520 520 R->L: Abrogates binding to CCNB1; when
associated with L-514.
{ECO:0000269|PubMed:14559997}.
CONFLICT 6 10 EPPHR -> SPAP (in Ref. 1; AAA58415).
{ECO:0000305}.
CONFLICT 180 181 PA -> QL (in Ref. 1; AAA58415).
{ECO:0000305}.
STRAND 341 344 {ECO:0000244|PDB:1C25}.
HELIX 362 369 {ECO:0000244|PDB:1C25}.
TURN 370 376 {ECO:0000244|PDB:1C25}.
STRAND 377 384 {ECO:0000244|PDB:1C25}.
HELIX 388 392 {ECO:0000244|PDB:1C25}.
HELIX 405 411 {ECO:0000244|PDB:1C25}.
TURN 412 414 {ECO:0000244|PDB:1C25}.
STRAND 423 430 {ECO:0000244|PDB:1C25}.
STRAND 432 436 {ECO:0000244|PDB:1C25}.
HELIX 437 451 {ECO:0000244|PDB:1C25}.
STRAND 463 466 {ECO:0000244|PDB:1C25}.
HELIX 469 477 {ECO:0000244|PDB:1C25}.
HELIX 478 480 {ECO:0000244|PDB:1C25}.
STRAND 481 484 {ECO:0000244|PDB:1C25}.
SEQUENCE 524 AA; 59087 MW; B2F6B792D4E6122B CRC64;
MELGPEPPHR RRLLFACSPP PASQPVVKAL FGASAAGGLS PVTNLTVTMD QLQGLGSDYE
QPLEVKNNSN LQRMGSSEST DSGFCLDSPG PLDSKENLEN PMRRIHSLPQ KLLGCSPALK
RSHSDSLDHD IFQLIDPDEN KENEAFEFKK PVRPVSRGCL HSHGLQEGKD LFTQRQNSAP
ARMLSSNERD SSEPGNFIPL FTPQSPVTAT LSDEDDGFVD LLDGENLKNE EETPSCMASL
WTAPLVMRTT NLDNRCKLFD SPSLCSSSTR SVLKRPERSQ EESPPGSTKR RKSMSGASPK
ESTNPEKAHE TLHQSLSLAS SPKGTIENIL DNDPRDLIGD FSKGYLFHTV AGKHQDLKYI
SPEIMASVLN GKFANLIKEF VIIDCRYPYE YEGGHIKGAV NLHMEEEVED FLLKKPIVPT
DGKRVIVVFH CEFSSERGPR MCRYVRERDR LGNEYPKLHY PELYVLKGGY KEFFMKCQSY
CEPPSYRPMH HEDFKEDLKK FRTKSRTWAG EKSKREMYSR LKKL


Related products :

Catalog number Product name Quantity
EIAAB25266 CDC25A,Dual specificity phosphatase Cdc25A,Homo sapiens,Human,M-phase inducer phosphatase 1
EIAAB25268 Cdc25a,Cdc25m3,Dual specificity phosphatase Cdc25A,Mouse,M-phase inducer phosphatase 1,Mus musculus
EIAAB25267 Cdc25a,Dual specificity phosphatase Cdc25A,M-phase inducer phosphatase 1,Rat,Rattus norvegicus
EIAAB25265 Bos taurus,Bovine,CDC25A,Dual specificity phosphatase Cdc25A,M-phase inducer phosphatase 1
15-288-21526 M-phase inducer phosphatase 1 - EC 3.1.3.48; Dual specificity phosphatase Cdc25A Polyclonal 0.05 mg
15-288-21526 M-phase inducer phosphatase 1 - EC 3.1.3.48; Dual specificity phosphatase Cdc25A Polyclonal 0.1 mg
15-288-21532 M-phase inducer phosphatase 3 - EC 3.1.3.48; Dual specificity phosphatase Cdc25C Polyclonal 0.1 mg
15-288-21532 M-phase inducer phosphatase 3 - EC 3.1.3.48; Dual specificity phosphatase Cdc25C Polyclonal 0.05 mg
EIAAB25270 CDC25B,CDC25HU2,Dual specificity phosphatase Cdc25B,Homo sapiens,Human,M-phase inducer phosphatase 2
EIAAB25271 Cdc25b,Cdc25m2,Dual specificity phosphatase Cdc25B,Mouse,M-phase inducer phosphatase 2,Mus musculus
EIAAB25273 Cdc25c,Cdc25m1,Dual specificity phosphatase Cdc25C,Mouse,M-phase inducer phosphatase 3,Mus musculus
EIAAB25272 CDC25C,Dual specificity phosphatase Cdc25C,Homo sapiens,Human,M-phase inducer phosphatase 3
EIAAB25269 Cdc25b,Dual specificity phosphatase Cdc25B,M-phase inducer phosphatase 2,Rat,Rattus norvegicus
EIAAB25274 Bos taurus,Bovine,CDC25C,Dual specificity phosphatase Cdc25C,M-phase inducer phosphatase 3
EIAAB25275 CDC25C,Dual specificity phosphatase Cdc25C,M-phase inducer phosphatase 3,Pig,Sus scrofa
EIAAB12078 DSP-4,Dual specificity phosphatase SKRP3,Dual specificity protein phosphatase 26,DUSP24,DUSP26,Homo sapiens,Human,LDP4,LDP-4,Low-molecular-mass dual-specificity phosphatase 4,MAP kinase phosphatase 8,
EIAAB12065 Dual specificity phosphatase TS-DSP1,Dual specificity protein phosphatase 19,DUSP17,DUSP19,Homo sapiens,Human,LMWDSP3,LMW-DSP3,Low molecular weight dual specificity phosphatase 3,Protein phosphatase S
CSB-EL004994RA Rat M-phase inducer phosphatase 1(CDC25A) ELISA kit 96T
18-461-10231 Dual specificity phosphatase 26 - Low-molecular-mass dual-specificity phosphatase 4; Dual-specificity phosphatase SKRP3; Mitogen-activated protein kinase phosphatase 8; NATA1 protein; CDNA FLJ31142 fi 0.05 ml
18-461-10232 Dual specificity phosphatase 26 - Low-molecular-mass dual-specificity phosphatase 4; Dual-specificity phosphatase SKRP3; Mitogen-activated protein kinase phosphatase 8; NATA1 protein; CDNA FLJ31142 fi 0.05 ml
CSB-EL004994HU Human M-phase inducer phosphatase 1(CDC25A) ELISA kit 96T
CSB-EL004994RA Rat M-phase inducer phosphatase 1(CDC25A) ELISA kit SpeciesRat 96T
CSB-EL004994MO Mouse M-phase inducer phosphatase 1(CDC25A) ELISA kit 96T
CSB-EL004994BO Bovine M-phase inducer phosphatase 1(CDC25A) ELISA kit 96T
EIAAB12073 Dual specificity protein phosphatase 22,DUSP22,Homo sapiens,Human,JNK-stimulatory phosphatase-1,JSP1,JSP-1,LMWDSP2,LMW-DSP2,Low molecular weight dual specificity phosphatase 2,MAP kinase phosphatase x


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur