CDC25A
entrez
993
canonical
uniprot
P30304
canonical
ensembl
ENSG00000164045
resolver
ensp
ENSP00000303706
resolver
ensp
ENSP00000343166
resolver
ensp
ENSP00000550493
resolver
ensp
ENSP00000550494
resolver
ensp
ENSP00000754404
resolver
genesymbol
CDC25A
resolver
hgnc
HGNC:1725
resolver
uniprot
D8KXX0
resolver
uniprot
K7N7S0
resolver
uniprot
Q8IZH5
resolver
uniprot
Q96IL3
resolver
uniprot
Q9H2F2
resolver
uniprot_entry
D8KXX0_HUMAN
resolver
uniprot_entry
K7N7S0_HUMAN
resolver
uniprot_entry
MPIP1_HUMAN
resolver
uniprot_sec
Q8IZH5
resolver
uniprot_sec
Q96IL3
resolver
uniprot_sec
Q9H2F2
resolver
activity_regulation
ACTIVITY REGULATION: Stimulated by B-type cyclins (PubMed:1836978). Stimulated by PIM1-mediated phosphorylation (PubMed:16356754). {ECO:0000269|PubMed:16356754, ECO:0000269|PubMed:1836978}.
uniprot
proteins
amino_acid_sequence
MELGPEPPHRRRLLFACSPPPASQPVVKALFGASAAGGLSPVTNLTVTMDQLQGLGSDYEQPLEVKNNSNLQRMGSSESTDSGFCLDSPGPLDSKENLENPMRRIHSLPQKLLGCSPALKRSHSDSLDHDIFQLIDPDENKENEAFEFKKPVRPVSRGCLHSHGLQEGKDLFTQRQNSAPARMLSSNERDSSEPGNFIPLFTPQSPVTATLSDEDDGFVDLLDGENLKNEEETPSCMASLWTAPLVMRTTNLDNRCKLFDSPSLCSSSTRSVLKRPERSQEESPPGSTKRRKSMSGASPKESTNPEKAHETLHQSLSLASSPKGTIENILDNDPRDLIGDFSKGYLFHTVAGKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSERGPRMCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPMHHEDFKEDLKKFRTKSRTWAGEKSKREMYSRLKKL
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression (PubMed:12676925, PubMed:14559997, PubMed:1836978, PubMed:20360007). Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:20360007). Also dephosphorylates CDK2 in complex with cyclin-E, in vitro (PubMed:20360007). {ECO:0000269|PubMed:12676925, ECO:0000269|PubMed:14559997, ECO:0000269|PubMed:1836978, ECO:0000269|PubMed:20360007}.
uniprot
proteins
mass_dalton
59087
uniprot
proteins
mutagenesis
MUTAGEN 76; /note="S->A: Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation."; /evidence="ECO:0000269|PubMed:12759351, ECO:0000269|PubMed:14681206"; MUTAGEN 79; /note="S->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination."; /evidence="ECO:0000269|PubMed:14681206"; MUTAGEN 81; /note="D->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination."; /evidence="ECO:0000269|PubMed:14681206"; MUTAGEN 82; /note="S->A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination."; /evidence="ECO:0000269|PubMed:14681206"; MUTAGEN 124; /note="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."; /evidence="ECO:0000269|PubMed:11298456, ECO:0000269|PubMed:12399544, ECO:0000269|PubMed:12676583, ECO:0000269|PubMed:12759351"; MUTAGEN 141..143; /note="KEN->AAA: Prevents ubiquitination and subsequent degradation by the APC/C ubiquitin ligase complex."; /evidence="ECO:0000269|PubMed:12234927"; MUTAGEN 178; /note="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."; /evidence="ECO:0000269|PubMed:12676583, ECO:0000269|PubMed:12759351, ECO:0000269|PubMed:14559997"; MUTAGEN 279; /note="S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293."; /evidence="ECO:0000269|PubMed:12676583"; MUTAGEN 293; /note="S->A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279."; /evidence="ECO:0000269|PubMed:12676583"; MUTAGEN 431; /note="C->S: Abolishes phosphatase activity."; /evidence="ECO:0000269|PubMed:12676925, ECO:0000269|PubMed:14559997"; MUTAGEN 507; /note="T->A: Abrogates 14-3-3 protein binding; increases binding to cyclin B1."; /evidence="ECO:0000269|PubMed:14559997"; MUTAGEN 513; /note="S->A: Increased stability following IR treatment."; /evidence="ECO:0000269|PubMed:21376736"; MUTAGEN 513; /note="S->D: Mimicks phosphorylation state, leading to promote degradation following IR treatment."; /evidence="ECO:0000269|PubMed:21376736"; MUTAGEN 514; /note="K->L: Abrogates binding to CCNB1; when associated with L-520."; /evidence="ECO:0000269|PubMed:14559997"; MUTAGEN 519; /note="S->A: Increased stability following IR treatment."; /evidence="ECO:0000269|PubMed:21376736"; MUTAGEN 519; /note="S->D: Mimicks phosphorylation state, leading to promote degradation following IR treatment."; /evidence="ECO:0000269|PubMed:21376736"; MUTAGEN 520; /note="R->L: Abrogates binding to CCNB1; when associated with L-514."; /evidence="ECO:0000269|PubMed:14559997
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
protein_family
MPI phosphatase family
uniprot
proteins
pubmed
11139144
uniprot
proteins
pubmed
11298456
uniprot
proteins
pubmed
12234927
uniprot
proteins
pubmed
12399544
uniprot
proteins
pubmed
12676583
uniprot
proteins
pubmed
12676925
uniprot
proteins
pubmed
12759351
uniprot
proteins
pubmed
14559997
uniprot
proteins
pubmed
14681206
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16356754
uniprot
proteins
pubmed
1836978
uniprot
proteins
pubmed
19734889
uniprot
proteins
pubmed
20090422
uniprot
proteins
pubmed
20228808
uniprot
proteins
pubmed
20360007
uniprot
proteins
pubmed
21376736
uniprot
proteins
pubmed
22843495
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
9604936
uniprot
proteins
sequence_length
524
uniprot
proteins