Cdc25a
entrez
171102
canonical
uniprot
P48965
canonical
ensembl
ENSRNOG00000020737
resolver
ensp
ENSRNOP00000028141
resolver
ensp
ENSRNOP00000082319
resolver
ensp
ENSRNOP00000102479
resolver
enst
ENSRNOT00000028141
resolver
genesymbol
Cdc25a
resolver
uniprot
G3V8T0
resolver
uniprot_entry
G3V8T0_RAT
resolver
uniprot_entry
MPIP1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Stimulated by B-type cyclins (By similarity). Stimulated by PIM1-mediated phosphorylation (PubMed:10373478). {ECO:0000250|UniProtKB:P30304, ECO:0000269|PubMed:10373478}.
uniprot
proteins
amino_acid_sequence
MELGPEPPHRRRLLFTCSPTPAPQPTGKVQFGASRAGGLSPVTNLTVTMDQLEGLGSDYEKPMDVRNSSSLQRMGSSESTDSGFCLDSPGPLDSKENLEISLRRINCLPQKLLGCSPALKRSHSDSLDHDIFQLIDQDENKENEAFEFKKPIRPASRGCLNAHVHEESKDPFTHRQNSAPARMLSSNESDISESGNFSPLFTPQSPVKASLSDEDDGFIDLLDGENLKNDEETPSCMSSLWTAPLVMRRPTNLADRCGLFDSPSPCSSTSSCSTRAVKRADRSHEESPRGTKRRKSSEASPVKADVPEPTQLPHQSLSLTSFPKGTIENIFHSDPRDLIGDFSKGYLFHTVSGKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEEFLLKKPIVPADGKRVIVVFHCEFSSERGPRMCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFLKCQSHCEPPSYRPMHHEDFKEDLKKFRTKSRTWAGEKSKREMYSRLKKL
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:10373478). Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:10373478). Also dephosphorylates CDK2 in complex with cyclin-E, in vitro (By similarity). {ECO:0000250|UniProtKB:P30304, ECO:0000269|PubMed:10373478}.
uniprot
proteins
mass_dalton
59218
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-283, Ser-296 and Thr-508 during checkpoint mediated cell cycle arrest (By similarity). Also phosphorylated by CHEK2 on Ser-124, Ser-283, and Ser-296 during checkpoint mediated cell cycle arrest (By similarity). Phosphorylation on Ser-178 and Thr-508 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A (By similarity). Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-283 and Ser-296 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex (By similarity). Phosphorylation of CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation at Ser-79, Ser-82 and Ser-88 by NEK11 (By similarity). Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation (By similarity). Phosphorylation by PIM1 leads to an increase in phosphatase activity (PubMed:10373478). Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation (By similarity). {ECO:0000250|UniProtKB:P30304, ECO:0000269|PubMed:10373478}.; 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 (By similarity). {ECO:0000250|UniProtKB:P30304}.
uniprot
proteins
protein_family
MPI phosphatase family
uniprot
proteins
pubmed
10373478
uniprot
proteins
pubmed
8156993
uniprot
proteins
sequence_length
525
uniprot
proteins