Cdc25a
entrez
12530
canonical
uniprot
P48964
canonical
ensembl
ENSMUSG00000032477
resolver
ensp
ENSMUSP00000091882
resolver
ensp
ENSMUSP00000221199
resolver
ensp
ENSMUSP00000221200
resolver
enst
ENSMUST00000094324
resolver
genesymbol
Cdc25a
resolver
genesymbol_syn
Cdc25m3
resolver
uniprot
E9PVD0
resolver
uniprot_entry
MPIP1_MOUSE
resolver
uniprot_sec
E9PVD0
resolver
activity_regulation
ACTIVITY REGULATION: Stimulated by B-type cyclins. Stimulated by PIM1-mediated phosphorylation (By similarity). {ECO:0000250|UniProtKB:P30304}.
uniprot
proteins
amino_acid_sequence
MELGPEPPHRRRLFFACSPTPAPQPTGKMLFGASAAGGLSPVTNLTVTMDQLEGLGSDCEKMEVRNNSSLQRMGSSESTDSGFCLDSPGPLDSKENLEISLTRINSLPQKLLGCSPALKRSHSDSLDHDTFHLIDQDENKENEAFEFKKPIRPASRHIYEESKDPFTHRQNSAPARMLSSNESESGNFSPLFIPQSPVKATLSDEDDGFIDLLDGENMKNDEETPSCMASLWTAPLVMRRPANLADRCGLFDSPSPCGSSTRAVLKRADRSHEEPPRGTKRRKSVPSPVKAKADVPEPAQLPSQSLSLMSSPKGTIENILDSDPRDLIGDFSKGYLFNTVSGKHQDLKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTDGKRVIVVFHCEFSSERGPRMCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFLKCQSHCEPPSYRPMHHEDFKEDLKKFRTKSRTWAGEKSKREMYSRLKKL
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. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin-E, in vitro. {ECO:0000250|UniProtKB:P30304}.
uniprot
proteins
mass_dalton
57806
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CHEK1 on Ser-75, Ser-123, Ser-172, Ser-271, Ser-284 and Thr-497 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-123, Ser-271, and Ser-284 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-172 and Thr-497 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-75, Ser-123, Ser-172, Ser-271 and Ser-284 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-75 by CHEK1 primes it for subsequent phosphorylation at Ser-75, Ser-81 and Ser-87 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 (By similarity). {ECO:0000250|UniProtKB:P30304}.; 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
19468303
uniprot
proteins
pubmed
7635051
uniprot
proteins
sequence_length
514
uniprot
proteins