CDC25C
entrez
995
canonical
uniprot
P30307
canonical
ensembl
ENSG00000158402
resolver
ensp
ENSP00000321656
resolver
ensp
ENSP00000424795
resolver
ensp
ENSP00000545259
resolver
ensp
ENSP00000545260
resolver
ensp
ENSP00000590955
resolver
ensp
ENSP00000590963
resolver
genesymbol
CDC25C
resolver
hgnc
HGNC:1727
resolver
uniprot
B4DX61
resolver
uniprot
D3DQB8
resolver
uniprot
Q96PL3
resolver
uniprot
Q9H168
resolver
uniprot
Q9H2E8
resolver
uniprot
Q9H2E9
resolver
uniprot
Q9H2F1
resolver
uniprot_entry
B4DX61_HUMAN
resolver
uniprot_entry
MPIP3_HUMAN
resolver
uniprot_sec
D3DQB8
resolver
uniprot_sec
Q96PL3
resolver
uniprot_sec
Q9H168
resolver
uniprot_sec
Q9H2E8
resolver
uniprot_sec
Q9H2E9
resolver
uniprot_sec
Q9H2F1
resolver
amino_acid_sequence
MSTELFSSTREEGSSGSGPSFRSNQRKMLNLLLERDTSFTVCPDVPRTPVGKFLGDSANLSILSGGTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSPAQLLCSTPNGLDRGHRKRDAMCSSSANKENDNGNLVDSEMKYLGSPITTVPKLDKNPNLGEDQAEEISDELMEFSLKDQEAKVSRSGLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVKKKYFSGQGKLRKGLCLKKTVSLCDITITQMLEEDSNQGHLIGDFSKVCALPTVSGKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQYPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHKTELLRCRSQSKVQEGERQLREQIALLVKDMSP
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle (PubMed:8119945). When phosphorylated, highly effective in activating G2 cells into prophase (PubMed:8119945). Directly dephosphorylates CDK1 and activates its kinase activity (PubMed:8119945). {ECO:0000269|PubMed:8119945}.
uniprot
proteins
mass_dalton
53365
uniprot
proteins
mutagenesis
MUTAGEN 129; /note="S->V: Loss of phosphorylation. Severely impairs PLK1-binding."; /evidence="ECO:0000269|PubMed:12595692"; MUTAGEN 130; /note="T->A: Loss of phosphorylation. Severely impairs PLK1-binding."; /evidence="ECO:0000269|PubMed:12595692"; MUTAGEN 191; /note="S->A: Facilitates nuclear exclusion."; /evidence="ECO:0000269|PubMed:14968113"; MUTAGEN 191; /note="S->D: Mimicks phosphorylation state, leading to enhanced accumulation in the nucleus."; /evidence="ECO:0000269|PubMed:14968113"; MUTAGEN 211; /note="L->A: Reduces phosphorylation by MARK3 and CHEK1."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 216; /note="S->A: No effect on interaction with MARK3. Abolishes phosphorylation by MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 221; /note="L->A: Abolishes interaction with MARK3. Reduces phosphorylation of S-216 by MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 242..244; /note="KKK->AAA: No effect on interaction with MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 352; /note="E->K: Partial loss of HIV-1 Vpr binding."; /evidence="ECO:0000269|PubMed:14972559"; MUTAGEN 359; /note="K->E: No effect on HIV-1 Vpr binding."; /evidence="ECO:0000269|PubMed:14972559
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CHEK1 and MAPK14 at Ser-216. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-191 promotes nuclear translocation. Ser-198 is a minor phosphorylation site. Was initially reported to be phosphorylated by PLK3 at Ser-216 (PubMed:10557092). However, such phosphorylation by PLK3 was not confirmed by other groups. Phosphorylation at Thr-48, Thr-67, Ser-122, Thr-130, Ser-168 and Ser-214 occurs at G2 and G2-M transition and is probably catalyzed by CDK1. Ser-168 phosphorylation levels are lower than those at the other 5 CDK1 sites. Phosphorylation by CDK1 leads to increased activity. {ECO:0000269|PubMed:10557092, ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:14968113, ECO:0000269|PubMed:15150265, ECO:0000269|PubMed:15629715, ECO:0000269|PubMed:18239451, ECO:0000269|PubMed:8119945}.
uniprot
proteins
protein_family
MPI phosphatase family
uniprot
proteins
pubmed
10557092
uniprot
proteins
pubmed
11078813
uniprot
proteins
pubmed
11139144
uniprot
proteins
pubmed
11202906
uniprot
proteins
pubmed
11304565
uniprot
proteins
pubmed
11333986
uniprot
proteins
pubmed
12595692
uniprot
proteins
pubmed
12941695
uniprot
proteins
pubmed
14968113
uniprot
proteins
pubmed
14972559
uniprot
proteins
pubmed
15150265
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15629715
uniprot
proteins
pubmed
18239451
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
2195549
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
8119945
uniprot
proteins
sequence_length
473
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14968113, ECO:0000269|PubMed:8119945}.
uniprot
proteins