CDC25A

CDC25A (Cell Division Cycle 25A) is a Protein Coding gene. Diseases associated with CDC25A include Breast Cancer. Among its related pathways are Metabolism of proteins and CDK-mediated phosphorylation and removal of Cdc6. Gene Ontology (GO) annotations related to this gene include protein kinase binding and protein tyrosine phosphatase activity. An important paralog of this gene is CDC25B.

Full Name

Cell Division Cycle 25A

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.

Biological Process

Cell division Source: UniProtKB-KW
Cell population proliferation Source: UniProtKB
Cellular response to UV Source: UniProtKB
G1/S transition of mitotic cell cycle Source: Reactome
G2/M transition of mitotic cell cycle Source: GO_Central
Positive regulation of G2/MI transition of meiotic cell cycle Source: GO_Central
Positive regulation of G2/M transition of mitotic cell cycle Source: GO_Central
Protein deubiquitination Source: Reactome
Regulation of cell cycle Source: Reactome
Regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
Response to radiation Source: UniProtKB

Cellular Location

Cytosol; Nucleoplasm; Nucleus; Cytoplasm

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.
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.