Phospho-CDC25C (Thr48)

CDC25C (Cell Division Cycle 25C) is a Protein Coding gene. Diseases associated with CDC25C include Plague and Prostate Cancer. Among its related pathways are Gene Expression and Akt Signaling. Gene Ontology (GO) annotations related to this gene include protein kinase binding and WW domain binding. An important paralog of this gene is CDC25B.

Full Name

Cell Division Cycle 25C

Function

Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity.

Biological Process

Cell division Source: UniProtKB-KW
Cell population proliferation Source: ProtInc
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
G2/M transition of mitotic cell cycle Source: UniProtKB
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
Regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
Regulation of mitotic nuclear division Source: ProtInc
Spermatogenesis Source: Ensembl
Viral process Source: UniProtKB-KW

Cellular Location

Nucleus

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.