Cdc25B Recombinant Rabbit Monoclonal Antibody [JJ091-2]

Function

The Cdc2/cyclin B enzyme, involved in regulation of mitosis in eukaryotic cells, is subject to multiple levels of control. Among these, the regulation of the catalytic subunit by Tyrosine phosphorylation is the best understood. Tyrosine phosphorylation inhibits the Cdc2/cyclin B complex, while Tyrosine dephosphorylation, which occurs at the onset of mitosis, directly activates the pre-MPH complex. The Cdc25 gene serves as a rate-limiting mitotic activator, apparently due to its action as the Cdc2 Tyrosine phosphatase. In the absence of Cdc25, Cdc2 accumulates in a Tyrosine phosphorylated state. In addition, Cdc25 proteins from a variety of species have been shown to share a low degree of sequence similarity with other Tyrosine phosphatases. The Cdc25 gene family consists of at least three members that share approximately 40% identity in their most conserved carboxy-terminal sequences.

Background References

1. Hein M.Y., et al. 2015. A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 163:712-723.

2. Lund G., et al. 2015. Inhibition of CDC25B phosphatase through disruption of protein-protein interaction. ACS Chem. Biol. 10:390-394.

Sequence Similarity

Belongs to the MPI phosphatase family.

Post-translational Modification

Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-353 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-169 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-323 and Ser-375 by MAPK14 is required for binding to 14-3-3 proteins.

Subcellular Location

Cytoplasm, Cytoskeleton.

UNIPROT

SwissProt: P30305 Human

Synonyms