| Modification Notes |
In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. PPP2R5E (protein phosphatase 2, regulatory subunit B', epsilon isoform) is a 467 amino acid protein that localizes to the cytoplasm and exists as an isoform of the B regulatory subunit within the PP multimeric complex. Functioning as a regulatory subunit, PPP2R5E is thought to modulate both the catalytic activity and the substrate specificity of the PP holoenzyme and may also be responsible for the localization of the complex to subcellular compartments. |