| 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. PPP1R6 (protein phosphatase 1, regulatory subunit 6), also known as PPP1R3D in humans and Ppp1r3d in rodents, is a 299 amino acid protein that contains one CBM21 (carbohydrate binding type-21) domain and exists as a regulatory subunit of the PP1 holoenzyme. Expressed ubiquitously with highest expression in heart and skeletal muscle, PPP1R6 functions as a glycogen-targeting subunit of PP1 and participates in cell division, glycogen metabolism and protein synthesis. |