PPP6C belongs to the PPP phosphatase family, PP-V subfamily. Reversible phosphorylation of proteins on serine and threonine residues is an important biochemical event that regulates a broad variety of intracellular processes. The phosphorylation state is determined by the well-controlled balance of activities of serine/threonine-specific protein kinases and protein phosphatases, including PPP6C. Expression levels are highest in testis, heart, and skeletal muscle and lowest in placenta, lung, and kidney. PPP6C can complement mutations in the S. cerevisiae Sit4 and S. pombe ppe1 genes, indicating that PPP6C is the functional homolog of yeast Sit4p and ppe1. Since Sit4p is required for the G1 to S transition of the cell cycle and ppe1 is involved in cell shape control and mitotic division, it has been suggested that PPP6C functions in cell cycle regulation.

HUMAN

2-8°C (short-term); -20°C (long-term)