Protein Phosphatase 6, Catalytic Subunit (PPP6C)

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. PPP6C is the catalytic subunit of human serine/threonine protein phosphatase-6. Northern blot analysis showed that PPP6C was expressed as 3 transcripts of 1.8 kb, 4.2 kb, and 4.7 kb in all 16 human tissues examined. Expression levels were highest in testis, heart, and skeletal muscle and lowest in placenta, lung, and kidney. Immunoblot analysis detected a 35-kD PPP6C protein in lysates from human heart muscle and bull testis.