Protein serine/threonine phosphatase (PSP)[1] is a form of phosphoprotein phosphatase that acts upon serine/threonine residues.
Serine and threonine phosphates are stable under physiological conditions, so a phosphatase has to remove the phosphate to reverse the regulation.
Ser/Thr-specific protein phosphatases are regulated by their location within the cell and by specific inhibitor proteins.
There are several known groups with numerous members in each:
(links are to the catalytic subunit)
All but PPP2C have sequence homology in the catalytic domain, but differ in substrate specificity.
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