Protein serine/threonine phosphatase

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protein-serine/threonine phosphatase
Protein serine/threonine phosphatase dodekamer, Human
EC number3.1.3.16
CAS number9025-75-6
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

Protein serine/threonine phosphatase (PSP)[1] is a form of phosphoprotein phosphatase that acts upon phosphorylated serine/threonine residues.

Serine and threonine phosphates are stable under physiological conditions, so a phosphatase enzyme has to remove the phosphate to reverse the regulation signal. Ser/Thr-specific protein phosphatases are regulated partly by their location within the cell and by specific inhibitor proteins.

Serine and threonine are amino acids which have similar side-chain compositions that contain a hydroxyl group and thus can be phosphorylated by enzymes called serine/threonine protein kinases. The addition of the phosphate group can be reversed by enzymes called serine/threonine phosphatases. The addition and removal of phosphate groups regulates many cellular pathways involved in cell proliferation, programmed cell death (apoptosis), embryonic development, and cell differentiation.


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.[citation needed]


  1. ^ Shi Y (October 2009). "Serine/threonine phosphatases: mechanism through structure". Cell. 139 (3): 468–84. doi:10.1016/j.cell.2009.10.006. PMID 19879837.

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