Protein Ser/Thr Phosphatases

Supporting information

Protein Ser/Thr phosphatases are a group of enzymes that catalyze the removal of phosphate groups from serine and/or threonine residues by the hydrolysis of phosphoric acid monoesters. They directly oppose the actions of kinases and phosphorylases and therefore play an integral role in many signal transduction pathways.

There are two groups of serine/threonine phosphatases: phosphoprotein phosphatases (e.g. PP1, calcineurin), which are sensitive to okadaic acid; and metallo-phosphatases (e.g. PP2C), which require a divalent cation, commonly Mg2+, for catalytic activity. Dephosphorylation, depending on the residue that the phosphate group is removed from, can have a stimulatory or inhibitory effect on the target molecule. This makes protein Ser/Thr phosphatases essential for many signal transduction pathways, including histone dephosphorylation during epigenetic modification. Protein Ser/Thr phosphatase are regulated by their subcellular localization and by inhibitor proteins, which are subtype-specific.

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
PP1α Human PPP1CA NM_206873 P62136
Mouse Ppp1ca NM_031868 P62137
Rat Ppp1ca NM_031527 P62138
PP1β Human PPP1CB NM_002709 P62140
Mouse Ppp1cb NM_172707 P62141
Rat Ppp1cb NM_013065 P62142
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Literature for Protein Ser/Thr Phosphatases

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