Protein Tyrosine Phosphatases

Protein tyrosine phosphatases (PTPs) are a group of enzymes that catalyze the removal of phosphate groups from tyrosine 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, including histone dephosphorylation during epigenetic modification.

PTPs are cysteine-dependent phosphatases that contain a conserved C[X]₅R motif essential for enzymatic activity. PTPs are currently divided into five subtypes: tyrosine-specific phosphatases (e.g. PTP1B); dual specificity phosphatases (DSPs) (e.g. DUSP1); Cdc25 phosphatases (e.g. Cdc25A); myotubularin-related phosphatases (e.g. MTMR13); and low molecular weight phosphatases (e.g. PTPase A). Perturbations in PTP activity have been implicated in human diseases, including type II diabetes. In cancers, PTPs dephosphorylate EGFR, JAK2 and TYK2 kinases, promoting oncogenic transformation.

External sources of pharmacological information for Protein Tyrosine Phosphatases :

• BJP Guide

Literature for Protein Tyrosine Phosphatases

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Cancer Research Product Guide

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Protein Tyrosine Phosphatase Gene Data