Protein Tyrosine Phosphatases

Supporting information

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. PTPs have been identified as a negative regulator of insulin signaling due to its ability to dephosphorylate phosphotyrosine residues of insulin receptor kinase. In cancers, PTPs dephosphorylate EGFR, JAK2 and TYK2 kinases, promoting oncogenic transformation.

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
PTP1B Human PTPN1 NM_002827 P18031
Mouse Ptpn1 NM_011201 P35821
Rat Ptpn1 NM_012637 P20417
DUSP1 Human DUSP1 NM_004417 P28562
Mouse Dusp1 NM_013642 P28563
Rat Dusp1 NM_053769 Q63683
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Literature for Protein Tyrosine Phosphatases

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