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. 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.View all products for Protein Tyrosine Phosphatases »
|Gene||Species||Gene Symbol||Gene Accession No.||Protein Accession No.|
|View all Protein Tyrosine Phosphatase Gene Data »|
Literature for Protein Tyrosine Phosphatases
A collection of over 750 products for cancer research, the guide includes research tools for the study of:
- Cancer Metabolism
- Epigenetics in Cancer
- Receptor Signaling
- Cell Cycle and DNA Damage Repair
- Invasion and Metastasis
Find multiple products by catalog number
Follow @Tocris on Twitter
Tocris is now actively tweeting. For regular updates on news, events and special offers, follow @Tocris on Twitter.