FUNCTION Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET.CATALYTIC ACTIVITY O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphateSUBUNIT Interacts with EPHA3 (phosphorylated); dephosphorylates EPHA3 and may regulate its trafficking and function (PubMed:21135139). Interacts with MET (PubMed:18819921). Interacts with NCK1 (PubMed:21707536).INTERACTION Interacts with EPHA3 at the cell membrane.TISSUE SPECIFICITY Expressed in keratinocytes (at protein level).PTM Oxidized on Cys-215; the Cys-SOH formed in response to redox signaling reacts with the alpha-amido of the following residue to form a sulfenamide cross-link, triggering a conformational change that inhibits substrate binding and activity. The active site can be restored by reduction.PTM Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50.PTM S-nitrosylation of Cys-215 inactivates the enzyme activity.PTM Sulfhydration at Cys-215 following endoplasmic reticulum stress inactivates the enzyme activity, promoting EIF2AK3/PERK activity.SIMILARITY Belongs to the protein-tyrosine phosphatase family. Non-receptor class 1 subfamily.
This website requires cookies and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.