PERK (protein kinase-like endoplasmic reticulum kinase) is a type I membrane protein located in the endoplasmic reticulum (ER). ER stress increases the activity of PERK, which then phosphorylates eIF2alpha to promote reduced translation, leading to its inactivation, and thus to a rapid reduction of translational initiation and repression of global protein synthesis. PERK-deficient mice have defects in pancreatic beta cells several weeks after birth, suggesting a role for PERK-mediated translational control in protecting secretory cells from ER stress. PERK activation during ER stress correlates with autophosphorylation of its cytoplasmic kinase domain. Phosphorylation of PERK at Ser713 can be used as a marker for its activation status. The predicted phosphorylation site and surrounding residues of Ser713 are: HIEIIAPS*PQRSRSF.