EGFR autophosphorylation Authored: Castagnoli, L, 2006-10-10 13:09:34 EC Number: 2.7.10 Edited: Orlic-Milacic, Marija, 2011-08-25 Pubmed1688559 Pubmed2022652 Pubmed2543678 Reactome Database ID Release 43177934 Reactome, http://www.reactome.org ReactomeREACT_9388 Reviewed: Muthuswamy, S, 2007-02-16 20:08:05 The cytoplasmic domain of EGFR contains tyrosine, serine and threonine phosphorylation sites. Dimerization of EGFR activates its intrinsic protein kinase activity and results in autophosphorylation of 6 tyrosine residues in the cytoplasmic tail of EGFR. Tyrosine autophosphorylation is crucial for normal receptor signalling. Five of these tyrosine residues (Y992, Y1068, Y1086, Y1148 and Y1173) serve as specific binding sites for cytosolic target proteins involved in signal transmission, while the tyrosine residue Y1045 is involved in recruitment of CBL ubiquitin ligase and downregulation of EGFR signaling through degradation of activated EGFR. has a Stoichiometric coefficient of 12 EGF:p-6Y-EGFR EGF:EGFR dimer