EGFR autophosphorylation

Stable Identifier
R-HSA-177934
Type
Reaction
Species
Homo sapiens
Compartment
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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.

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Participates
Catalyst Activity

protein tyrosine kinase activity of EGF-like ligands:EGFR dimer [plasma membrane]

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