Abstract
Epidermal growth factor receptor (EGFR) binds to EGF activating tyrosine phosphorylation through receptor dimerization prompting uncontrolled multiplication. Domain organization, secondary structure combinations in motifs and interactome define such transitory changes responsible for the multi-functionality of human EGFR. We report the predicted phosphorylation sites on Ser, Thr and Tyr residues in addition to 74 auto-phosphorylation sites on Tyr in human EGFR. These data suggest a complex interplay between phosphorylation types for modification resulting in the modulation of human EGFR functionality. It is of further interest in future to thoroughly understand the associated data to clarify the various roles played by post translational modifications (PTM) in human EGFR.