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Bioinformation. 2019 Jul 31;15(7):448-456. doi: 10.6026/97320630015448. eCollection 2019.

Networking of predicted post-translational modification (PTM) sites in human EGFR.

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Department of Clinical Biochemistry, College of Medicine, King Khalid University, Abha Kingdom of Saudi Arabia-61421.
Department of Biological Sciences, Faculty of Science, King Abdulaziz University, Jeddah 21589, Saudi Arabia.


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.


Cancer; EGFR; PTMs; interaction; pathways

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