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


Arshi Malik1,*, Sarah Afaq1, Afaf S. Alwabli2 and Khalid Al-ghmady2



1Department of Clinical Biochemistry, College of Medicine, King Khalid University, Abha Kingdom of Saudi Arabia 61421; 2Department of Biological Sciences, Faculty of Science, King Abdulaziz University, Jeddah 21589, Saudi Arabia.



Arshi Malik - Email:


Article Type

Research Article



Received May 23, 2019; Accepted June 6, 2019; Published July 31, 2019



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, pathways and interaction.



Malik et al. Bioinformation 15(7): 448-454 (2019)


Edited by

P Kangueane






Biomedical Informatics



 This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.