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

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-funct...

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Autores principales: Malik, Arshi, Afaq, Sarah, Alwabli, Afaf S, Al-ghmady, Khalid
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2019
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6704328/
https://www.ncbi.nlm.nih.gov/pubmed/31485130
http://dx.doi.org/10.6026/97320630015448
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author Malik, Arshi
Afaq, Sarah
Alwabli, Afaf S
Al-ghmady, Khalid
author_facet Malik, Arshi
Afaq, Sarah
Alwabli, Afaf S
Al-ghmady, Khalid
author_sort Malik, Arshi
collection PubMed
description 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.
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spelling pubmed-67043282019-09-04 Networking of predicted post-translational modification (PTM) sites in human EGFR Malik, Arshi Afaq, Sarah Alwabli, Afaf S Al-ghmady, Khalid Bioinformation Research Article 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. Biomedical Informatics 2019-07-31 /pmc/articles/PMC6704328/ /pubmed/31485130 http://dx.doi.org/10.6026/97320630015448 Text en © 2019 Biomedical Informatics http://creativecommons.org/licenses/by/3.0/ 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.
spellingShingle Research Article
Malik, Arshi
Afaq, Sarah
Alwabli, Afaf S
Al-ghmady, Khalid
Networking of predicted post-translational modification (PTM) sites in human EGFR
title Networking of predicted post-translational modification (PTM) sites in human EGFR
title_full Networking of predicted post-translational modification (PTM) sites in human EGFR
title_fullStr Networking of predicted post-translational modification (PTM) sites in human EGFR
title_full_unstemmed Networking of predicted post-translational modification (PTM) sites in human EGFR
title_short Networking of predicted post-translational modification (PTM) sites in human EGFR
title_sort networking of predicted post-translational modification (ptm) sites in human egfr
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6704328/
https://www.ncbi.nlm.nih.gov/pubmed/31485130
http://dx.doi.org/10.6026/97320630015448
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