Data on evolution of intrinsically disordered regions of the human kinome and contribution of FAK1 IDRs to cytoskeletal remodeling

We present data on the evolution of intrinsically disordered regions (IDRs) taking into account the entire human protein kinome. The evolutionary data of the IDRs with respect to the kinase domains (KDs) and kinases as a whole protein (WP) are reported. Further, we have reported its post translation...

Descripción completa

Detalles Bibliográficos
Autores principales: Kathiriya, Jaymin J., Pathak, Ravi Ramesh, Bezginov, Alexandr, Xue, Bin, Uversky, Vladimir N., Tillier, Elisabeth R.M., Davé, Vrushank
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Data Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5157709/
https://www.ncbi.nlm.nih.gov/pubmed/28004021
http://dx.doi.org/10.1016/j.dib.2016.11.099
Descripción
Sumario:We present data on the evolution of intrinsically disordered regions (IDRs) taking into account the entire human protein kinome. The evolutionary data of the IDRs with respect to the kinase domains (KDs) and kinases as a whole protein (WP) are reported. Further, we have reported its post translational modifications of FAK1 IDRs and their contribution to the cytoskeletal remodeling. We also report the data to build a protein-protein interaction (PPI) network of primary and secondary FAK1-interacting hybrid proteins. Detailed analysis of the data and its effect on FAK1-related functions have been described in “Structural pliability adjacent to the kinase domain highlights contribution of FAK1 IDRs to cytoskeletal remodeling” (Kathiriya et. al., 2016) [1].

Ejemplares similares