Document Type
Article
Publication Date
2017
Keywords
Focal adhesion Kinase-1, Protein kinases, Evolution of intrinsically disordered regions, Cytoskeletal remodeling
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.dib.2016.11.099
Abstract
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].
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Data in Brief, v. 10, p. 315-324
Scholar Commons Citation
Kathiriya, Jaymin J.; Pathak, Ravi Ramesh; Bezginov, Alexandr; Xue, Bin; Uversky, Vladimir N.; Tillier, Elisabeth R.M.; and Davé, Vrushank, "Data on Evolution of Intrinsically Disordered Regions of the Human Kinome and Contribution of FAK1 IDRs to Cytoskeletal Remodeling" (2017). Molecular Medicine Faculty Publications. 308.
https://digitalcommons.usf.edu/mme_facpub/308
Supplementary Information
