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

Jaymin J. Kathiriya; Ravi Ramesh Pathak; Alexandr Bezginov; Bin Xue; Vladimir N. Uversky; Elisabeth R.M. Tillier; Vrushank Davé

doi:10.1016/j.dib.2016.11.099

Data in Brief (Feb 2017)

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

Jaymin J. Kathiriya,
Ravi Ramesh Pathak,
Alexandr Bezginov,
Bin Xue,
Vladimir N. Uversky,
Elisabeth R.M. Tillier,
Vrushank Davé

Affiliations

Jaymin J. Kathiriya: Morsani College of Medicine, Department of Pathology and Cell Biology, University of South Florida, Tampa, FL 33612, USA
Ravi Ramesh Pathak: Morsani College of Medicine, Department of Pathology and Cell Biology, University of South Florida, Tampa, FL 33612, USA
Alexandr Bezginov: Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada
Bin Xue: Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, FL 33620, USA
Vladimir N. Uversky: Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA
Elisabeth R.M. Tillier: Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada
Vrushank Davé: Morsani College of Medicine, Department of Pathology and Cell Biology, University of South Florida, Tampa, FL 33612, USA

DOI: https://doi.org/10.1016/j.dib.2016.11.099
Journal volume & issue: Vol. 10, no. C
pp. 315 – 324

Abstract

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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].

Published in Data in Brief

ISSN: 2352-3409 (Online)
Publisher: Elsevier
Country of publisher: United States
LCC subjects: Medicine: Medicine (General): Computer applications to medicine. Medical informatics; Science: Science (General)
Website: http://www.journals.elsevier.com/data-in-brief/

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