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Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
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Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe

Jun Adachi1, Marina Kishida1, Shio Watanabe1

  • 1Laboratory of Proteome Research, National Institute of Biomedical Innovation, Health and Nutrition, Ibaraki, Osaka, Japan.

Data in Brief
|December 23, 2015
PubMed

Insights

Researchers identified 539 ATP-binding proteins (ATPome), including 178 novel candidates, using an ATP competition assay. This work also established ATPome selectivity profiling for kinase inhibitors.

Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • ATP-binding proteins (ATPome) are crucial for cellular processes and disease pathogenesis.
  • Identifying and quantifying ATPome interactions is essential for biological understanding.

Purpose of the Study:

  • To identify and quantify ATP-binding proteins using a novel assay.
  • To establish an ATPome-wide selectivity profiling method for kinase inhibitors.

Main Methods:

  • Utilized an ATP competition assay to differentiate specific ATP-binding proteins from non-specific ones.
  • Developed ATPome selectivity profiling by expanding target analysis beyond the kinome.

Main Results:

  • Identified 539 proteins belonging to the ATPome, with 178 novel candidates.
  • Generated target profiles for staurosporine and (S)-crizotinib using the new profiling method.
  • Data deposited in ProteomeXchange (PXD001200).

Conclusions:

  • The study provides a comprehensive catalog of ATP-binding proteins.
  • Introduced a novel method for broader kinase inhibitor selectivity profiling, advancing drug discovery and understanding of cellular mechanisms.

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