Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe.
Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe.
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DOI：
10.1016/j.dib.2015.10.018
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发表时间：
2015-12
期刊：
影响因子：
1.2
通讯作者：
Tomonaga T
中科院分区：
文献类型：
--
作者：
Adachi J;Kishida M;Watanabe S;Hashimoto Y;Fukamizu K;Tomonaga T
ATP和ATP结合蛋白（ATPome）之间的相互作用是常见的，并且是大多数细胞过程所必需的。因此，识别和量化这些相互作用对于理解基本的细胞机制和各种疾病的发病机制显然是重要的。我们使用ATP竞争试验（ATP和酰基-ATP探针之间的竞争），使我们能够区分特异性ATP结合蛋白和非特异性蛋白（Adachi等，2014）。结果，我们鉴定了539个蛋白，包括178个新的atp结合蛋白候选蛋白。我们还利用我们编目的ATPome列表建立了激酶抑制剂的ATPome选择性分析方法。通常情况下，激酶抑制剂的选择性分析只分析激酶组的选择性。在这个数据中，我们通过ATPome选择性分析的性能将分析目标从kinome扩展到ATPome，并获得了staurosporine和(S)-crizotinib的目标谱。采用这种方法的稿件所附带的数据（Adachi et al., 2014）已存入ProteomeXchange，识别码为PXD001200。
Interactions between ATP and ATP-binding proteins (ATPome) are common and are required for most cellular processes. Thus, it is clearly important to identify and quantify these interactions for understanding basic cellular mechanisms and the pathogenesis of various diseases. We used an ATP competition assay (competition between ATP and acyl-ATP probes) that enabled us to distinguish specific ATP-binding proteins from non-specific proteins (Adachi et al., 2014). As a result, we identified 539 proteins, including 178 novel ATP-binding protein candidates. We also established an ATPome selectivity profiling method for kinase inhibitors using our cataloged ATPome list. Normally only kinome selectivity is profiled in selectivity profiling of kinase inhibitors. In this data, we expand the profiled targets from the kinome to the ATPome through performance of ATPome selectivity profiling and obtained target profiles of staurosporine and (S)-crizotinib. The data accompanying the manuscript on this approach (Adachi et al., 2014) have been deposited to the ProteomeXchange with identifier PXD001200.