Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe
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 competiti...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2015-12-01
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| Series: | Data in Brief |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340915002668 |
| _version_ | 1818217875416023040 |
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| author | Jun Adachi Marina Kishida Shio Watanabe Yuuki Hashimoto Kazuna Fukamizu Takeshi Tomonaga |
| author_facet | Jun Adachi Marina Kishida Shio Watanabe Yuuki Hashimoto Kazuna Fukamizu Takeshi Tomonaga |
| author_sort | Jun Adachi |
| collection | DOAJ |
| description | 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) [1]. 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) [1] have been deposited to the ProteomeXchange with identifier PXD001200. |
| first_indexed | 2024-12-12T07:14:49Z |
| format | Article |
| id | doaj.art-63dc63c9039a478894c8ebb14a1b6805 |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-12T07:14:49Z |
| publishDate | 2015-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-63dc63c9039a478894c8ebb14a1b68052022-12-22T00:33:33ZengElsevierData in Brief2352-34092015-12-015C72672910.1016/j.dib.2015.10.018Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probeJun AdachiMarina KishidaShio WatanabeYuuki HashimotoKazuna FukamizuTakeshi TomonagaInteractions 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) [1]. 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) [1] have been deposited to the ProteomeXchange with identifier PXD001200.http://www.sciencedirect.com/science/article/pii/S2352340915002668 |
| spellingShingle | Jun Adachi Marina Kishida Shio Watanabe Yuuki Hashimoto Kazuna Fukamizu Takeshi Tomonaga Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe Data in Brief |
| title | Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe |
| title_full | Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe |
| title_fullStr | Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe |
| title_full_unstemmed | Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe |
| title_short | Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe |
| title_sort | data for proteomic analysis of atp binding proteins and kinase inhibitor target proteins using an atp probe |
| url | http://www.sciencedirect.com/science/article/pii/S2352340915002668 |
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