Datasets from an interaction proteomics screen for substrates of the SCFβTrCP ubiquitin ligase
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Publication date
2015-09-01
Authors
Magliozzi, Roberto
Peng, M
Mohammed, Shabaz
Guardavaccaro, Daniele
Heck, Albert J R
Low, T.Y.
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Document Type
Article
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Abstract
An affinity purification-mass spectrometry (AP-MS) method was employed to identify novel substrates of the SCFβTrCP ubiquitin ligase. A FLAG-HA tagged version of the F-box protein βTrCP2, the substrate recognition subunit of SCFβTrCP, was used as bait. βTrCP2 wild type and the two mutants βTrCP2-R447A and βTrCP2-ΔF were expressed and purified from HEK293T cells to be able to discriminate between potential substrates of SCFβTrCP and unspecific binders. Affinity-purified samples were analyzed by mass spectrometry-based proteomics, applying ultra-high performance liquid chromatography (UHPLC) coupled to high-resolution tandem mass spectrometry. The raw mass spectrometry data have been deposited to the PRIDE partner repository with the identifiers PXD001088 and PXD001224. The present dataset is associated with a research resource published in T.Y. Low, M. Peng, R. Magliozzi, S. Mohammed, D. Guardavaccaro, A.J.R. Heck, A systems-wide screen identifies substrates of the SCFβTrCP ubiquitin ligase.
Keywords
Affinity purification-mass spectrometry (AP-MS), F-box protein, Proteomics, SCF ubiquitin ligase, βTrCP, General, Education
Citation
Magliozzi, R, Peng, M, Mohammed, S, Guardavaccaro, D, Heck, A J R & Low, T Y 2015, 'Datasets from an interaction proteomics screen for substrates of the SCF βTrCP ubiquitin ligase', Data in Brief, vol. 4, pp. 229-234. https://doi.org/10.1016/j.dib.2015.05.003