Datasets from an interaction proteomics screen for substrates of the SCFβTrCP ubiquitin ligase

Data in Brief

Shabaz Mohammed¹  Albert J.R. Heck¹  Mao Peng¹  Teck Yew Low¹  Roberto Magliozzi²  Daniele Guardavaccaro² 

[1] Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 H Utrecht, The Netherlands;Hubrecht Institute-KNAW and University Medical Center Utrecht, Uppsalalaan 8, 3584 CH Utrecht, The Netherlands;

关键词: βTrCP;    SCF ubiquitin ligase;    F-box protein;    Affinity purification-mass spectrometry (AP-MS);    Proteomics;   

DOI  :  10.1016/j.dib.2015.05.003

来源: DOAJ

【 摘 要 】

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. Sci. Signal. 7 (2014) rs8–rs8, 10.1126/scisignal.2005882.

【 授权许可】

Unknown