Datasets from an interaction proteomics screen for substrates of the SCF(βTrCP) ubiquitin ligase

Roberto Magliozzi, Mao Peng, Shabaz Mohammed, Daniele Guardavaccaro, Albert J R Heck, Teck Yew Low

Research output: Contribution to journal/periodicalArticleScientificpeer-review

Abstract

An affinity purification-mass spectrometry (AP-MS) method was employed to identify novel substrates of the SCF(βTrCP) ubiquitin ligase. A FLAG-HA tagged version of the F-box protein βTrCP2, the substrate recognition subunit of SCF(βTrCP), 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 SCF(βTrCP) 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 SCF(βTrCP) ubiquitin ligase. Sci. Signal. 7 (2014) rs8-rs8, 10.1126/scisignal.2005882.

Original languageEnglish
Pages (from-to)229-34
Number of pages6
JournalData in Brief
Volume4
DOIs
Publication statusPublished - Sep 2015

Fingerprint

Dive into the research topics of 'Datasets from an interaction proteomics screen for substrates of the SCF(βTrCP) ubiquitin ligase'. Together they form a unique fingerprint.

Cite this