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

## TL;DR

This paper presents datasets from a study identifying new substrates of the SCFβTrCP ubiquitin ligase using proteomics methods.

## Contribution

The study provides novel datasets of potential substrates of SCFβTrCP ubiquitin ligase identified through an interaction proteomics screen.

## Key findings

- Used AP-MS to identify substrates of SCFβTrCP ligase using βTrCP2 as bait.
- Distinguished substrates from non-specific binders using βTrCP2 mutants.
- Mass spectrometry data are publicly available in the PRIDE repository.

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