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. 2017 Apr 15;31(8):802–815. doi: 10.1101/gad.296145.117

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© 2017 Liang et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 3. — The Ulp2 C-terminal domain and Csm1 contribute to desumoylation of nucleolar and kinetochore proteins. (A) Experimental scheme for SILAC-MS to quantify differential sumoylation in ulp2-781Δ versus wild-type using HIS₆-3xFlag-SMT3 (HF-SUMO). (B) Quantitative MS analysis. (Top panel) ulp2Δ versus wild type (gray bars) (de Albuquerque et al. 2016). (Middle panel) ulp2-781Δ versus wild type (black bars). (Bottom panel) csm1Δ versus wild type (black-outlined bars). Positive log₂ values indicate proteins whose sumoylation increases in the mutant. Shown is a subset of proteins previously shown by other studies to be sumoylated and/or to be Ulp2 substrates (see Supplemental Tables 2, 3 for a complete list of the modified proteins identified). The asterisk indicates protein not found with at least three unique peptides.