Table of Contents
International Journal of Proteomics
Volume 2013 (2013), Article ID 857918, 12 pages
http://dx.doi.org/10.1155/2013/857918
Research Article

A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway

1Division of Immunology and Pathogenesis, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3200, USA
2Department of Protein Chemistry, Genentech Inc., South San Francisco, CA 94080, USA

Received 6 September 2012; Accepted 13 December 2012

Academic Editor: Mu Wang

Copyright © 2013 Veronica G. Anania et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

The supplemental figures included with this manuscript are biochemical analyses that demonstrate that KR-TCR╬▒ is modified on an internal, non-lysine residue. In addition, also included is a figure demonstrating that an endogenous, human protein is also ubiquitinated and degraded by the proteasome.

  1. Supplementary Figures