Protein ubiquitination plays critical roles in many biological processes. However, functional studies of protein ubiquitination in eukaryotic cells are limited by the ability to identify protein ubiquitination sites. Unbiased high-throughput screening methods are necessary to discover novel ubiquitination sites that play important roles in cellular regulation. Here, we describe an immunopurifi cation approach that enriches ubiquitin remnant-containing peptides to facilitate downstream mass spectrometry (MS) identifi cation of lysine ubiquitination sites. This approach can be utilized to identify ubiquitination sites from proteins in a complex mixture.
Xu, G., Deglincerti, A., Paige, J. S., & Jaffrey, S. R. (2014). Profiling lysine ubiquitination by selective enrichment of ubiquitin remnant-containing peptides. Methods in Molecular Biology, 1174, 57–71. https://doi.org/10.1007/978-1-4939-0944-5_4