A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles
University of Copenhagen · Max Planck Institute of Biochemistry
Abstract
Post-translational modification of proteins by ubiquitin is a fundamentally important regulatory mechanism. However, proteome-wide analysis of endogenous ubiquitylation remains a challenging task, and almost always has relied on cells expressing affinity tagged ubiquitin. Here we combine single-step immunoenrichment of ubiquitylated peptides with peptide fractionation and high-resolution mass spectrometry to investigate endogenous ubiquitylation sites. We precisely map 11,054 endogenous putative ubiquitylation sites (diglycine-modified lysines) on 4,273 human proteins. The presented data set covers 67% of the known ubiquitylation sites and contains 10,254 novel sites on proteins with diverse cellular functions…
Citation impact
- FWCI
- 32.72
- Percentile
- 100%
- References
- 62
Authors
7Topics & keywords
- Ubiquitin
- Proteasome
- Proteome
- Cell biology
- Chemistry
- Endogeny
- Biology
- Biochemistry