[HTML][HTML] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
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 …
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 …