Advances in characterizing ubiquitylation sites by mass spectrometry

Curr Opin Chem Biol. 2013 Feb;17(1):49-58. doi: 10.1016/j.cbpa.2012.12.009. Epub 2013 Jan 5.


The attachment of one or more ubiquitin moieties to proteins plays a central regulatory mechanism in eukaryotic cells. Protein ubiquitylation regulates numerous cellular processes, including protein degradation, signal transduction, DNA repair and cell division. The characterization of ubiquitylation is a two-fold challenge that involves the mapping of ubiquitylation sites and the determination of ubiquitin chain topology. This review focuses on the technical advances in the mass spectrometry-based characterization of ubiquitylation sites, which have recently involved the large-scale identification of ubiquitylation sites by peptide-level enrichment strategies. The discovery that ubiquitylation is a widespread modification similar to phosphorylation and acetylation suggests cross-talk may also occur at the post translational modification level.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Humans
  • Mass Spectrometry / methods*
  • Molecular Sequence Data
  • Ubiquitin / chemistry
  • Ubiquitin / metabolism*
  • Ubiquitinated Proteins / chemistry
  • Ubiquitinated Proteins / metabolism*
  • Ubiquitination*


  • Ubiquitin
  • Ubiquitinated Proteins