Skip to main content
. 2014 Dec 19;16(2):192–201. doi: 10.15252/embr.201439152

Figure 1.

Figure 1

Ubiquitin is acetylated at K6 and K48
  1. Preparation of conjugated ubiquitin from cell lines. Cell lysates were subjected to immunoprecipitation using an anti-Ub (FK2) antibody. Asterisks indicate the antibody heavy and light chains.
  2. Summary of the identified PTMs modifying ubiquitin. More details are provided in Supplementary Fig S2.
  3. Structural view of the ubiquitin modification sites. The images were drawn from PDB 1F9J. Acetylation sites, blue. Phosphorylation sites, yellow. Hydrophobic patch, orange.
  4. MS/MS spectra identifying acetylation on endogenous ubiquitin at K6 (D) and K48 (E). For each panel, the upper spectra are obtained from cell-derived ubiquitin prepared in (A), and the lower spectra are from synthetic, isotopically labeled AQUA peptides. Identified b and y fragment ions are shown.
  5. Sample-derived peptides containing acetyllysine at either K6 (left) or K48 (right), and the synthetic, isotopically labeled counterparts co-eluted at the same retention times. The detected fragment ions are listed.

Source data are available online for this figure.