Proteome-Wide Mapping of the Drosophila Acetylome Demonstrates a High Degree of Conservation of Lysine Acetylation

Brian T. Weinert, Sebastian A. Wagner, Heiko Horn, Peter Henriksen, Wenshe R. Liu, Jesper V. Olsen, Lars J. Jensen, Chunaram Choudhary*

*To whom correspondence should be addressed. E-mail: chuna.choudhary{at}cpr.ku.dk

This PDF file includes:

• Fig. S1. Functional annotation of Drosophila and human acetylomes.
• Fig. S2. Conservation of serine and threonine phosphorylation sites to either serine or threonine.
• Fig. S3. Summary of acetylation sites identified in E2-conjugating enzymes.
• Fig. S4. Sequence alignment of human E2 ubiquitin-conjugating enzymes.
• Fig. S5. Identification of UBC4 Lys⁹ acetylation in S. cerevisiae.
• Fig. S6. Identification of in vivo UBE2D3 Lys⁸ acetylation in human cells.
• Fig. S7. Confirmation of Lys⁸ acetylation in recombinant UBE2D3 purified from E. coli.
• Fig. S8. Effect of UBE2D3 Lys⁸ acetylation on ubiquitin thiolester formation.
• Fig. S9. Rescue of growth sensitivity in S. cerevisiae ubc4 mutant cells.
• Definitions of the columns for Tables S1 to S3
• Details regarding data availability
  

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Other Supplementary Material for this manuscript includes the following:

• Table S1 (Microsoft Excel format). List of Drosophila in vivo acetylation sites.
• Table S2 (Microsoft Excel format). Drosophila acetylated lysine conservation.
• Table S3 (Microsoft Excel format). Human acetylated lysine conservation.

[Download Tables S1 to S3 (Compressed)]

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© 2011 American Association for the Advancement of Science