A method of mapping protein sumoylation sites by mass spectrometry using a modified small ubiquitin-like modifier 1 (SUMO-1) and a computational program.

@article{Knuesel2005AMO,
  title={A method of mapping protein sumoylation sites by mass spectrometry using a modified small ubiquitin-like modifier 1 (SUMO-1) and a computational program.},
  author={Matthew T. Knuesel and H. T. A. Cheung and Micah Hamady and Kristen K. B. Barthel and Xuedong Liu},
  journal={Molecular & cellular proteomics : MCP},
  year={2005},
  volume={4 10},
  pages={1626-36}
}
Post-translational modification by small ubiquitin-like modifier 1 (SUMO-1) is a highly conserved process from yeast to humans and plays important regulatory roles in many cellular processes. Sumoylation occurs at certain internal lysine residues of target proteins via an isopeptide bond linkage. Unlike ubiquitin whose carboxyl-terminal sequence is RGG, the tripeptide at the carboxyl terminus of SUMO is TGG. The presence of the arginine residue at the carboxyl terminus of ubiquitin allows… CONTINUE READING
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