[Bioinformatics advances in protein ubiquitination]

Yi Chuan. 2013 Jan;35(1):17-26. doi: 10.3724/sp.j.1005.2013.00017.
[Article in Chinese]

Abstract

Ubiquitin-proteasome system (UPS) mediates 80% to 85% of the protein degradation in eukaryotic cells. The characteristics of UPS pathway are dependent on ATP, efficient and highly selective. Ubiquitination not only participates in protein degradation, but also directly affects protein activity and localization. Ubiquitination can regulate multiple cellular processes including cell cycle progression, apoptosis, transcriptional regulation, DNA damage repair and immune response. More and more datasets about UPS are published, and it is necessary to organize and analyze these data efficiently. We re-view the related bioinformatics studies in UPS datasets, such as collection of UPS related proteins, construction and analysis of ubiquitination networks, prediction of ubiquitination sites and motifs. Some potential perspectives are also discussed.

Publication types

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

MeSH terms

  • Animals
  • Computational Biology*
  • Humans
  • Proteasome Endopeptidase Complex / chemistry
  • Proteasome Endopeptidase Complex / genetics
  • Proteasome Endopeptidase Complex / metabolism
  • Proteins / chemistry
  • Proteins / genetics
  • Proteins / metabolism*
  • Ubiquitin
  • Ubiquitination

Substances

  • Proteins
  • Ubiquitin
  • Proteasome Endopeptidase Complex