A potential proteasome-interacting motif within the ubiquitin-like domain of parkin and other proteins

Trends Biochem Sci. 2003 Jun;28(6):280-3. doi: 10.1016/S0968-0004(03)00092-6.


Parkin and other unrelated proteins contain a ubiquitin-like domain (UbLD). This article describes a motif that might be important in the interaction of UbLD-containing proteins (UbLPs) with the proteasome. The proteasome-interacting motif, which is conserved in a subset of UbLPs, such as parkin, Rad23 and several transcription factors, is likely to enable the UbLPs to form a complex with the proteasome for proteolysis or the recently discovered non-proteolytic functions of the proteasome.

Publication types

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

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Cysteine Endopeptidases / metabolism*
  • DNA Repair Enzymes
  • DNA Repair*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Humans
  • Ligases / metabolism*
  • Molecular Sequence Data
  • Multienzyme Complexes / metabolism*
  • Parkinson Disease / metabolism
  • Peptide Hydrolases / metabolism
  • Phylogeny
  • Proteasome Endopeptidase Complex
  • Sequence Homology, Amino Acid
  • Ubiquitin-Protein Ligases*
  • Ubiquitins / metabolism*


  • DNA-Binding Proteins
  • Multienzyme Complexes
  • Ubiquitins
  • RAD23A protein, human
  • Ubiquitin-Protein Ligases
  • parkin protein
  • Peptide Hydrolases
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex
  • Ligases
  • DNA Repair Enzymes