TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum

Biochem J. 2005 Jun 1;388(Pt 2):647-55. doi: 10.1042/BJ20041241.


In the present study, the human TEB4 is identified as a novel ER (endoplasmic reticulum)-resident ubiquitin ligase. TEB4 has homologues in many species and has a number of remarkable properties. TEB4 contains a conserved RING (really interesting new gene) finger and 13 predicted transmembrane domains. The RING finger of TEB4 and its homologues is situated at the N-terminus and has the unconventional C4HC3 configuration. The N-terminus of TEB4 is located in the cytosol. We show that the isolated TEB4 RING domain catalyses ubiquitin ligation in vitro in a reaction that is ubiquitin Lys48-specific and involves UBC7 (ubiquitin-conjugating enzyme 7). These properties are reminiscent of E3 enzymes, which are involved in ER-associated protein degradation. TEB4 is an ER degradation substrate itself, promoting its own degradation in a RING finger- and proteasome-dependent manner.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Endoplasmic Reticulum / enzymology*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Protein Binding
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Ubiquitin / chemistry
  • Ubiquitin-Conjugating Enzymes / chemistry
  • Ubiquitin-Conjugating Enzymes / physiology
  • Ubiquitin-Protein Ligases / chemistry*
  • Ubiquitin-Protein Ligases / metabolism
  • Zinc Fingers


  • Membrane Proteins
  • Ubiquitin
  • UBE2G2 protein, human
  • Ubiquitin-Conjugating Enzymes
  • MARCHF6 protein, human
  • Ubiquitin-Protein Ligases