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A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1.

The yeast hHrd1 is a ubiquitin-protein ligase (E3) involved in ER-associated degradation. It was originally identified by genetic methods as an E3 of the yeast cholesterol biosynthetic enzyme HMG-CoA reductase (HMGR). We report the identification and cloning of a human homologue of Hrd1 (hHrd1). Immunofluorescence imaging confirms that the endogenous hHrd1 resides in the ER and in vitro assay demonstrates that it has a ubiquitin-ligase activity. However, the homology between the human and yeast Hrd1 is limited to the N-terminal domain of the proteins, and hHrd1 does not appear to be involved in the degradation of mammalian HMGR.

Pubmed ID: 12646171


  • Nadav E
  • Shmueli A
  • Barr H
  • Gonen H
  • Ciechanover A
  • Reiss Y


Biochemical and biophysical research communications

Publication Data

March 28, 2003

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • CHO Cells
  • Cloning, Molecular
  • Cricetinae
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • DNA, Complementary
  • Endoplasmic Reticulum
  • HeLa Cells
  • Humans
  • Ligases
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Sequence Homology, Amino Acid
  • Time Factors
  • Tissue Distribution
  • Transfection
  • Ubiquitin
  • Ubiquitin-Protein Ligases