Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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 RIS Download

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

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.