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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2003-3-20
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CFTR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cystic Fibrosis Transmembrane...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/HRD1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
303
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
91-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12646171-Amino Acid Sequence,
pubmed-meshheading:12646171-Animals,
pubmed-meshheading:12646171-Blotting, Western,
pubmed-meshheading:12646171-CHO Cells,
pubmed-meshheading:12646171-Cloning, Molecular,
pubmed-meshheading:12646171-Cricetinae,
pubmed-meshheading:12646171-Cystic Fibrosis Transmembrane Conductance Regulator,
pubmed-meshheading:12646171-DNA, Complementary,
pubmed-meshheading:12646171-Endoplasmic Reticulum,
pubmed-meshheading:12646171-HeLa Cells,
pubmed-meshheading:12646171-Humans,
pubmed-meshheading:12646171-Ligases,
pubmed-meshheading:12646171-Microscopy, Fluorescence,
pubmed-meshheading:12646171-Molecular Sequence Data,
pubmed-meshheading:12646171-Protein Structure, Tertiary,
pubmed-meshheading:12646171-Recombinant Proteins,
pubmed-meshheading:12646171-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12646171-Sequence Homology, Amino Acid,
pubmed-meshheading:12646171-Time Factors,
pubmed-meshheading:12646171-Tissue Distribution,
pubmed-meshheading:12646171-Transfection,
pubmed-meshheading:12646171-Ubiquitin,
pubmed-meshheading:12646171-Ubiquitin-Protein Ligases
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pubmed:year |
2003
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pubmed:articleTitle |
A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1.
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pubmed:affiliation |
Department of Biochemistry, George S. Wise Faculty of Life sciences, Tel Aviv University, Tel Aviv 69978, Israel. nadavera@post.tau.ac.il
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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