Difference between revisions of "YMR161W"
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− | '''Description of YMR161W:''' Co-chaperone for Hsp40p, anchored in the ER membrane; with its homolog Ydj1p promotes ER-associated protein degradation (ERAD) of integral membrane substrates; similar to E. coli DnaJ<ref name=' | + | '''Description of YMR161W:''' Co-chaperone for Hsp40p, anchored in the ER membrane; with its homolog Ydj1p promotes ER-associated protein degradation (ERAD) of integral membrane substrates; similar to E. coli DnaJ<ref name='S000072636'>Beilharz T, et al. (2003) Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae. J Biol Chem 278(10):8219-23 {{SGDpaper|S000072636}} PMID 12514182</ref><ref name='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 {{SGDpaper|S000074185}} PMID 14562095</ref><ref name='S000077133'>Huyer G, et al. (2004) Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J Biol Chem 279(37):38369-78 {{SGDpaper|S000077133}} PMID 15252059</ref><ref name='S000077458'>Youker RT, et al. (2004) Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol Biol Cell 15(11):4787-97 |
− | {{SGDpaper| | + | {{SGDpaper|S000077458}} PMID 15342786</ref> |
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Revision as of 14:05, 25 February 2010
Share your knowledge...Edit this entry! <protect>
Systematic name | YMR161W |
Gene name | HLJ1 |
Aliases | |
Feature type | ORF, Verified |
Coordinates | Chr XIII:577717..578391 |
Primary SGDID | S000004771 |
Description of YMR161W: Co-chaperone for Hsp40p, anchored in the ER membrane; with its homolog Ydj1p promotes ER-associated protein degradation (ERAD) of integral membrane substrates; similar to E. coli DnaJ[1][2][3][4]
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References
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- ↑ Beilharz T, et al. (2003) Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae. J Biol Chem 278(10):8219-23 SGD PMID 12514182
- ↑ Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 SGD PMID 14562095
- ↑ Huyer G, et al. (2004) Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J Biol Chem 279(37):38369-78 SGD PMID 15252059
- ↑ Youker RT, et al. (2004) Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol Biol Cell 15(11):4787-97 SGD PMID 15342786
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