Difference between revisions of "YGL141W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003109 YGL141W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HUL5 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HUL5 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr VII: | + | |nowrap| Chr VII:238353..241085 |
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| − | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003109 |
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| − | '''Description of {{ | + | '''Description of YGL141W:''' Multiubiquitin chain assembly factor (E4); proteasome processivity factor that elongates polyUb chains on substrates, opposing Ubp6p, a branched polyubiquitin protease; required for retrograde transport of misfolded proteins during ERAD<ref name='S000134383'>Aviram S and Kornitzer D (2010) The ubiquitin ligase Hul5 promotes proteasomal processivity. Mol Cell Biol 30(4):985-94 {{SGDpaper|S000134383}} PMID 20008553</ref><ref name='S000123199'>Crosas B, et al. (2006) Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell 127(7):1401-13 {{SGDpaper|S000123199}} PMID 17190603</ref><ref name='S000126190'>Kohlmann S, et al. (2008) Ubiquitin Ligase Hul5 Is Required for Fragment-specific Substrate Degradation in Endoplasmic Reticulum-associated Degradation. J Biol Chem 283(24):16374-83 {{SGDpaper|S000126190}} PMID 18436532</ref><ref name='S000042659'>Wang G, et al. (1999) Functional domains of the Rsp5 ubiquitin-protein ligase. Mol Cell Biol 19(1):342-52 |
{{SGDpaper|S000042659}} PMID 9858558</ref> | {{SGDpaper|S000042659}} PMID 9858558</ref> | ||
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==Community Commentary== | ==Community Commentary== | ||
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| + | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
| + | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
| + | J Biol Chem 278(5):3265-74</ref> | ||
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==References== | ==References== | ||
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Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YGL141W |
| Gene name | HUL5 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr VII:238353..241085 |
| Primary SGDID | S000003109 |
Description of YGL141W: Multiubiquitin chain assembly factor (E4); proteasome processivity factor that elongates polyUb chains on substrates, opposing Ubp6p, a branched polyubiquitin protease; required for retrograde transport of misfolded proteins during ERAD[1][2][3][4]
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Contents
Community Commentary
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References
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- ↑ Aviram S and Kornitzer D (2010) The ubiquitin ligase Hul5 promotes proteasomal processivity. Mol Cell Biol 30(4):985-94 SGD PMID 20008553
- ↑ Crosas B, et al. (2006) Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell 127(7):1401-13 SGD PMID 17190603
- ↑ Kohlmann S, et al. (2008) Ubiquitin Ligase Hul5 Is Required for Fragment-specific Substrate Degradation in Endoplasmic Reticulum-associated Degradation. J Biol Chem 283(24):16374-83 SGD PMID 18436532
- ↑ Wang G, et al. (1999) Functional domains of the Rsp5 ubiquitin-protein ligase. Mol Cell Biol 19(1):342-52 SGD PMID 9858558
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