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 '' | ||
Latest revision as of 07:45, 23 January 2012
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| 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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