Difference between revisions of "YGL141W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003109 YGL141W]  
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|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:238358..241090
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|nowrap| Chr VII:238353..241085
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003109
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003109
 
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'''Description of YGL141W:''' Ubiquitin-conjugating enzyme (E4), elongates polyubiquitin chains on substrate proteins; works in opposition to Ubp6p polyubiquitin-shortening activity; required for retrograde transport of misfolded proteins into cytoplasm during ERAD<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><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
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'''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|S000126190}} PMID 18436532</ref>
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  {{SGDpaper|S000042659}} PMID 9858558</ref>
 
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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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References

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  1. Aviram S and Kornitzer D (2010) The ubiquitin ligase Hul5 promotes proteasomal processivity. Mol Cell Biol 30(4):985-94 SGD PMID 20008553
  2. 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
  3. 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
  4. 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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