Difference between revisions of "YLR128W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YLR128W YLR128W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004118 YLR128W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''DCN1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''DCN1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XII:398531..399434
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|nowrap| Chr XII:398530..399433
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004118
 
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'''Description of {{PAGENAME}}:''' Putative Nedd8 ligase; binds Nedd8; involved in cullin neddylation; not essential; similar to C.elegans DCN-1; contains UBA-like ubiquitin-binding domain and a DUF298 domain<ref name='S000082188'>Kurz T, et al. (2005) The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature 435(7046):1257-61 {{SGDpaper|S000082188}} PMID 15988528</ref><ref name='S000059095'>Willer M, et al. (2000) Disruption and functional analysis of six ORFs on chromosome XII of saccharomyces cerevisiae: YLR124w, YLR125w, YLR126c, YLR127c, YLR128w and YLR129w. Yeast 16(15):1429-35
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'''Description of YLR128W:''' Scaffold-type E3 ligase required for cullin neddylation and ubiquitin ligase activation; contains a ubiquitin-binding domain (UBA) for ubiquitin and Nedd8 (Rub1p) interaction and a PONY domain involved in cullin binding and neddylation<ref name='S000082188'>Kurz T, et al. (2005) The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature 435(7046):1257-61 {{SGDpaper|S000082188}} PMID 15988528</ref><ref name='S000125334'>Kurz T, et al. (2008) Dcn1 functions as a scaffold-type e3 ligase for cullin neddylation. Mol Cell 29(1):23-35
  {{SGDpaper|S000059095}} PMID 11054824</ref>
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  {{SGDpaper|S000125334}} PMID 18206966</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 07:45, 23 January 2012

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Systematic name YLR128W
Gene name DCN1
Aliases
Feature type ORF, Verified
Coordinates Chr XII:398530..399433
Primary SGDID S000004118


Description of YLR128W: Scaffold-type E3 ligase required for cullin neddylation and ubiquitin ligase activation; contains a ubiquitin-binding domain (UBA) for ubiquitin and Nedd8 (Rub1p) interaction and a PONY domain involved in cullin binding and neddylation[1][2]




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References

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  1. Kurz T, et al. (2005) The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature 435(7046):1257-61 SGD PMID 15988528
  2. Kurz T, et al. (2008) Dcn1 functions as a scaffold-type e3 ligase for cullin neddylation. Mol Cell 29(1):23-35 SGD PMID 18206966

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