Difference between revisions of "YDR255C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YDR255C YDR255C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002663 YDR255C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''RMD5 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''RMD5 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr IV:967818..966553
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|nowrap| Chr IV:967822..966557
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000002663
 
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'''Description of {{PAGENAME}}:''' Cytosolic protein required for sporulation; also required for the ubiquitination of the gluconeogenetic enzyme fructose-1,6-bisphosphatase, which is degraded rapidly after the switch from gluconeogenesis to glycolysis<ref name='S000072993'>Regelmann J, et al. (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63 {{SGDpaper|S000072993}} PMID 12686616</ref><ref name='S000072583'>Enyenihi AH and Saunders WS (2003) Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics 163(1):47-54
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'''Description of YDR255C:''' Component of GID Complex that confers ubiquitin ligase (U3) activity; necessary for polyubiquitination and degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase; forms dimer with Fyv10p that is then recruited to GID Complex by Gid8p; also required for sporulation; conserved protein that has a degenerate RING finger domain<ref name='S000072583'>Enyenihi AH and Saunders WS (2003) Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics 163(1):47-54 {{SGDpaper|S000072583}} PMID 12586695</ref><ref name='S000149618'>Menssen R, et al. (2012) Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite induced degradation of gluconeogenic enzymes. J Biol Chem () {{SGDpaper|S000149618}} PMID 22645139</ref><ref name='S000072993'>Regelmann J, et al. (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63 {{SGDpaper|S000072993}} PMID 12686616</ref><ref name='S000126559'>Santt O, et al. (2008) The Yeast GID Complex, a Novel Ubiquitin Ligase (E3) Involved in the Regulation of Carbohydrate Metabolism. Mol Biol Cell 19(8):3323-33
  {{SGDpaper|S000072583}} PMID 12586695</ref>
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  {{SGDpaper|S000126559}} PMID 18508925</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 13:05, 27 August 2012

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Systematic name YDR255C
Gene name RMD5
Aliases GID2
Feature type ORF, Verified
Coordinates Chr IV:967822..966557
Primary SGDID S000002663


Description of YDR255C: Component of GID Complex that confers ubiquitin ligase (U3) activity; necessary for polyubiquitination and degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase; forms dimer with Fyv10p that is then recruited to GID Complex by Gid8p; also required for sporulation; conserved protein that has a degenerate RING finger domain[1][2][3][4]




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Community Commentary

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References

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  1. Enyenihi AH and Saunders WS (2003) Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics 163(1):47-54 SGD PMID 12586695
  2. Menssen R, et al. (2012) Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite induced degradation of gluconeogenic enzymes. J Biol Chem () SGD PMID 22645139
  3. Regelmann J, et al. (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63 SGD PMID 12686616
  4. Santt O, et al. (2008) The Yeast GID Complex, a Novel Ubiquitin Ligase (E3) Involved in the Regulation of Carbohydrate Metabolism. Mol Biol Cell 19(8):3323-33 SGD PMID 18508925

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