Difference between revisions of "YIL097W"
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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=S000001359 YIL097W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''FYV10 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''FYV10 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr IX: | + | |nowrap| Chr IX:180427..181977 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001359 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''Description of YIL097W:''' Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin<ref name='S000147292'>Braun B, et al. (2011) Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation. FEBS Lett () {{SGDpaper|S000147292}} PMID 22044534</ref><ref name='S000125883'>Khoury CM, et al. (2008) A TSC22-like motif defines a novel antiapoptotic protein family. FEMS Yeast Res 8(4):540-63 {{SGDpaper|S000125883}} PMID 18355271</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='S000072994'>Page N, et al. (2003) A Saccharomyces cerevisiae genome-wide mutant screen for altered sensitivity to K1 killer toxin. Genetics 163(3):875-94 {{SGDpaper|S000072994}} PMID 12663529</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> | {{SGDpaper|S000072993}} PMID 12686616</ref> | ||
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==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
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| + | <!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation --> | ||
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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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Latest revision as of 14:05, 27 August 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YIL097W |
| Gene name | FYV10 |
| Aliases | GID9 |
| Feature type | ORF, Verified |
| Coordinates | Chr IX:180427..181977 |
| Primary SGDID | S000001359 |
Description of YIL097W: Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin[1][2][3][4][5]
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Contents
Community Commentary
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References
See Help:References on how to add references
- ↑ Braun B, et al. (2011) Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation. FEBS Lett () SGD PMID 22044534
- ↑ Khoury CM, et al. (2008) A TSC22-like motif defines a novel antiapoptotic protein family. FEMS Yeast Res 8(4):540-63 SGD PMID 18355271
- ↑ 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
- ↑ Page N, et al. (2003) A Saccharomyces cerevisiae genome-wide mutant screen for altered sensitivity to K1 killer toxin. Genetics 163(3):875-94 SGD PMID 12663529
- ↑ 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
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