Difference between revisions of "YGL227W"

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'''Description of YGL227W:''' Protein involved in proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase); binds FBPase; shifts the balance of nitrogen metabolism toward glutamate production; localizes to the nucleus and the cytoplasm<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|S000126559}} PMID 18508925</ref><ref name='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 {{SGDpaper|S000074185}} PMID 14562095</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='S000061424'>van der Merwe GK, et al. (2001) Ammonia regulates VID30 expression and Vid30p function shifts nitrogen metabolism toward glutamate formation especially when Saccharomyces cerevisiae is grown in low concentrations of ammonia. J Biol Chem 276(31):28659-66
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'''Description of YGL227W:''' Protein involved in proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase); binds FBPase; shifts the balance of nitrogen metabolism toward glutamate production; localizes to the nucleus and the cytoplasm<ref name='S000061424'>van der Merwe GK, et al. (2001) Ammonia regulates VID30 expression and Vid30p function shifts nitrogen metabolism toward glutamate formation especially when Saccharomyces cerevisiae is grown in low concentrations of ammonia. J Biol Chem 276(31):28659-66 {{SGDpaper|S000061424}} PMID 11356843</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='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 {{SGDpaper|S000074185}} PMID 14562095</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
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  {{SGDpaper|S000126559}} PMID 18508925</ref>
 
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Revision as of 14:05, 31 March 2009

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Systematic name YGL227W
Gene name VID30
Aliases GID1
Feature type ORF, Verified
Coordinates Chr VII:69671..72547
Primary SGDID S000003196


Description of YGL227W: Protein involved in proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase); binds FBPase; shifts the balance of nitrogen metabolism toward glutamate production; localizes to the nucleus and the cytoplasm[1][2][3][4]




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References

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  1. van der Merwe GK, et al. (2001) Ammonia regulates VID30 expression and Vid30p function shifts nitrogen metabolism toward glutamate formation especially when Saccharomyces cerevisiae is grown in low concentrations of ammonia. J Biol Chem 276(31):28659-66 SGD PMID 11356843
  2. 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
  3. Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 SGD PMID 14562095
  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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