Difference between revisions of "YBR105C"
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| − | '''Description of YBR105C:''' Peripheral membrane protein located at Vid (vacuole import and degradation) vesicles; regulates fructose-1,6-bisphosphatase (FBPase) targeting to the vacuole; promotes proteasome-dependent catabolite degradation of FBPase<ref name=' | + | '''Description of YBR105C:''' Peripheral membrane protein located at Vid (vacuole import and degradation) vesicles; regulates fructose-1,6-bisphosphatase (FBPase) targeting to the vacuole; promotes proteasome-dependent catabolite degradation of FBPase<ref name='S000045301'>Chiang MC and Chiang HL (1998) Vid24p, a novel protein localized to the fructose-1, 6-bisphosphatase-containing vesicles, regulates targeting of fructose-1,6-bisphosphatase from the vesicles to the vacuole for degradation. J Cell Biol 140(6):1347-56 {{SGDpaper|S000045301}} PMID 9508768</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| | + | {{SGDpaper|S000126559}} PMID 18508925</ref> |
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Revision as of 14:05, 31 March 2009
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| Systematic name | YBR105C |
| Gene name | VID24 |
| Aliases | GID4 |
| Feature type | ORF, Verified |
| Coordinates | Chr II:451963..450875 |
| Primary SGDID | S000000309 |
Description of YBR105C: Peripheral membrane protein located at Vid (vacuole import and degradation) vesicles; regulates fructose-1,6-bisphosphatase (FBPase) targeting to the vacuole; promotes proteasome-dependent catabolite degradation of FBPase[1][2][3]
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References
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- ↑ Chiang MC and Chiang HL (1998) Vid24p, a novel protein localized to the fructose-1, 6-bisphosphatase-containing vesicles, regulates targeting of fructose-1,6-bisphosphatase from the vesicles to the vacuole for degradation. J Cell Biol 140(6):1347-56 SGD PMID 9508768
- ↑ 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
- ↑ 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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