Difference between revisions of "YFR010W"
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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=S000001906 YFR010W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''UBP6 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''UBP6 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr VI: | + | |nowrap| Chr VI:165067..166566 |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001906 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001906 | ||
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| − | '''Description of YFR010W:''' Ubiquitin-specific protease situated in the base subcomplex of the 26S proteasome, releases free ubiquitin from branched polyubiquitin chains; works in opposition to polyubiquitin elongation activity | + | '''Description of YFR010W:''' Ubiquitin-specific protease situated in the base subcomplex of the 26S proteasome, releases free ubiquitin from branched polyubiquitin chains; works in opposition to Hul5p polyubiquitin elongation activity; mutant has aneuploidy tolerance<ref name='S000075272'>Chernova TA, et al. (2003) Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. J Biol Chem 278(52):52102-15 {{SGDpaper|S000075272}} PMID 14559899</ref><ref name='S000123199'>Crosas B, et al. (2006) Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell 127(7):1401-13 {{SGDpaper|S000123199}} PMID 17190603</ref><ref name='S000074981'>Guterman A and Glickman MH (2004) Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. J Biol Chem 279(3):1729-38 {{SGDpaper|S000074981}} PMID 14581483</ref><ref name='S000075243'>Hanna J, et al. (2003) Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Mol Cell Biol 23(24):9251-61 {{SGDpaper|S000075243}} PMID 14645527</ref><ref name='S000039756'>Park KC, et al. (1997) Purification and characterization of UBP6, a new ubiquitin-specific protease in Saccharomyces cerevisiae. Arch Biochem Biophys 347(1):78-84 {{SGDpaper|S000039756}} PMID 9344467</ref><ref name='S000136872'>Torres EM, et al. (2010) Identification of aneuploidy-tolerating mutations. Cell 143(1):71-83 |
| − | {{SGDpaper| | + | {{SGDpaper|S000136872}} PMID 20850176</ref> |
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Latest revision as of 07:45, 23 January 2012
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| Systematic name | YFR010W |
| Gene name | UBP6 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr VI:165067..166566 |
| Primary SGDID | S000001906 |
Description of YFR010W: Ubiquitin-specific protease situated in the base subcomplex of the 26S proteasome, releases free ubiquitin from branched polyubiquitin chains; works in opposition to Hul5p polyubiquitin elongation activity; mutant has aneuploidy tolerance[1][2][3][4][5][6]
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References
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- ↑ Chernova TA, et al. (2003) Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. J Biol Chem 278(52):52102-15 SGD PMID 14559899
- ↑ Crosas B, et al. (2006) Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell 127(7):1401-13 SGD PMID 17190603
- ↑ Guterman A and Glickman MH (2004) Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. J Biol Chem 279(3):1729-38 SGD PMID 14581483
- ↑ Hanna J, et al. (2003) Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Mol Cell Biol 23(24):9251-61 SGD PMID 14645527
- ↑ Park KC, et al. (1997) Purification and characterization of UBP6, a new ubiquitin-specific protease in Saccharomyces cerevisiae. Arch Biochem Biophys 347(1):78-84 SGD PMID 9344467
- ↑ Torres EM, et al. (2010) Identification of aneuploidy-tolerating mutations. Cell 143(1):71-83 SGD PMID 20850176
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