Difference between revisions of "YFR010W"
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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 of Hul5p<ref name=' | + | '''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 of Hul5p<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='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='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='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| | + | {{SGDpaper|S000123199}} PMID 17190603</ref> |
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Revision as of 13:05, 31 March 2009
Share your knowledge...Edit this entry! <protect>
| Systematic name | YFR010W |
| Gene name | UBP6 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr VI:165060..166559 |
| 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 polyubiquitin elongation activity of Hul5p[1][2][3][4][5]
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References
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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
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