Difference between revisions of "YFR010W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YFR010W YFR010W]  
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|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:165060..166559
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|nowrap| Chr VI:165067..166566
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000001906
 
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'''Description of {{PAGENAME}}:''' Ubiquitin-specific protease situated in the base subcomplex of the 26S proteasome, releases free ubiquitin from branched polyubiquitin chains; deletion causes hypersensitivity to cycloheximide and other toxic compounds<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='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='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='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
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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 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|S000039756}} PMID 9344467</ref>
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  {{SGDpaper|S000136872}} PMID 20850176</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 06:45, 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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  1. 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
  2. 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
  3. 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
  4. 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
  5. 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
  6. Torres EM, et al. (2010) Identification of aneuploidy-tolerating mutations. Cell 143(1):71-83 SGD PMID 20850176

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