YFR010W - Revision history

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2008-12-19T11:15:51Z

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@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001906 YFR010W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001906 YFR010W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''UBP6 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr VI:165060..166559
+|nowrap| Chr VI:165067..166566
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000001906

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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='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
+'''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>
+  {{SGDpaper|S000136872}} PMID 20850176</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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
+'''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='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|S000123199}} PMID 17190603</ref>
+  {{SGDpaper|S000039756}} PMID 9344467</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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='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='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='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
+'''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|S000039756}} PMID 9344467</ref>
+  {{SGDpaper|S000123199}} PMID 17190603</ref>
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 <br>