Difference between revisions of "YEL012W"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YEL012W YEL012W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000738 YEL012W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''UBC8 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''UBC8 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|nowrap| Chr V:131772..132551
 
|nowrap| Chr V:131772..132551
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000738
 
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'''Description of {{PAGENAME}}:''' Ubiquitin-conjugating enzyme that negatively regulates gluconeogenesis by mediating the glucose-induced ubiquitination of fructose-1,6-bisphosphatase (FBPase); cytoplasmic enzyme that catalyzes the ubiquitination of histones in vitro<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='S000057612'>Kaiser P, et al. (1994) A human ubiquitin-conjugating enzyme homologous to yeast UBC8. J Biol Chem 269(12):8797-802 {{SGDpaper|S000057612}} PMID 8132613</ref><ref name='S000051223'>Qin S, et al. (1991) Cloning and characterization of a Saccharomyces cerevisiae gene encoding a new member of the ubiquitin-conjugating protein family. J Biol Chem 266(23):15549-54
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'''Description of YEL012W:''' Ubiquitin-conjugating enzyme that negatively regulates gluconeogenesis by mediating the glucose-induced ubiquitination of fructose-1,6-bisphosphatase (FBPase); cytoplasmic enzyme that catalyzes the ubiquitination of histones in vitro<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='S000057612'>Kaiser P, et al. (1994) A human ubiquitin-conjugating enzyme homologous to yeast UBC8. J Biol Chem 269(12):8797-802 {{SGDpaper|S000057612}} PMID 8132613</ref><ref name='S000051223'>Qin S, et al. (1991) Cloning and characterization of a Saccharomyces cerevisiae gene encoding a new member of the ubiquitin-conjugating protein family. J Biol Chem 266(23):15549-54
 
  {{SGDpaper|S000051223}} PMID 1869573</ref>
 
  {{SGDpaper|S000051223}} PMID 1869573</ref>
 
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Revision as of 07:45, 27 February 2007

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Systematic name YEL012W
Gene name UBC8
Aliases GID3
Feature type ORF, Verified
Coordinates Chr V:131772..132551
Primary SGDID S000000738


Description of YEL012W: Ubiquitin-conjugating enzyme that negatively regulates gluconeogenesis by mediating the glucose-induced ubiquitination of fructose-1,6-bisphosphatase (FBPase); cytoplasmic enzyme that catalyzes the ubiquitination of histones in vitro[1][2][3]




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References

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  1. 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
  2. Kaiser P, et al. (1994) A human ubiquitin-conjugating enzyme homologous to yeast UBC8. J Biol Chem 269(12):8797-802 SGD PMID 8132613
  3. Qin S, et al. (1991) Cloning and characterization of a Saccharomyces cerevisiae gene encoding a new member of the ubiquitin-conjugating protein family. J Biol Chem 266(23):15549-54 SGD PMID 1869573

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