Difference between revisions of "YJL130C"

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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=YJL130C YJL130C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003666 YJL130C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''URA2 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''URA2 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr X:172364..165720
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|nowrap| Chr X:172367..165723
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003666
 
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'''Description of {{PAGENAME}}:''' Bifunctional carbamoylphosphate synthetase (CPSase)-aspartate transcarbamylase (ATCase), catalyzes the first two enzymatic steps in the de novo biosynthesis of pyrimidines; both activities are subject to feedback inhibition by UTP<ref name='S000065636'>Lue PF and Kaplan JG (1969) The aspartate transcarbamylase and carbamoyl phosphate synthetase of yeast: a multi-functional enzyme complex. Biochem Biophys Res Commun 34(4):426-33 {{SGDpaper|S000065636}} PMID 5776390</ref><ref name='S000065623'>Lacroute F (1968) Regulation of pyrimidine biosynthesis in Saccharomyces cerevisiae. J Bacteriol 95(3):824-32 {{SGDpaper|S000065623}} PMID 5651325</ref><ref name='S000053452'>Denis-Duphil M (1989) Pyrimidine biosynthesis in Saccharomyces cerevisiae: the ura2 cluster gene, its multifunctional enzyme product, and other structural or regulatory genes involved in de novo UMP synthesis. Biochem Cell Biol 67(9):612-31 {{SGDpaper|S000053452}} PMID 2679804</ref><ref name='S000052014'>Antonelli R, et al. (1998) Carbamyl-phosphate synthetase domain of the yeast multifunctional protein Ura2 is necessary for aspartate transcarbamylase inhibition by UTP. FEBS Lett 422(2):170-4 {{SGDpaper|S000052014}} PMID 9489999</ref><ref name='S000050154'>Serre V, et al. (1999) Half of Saccharomyces cerevisiae carbamoyl phosphate synthetase produces and channels carbamoyl phosphate to the fused aspartate transcarbamoylase domain. J Biol Chem 274(34):23794-801
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'''Description of YJL130C:''' Bifunctional carbamoylphosphate synthetase (CPSase)-aspartate transcarbamylase (ATCase), catalyzes the first two enzymatic steps in the de novo biosynthesis of pyrimidines; both activities are subject to feedback inhibition by UTP<ref name='S000052014'>Antonelli R, et al. (1998) Carbamyl-phosphate synthetase domain of the yeast multifunctional protein Ura2 is necessary for aspartate transcarbamylase inhibition by UTP. FEBS Lett 422(2):170-4 {{SGDpaper|S000052014}} PMID 9489999</ref><ref name='S000053452'>Denis-Duphil M (1989) Pyrimidine biosynthesis in Saccharomyces cerevisiae: the ura2 cluster gene, its multifunctional enzyme product, and other structural or regulatory genes involved in de novo UMP synthesis. Biochem Cell Biol 67(9):612-31 {{SGDpaper|S000053452}} PMID 2679804</ref><ref name='S000065623'>Lacroute F (1968) Regulation of pyrimidine biosynthesis in Saccharomyces cerevisiae. J Bacteriol 95(3):824-32 {{SGDpaper|S000065623}} PMID 5651325</ref><ref name='S000065636'>Lue PF and Kaplan JG (1969) The aspartate transcarbamylase and carbamoyl phosphate synthetase of yeast: a multi-functional enzyme complex. Biochem Biophys Res Commun 34(4):426-33 {{SGDpaper|S000065636}} PMID 5776390</ref><ref name='S000050154'>Serre V, et al. (1999) Half of Saccharomyces cerevisiae carbamoyl phosphate synthetase produces and channels carbamoyl phosphate to the fused aspartate transcarbamoylase domain. J Biol Chem 274(34):23794-801
 
  {{SGDpaper|S000050154}} PMID 10446140</ref>
 
  {{SGDpaper|S000050154}} PMID 10446140</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
{{CommentaryHelp}}
 
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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<!--
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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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Latest revision as of 07:45, 23 January 2012

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Systematic name YJL130C
Gene name URA2
Aliases
Feature type ORF, Verified
Coordinates Chr X:172367..165723
Primary SGDID S000003666


Description of YJL130C: Bifunctional carbamoylphosphate synthetase (CPSase)-aspartate transcarbamylase (ATCase), catalyzes the first two enzymatic steps in the de novo biosynthesis of pyrimidines; both activities are subject to feedback inhibition by UTP[1][2][3][4][5]




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Community Commentary

About Community Commentary. Please share your knowledge!




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References

See Help:References on how to add references

  1. Antonelli R, et al. (1998) Carbamyl-phosphate synthetase domain of the yeast multifunctional protein Ura2 is necessary for aspartate transcarbamylase inhibition by UTP. FEBS Lett 422(2):170-4 SGD PMID 9489999
  2. Denis-Duphil M (1989) Pyrimidine biosynthesis in Saccharomyces cerevisiae: the ura2 cluster gene, its multifunctional enzyme product, and other structural or regulatory genes involved in de novo UMP synthesis. Biochem Cell Biol 67(9):612-31 SGD PMID 2679804
  3. Lacroute F (1968) Regulation of pyrimidine biosynthesis in Saccharomyces cerevisiae. J Bacteriol 95(3):824-32 SGD PMID 5651325
  4. Lue PF and Kaplan JG (1969) The aspartate transcarbamylase and carbamoyl phosphate synthetase of yeast: a multi-functional enzyme complex. Biochem Biophys Res Commun 34(4):426-33 SGD PMID 5776390
  5. Serre V, et al. (1999) Half of Saccharomyces cerevisiae carbamoyl phosphate synthetase produces and channels carbamoyl phosphate to the fused aspartate transcarbamoylase domain. J Biol Chem 274(34):23794-801 SGD PMID 10446140

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