Difference between revisions of "YOR202W"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
(Automated import of articles)
 
(7 intermediate revisions by the same user not shown)
Line 4: Line 4:
 
{|{{Prettytable}} align = 'right' width = '200px'
 
{|{{Prettytable}} align = 'right' width = '200px'
 
|-
 
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YOR202W YOR202W]  
+
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005728 YOR202W]  
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HIS3 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HIS3 ''
 
|-
 
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''          ||''HIS10''
+
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''          ||''HIS10, HIS8''
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''          || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''          || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XV:721947..722609
+
|nowrap| Chr XV:721946..722608
 +
|-
 +
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005728
 
|}
 
|}
 
<br>
 
<br>
'''Description of {{PAGENAME}}:''' Imidazoleglycerol-phosphate dehydratase, catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p<ref name='S000057959'>Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69 {{SGDpaper|S000057959}} PMID 8852895</ref><ref name='S000053704'>Pearce DA and Sherman F (1999) Toxicity of copper, cobalt, and nickel salts is dependent on histidine metabolism in the yeast Saccharomyces cerevisiae. J Bacteriol 181(16):4774-9 {{SGDpaper|S000053704}} PMID 10438744</ref><ref name='S000051610'>Hope IA and Struhl K (1985) GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthetic genes in yeast. Cell 43(1):177-88 {{SGDpaper|S000051610}} PMID 3907851</ref><ref name='S000048780'>Struhl K and Davis RW (1977) Production of a functional eukaryotic enzyme in Escherichia coli: cloning and expression of the yeast structural gene for imidazole-glycerolphosphate dehydratase (his3). Proc Natl Acad Sci U S A 74(12):5255-9
+
'''Description of YOR202W:''' Imidazoleglycerol-phosphate dehydratase, catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p<ref name='S000057959'>Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69 {{SGDpaper|S000057959}} PMID 8852895</ref><ref name='S000122080'>Fink GR (1964) GENE-ENZYME RELATIONS IN HISTIDINE BIOSYNTHESIS IN YEAST. Science 146(3643):525-7 {{SGDpaper|S000122080}} PMID 14190241</ref><ref name='S000051610'>Hope IA and Struhl K (1985) GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthetic genes in yeast. Cell 43(1):177-88 {{SGDpaper|S000051610}} PMID 3907851</ref><ref name='S000053704'>Pearce DA and Sherman F (1999) Toxicity of copper, cobalt, and nickel salts is dependent on histidine metabolism in the yeast Saccharomyces cerevisiae. J Bacteriol 181(16):4774-9 {{SGDpaper|S000053704}} PMID 10438744</ref><ref name='S000048780'>Struhl K and Davis RW (1977) Production of a functional eukaryotic enzyme in Escherichia coli: cloning and expression of the yeast structural gene for imidazole-glycerolphosphate dehydratase (his3). Proc Natl Acad Sci U S A 74(12):5255-9
 
  {{SGDpaper|S000048780}} PMID 341150</ref>
 
  {{SGDpaper|S000048780}} PMID 341150</ref>
 
<br>
 
<br>
Line 37: Line 39:
 
J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
-->
 
-->
 +
 +
  
 
<protect>
 
<protect>

Latest revision as of 07:45, 23 January 2012

Share your knowledge...Edit this entry! <protect>

Systematic name YOR202W
Gene name HIS3
Aliases HIS10, HIS8
Feature type ORF, Verified
Coordinates Chr XV:721946..722608
Primary SGDID S000005728


Description of YOR202W: Imidazoleglycerol-phosphate dehydratase, catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p[1][2][3][4][5]




</protect>

Community Commentary

About Community Commentary. Please share your knowledge!




<protect>

References

See Help:References on how to add references

  1. Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69 SGD PMID 8852895
  2. Fink GR (1964) GENE-ENZYME RELATIONS IN HISTIDINE BIOSYNTHESIS IN YEAST. Science 146(3643):525-7 SGD PMID 14190241
  3. Hope IA and Struhl K (1985) GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthetic genes in yeast. Cell 43(1):177-88 SGD PMID 3907851
  4. Pearce DA and Sherman F (1999) Toxicity of copper, cobalt, and nickel salts is dependent on histidine metabolism in the yeast Saccharomyces cerevisiae. J Bacteriol 181(16):4774-9 SGD PMID 10438744
  5. Struhl K and Davis RW (1977) Production of a functional eukaryotic enzyme in Escherichia coli: cloning and expression of the yeast structural gene for imidazole-glycerolphosphate dehydratase (his3). Proc Natl Acad Sci U S A 74(12):5255-9 SGD PMID 341150

See Help:Categories on how to add the wiki page for this gene to a Category </protect>