Difference between revisions of "YDR304C"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
 
(Automated import of articles)
 
(8 intermediate revisions by the same user not shown)
Line 1: Line 1:
 
<!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN-->
 
<!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN-->
 
{{PageTop}}
 
{{PageTop}}
 +
<protect>
 
{|{{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=YDR304C YDR304C]  
+
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002712 YDR304C]  
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''CPR5 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''CPR5 ''
Line 12: Line 13:
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr IV:1072553..1071876
+
|nowrap| Chr IV:1072557..1071880
 
|-
 
|-
|colspan = '3'|{{Don'tEditThisBox}}
+
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000002712
 
|}
 
|}
 
<br>
 
<br>
'''Description of {{PAGENAME}}:''' Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the endoplasmic reticulum, catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER<ref name='S000057713'>Frigerio G and Pelham HR (1993) A Saccharomyces cerevisiae cyclophilin resident in the endoplasmic reticulum. J Mol Biol 233(1):183-8 {{SGDpaper|S000057713}} PMID 8377189</ref><ref name='S000046250'>Dolinski K, et al. (1997) All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 94(24):13093-8
+
'''Description of YDR304C:''' Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the endoplasmic reticulum, catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER<ref name='S000046250'>Dolinski K, et al. (1997) All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 94(24):13093-8 {{SGDpaper|S000046250}} PMID 9371805</ref><ref name='S000057713'>Frigerio G and Pelham HR (1993) A Saccharomyces cerevisiae cyclophilin resident in the endoplasmic reticulum. J Mol Biol 233(1):183-8
  {{SGDpaper|S000046250}} PMID 9371805</ref>
+
  {{SGDpaper|S000057713}} PMID 8377189</ref>
 
<br>
 
<br>
 
<br>
 
<br>
 
<br>
 
<br>
 
<br>
 
<br>
 
+
<br>
 +
</protect>
 
__TOC__
 
__TOC__
 
==Community Commentary==
 
==Community Commentary==
 
{{CommentaryHelp}}
 
{{CommentaryHelp}}
  
 +
 +
 +
 +
<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
 +
<!--
 +
Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
 +
<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.
 +
J Biol Chem 278(5):3265-74</ref>
 +
-->
 +
 +
 +
 +
<protect>
 
==References==
 
==References==
 
<!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 
<!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 
{{RefHelp}}
 
{{RefHelp}}
 +
</protect>

Latest revision as of 07:45, 23 January 2012

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

Systematic name YDR304C
Gene name CPR5
Aliases CYP5
Feature type ORF, Verified
Coordinates Chr IV:1072557..1071880
Primary SGDID S000002712


Description of YDR304C: Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the endoplasmic reticulum, catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER[1][2]




</protect>

Community Commentary

About Community Commentary. Please share your knowledge!




<protect>

References

See Help:References on how to add references

  1. Dolinski K, et al. (1997) All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 94(24):13093-8 SGD PMID 9371805
  2. Frigerio G and Pelham HR (1993) A Saccharomyces cerevisiae cyclophilin resident in the endoplasmic reticulum. J Mol Biol 233(1):183-8 SGD PMID 8377189

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