Difference between revisions of "YDR304C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YDR304C YDR304C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002712 YDR304C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''CPR5 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''CPR5 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr IV:1072553..1071876
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|nowrap| Chr IV:1072557..1071880
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000002712
 
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'''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
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'''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>
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  {{SGDpaper|S000057713}} PMID 8377189</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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Latest revision as of 07:45, 23 January 2012

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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]




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References

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  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

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