Difference between revisions of "YDR304C"

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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
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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='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
{{SGDpaper|S000057713}} PMID 8377189</ref>
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{{SGDpaper|S000046250}} PMID 9371805</ref>
 
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Revision as of 14:05, 16 January 2009

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Systematic name YDR304C
Gene name CPR5
Aliases CYP5
Feature type ORF, Verified
Coordinates Chr IV:1072554..1071877
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. 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
  2. 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

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