Difference between revisions of "YDR304C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.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 | |nowrap| Chr IV:1072553..1071876 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002712 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''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|S000046250}} PMID 9371805</ref> | {{SGDpaper|S000046250}} PMID 9371805</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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<protect> | <protect> | ||
Revision as of 08:46, 27 February 2007
Share your knowledge...Edit this entry! <protect>
| Systematic name | YDR304C |
| Gene name | CPR5 |
| Aliases | CYP5 |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:1072553..1071876 |
| 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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- ↑ 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
- ↑ 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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