Difference between revisions of "YCR069W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000665 YCR069W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CPR4 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CPR4 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr III: | + | |nowrap| Chr III:239055..240011 |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000665 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000665 | ||
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| − | '''Description of YCR069W:''' Peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway<ref name=' | + | '''Description of YCR069W:''' Peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway<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='S000040196'>Franco L, et al. (1991) The nucleotide sequence of a third cyclophilin-homologous gene from Saccharomyces cerevisiae. Yeast 7(9):971-9 |
| − | {{SGDpaper| | + | {{SGDpaper|S000040196}} PMID 1803821</ref> |
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Latest revision as of 07:45, 23 January 2012
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| Systematic name | YCR069W |
| Gene name | CPR4 |
| Aliases | CYP4, SCC3, YCR070W |
| Feature type | ORF, Verified |
| Coordinates | Chr III:239055..240011 |
| Primary SGDID | S000000665 |
Description of YCR069W: Peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway[1][2]
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References
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- ↑ 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
- ↑ Franco L, et al. (1991) The nucleotide sequence of a third cyclophilin-homologous gene from Saccharomyces cerevisiae. Yeast 7(9):971-9 SGD PMID 1803821
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