Difference between revisions of "YNR028W"
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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=S000005311 YNR028W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CPR8 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CPR8 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XIV: | + | |nowrap| Chr XIV:676177..677103 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005311 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''Description of YNR028W:''' Peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; similarity to Cpr4p suggests 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> | {{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> | ||
Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YNR028W |
| Gene name | CPR8 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XIV:676177..677103 |
| Primary SGDID | S000005311 |
Description of YNR028W: Peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; similarity to Cpr4p suggests a potential role in the secretory pathway[1]
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