Difference between revisions of "YHR057C"
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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=S000001099 YHR057C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CPR2 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CPR2 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr VIII: | + | |nowrap| Chr VIII:218843..218226 |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001099 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001099 | ||
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| − | '''Description of YHR057C:''' 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='S000047852'>Koser PL, et al. (1991) The CYP2 gene of Saccharomyces cerevisiae encodes a cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase with an N-terminal signal sequence. Gene 108(1):73-80 {{SGDpaper|S000047852}} PMID 1761234 | + | '''Description of YHR057C:''' 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='S000047852'>Koser PL, et al. (1991) The CYP2 gene of Saccharomyces cerevisiae encodes a cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase with an N-terminal signal sequence. Gene 108(1):73-80 {{SGDpaper|S000047852}} PMID 1761234</ref><ref name='S000039299'>Sykes K, et al. (1993) Proline isomerases function during heat shock. Proc Natl Acad Sci U S A 90(12):5853-7 |
{{SGDpaper|S000039299}} PMID 7685914</ref> | {{SGDpaper|S000039299}} PMID 7685914</ref> | ||
<br> | <br> | ||
Latest revision as of 07:45, 23 January 2012
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| Systematic name | YHR057C |
| Gene name | CPR2 |
| Aliases | CYP2 |
| Feature type | ORF, Verified |
| Coordinates | Chr VIII:218843..218226 |
| Primary SGDID | S000001099 |
Description of YHR057C: 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][3]
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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
- ↑ Koser PL, et al. (1991) The CYP2 gene of Saccharomyces cerevisiae encodes a cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase with an N-terminal signal sequence. Gene 108(1):73-80 SGD PMID 1761234
- ↑ Sykes K, et al. (1993) Proline isomerases function during heat shock. Proc Natl Acad Sci U S A 90(12):5853-7 SGD PMID 7685914
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