Difference between revisions of "YHR057C"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YHR057C YHR057C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.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:218845..218228
 
|nowrap| Chr VIII:218845..218228
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000001099
 
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'''Description of {{PAGENAME}}:''' 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</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><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
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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</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><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>
 
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Revision as of 08:45, 27 February 2007

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Systematic name YHR057C
Gene name CPR2
Aliases CYP2
Feature type ORF, Verified
Coordinates Chr VIII:218845..218228
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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  1. 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
  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
  3. 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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