Difference between revisions of "YDR155C"
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| − | '''Description of YDR155C:''' Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A<ref name=' | + | '''Description of YDR155C:''' Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A<ref name='S000056928'>Haendler B, et al. (1989) Yeast cyclophilin: isolation and characterization of the protein, cDNA and gene. Gene 83(1):39-46 {{SGDpaper|S000056928}} PMID 2687115</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| | + | {{SGDpaper|S000046250}} PMID 9371805</ref> |
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Revision as of 14:05, 16 January 2009
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| Systematic name | YDR155C |
| Gene name | CPR1 |
| Aliases | CPH1, CYP1 |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:768998..768510 |
| Primary SGDID | S000002562 |
Description of YDR155C: Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A[1][2]
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References
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- ↑ Haendler B, et al. (1989) Yeast cyclophilin: isolation and characterization of the protein, cDNA and gene. Gene 83(1):39-46 SGD PMID 2687115
- ↑ 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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