Difference between revisions of "YNL135C"
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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=S000005079 YNL135C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''FPR1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''FPR1 '' | ||
Latest revision as of 07:45, 23 January 2012
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| Systematic name | YNL135C |
| Gene name | FPR1 |
| Aliases | FKB1, RBP1 |
| Feature type | ORF, Verified |
| Coordinates | Chr XIV:372226..371882 |
| Primary SGDID | S000005079 |
Description of YNL135C: Peptidyl-prolyl cis-trans isomerase (PPIase), binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function[1][2][3]
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Community Commentary
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References
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- ↑ Dolinski KJ and Heitman J (1999) Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase. Genetics 151(3):935-44 SGD PMID 10049913
- ↑ Heitman J, et al. (1991) FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 88(5):1948-52 SGD PMID 1705713
- ↑ Koltin Y, et al. (1991) Rapamycin sensitivity in Saccharomyces cerevisiae is mediated by a peptidyl-prolyl cis-trans isomerase related to human FK506-binding protein. Mol Cell Biol 11(3):1718-23 SGD PMID 1996117
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