Difference between revisions of "YNL135C"
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{|{{Prettytable}} align = 'right' width = '200px' | {|{{Prettytable}} align = 'right' width = '200px' | ||
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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 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XIV: | + | |nowrap| Chr XIV:372226..371882 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005079 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''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<ref name='S000063091'>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 {{SGDpaper|S000063091}} PMID 10049913</ref><ref name='S000054822'>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 {{SGDpaper|S000054822}} PMID 1705713</ref><ref name='S000041838'>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 |
{{SGDpaper|S000041838}} PMID 1996117</ref> | {{SGDpaper|S000041838}} PMID 1996117</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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Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| 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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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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