Difference between revisions of "YNL135C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YNL135C YNL135C]  
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|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:372228..371884
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|nowrap| Chr XIV:372226..371882
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005079
 
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'''Description of {{PAGENAME}}:''' 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
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'''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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==Community Commentary==
 
==Community Commentary==
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 06:45, 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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References

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  1. 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
  2. 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
  3. 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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