Difference between revisions of "YLR449W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YLR449W YLR449W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004441 YLR449W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''FPR4 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''FPR4 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XII:1030830..1032008
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|nowrap| Chr XII:1030834..1032012
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004441
 
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'''Description of {{PAGENAME}}:''' Peptidyl-prolyl cis-trans isomerase (PPIase) (proline isomerase) localized to the nucleus; catalyzes isomerization of proline residues in histones H3 and H4, which affects lysine methylation of those histones<ref name='S000118781'>Nelson CJ, et al. (2006) Proline isomerization of histone h3 regulates lysine methylation and gene expression. Cell 126(5):905-16 {{SGDpaper|S000118781}} PMID 16959570</ref><ref name='S000061678'>Davey M, et al. (2000) The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Mol Gen Genet 263(3):520-6 {{SGDpaper|S000061678}} PMID 10821187</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
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'''Description of YLR449W:''' Peptidyl-prolyl cis-trans isomerase (PPIase) (proline isomerase) localized to the nucleus; catalyzes isomerization of proline residues in histones H3 and H4, which affects lysine methylation of those histones<ref name='S000061678'>Davey M, et al. (2000) The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Mol Gen Genet 263(3):520-6 {{SGDpaper|S000061678}} PMID 10821187</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='S000118781'>Nelson CJ, et al. (2006) Proline isomerization of histone h3 regulates lysine methylation and gene expression. Cell 126(5):905-16
  {{SGDpaper|S000046250}} PMID 9371805</ref>
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  {{SGDpaper|S000118781}} PMID 16959570</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 YLR449W
Gene name FPR4
Aliases
Feature type ORF, Verified
Coordinates Chr XII:1030834..1032012
Primary SGDID S000004441


Description of YLR449W: Peptidyl-prolyl cis-trans isomerase (PPIase) (proline isomerase) localized to the nucleus; catalyzes isomerization of proline residues in histones H3 and H4, which affects lysine methylation of those histones[1][2][3]




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References

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  1. Davey M, et al. (2000) The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Mol Gen Genet 263(3):520-6 SGD PMID 10821187
  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. Nelson CJ, et al. (2006) Proline isomerization of histone h3 regulates lysine methylation and gene expression. Cell 126(5):905-16 SGD PMID 16959570

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