YLR449W - Revision history

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{{PageTop}}
{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YLR449W YLR449W]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''FPR4 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||'' ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XII:1030830..1032008
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''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
{{SGDpaper|S000046250}} PMID 9371805</ref>
 
 
 
 

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==Community Commentary==
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==References==

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@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XII:1030830..1032008
+|nowrap| Chr XII:1030834..1032012
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000004441

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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='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='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='S000118781'>Nelson CJ, et al. (2006) Proline isomerization of histone h3 regulates lysine methylation and gene expression. Cell 126(5):905-16
+'''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|S000118781}} PMID 16959570</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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='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
+'''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='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='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='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>
+  {{SGDpaper|S000118781}} PMID 16959570</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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		+
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		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<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.
		+	J Biol Chem 278(5):3265-74</ref>
		+	-->

	<protect>		<protect>

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 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004441 YLR449W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004441 YLR449W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''FPR4 ''

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 {|{{Prettytable}} align = 'right' width = '200px'
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XII:1030830..1032008
 |}
 <br>
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 __TOC__
 ==Community Commentary==
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 ==References==
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 {{RefHelp}}