YPR031W - Revision history

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@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006235 YPR031W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006235 YPR031W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''NTO1 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XVI:631512..633758
+|nowrap| Chr XVI:631515..633761
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000006235

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YPR031W:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3<ref name='S000121976'>Taverna SD, et al. (2006) Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell 24(5):785-96 {{SGDpaper|S000121976}} PMID 17157260</ref><ref name='S000119974'>Shi X, et al. (2007) Proteome-wide Analysis in Saccharomyces cerevisiae Identifies Several PHD Fingers as Novel Direct and Selective Binding Modules of Histone H3 Methylated at Either Lysine 4 or Lysine 36. J Biol Chem 282(4):2450-5
+'''Description of YPR031W:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3<ref name='S000119974'>Shi X, et al. (2007) Proteome-wide Analysis in Saccharomyces cerevisiae Identifies Several PHD Fingers as Novel Direct and Selective Binding Modules of Histone H3 Methylated at Either Lysine 4 or Lysine 36. J Biol Chem 282(4):2450-5 {{SGDpaper|S000119974}} PMID 17142463</ref><ref name='S000121976'>Taverna SD, et al. (2006) Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell 24(5):785-96
-  {{SGDpaper|S000119974}} PMID 17142463</ref>
+  {{SGDpaper|S000121976}} PMID 17157260</ref>
 <br>
 <br>

← Older revision		Revision as of 11:32, 21 May 2007
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	{{CommentaryHelp}}		{{CommentaryHelp}}

		+
		+
		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
		+	<!--
		+	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>
		+	-->

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YPR031W:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3<ref name='S000121976'>Taverna SD, et al. (2006) Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell 24(5):785-96
+'''Description of YPR031W:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3<ref name='S000121976'>Taverna SD, et al. (2006) Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell 24(5):785-96 {{SGDpaper|S000121976}} PMID 17157260</ref><ref name='S000119974'>Shi X, et al. (2007) Proteome-wide Analysis in Saccharomyces cerevisiae Identifies Several PHD Fingers as Novel Direct and Selective Binding Modules of Histone H3 Methylated at Either Lysine 4 or Lysine 36. J Biol Chem 282(4):2450-5
-  {{SGDpaper|S000121976}} PMID 17157260</ref>
+  {{SGDpaper|S000119974}} PMID 17142463</ref>
 <br>
 <br>

← Older revision	Revision as of 23:20, 21 May 2007
(No difference)

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||'' ''
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''           || ORF, Uncharacterized[[Category:ORF]][[Category:ORF, Uncharacterized]]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''           || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YPR031W:''' Component of the histone acetyltransferase complex<ref name='S000073348'>SGD (2003) Information without a citation in SGD  ()
+'''Description of YPR031W:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3<ref name='S000121976'>Taverna SD, et al. (2006) Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell 24(5):785-96
-  {{SGDpaper|S000073348}} PMID </ref>
+  {{SGDpaper|S000121976}} PMID 17157260</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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	{{CommentaryHelp}}		{{CommentaryHelp}}

		+
		+
		+
		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
		+	<!--
		+	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'
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XVI:631512..633758
 |}
 <br>
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 <br>
+<br>
 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
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