YOR064C - Revision history

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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=S000005590 YOR064C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005590 YOR064C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''YNG1 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XV:446740..446081
+|nowrap| Chr XV:446738..446079
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005590

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 |}
 <br>
-'''Description of YOR064C:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3, has similarity to the human tumor suppressor ING1<ref name='S000043268'>Loewith R, et al. (2000) Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities. Mol Cell Biol 20(11):3807-16 {{SGDpaper|S000043268}} PMID 10805724</ref><ref name='S000070253'>Howe L, et al. (2002) Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 Hhistone acetyltransferase complex. Mol Cell Biol 22(14):5047-53 {{SGDpaper|S000070253}} PMID 12077334</ref><ref name='S000118056'>Martin DG, et al. (2006) The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3. Mol Cell Biol 26(21):7871-9 {{SGDpaper|S000118056}} PMID 16923967</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
+'''Description of YOR064C:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3, has similarity to the human tumor suppressor ING1<ref name='S000070253'>Howe L, et al. (2002) Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 Hhistone acetyltransferase complex. Mol Cell Biol 22(14):5047-53 {{SGDpaper|S000070253}} PMID 12077334</ref><ref name='S000043268'>Loewith R, et al. (2000) Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities. Mol Cell Biol 20(11):3807-16 {{SGDpaper|S000043268}} PMID 10805724</ref><ref name='S000118056'>Martin DG, et al. (2006) The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3. Mol Cell Biol 26(21):7871-9 {{SGDpaper|S000118056}} PMID 16923967</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|S000121976}} PMID 17157260</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YOR064C:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3, has similarity to the human tumor suppressor ING1<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='S000118056'>Martin DG, et al. (2006) The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3. Mol Cell Biol 26(21):7871-9 {{SGDpaper|S000118056}} PMID 16923967</ref><ref name='S000070253'>Howe L, et al. (2002) Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 Hhistone acetyltransferase complex. Mol Cell Biol 22(14):5047-53 {{SGDpaper|S000070253}} PMID 12077334</ref><ref name='S000043268'>Loewith R, et al. (2000) Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities. Mol Cell Biol 20(11):3807-16
+'''Description of YOR064C:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3, has similarity to the human tumor suppressor ING1<ref name='S000043268'>Loewith R, et al. (2000) Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities. Mol Cell Biol 20(11):3807-16 {{SGDpaper|S000043268}} PMID 10805724</ref><ref name='S000070253'>Howe L, et al. (2002) Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 Hhistone acetyltransferase complex. Mol Cell Biol 22(14):5047-53 {{SGDpaper|S000070253}} PMID 12077334</ref><ref name='S000118056'>Martin DG, et al. (2006) The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3. Mol Cell Biol 26(21):7871-9 {{SGDpaper|S000118056}} PMID 16923967</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|S000043268}} PMID 10805724</ref>
+  {{SGDpaper|S000121976}} PMID 17157260</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YOR064C:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3, has similarity to the human tumor suppressor ING1<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='S000118056'>Martin DG, et al. (2006) The yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone h3. Mol Cell Biol 26(21):7871-9 {{SGDpaper|S000118056}} PMID 16923967</ref><ref name='S000070253'>Howe L, et al. (2002) Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 Hhistone acetyltransferase complex. Mol Cell Biol 22(14):5047-53 {{SGDpaper|S000070253}} PMID 12077334</ref><ref name='S000043268'>Loewith R, et al. (2000) Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities. Mol Cell Biol 20(11):3807-16
+'''Description of YOR064C:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3, has similarity to the human tumor suppressor ING1<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='S000118056'>Martin DG, et al. (2006) The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3. Mol Cell Biol 26(21):7871-9 {{SGDpaper|S000118056}} PMID 16923967</ref><ref name='S000070253'>Howe L, et al. (2002) Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 Hhistone acetyltransferase complex. Mol Cell Biol 22(14):5047-53 {{SGDpaper|S000070253}} PMID 12077334</ref><ref name='S000043268'>Loewith R, et al. (2000) Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities. Mol Cell Biol 20(11):3807-16
   {{SGDpaper|S000043268}} PMID 10805724</ref>
 <br>

← Older revision	Revision as of 23:20, 21 May 2007
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← Older revision		Revision as of 11:32, 21 May 2007
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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>
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