YNL246W - 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=S000005190 YNL246W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005190 YNL246W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''VPS75 ''

@@ Line 13: / Line 13: @@
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIV:185461..186350
+|nowrap| Chr XIV:185460..186349
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005190

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNL246W:''' NAP family histone chaperone; binds to histones and Rtt109p, stimulating histone acetyltransferase activity; possesses nucleosome assembly activity in vitro; proposed role in vacuolar protein sorting and in double-strand break repair<ref name='S000070264'>Bonangelino CJ, et al. (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell 13(7):2486-501 {{SGDpaper|S000070264}} PMID 12134085</ref><ref name='S000129115'>Park YJ, et al. (2008) Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol 15(9):957-64 {{SGDpaper|S000129115}} PMID 19172749</ref><ref name='S000121319'>Selth L and Svejstrup JQ (2007) Vps75, A New Yeast Member of the NAP Histone Chaperone Family. J Biol Chem 282(17):12358-62 {{SGDpaper|S000121319}} PMID 17344218</ref><ref name='S000122001'>Han J, et al. (2007) The Rtt109-Vps75 Histone Acetyltransferase Complex Acetylates Non-nucleosomal Histone H3. J Biol Chem 282(19):14158-64 {{SGDpaper|S000122001}} PMID 17369253</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53
+'''Description of YNL246W:''' NAP family histone chaperone; binds to histones and Rtt109p, stimulating histone acetyltransferase activity; possesses nucleosome assembly activity in vitro; proposed role in vacuolar protein sorting and in double-strand break repair<ref name='S000070264'>Bonangelino CJ, et al. (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell 13(7):2486-501 {{SGDpaper|S000070264}} PMID 12134085</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 {{SGDpaper|S000126328}} PMID 18458063</ref><ref name='S000122001'>Han J, et al. (2007) The Rtt109-Vps75 Histone Acetyltransferase Complex Acetylates Non-nucleosomal Histone H3. J Biol Chem 282(19):14158-64 {{SGDpaper|S000122001}} PMID 17369253</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000129115'>Park YJ, et al. (2008) Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol 15(9):957-64 {{SGDpaper|S000129115}} PMID 19172749</ref><ref name='S000121319'>Selth L and Svejstrup JQ (2007) Vps75, A New Yeast Member of the NAP Histone Chaperone Family. J Biol Chem 282(17):12358-62
-  {{SGDpaper|S000126328}} PMID 18458063</ref>
+  {{SGDpaper|S000121319}} PMID 17344218</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNL246W:''' NAP family histone chaperone; binds to histones and Rtt109p, stimulating histone acetyltransferase activity; possesses nucleosome assembly activity in vitro; proposed role in vacuolar protein sorting and in double-strand break repair<ref name='S000070264'>Bonangelino CJ, et al. (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell 13(7):2486-501 {{SGDpaper|S000070264}} PMID 12134085</ref><ref name='S000121319'>Selth L and Svejstrup JQ (2007) Vps75, A New Yeast Member of the NAP Histone Chaperone Family. J Biol Chem 282(17):12358-62 {{SGDpaper|S000121319}} PMID 17344218</ref><ref name='S000122001'>Han J, et al. (2007) The Rtt109-Vps75 Histone Acetyltransferase Complex Acetylates Non-nucleosomal Histone H3. J Biol Chem 282(19):14158-64 {{SGDpaper|S000122001}} PMID 17369253</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 {{SGDpaper|S000126328}} PMID 18458063</ref><ref name='S000127394'>Park YJ, et al. (2008) Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol
+'''Description of YNL246W:''' NAP family histone chaperone; binds to histones and Rtt109p, stimulating histone acetyltransferase activity; possesses nucleosome assembly activity in vitro; proposed role in vacuolar protein sorting and in double-strand break repair<ref name='S000070264'>Bonangelino CJ, et al. (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell 13(7):2486-501 {{SGDpaper|S000070264}} PMID 12134085</ref><ref name='S000129115'>Park YJ, et al. (2008) Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol 15(9):957-64 {{SGDpaper|S000129115}} PMID 19172749</ref><ref name='S000121319'>Selth L and Svejstrup JQ (2007) Vps75, A New Yeast Member of the NAP Histone Chaperone Family. J Biol Chem 282(17):12358-62 {{SGDpaper|S000121319}} PMID 17344218</ref><ref name='S000122001'>Han J, et al. (2007) The Rtt109-Vps75 Histone Acetyltransferase Complex Acetylates Non-nucleosomal Histone H3. J Biol Chem 282(19):14158-64 {{SGDpaper|S000122001}} PMID 17369253</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53
- {{SGDpaper|S000127394}} PMID 18690240</ref>
+ {{SGDpaper|S000126328}} PMID 18458063</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNL246W:''' NAP family histone chaperone; binds to histones and Rtt109p, stimulating histone acetyltransferase activity; possesses nucleosome assembly activity in vitro; proposed role in vacuolar protein sorting and in double-strand break repair<ref name='S000127394'>Park YJ, et al. (2008) Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol  {{SGDpaper|S000127394}} PMID 18690240</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 {{SGDpaper|S000126328}} PMID 18458063</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000122001'>Han J, et al. (2007) The Rtt109-Vps75 Histone Acetyltransferase Complex Acetylates Non-nucleosomal Histone H3. J Biol Chem 282(19):14158-64 {{SGDpaper|S000122001}} PMID 17369253</ref><ref name='S000121319'>Selth L and Svejstrup JQ (2007) Vps75, A New Yeast Member of the NAP Histone Chaperone Family. J Biol Chem 282(17):12358-62 {{SGDpaper|S000121319}} PMID 17344218</ref><ref name='S000070264'>Bonangelino CJ, et al. (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell 13(7):2486-501
+'''Description of YNL246W:''' NAP family histone chaperone; binds to histones and Rtt109p, stimulating histone acetyltransferase activity; possesses nucleosome assembly activity in vitro; proposed role in vacuolar protein sorting and in double-strand break repair<ref name='S000070264'>Bonangelino CJ, et al. (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell 13(7):2486-501 {{SGDpaper|S000070264}} PMID 12134085</ref><ref name='S000121319'>Selth L and Svejstrup JQ (2007) Vps75, A New Yeast Member of the NAP Histone Chaperone Family. J Biol Chem 282(17):12358-62 {{SGDpaper|S000121319}} PMID 17344218</ref><ref name='S000122001'>Han J, et al. (2007) The Rtt109-Vps75 Histone Acetyltransferase Complex Acetylates Non-nucleosomal Histone H3. J Biol Chem 282(19):14158-64 {{SGDpaper|S000122001}} PMID 17369253</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 {{SGDpaper|S000126328}} PMID 18458063</ref><ref name='S000127394'>Park YJ, et al. (2008) Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol
-  {{SGDpaper|S000070264}} PMID 12134085</ref>
+  {{SGDpaper|S000127394}} PMID 18690240</ref>
 <br>
 <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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		+	<!-- 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>
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