YBR111W-A - 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=S000028510 YBR111W-A]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000028510 YBR111W-A]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''SUS1 ''

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBR111W-A:''' Component of both the SAGA histone acetylase complex and TREX-2; interacts with RNAPII; involved in mRNA export coupled transcription activation and elongation;<ref name='S000116290'>Cabal GG, et al. (2006) SAGA interacting factors confine sub-diffusion of transcribed genes to the nuclear envelope. Nature 441(7094):770-3 {{SGDpaper|S000116290}} PMID 16760982</ref><ref name='S000127258'>Gonzalez-Aguilera C, et al. (2008) The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA export preventing RNA-mediated genome instability. Mol Biol Cell 19(10):4310-8 {{SGDpaper|S000127258}} PMID 18667528</ref><ref name='S000123642'>Kohler A, et al. (2006) The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-mediated H2B deubiquitinylation through its interaction with Ubp8 and Sgf11. Mol Biol Cell 17(10):4228-36 {{SGDpaper|S000123642}} PMID 16855026</ref><ref name='S000129299'>Pascual-Garcia P, et al. (2008) Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. Genes Dev 22(20):2811-22 {{SGDpaper|S000129299}} PMID 18923079</ref><ref name='S000074416'>Rodriguez-Navarro S, et al. (2004) Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell 116(1):75-86 {{SGDpaper|S000074416}} PMID 14718168</ref><ref name='S000146226'>Tous C, et al. (2011) A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors. EMBO J 30(10):1953-64
+'''Description of YBR111W-A:''' Component of both the SAGA histone acetylase and TREX-2 complexes; interacts with RNA polymerase II; involved in mRNA export coupled transcription activation and elongation; involved in post-transcriptional tethering of active genes to the nuclear periphery and to non-nascent mRNP<ref name='S000116290'>Cabal GG, et al. (2006) SAGA interacting factors confine sub-diffusion of transcribed genes to the nuclear envelope. Nature 441(7094):770-3 {{SGDpaper|S000116290}} PMID 16760982</ref><ref name='S000136082'>Chekanova JA, et al. (2008) Sus1, Sac3, and Thp1 mediate post-transcriptional tethering of active genes to the nuclear rim as well as to non-nascent mRNP. RNA 14(1):66-77 {{SGDpaper|S000136082}} PMID 18003937</ref><ref name='S000127258'>Gonzalez-Aguilera C, et al. (2008) The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA export preventing RNA-mediated genome instability. Mol Biol Cell 19(10):4310-8 {{SGDpaper|S000127258}} PMID 18667528</ref><ref name='S000123642'>Kohler A, et al. (2006) The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-mediated H2B deubiquitinylation through its interaction with Ubp8 and Sgf11. Mol Biol Cell 17(10):4228-36 {{SGDpaper|S000123642}} PMID 16855026</ref><ref name='S000129299'>Pascual-Garcia P, et al. (2008) Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. Genes Dev 22(20):2811-22 {{SGDpaper|S000129299}} PMID 18923079</ref><ref name='S000074416'>Rodriguez-Navarro S, et al. (2004) Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell 116(1):75-86 {{SGDpaper|S000074416}} PMID 14718168</ref><ref name='S000146226'>Tous C, et al. (2011) A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors. EMBO J 30(10):1953-64
   {{SGDpaper|S000146226}} PMID 21478823</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBR111W-A:''' Protein involved in mRNA export coupled transcription activation and elongation; component of both the SAGA histone acetylase complex and TREX-2, and interacts with RNAPII<ref name='S000116290'>Cabal GG, et al. (2006) SAGA interacting factors confine sub-diffusion of transcribed genes to the nuclear envelope. Nature 441(7094):770-3 {{SGDpaper|S000116290}} PMID 16760982</ref><ref name='S000127258'>Gonzalez-Aguilera C, et al. (2008) The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA export preventing RNA-mediated genome instability. Mol Biol Cell 19(10):4310-8 {{SGDpaper|S000127258}} PMID 18667528</ref><ref name='S000123642'>Kohler A, et al. (2006) The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-mediated H2B deubiquitinylation through its interaction with Ubp8 and Sgf11. Mol Biol Cell 17(10):4228-36 {{SGDpaper|S000123642}} PMID 16855026</ref><ref name='S000129299'>Pascual-Garcia P, et al. (2008) Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. Genes Dev 22(20):2811-22 {{SGDpaper|S000129299}} PMID 18923079</ref><ref name='S000074416'>Rodriguez-Navarro S, et al. (2004) Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell 116(1):75-86
+'''Description of YBR111W-A:''' Component of both the SAGA histone acetylase complex and TREX-2; interacts with RNAPII; involved in mRNA export coupled transcription activation and elongation;<ref name='S000116290'>Cabal GG, et al. (2006) SAGA interacting factors confine sub-diffusion of transcribed genes to the nuclear envelope. Nature 441(7094):770-3 {{SGDpaper|S000116290}} PMID 16760982</ref><ref name='S000127258'>Gonzalez-Aguilera C, et al. (2008) The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA export preventing RNA-mediated genome instability. Mol Biol Cell 19(10):4310-8 {{SGDpaper|S000127258}} PMID 18667528</ref><ref name='S000123642'>Kohler A, et al. (2006) The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-mediated H2B deubiquitinylation through its interaction with Ubp8 and Sgf11. Mol Biol Cell 17(10):4228-36 {{SGDpaper|S000123642}} PMID 16855026</ref><ref name='S000129299'>Pascual-Garcia P, et al. (2008) Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. Genes Dev 22(20):2811-22 {{SGDpaper|S000129299}} PMID 18923079</ref><ref name='S000074416'>Rodriguez-Navarro S, et al. (2004) Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell 116(1):75-86 {{SGDpaper|S000074416}} PMID 14718168</ref><ref name='S000146226'>Tous C, et al. (2011) A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors. EMBO J 30(10):1953-64
-  {{SGDpaper|S000074416}} PMID 14718168</ref>
+  {{SGDpaper|S000146226}} PMID 21478823</ref>
 <br>
 <br>

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr II:462133..462573
+|nowrap| Chr II:462139..462579
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000028510

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBR111W-A:''' Protein involved in mRNA export coupled transcription activation and elongation; component of both the SAGA histone acetylase complex and TREX-2, and interacts with RNAPII<ref name='S000116290'>Cabal GG, et al. (2006) SAGA interacting factors confine sub-diffusion of transcribed genes to the nuclear envelope. Nature 441(7094):770-3 {{SGDpaper|S000116290}} PMID 16760982</ref><ref name='S000074416'>Rodriguez-Navarro S, et al. (2004) Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell 116(1):75-86 {{SGDpaper|S000074416}} PMID 14718168</ref><ref name='S000123642'>Kohler A, et al. (2006) The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-mediated H2B deubiquitinylation through its interaction with Ubp8 and Sgf11. Mol Biol Cell 17(10):4228-36 {{SGDpaper|S000123642}} PMID 16855026</ref><ref name='S000129299'>Pascual-Garcia P, et al. (2008) Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. Genes Dev 22(20):2811-22 {{SGDpaper|S000129299}} PMID 18923079</ref><ref name='S000127258'>Gonzalez-Aguilera C, et al. (2008) The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA export preventing RNA-mediated genome instability. Mol Biol Cell 19(10):4310-8
+'''Description of YBR111W-A:''' Protein involved in mRNA export coupled transcription activation and elongation; component of both the SAGA histone acetylase complex and TREX-2, and interacts with RNAPII<ref name='S000116290'>Cabal GG, et al. (2006) SAGA interacting factors confine sub-diffusion of transcribed genes to the nuclear envelope. Nature 441(7094):770-3 {{SGDpaper|S000116290}} PMID 16760982</ref><ref name='S000127258'>Gonzalez-Aguilera C, et al. (2008) The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA export preventing RNA-mediated genome instability. Mol Biol Cell 19(10):4310-8 {{SGDpaper|S000127258}} PMID 18667528</ref><ref name='S000123642'>Kohler A, et al. (2006) The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-mediated H2B deubiquitinylation through its interaction with Ubp8 and Sgf11. Mol Biol Cell 17(10):4228-36 {{SGDpaper|S000123642}} PMID 16855026</ref><ref name='S000129299'>Pascual-Garcia P, et al. (2008) Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. Genes Dev 22(20):2811-22 {{SGDpaper|S000129299}} PMID 18923079</ref><ref name='S000074416'>Rodriguez-Navarro S, et al. (2004) Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell 116(1):75-86
-  {{SGDpaper|S000127258}} PMID 18667528</ref>
+  {{SGDpaper|S000074416}} PMID 14718168</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 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>
		+	-->

	<protect>		<protect>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr II:462133..462573
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 ==Community Commentary==
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