YER162C - 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=S000000964 YER162C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000964 YER162C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''RAD4 ''

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 |}
 <br>
-'''Description of YER162C:''' Protein that recognizes and binds damaged DNA (with Rad23p) during nucleotide excision repair; subunit of Nuclear Excision Repair Factor 2 (NEF2); homolog of human XPC protein<ref name='S000073199'>Lommel L, et al. (2002) Proteolysis of a nucleotide excision repair protein by the 26 S proteasome. Curr Genet 42(1):9-20 {{SGDpaper|S000073199}} PMID 12420141</ref><ref name='S000070118'>Prakash S and Prakash L (2000) Nucleotide excision repair in yeast. Mutat Res 451(1-2):13-24 {{SGDpaper|S000070118}} PMID 10915862</ref><ref name='S000074162'>de Laat WL, et al. (1999) Molecular mechanism of nucleotide excision repair. Genes Dev 13(7):768-85
+'''Description of YER162C:''' Protein that recognizes and binds damaged DNA (with Rad23p) during nucleotide excision repair; subunit of Nuclear Excision Repair Factor 2 (NEF2); also involved, with Rad23p, in turnover of ubiquitylated proteins<ref name='S000134867'>Li Y, et al. (2010) Rad4 regulates protein turnover at a postubiquitylation step. Mol Biol Cell 21(1):177-85 {{SGDpaper|S000134867}} PMID 19889839</ref><ref name='S000073199'>Lommel L, et al. (2002) Proteolysis of a nucleotide excision repair protein by the 26 S proteasome. Curr Genet 42(1):9-20 {{SGDpaper|S000073199}} PMID 12420141</ref><ref name='S000070118'>Prakash S and Prakash L (2000) Nucleotide excision repair in yeast. Mutat Res 451(1-2):13-24 {{SGDpaper|S000070118}} PMID 10915862</ref><ref name='S000074162'>de Laat WL, et al. (1999) Molecular mechanism of nucleotide excision repair. Genes Dev 13(7):768-85
   {{SGDpaper|S000074162}} PMID 10197977</ref>
 <br>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr V:502889..500625
+|nowrap| Chr V:502894..500630
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000000964

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YER162C:''' Protein that recognizes and binds damaged DNA (with Rad23p) during nucleotide excision repair; subunit of Nuclear Excision Repair Factor 2 (NEF2); homolog of human XPC protein<ref name='S000070118'>Prakash S and Prakash L (2000) Nucleotide excision repair in yeast. Mutat Res 451(1-2):13-24 {{SGDpaper|S000070118}} PMID 10915862</ref><ref name='S000073199'>Lommel L, et al. (2002) Proteolysis of a nucleotide excision repair protein by the 26 S proteasome. Curr Genet 42(1):9-20 {{SGDpaper|S000073199}} PMID 12420141</ref><ref name='S000074162'>de Laat WL, et al. (1999) Molecular mechanism of nucleotide excision repair. Genes Dev 13(7):768-85
+'''Description of YER162C:''' Protein that recognizes and binds damaged DNA (with Rad23p) during nucleotide excision repair; subunit of Nuclear Excision Repair Factor 2 (NEF2); homolog of human XPC protein<ref name='S000073199'>Lommel L, et al. (2002) Proteolysis of a nucleotide excision repair protein by the 26 S proteasome. Curr Genet 42(1):9-20 {{SGDpaper|S000073199}} PMID 12420141</ref><ref name='S000070118'>Prakash S and Prakash L (2000) Nucleotide excision repair in yeast. Mutat Res 451(1-2):13-24 {{SGDpaper|S000070118}} PMID 10915862</ref><ref name='S000074162'>de Laat WL, et al. (1999) Molecular mechanism of nucleotide excision repair. Genes Dev 13(7):768-85
   {{SGDpaper|S000074162}} PMID 10197977</ref>
 <br>

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 |}
 <br>
-'''Description of YER162C:''' Protein that recognizes and binds damaged DNA (with Rad23p) during nucleotide excision repair; subunit of Nuclear Excision Repair Factor 2 (NEF2); homolog of human XPC protein<ref name='S000074162'>de Laat WL, et al. (1999) Molecular mechanism of nucleotide excision repair. Genes Dev 13(7):768-85 {{SGDpaper|S000074162}} PMID 10197977</ref><ref name='S000073199'>Lommel L, et al. (2002) Proteolysis of a nucleotide excision repair protein by the 26 S proteasome. Curr Genet 42(1):9-20 {{SGDpaper|S000073199}} PMID 12420141</ref><ref name='S000070118'>Prakash S and Prakash L (2000) Nucleotide excision repair in yeast. Mutat Res 451(1-2):13-24
+'''Description of YER162C:''' Protein that recognizes and binds damaged DNA (with Rad23p) during nucleotide excision repair; subunit of Nuclear Excision Repair Factor 2 (NEF2); homolog of human XPC protein<ref name='S000070118'>Prakash S and Prakash L (2000) Nucleotide excision repair in yeast. Mutat Res 451(1-2):13-24 {{SGDpaper|S000070118}} PMID 10915862</ref><ref name='S000073199'>Lommel L, et al. (2002) Proteolysis of a nucleotide excision repair protein by the 26 S proteasome. Curr Genet 42(1):9-20 {{SGDpaper|S000073199}} PMID 12420141</ref><ref name='S000074162'>de Laat WL, et al. (1999) Molecular mechanism of nucleotide excision repair. Genes Dev 13(7):768-85
-  {{SGDpaper|S000070118}} PMID 10915862</ref>
+  {{SGDpaper|S000074162}} PMID 10197977</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 V:502889..500625
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 ==Community Commentary==
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 ==References==
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