YPL046C - 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=S000005967 YPL046C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005967 YPL046C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''ELC1 ''

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YPL046C:''' Elongin C, involved in transcription elongation as a heterodimer with Ela1p; forms a complex with Cul3p that polyubiquitylates monoubiquitylated RNA polymerase II to trigger its proteolysis; plays a role in global genomic repair<ref name='S000058265'>Aso T and Conrad MN (1997) Molecular cloning of DNAs encoding the regulatory subunits of elongin from Saccharomyces cerevisiae and Drosophila melanogaster. Biochem Biophys Res Commun 241(2):334-40 {{SGDpaper|S000058265}} PMID 9425272</ref><ref name='S000040848'>Botuyan MV, et al. (1999) Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C. Proc Natl Acad Sci U S A 96(16):9033-8 {{SGDpaper|S000040848}} PMID 10430890</ref><ref name='S000136358'>Harreman M, et al. (2009) Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proc Natl Acad Sci U S A 106(49):20705-10 {{SGDpaper|S000136358}} PMID 19920177</ref><ref name='S000069764'>Hyman LE, et al. (2002) Binding to Elongin C inhibits degradation of interacting proteins in yeast. J Biol Chem 277(18):15586-91 {{SGDpaper|S000069764}} PMID 11864988</ref><ref name='S000127847'>Lejeune D, et al. (2009) Yeast Elc1 plays an important role in global genomic repair but not in transcription coupled repair. DNA Repair (Amst) 8(1):40-50 {{SGDpaper|S000127847}} PMID 18817898</ref><ref name='S000120848'>Ribar B, et al. (2007) ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells. Mol Cell Biol 27(8):3211-6
+'''Description of YPL046C:''' Elongin C, conserved among eukaryotes; forms a complex with Cul3p that polyubiquitylates monoubiquitylated RNA polymerase II to trigger its proteolysis; plays a role in global genomic repair<ref name='S000058265'>Aso T and Conrad MN (1997) Molecular cloning of DNAs encoding the regulatory subunits of elongin from Saccharomyces cerevisiae and Drosophila melanogaster. Biochem Biophys Res Commun 241(2):334-40 {{SGDpaper|S000058265}} PMID 9425272</ref><ref name='S000040848'>Botuyan MV, et al. (1999) Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C. Proc Natl Acad Sci U S A 96(16):9033-8 {{SGDpaper|S000040848}} PMID 10430890</ref><ref name='S000136358'>Harreman M, et al. (2009) Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proc Natl Acad Sci U S A 106(49):20705-10 {{SGDpaper|S000136358}} PMID 19920177</ref><ref name='S000069764'>Hyman LE, et al. (2002) Binding to Elongin C inhibits degradation of interacting proteins in yeast. J Biol Chem 277(18):15586-91 {{SGDpaper|S000069764}} PMID 11864988</ref><ref name='S000127847'>Lejeune D, et al. (2009) Yeast Elc1 plays an important role in global genomic repair but not in transcription coupled repair. DNA Repair (Amst) 8(1):40-50 {{SGDpaper|S000127847}} PMID 18817898</ref><ref name='S000120848'>Ribar B, et al. (2007) ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells. Mol Cell Biol 27(8):3211-6
   {{SGDpaper|S000120848}} PMID 17296727</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YPL046C:''' Elongin C, involved in transcription elongation as a heterodimer with Ela1p; required for ubiquitin-dependent degradation of Rpo21p; plays a role in global genomic nucleotide excision repair; expression highly upregulated during sporulation<ref name='S000058265'>Aso T and Conrad MN (1997) Molecular cloning of DNAs encoding the regulatory subunits of elongin from Saccharomyces cerevisiae and Drosophila melanogaster. Biochem Biophys Res Commun 241(2):334-40 {{SGDpaper|S000058265}} PMID 9425272</ref><ref name='S000040848'>Botuyan MV, et al. (1999) Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C. Proc Natl Acad Sci U S A 96(16):9033-8 {{SGDpaper|S000040848}} PMID 10430890</ref><ref name='S000069764'>Hyman LE, et al. (2002) Binding to Elongin C inhibits degradation of interacting proteins in yeast. J Biol Chem 277(18):15586-91 {{SGDpaper|S000069764}} PMID 11864988</ref><ref name='S000127847'>Lejeune D, et al. (2009) Yeast Elc1 plays an important role in global genomic repair but not in transcription coupled repair. DNA Repair (Amst) 8(1):40-50 {{SGDpaper|S000127847}} PMID 18817898</ref><ref name='S000120848'>Ribar B, et al. (2007) ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells. Mol Cell Biol 27(8):3211-6
+'''Description of YPL046C:''' Elongin C, involved in transcription elongation as a heterodimer with Ela1p; forms a complex with Cul3p that polyubiquitylates monoubiquitylated RNA polymerase II to trigger its proteolysis; plays a role in global genomic repair<ref name='S000058265'>Aso T and Conrad MN (1997) Molecular cloning of DNAs encoding the regulatory subunits of elongin from Saccharomyces cerevisiae and Drosophila melanogaster. Biochem Biophys Res Commun 241(2):334-40 {{SGDpaper|S000058265}} PMID 9425272</ref><ref name='S000040848'>Botuyan MV, et al. (1999) Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C. Proc Natl Acad Sci U S A 96(16):9033-8 {{SGDpaper|S000040848}} PMID 10430890</ref><ref name='S000136358'>Harreman M, et al. (2009) Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proc Natl Acad Sci U S A 106(49):20705-10 {{SGDpaper|S000136358}} PMID 19920177</ref><ref name='S000069764'>Hyman LE, et al. (2002) Binding to Elongin C inhibits degradation of interacting proteins in yeast. J Biol Chem 277(18):15586-91 {{SGDpaper|S000069764}} PMID 11864988</ref><ref name='S000127847'>Lejeune D, et al. (2009) Yeast Elc1 plays an important role in global genomic repair but not in transcription coupled repair. DNA Repair (Amst) 8(1):40-50 {{SGDpaper|S000127847}} PMID 18817898</ref><ref name='S000120848'>Ribar B, et al. (2007) ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells. Mol Cell Biol 27(8):3211-6
   {{SGDpaper|S000120848}} PMID 17296727</ref>
 <br>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XVI:466940..466641
+|nowrap| Chr XVI:466943..466644
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005967

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YPL046C:''' Elongin C, involved in transcription elongation as a heterodimer with Ela1p; required for ubiquitin-dependent degradation of Rpo21p; plays a role in global genomic nucleotide excision repair; expression highly upregulated during sporulation<ref name='S000040848'>Botuyan MV, et al. (1999) Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C. Proc Natl Acad Sci U S A 96(16):9033-8 {{SGDpaper|S000040848}} PMID 10430890</ref><ref name='S000058265'>Aso T and Conrad MN (1997) Molecular cloning of DNAs encoding the regulatory subunits of elongin from Saccharomyces cerevisiae and Drosophila melanogaster. Biochem Biophys Res Commun 241(2):334-40 {{SGDpaper|S000058265}} PMID 9425272</ref><ref name='S000069764'>Hyman LE, et al. (2002) Binding to Elongin C inhibits degradation of interacting proteins in yeast. J Biol Chem 277(18):15586-91 {{SGDpaper|S000069764}} PMID 11864988</ref><ref name='S000120848'>Ribar B, et al. (2007) ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells. Mol Cell Biol 27(8):3211-6 {{SGDpaper|S000120848}} PMID 17296727</ref><ref name='S000127847'>Lejeune D, et al. (2009) Yeast Elc1 plays an important role in global genomic repair but not in transcription coupled repair. DNA Repair (Amst) 8(1):40-50
+'''Description of YPL046C:''' Elongin C, involved in transcription elongation as a heterodimer with Ela1p; required for ubiquitin-dependent degradation of Rpo21p; plays a role in global genomic nucleotide excision repair; expression highly upregulated during sporulation<ref name='S000058265'>Aso T and Conrad MN (1997) Molecular cloning of DNAs encoding the regulatory subunits of elongin from Saccharomyces cerevisiae and Drosophila melanogaster. Biochem Biophys Res Commun 241(2):334-40 {{SGDpaper|S000058265}} PMID 9425272</ref><ref name='S000040848'>Botuyan MV, et al. (1999) Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C. Proc Natl Acad Sci U S A 96(16):9033-8 {{SGDpaper|S000040848}} PMID 10430890</ref><ref name='S000069764'>Hyman LE, et al. (2002) Binding to Elongin C inhibits degradation of interacting proteins in yeast. J Biol Chem 277(18):15586-91 {{SGDpaper|S000069764}} PMID 11864988</ref><ref name='S000127847'>Lejeune D, et al. (2009) Yeast Elc1 plays an important role in global genomic repair but not in transcription coupled repair. DNA Repair (Amst) 8(1):40-50 {{SGDpaper|S000127847}} PMID 18817898</ref><ref name='S000120848'>Ribar B, et al. (2007) ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells. Mol Cell Biol 27(8):3211-6
- {{SGDpaper|S000127847}} PMID 18817898</ref>
+ {{SGDpaper|S000120848}} PMID 17296727</ref>
 <br>
 <br>

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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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