Difference between revisions of "YPL046C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YPL046C YPL046C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005967 YPL046C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''ELC1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''ELC1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XVI:466940..466641
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|nowrap| Chr XVI:466943..466644
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005967
 
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'''Description of {{PAGENAME}}:''' Elongin C, forms heterodimer with Ela1p that participates in transcription elongation; ; required for ubiquitin-dependent degredation of the RNA Polymerase II subunit RPO21; expression dramatically upregulated during sporulation<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 () {{SGDpaper|S000120848}} PMID 17296727</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='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
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'''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|S000040848}} PMID 10430890</ref>
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  {{SGDpaper|S000120848}} PMID 17296727</ref>
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Latest revision as of 07:45, 23 January 2012

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Systematic name YPL046C
Gene name ELC1
Aliases
Feature type ORF, Verified
Coordinates Chr XVI:466943..466644
Primary SGDID S000005967


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[1][2][3][4][5][6]




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References

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  1. Jump up 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 SGD PMID 9425272
  2. Jump up 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 SGD PMID 10430890
  3. Jump up 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 SGD PMID 19920177
  4. Jump up Hyman LE, et al. (2002) Binding to Elongin C inhibits degradation of interacting proteins in yeast. J Biol Chem 277(18):15586-91 SGD PMID 11864988
  5. Jump up 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 SGD PMID 18817898
  6. Jump up 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 SGD PMID 17296727

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