Difference between revisions of "YPL046C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005967 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
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005967
 
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'''Description of YPL046C:''' Elongin C, forms heterodimer with Ela1p that participates in transcription elongation; required for ubiquitin-dependent degradation 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 27(8):3211-6 {{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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Latest revision as of 06:45, 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. 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. 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. 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. 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. 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. 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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