Difference between revisions of "YPL046C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |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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| − | '''Description of YPL046C:''' Elongin C, | + | '''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> | {{SGDpaper|S000120848}} PMID 17296727</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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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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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