Difference between revisions of "YEL037C"
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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=S000000763 YEL037C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RAD23 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RAD23 '' | ||
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| − | '''Description of YEL037C:''' Protein with ubiquitin-like N terminus | + | '''Description of YEL037C:''' Protein with ubiquitin-like N terminus, subunit of Nuclear Excision Repair Factor 2 (NEF2) with Rad4p that binds damaged DNA; enhances protein deglycosylation activity of Png1p; also involved, with Rad4p, in ubiquitylated protein turnover<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='S000132732'>Wang S, et al. (2009) N-terminal deletion of Peptide:N-glycanase results in enhanced deglycosylation activity. PLoS One 4(12):e8335 {{SGDpaper|S000132732}} PMID 20016784</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> | {{SGDpaper|S000074162}} PMID 10197977</ref> | ||
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Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YEL037C |
| Gene name | RAD23 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr V:82603..81407 |
| Primary SGDID | S000000763 |
Description of YEL037C: Protein with ubiquitin-like N terminus, subunit of Nuclear Excision Repair Factor 2 (NEF2) with Rad4p that binds damaged DNA; enhances protein deglycosylation activity of Png1p; also involved, with Rad4p, in ubiquitylated protein turnover[1][2][3][4][5]
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References
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- ↑ Li Y, et al. (2010) Rad4 regulates protein turnover at a postubiquitylation step. Mol Biol Cell 21(1):177-85 SGD PMID 19889839
- ↑ Lommel L, et al. (2002) Proteolysis of a nucleotide excision repair protein by the 26 S proteasome. Curr Genet 42(1):9-20 SGD PMID 12420141
- ↑ Prakash S and Prakash L (2000) Nucleotide excision repair in yeast. Mutat Res 451(1-2):13-24 SGD PMID 10915862
- ↑ Wang S, et al. (2009) N-terminal deletion of Peptide:N-glycanase results in enhanced deglycosylation activity. PLoS One 4(12):e8335 SGD PMID 20016784
- ↑ de Laat WL, et al. (1999) Molecular mechanism of nucleotide excision repair. Genes Dev 13(7):768-85 SGD PMID 10197977
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