Difference between revisions of "YDL074C"
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| − | '''Description of YDL074C:''' E3 ubiquitin ligase | + | '''Description of YDL074C:''' E3 ubiquitin ligase, forms heterodimer with Rad6p to monoubiquinate histone H2B-K123, which is required for the subsequent methylation of histone H3-K4 and H3-K79; required for DSBR, transcription, silencing, and checkpoint control<ref name='S000086737'>Wysocki R, et al. (2005) Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9. Mol Cell Biol 25(19):8430-43 {{SGDpaper|S000086737}} PMID 16166626</ref><ref name='S000072783'>Wood A, et al. (2003) Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter. Mol Cell 11(1):267-74 {{SGDpaper|S000072783}} PMID 12535539</ref><ref name='S000130696'>Kim J and Roeder RG (2009) Direct Bre1-Paf1 Complex Interactions and RING Finger-independent Bre1-Rad6 Interactions Mediate Histone H2B Ubiquitylation in Yeast. J Biol Chem 284(31):20582-92 |
| − | {{SGDpaper| | + | {{SGDpaper|S000130696}} PMID 19531475</ref> |
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Revision as of 14:05, 11 November 2009
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| Systematic name | YDL074C |
| Gene name | BRE1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:326149..324047 |
| Primary SGDID | S000002232 |
Description of YDL074C: E3 ubiquitin ligase, forms heterodimer with Rad6p to monoubiquinate histone H2B-K123, which is required for the subsequent methylation of histone H3-K4 and H3-K79; required for DSBR, transcription, silencing, and checkpoint control[1][2][3]
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Contents
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References
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- ↑ Wysocki R, et al. (2005) Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9. Mol Cell Biol 25(19):8430-43 SGD PMID 16166626
- ↑ Wood A, et al. (2003) Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter. Mol Cell 11(1):267-74 SGD PMID 12535539
- ↑ Kim J and Roeder RG (2009) Direct Bre1-Paf1 Complex Interactions and RING Finger-independent Bre1-Rad6 Interactions Mediate Histone H2B Ubiquitylation in Yeast. J Biol Chem 284(31):20582-92 SGD PMID 19531475
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