Difference between revisions of "YLL002W"
SGDwikiBot (talk | contribs) (Automated import of articles) |
SGDwikiBot (talk | contribs) (Automated import of articles) |
||
| Line 18: | Line 18: | ||
|} | |} | ||
<br> | <br> | ||
| − | '''Description of YLL002W:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p<ref name=' | + | '''Description of YLL002W:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p<ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65 {{SGDpaper|S000068874}} PMID 11779788</ref><ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 |
| − | {{SGDpaper| | + | {{SGDpaper|S000126328}} PMID 18458063</ref> |
<br> | <br> | ||
<br> | <br> | ||
Revision as of 13:05, 31 March 2009
Share your knowledge...Edit this entry! <protect>
| Systematic name | YLL002W |
| Gene name | RTT109 |
| Aliases | KIM2, REM50 |
| Feature type | ORF, Verified |
| Coordinates | Chr XII:146290..147600 |
| Primary SGDID | S000003925 |
Description of YLL002W: Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p[1][2][3][4][5]
</protect>
Contents
Community Commentary
About Community Commentary. Please share your knowledge!
<protect>
References
See Help:References on how to add references
- ↑ Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65 SGD PMID 11779788
- ↑ Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 SGD PMID 17272722
- ↑ Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 SGD PMID 17272723
- ↑ Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 SGD PMID 18036332
- ↑ Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 SGD PMID 18458063
See Help:Categories on how to add the wiki page for this gene to a Category </protect>
