Difference between revisions of "YNL216W"
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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=S000005160 YNL216W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RAP1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RAP1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XIV: | + | |nowrap| Chr XIV:241689..244172 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005160 | ||
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| − | '''Description of | + | '''Description of YNL216W:''' Essential DNA-binding transcription regulator that binds at many loci; involved in either transcription activation or repression, chromatin silencing, and telomere length maintenance; conserved protein with an N-terminal BRCT domain, a central region with homology to the Myb DNA binding domain, and a C-terminal Rap1-specific protein-interaction domain (RCT domain)<ref name='S000143073'>Chen Y, et al. (2011) A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms. Nat Struct Mol Biol 18(2):213-21 {{SGDpaper|S000143073}} PMID 21217703</ref><ref name='S000066410'>Konig P, et al. (1996) The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA. Cell 85(1):125-36 {{SGDpaper|S000066410}} PMID 8620531</ref><ref name='S000061169'>Lieb JD, et al. (2001) Promoter-specific binding of Rap1 revealed by genome-wide maps of protein-DNA association. Nat Genet 28(4):327-34 {{SGDpaper|S000061169}} PMID 11455386</ref><ref name='S000073219'>Pina B, et al. (2003) The different (sur)faces of Rap1p. Mol Genet Genomics 268(6):791-8 {{SGDpaper|S000073219}} PMID 12655405</ref><ref name='S000142168'>Zhang W, et al. (2011) Solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae reveals a novel fold. Biochem Biophys Res Commun 404(4):1055-9 |
| − | {{SGDpaper| | + | {{SGDpaper|S000142168}} PMID 21187076</ref> |
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J Biol Chem 278(5):3265-74</ref> | J Biol Chem 278(5):3265-74</ref> | ||
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<protect> | <protect> | ||
Latest revision as of 13:05, 2 May 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YNL216W |
| Gene name | RAP1 |
| Aliases | GRF1, TBA1, TUF1 |
| Feature type | ORF, Verified |
| Coordinates | Chr XIV:241689..244172 |
| Primary SGDID | S000005160 |
Description of YNL216W: Essential DNA-binding transcription regulator that binds at many loci; involved in either transcription activation or repression, chromatin silencing, and telomere length maintenance; conserved protein with an N-terminal BRCT domain, a central region with homology to the Myb DNA binding domain, and a C-terminal Rap1-specific protein-interaction domain (RCT domain)[1][2][3][4][5]
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References
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- ↑ Chen Y, et al. (2011) A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms. Nat Struct Mol Biol 18(2):213-21 SGD PMID 21217703
- ↑ Konig P, et al. (1996) The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA. Cell 85(1):125-36 SGD PMID 8620531
- ↑ Lieb JD, et al. (2001) Promoter-specific binding of Rap1 revealed by genome-wide maps of protein-DNA association. Nat Genet 28(4):327-34 SGD PMID 11455386
- ↑ Pina B, et al. (2003) The different (sur)faces of Rap1p. Mol Genet Genomics 268(6):791-8 SGD PMID 12655405
- ↑ Zhang W, et al. (2011) Solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae reveals a novel fold. Biochem Biophys Res Commun 404(4):1055-9 SGD PMID 21187076
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