Difference between revisions of "YNL021W"
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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=S000004966 YNL021W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HDA1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HDA1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XIV: | + | |nowrap| Chr XIV:593227..595347 |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004966 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004966 | ||
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| − | '''Description of YNL021W:''' Putative catalytic subunit of a class II histone deacetylase complex that also contains Hda2p and Hda3p; Hda1p interacts with the Hda2p-Hda3p subcomplex to form an active tetramer; deletion increases histone H2B, H3 and H4 acetylation<ref name=' | + | '''Description of YNL021W:''' Putative catalytic subunit of a class II histone deacetylase complex that also contains Hda2p and Hda3p; Hda1p interacts with the Hda2p-Hda3p subcomplex to form an active tetramer; deletion increases histone H2B, H3 and H4 acetylation<ref name='S000059710'>Bernstein BE, et al. (2000) Genomewide studies of histone deacetylase function in yeast. Proc Natl Acad Sci U S A 97(25):13708-13 {{SGDpaper|S000059710}} PMID 11095743</ref><ref name='S000050126'>Carmen AA, et al. (1996) HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex. J Biol Chem 271(26):15837-44 {{SGDpaper|S000050126}} PMID 8663039</ref><ref name='S000070188'>Robyr D, et al. (2002) Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell 109(4):437-46 {{SGDpaper|S000070188}} PMID 12086601</ref><ref name='S000047708'>Rundlett SE, et al. (1996) HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc Natl Acad Sci U S A 93(25):14503-8 {{SGDpaper|S000047708}} PMID 8962081</ref><ref name='S000060263'>Wu J, et al. (2001) HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1. Proc Natl Acad Sci U S A 98(8):4391-6 {{SGDpaper|S000060263}} PMID 11287668</ref><ref name='S000059991'>Wu J, et al. (2001) TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast. Mol Cell 7(1):117-26 |
| − | + | {{SGDpaper|S000059991}} PMID 11172717</ref> | |
<br> | <br> | ||
<br> | <br> | ||
Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YNL021W |
| Gene name | HDA1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XIV:593227..595347 |
| Primary SGDID | S000004966 |
Description of YNL021W: Putative catalytic subunit of a class II histone deacetylase complex that also contains Hda2p and Hda3p; Hda1p interacts with the Hda2p-Hda3p subcomplex to form an active tetramer; deletion increases histone H2B, H3 and H4 acetylation[1][2][3][4][5][6]
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References
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- ↑ Bernstein BE, et al. (2000) Genomewide studies of histone deacetylase function in yeast. Proc Natl Acad Sci U S A 97(25):13708-13 SGD PMID 11095743
- ↑ Carmen AA, et al. (1996) HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex. J Biol Chem 271(26):15837-44 SGD PMID 8663039
- ↑ Robyr D, et al. (2002) Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell 109(4):437-46 SGD PMID 12086601
- ↑ Rundlett SE, et al. (1996) HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc Natl Acad Sci U S A 93(25):14503-8 SGD PMID 8962081
- ↑ Wu J, et al. (2001) HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1. Proc Natl Acad Sci U S A 98(8):4391-6 SGD PMID 11287668
- ↑ Wu J, et al. (2001) TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast. Mol Cell 7(1):117-26 SGD PMID 11172717
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