Difference between revisions of "YDR457W"
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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=S000002865 YDR457W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''TOM1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''TOM1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr IV: | + | |nowrap| Chr IV:1369790..1379596 |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002865 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002865 | ||
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| − | '''Description of YDR457W:''' E3 ubiquitin ligase of the hect-domain class; has a role in mRNA export from the nucleus and may regulate transcriptional coactivators; involved in degradation of excess histones<ref name='S000061678'>Davey M, et al. (2000) The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Mol Gen Genet 263(3):520-6 {{SGDpaper|S000061678}} PMID 10821187</ref><ref name='S000064207'>Saleh A, et al. (1998) TOM1p, a yeast hect-domain protein which mediates transcriptional regulation through the ADA/SAGA coactivator complexes. J Mol Biol 282(5):933-46 {{SGDpaper|S000064207}} PMID 9753545 | + | '''Description of YDR457W:''' E3 ubiquitin ligase of the hect-domain class; has a role in mRNA export from the nucleus and may regulate transcriptional coactivators; involved in degradation of excess histones; interacts with Dia2p and is required for Dia2p degradation<ref name='S000061678'>Davey M, et al. (2000) The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Mol Gen Genet 263(3):520-6 {{SGDpaper|S000061678}} PMID 10821187</ref><ref name='S000074758'>Duncan K, et al. (2000) A putative ubiquitin ligase required for efficient mRNA export differentially affects hnRNP transport. Curr Biol 10(12):687-96 {{SGDpaper|S000074758}} PMID 10873801</ref><ref name='S000150670'>Kim DH and Koepp DM (2012) The Hect E3 ubiquitin ligase Tom1 controls Dia2 degradation during the cell cycle. Mol Biol Cell () {{SGDpaper|S000150670}} PMID 22933573</ref><ref name='S000064207'>Saleh A, et al. (1998) TOM1p, a yeast hect-domain protein which mediates transcriptional regulation through the ADA/SAGA coactivator complexes. J Mol Biol 282(5):933-46 {{SGDpaper|S000064207}} PMID 9753545</ref><ref name='S000130860'>Singh RK, et al. (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33 |
{{SGDpaper|S000130860}} PMID 19578373</ref> | {{SGDpaper|S000130860}} PMID 19578373</ref> | ||
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Latest revision as of 14:05, 13 September 2012
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| Systematic name | YDR457W |
| Gene name | TOM1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:1369790..1379596 |
| Primary SGDID | S000002865 |
Description of YDR457W: E3 ubiquitin ligase of the hect-domain class; has a role in mRNA export from the nucleus and may regulate transcriptional coactivators; involved in degradation of excess histones; interacts with Dia2p and is required for Dia2p degradation[1][2][3][4][5]
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References
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- ↑ Davey M, et al. (2000) The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Mol Gen Genet 263(3):520-6 SGD PMID 10821187
- ↑ Duncan K, et al. (2000) A putative ubiquitin ligase required for efficient mRNA export differentially affects hnRNP transport. Curr Biol 10(12):687-96 SGD PMID 10873801
- ↑ Kim DH and Koepp DM (2012) The Hect E3 ubiquitin ligase Tom1 controls Dia2 degradation during the cell cycle. Mol Biol Cell () SGD PMID 22933573
- ↑ Saleh A, et al. (1998) TOM1p, a yeast hect-domain protein which mediates transcriptional regulation through the ADA/SAGA coactivator complexes. J Mol Biol 282(5):933-46 SGD PMID 9753545
- ↑ Singh RK, et al. (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33 SGD PMID 19578373
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