Difference between revisions of "YDR143C"
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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=S000002550 YDR143C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SAN1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SAN1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr IV: | + | |nowrap| Chr IV:743874..742042 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002550 | ||
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| − | '''Description of | + | '''Description of YDR143C:''' Ubiquitin-protein ligase; involved in the proteasome-dependent degradation of aberrant nuclear proteins; targets substrates with regions of exposed hydrophobicity containing 5 or more contiguous hydrophobic residues; contains intrinsically disordered regions that contribute to substrate recognition<ref name='S000058946'>Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8 {{SGDpaper|S000058946}} PMID 15078868</ref><ref name='S000145368'>Fredrickson EK, et al. (2011) Exposed hydrophobicity is a key determinant of nuclear quality control degradation. Mol Biol Cell () {{SGDpaper|S000145368}} PMID 21551067</ref><ref name='S000081200'>Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15 {{SGDpaper|S000081200}} PMID 15797381</ref><ref name='S000142868'>Rosenbaum JC, et al. (2011) Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. Mol Cell 41(1):93-106 |
| − | {{SGDpaper| | + | {{SGDpaper|S000142868}} PMID 21211726</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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Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YDR143C |
| Gene name | SAN1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:743874..742042 |
| Primary SGDID | S000002550 |
Description of YDR143C: Ubiquitin-protein ligase; involved in the proteasome-dependent degradation of aberrant nuclear proteins; targets substrates with regions of exposed hydrophobicity containing 5 or more contiguous hydrophobic residues; contains intrinsically disordered regions that contribute to substrate recognition[1][2][3][4]
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Protein Details
Protein Function/Process
Nuclear-localized ubiquitin-protein ligase involved in the proteasome-dependent quality control degradation of aberrant nuclear proteins, including sir4-9, cdc68-1, sir3-8, and cdc13-1. [3] [5]
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References
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- ↑ Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8 SGD PMID 15078868
- ↑ Fredrickson EK, et al. (2011) Exposed hydrophobicity is a key determinant of nuclear quality control degradation. Mol Biol Cell () SGD PMID 21551067
- ↑ 3.0 3.1 Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15 SGD PMID 15797381
- ↑ Rosenbaum JC, et al. (2011) Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. Mol Cell 41(1):93-106 SGD PMID 21211726
- ↑ submitted by Richard G. Gardner on 2005-11-09
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