SIR4/YDR227W Literature Guide 
Other names published for SIR4: ASD1, STE9, UTH2, YDR227W
SIR4 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Protein Physical Properties
- Protein Processing/Modification/Regulation
- Protein Sequence Features
- Protein-Nucleic Acid Interactions
- Protein-protein Interactions
- Protein/Nucleic Acid Structure
- Substrates/Ligands/Cofactors
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
SIR4 - Protein Processing/Modification/Regulation (10)
| Reference | Other Genes Addressed |
|---|---|
| Burgess RJ, et al. (2012) The SCF(Dia2) Ubiquitin E3 Ligase Ubiquitylates Sir4 and Functions in Transcriptional Silencing. PLoS Genet 8(7):e1002846 |
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| Kueng S, et al. (2012) Regulating repression: roles for the sir4 N-terminus in linker DNA protection and stabilization of epigenetic States. PLoS Genet 8(5):e1002727 |
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| Nagesh P, et al. (2012) The SUMO E3 ligase Siz2 exerts a locus-dependent effect on gene silencing in Saccharomyces cerevisiae. Eukaryot Cell 11(4):452-62 |
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| Ferreira HC, et al. (2011) The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast.LID - 10.1038/ncb2263 [doi] Nat Cell Biol () |
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| Fredrickson EK, et al. (2011) Exposed hydrophobicity is a key determinant of nuclear quality control degradation. Mol Biol Cell 22(13):2384-95 |
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| Matsumoto R, et al. (2007) Exploring Novel Function of Yeast Ssa1/2p by Quantitative Profiling Proteomics Using NanoESI-LC-MS/MS. J Proteome Res 6(9):3465-3474 |
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| Denison C, et al. (2005) A proteomic strategy for gaining insights into protein sumoylation in yeast. Mol Cell Proteomics 4(3):246-54 |
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| Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15 |
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| Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8 |
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| Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 |
