| UniProt ID | SIR2_YEAST | |
|---|---|---|
| UniProt AC | P06700 | |
| Protein Name | NAD-dependent histone deacetylase SIR2 | |
| Gene Name | SIR2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 562 | |
| Subcellular Localization | Nucleus, nucleolus . Associated with nucleolar chromatin. Preferentially bound to the spacer regions of the rDNA repeats through its interaction with NET1. | |
| Protein Description | NAD-dependent deacetylase, which participates in a wide range of cellular events including chromosome silencing, chromosome segregation, DNA recombination and the determination of life span. Involved in transcriptional repression of the silent mating-type loci HML and HMR and telomeric silencing via its association with SIR3 and SIR4. Plays a central role in ribosomal DNA (rDNA) silencing via its association with the RENT complex, preventing hyperrecombination, and repressing transcription from foreign promoters, which contributes to extending life span. Probably represses transcription via the formation of heterochromatin structure, which involves the compaction of chromatin fiber into a more condensed form, although this complex in at least one case can still bind euchromatic levels of positive transcription regulators. Although it displays some NAD-dependent histone deacetylase activity on histone H3K9Ac and H3K14Ac and histone H4K16Ac in vitro, such activity is unclear in vivo and may not be essential.. | |
| Protein Sequence | MTIPHMKYAVSKTSENKVSNTVSPTQDKDAIRKQPDDIINNDEPSHKKIKVAQPDSLRETNTTDPLGHTKAALGEVASMELKPTNDMDPLAVSAASVVSMSNDVLKPETPKGPIIISKNPSNGIFYGPSFTKRESLNARMFLKYYGAHKFLDTYLPEDLNSLYIYYLIKLLGFEVKDQALIGTINSIVHINSQERVQDLGSAISVTNVEDPLAKKQTVRLIKDLQRAINKVLCTRLRLSNFFTIDHFIQKLHTARKILVLTGAGVSTSLGIPDFRSSEGFYSKIKHLGLDDPQDVFNYNIFMHDPSVFYNIANMVLPPEKIYSPLHSFIKMLQMKGKLLRNYTQNIDNLESYAGISTDKLVQCHGSFATATCVTCHWNLPGERIFNKIRNLELPLCPYCYKKRREYFPEGYNNKVGVAASQGSMSERPPYILNSYGVLKPDITFFGEALPNKFHKSIREDILECDLLICIGTSLKVAPVSEIVNMVPSHVPQVLINRDPVKHAEFDLSLLGYCDDIAAMVAQKCGWTIPHKKWNDLKNKNFKCQEKDKGVYVVTSDEHPKTL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MTIPHMKYA ------CCCCCCCEE | 43.12 | 30377154 | |
| 8 | Phosphorylation | MTIPHMKYAVSKTSE CCCCCCCEECCCCCC | 12.50 | 28132839 | |
| 19 | Phosphorylation | KTSENKVSNTVSPTQ CCCCCCCCCCCCCCC | 28.52 | 22369663 | |
| 21 | Phosphorylation | SENKVSNTVSPTQDK CCCCCCCCCCCCCCH | 18.17 | 22369663 | |
| 23 | Phosphorylation | NKVSNTVSPTQDKDA CCCCCCCCCCCCHHH | 21.86 | 25521595 | |
| 25 | Phosphorylation | VSNTVSPTQDKDAIR CCCCCCCCCCHHHHH | 41.72 | 22369663 | |
| 56 | Phosphorylation | IKVAQPDSLRETNTT CCCCCCCCCCCCCCC | 35.69 | 30377154 | |
| 109 | Phosphorylation | NDVLKPETPKGPIII CCCCCCCCCCCCEEE | 38.54 | 28889911 | |
| 201 | Phosphorylation | ERVQDLGSAISVTNV HHHHHHHHCCEECCC | 29.71 | 28889911 | |
| 204 | Phosphorylation | QDLGSAISVTNVEDP HHHHHCCEECCCCCH | 23.70 | 26447709 | |
| 400 | Phosphorylation | LPLCPYCYKKRREYF CCCCHHHHHHHHHHC | 17.44 | 28889911 | |
| 420 | Phosphorylation | NKVGVAASQGSMSER CCHHEECCCCCCCCC | 25.90 | 30377154 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of SIR2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SIR2_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of SIR2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-400, AND MASSSPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASSSPECTROMETRY. | |
