UniProt ID | SAS5_YEAST | |
---|---|---|
UniProt AC | Q99314 | |
Protein Name | Something about silencing protein 5 | |
Gene Name | SAS5 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 248 | |
Subcellular Localization | Nucleus . | |
Protein Description | Component of the SAS complex, a multiprotein complex that acetylates 'Lys-16' of histone H4 and 'Lys-14' of histone H3. The SAS complex is however unable to acetylate nucleosomal histones. The complex is involved in transcriptional silencing at telomeres and at HML locus. Also involved in rDNA silencing. In the complex, SAS5 is required for maximal histone acetyltransferase (HAT) activity of the complex, suggesting that it may be required to stabilize the complex or help in substrate recognition.. | |
Protein Sequence | MDHSIEVTFRVKTQQVIIPEQNIRGNELPLRRWQMELLMLDATGKEVEPTILSKCIYHLHSSFKQPKRRLNSLPFFIKETGWGEFNLKIECFFIGNAGKFSIEHDLTFEDDAYAVDYTVDVPHEFSHLNSELSKYFDLPWKVVSPEEEMSLRIADLPWIKSLALIDEDMMTDVVQMILNDPAVQRAIENHPRREQFFMFITQLPDDLLMKIQAFLKLPNKNSTKQERTNFGSDAIHKDEPVKAHNKLK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
62 | Phosphorylation | CIYHLHSSFKQPKRR HHHHHHHCCCCCCHH | 26.22 | 27017623 | |
72 | Phosphorylation | QPKRRLNSLPFFIKE CCCHHHHCCCEEEEE | 41.85 | 27017623 | |
144 | Phosphorylation | DLPWKVVSPEEEMSL CCCCCCCCHHHHHHH | 29.58 | 28152593 | |
237 | Acetylation | FGSDAIHKDEPVKAH CCCCCCCCCCCCCCC | 58.64 | 24489116 |
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 SAS5_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SAS5_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 SAS5_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
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-144, AND MASSSPECTROMETRY. |