| UniProt ID | SDS3_YEAST | |
|---|---|---|
| UniProt AC | P40505 | |
| Protein Name | Transcriptional regulatory protein SDS3 | |
| Gene Name | SDS3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 327 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SDS3 is required for the HDAC activity of the complex and for the RPD3-SIN3 association.. | |
| Protein Sequence | MAIQKVSNKDLSRKDKRRFNIESKVNKIYQNFYSERDNQYKDRLTALQTDLTSLHQGDNGQYARQVRDLEEERDLELVRLRLFEEYRVSRSGIEFQEDIEKAKAEHEKLIKLCKERLYSSIEQKIKKLQEERLLMDVANVHSYAMNYSRPQYQKNTRSHTVSGWDSSSNEYGRDTANESATDTGAGNDRRTLRRRNASKDTRGNNNNQDESDFQTGNGSGSNGHGSRQGSQFPHFNNLTYKSGMNSDSDFLQGINEGTDLYAFLFGEKNPKDNANGNEKKKNRGAQRYSTKTAPPLQSLKPDEVTEDISLIRELTGQPPAPFRLRSD | |
| 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 |
|---|---|---|---|---|---|
| 7 | Phosphorylation | -MAIQKVSNKDLSRK -CCCCCCCCCCCCHH | 45.24 | 30377154 | |
| 9 | Acetylation | AIQKVSNKDLSRKDK CCCCCCCCCCCHHHH | 53.17 | 24489116 | |
| 27 | Acetylation | NIESKVNKIYQNFYS CHHHHHHHHHHHHHH | 45.86 | 24489116 | |
| 41 | Acetylation | SERDNQYKDRLTALQ HHCCHHHHHHHHHHH | 26.97 | 24489116 | |
| 124 | Acetylation | LYSSIEQKIKKLQEE HHHHHHHHHHHHHHH | 43.64 | 24489116 | |
| 154 | Acetylation | YSRPQYQKNTRSHTV CCCCCCCCCCCCCCC | 56.18 | 25381059 | |
| 160 | Phosphorylation | QKNTRSHTVSGWDSS CCCCCCCCCCCCCCC | 20.01 | 28889911 | |
| 166 | Phosphorylation | HTVSGWDSSSNEYGR CCCCCCCCCCCCCCC | 29.20 | 25704821 | |
| 167 | Phosphorylation | TVSGWDSSSNEYGRD CCCCCCCCCCCCCCC | 34.41 | 27214570 | |
| 168 | Phosphorylation | VSGWDSSSNEYGRDT CCCCCCCCCCCCCCC | 37.32 | 28889911 | |
| 171 | Phosphorylation | WDSSSNEYGRDTANE CCCCCCCCCCCCCCC | 23.01 | 19779198 | |
| 175 | Phosphorylation | SNEYGRDTANESATD CCCCCCCCCCCCCCC | 29.98 | 28889911 | |
| 179 | Phosphorylation | GRDTANESATDTGAG CCCCCCCCCCCCCCC | 35.95 | 21082442 | |
| 181 | Phosphorylation | DTANESATDTGAGND CCCCCCCCCCCCCCC | 43.29 | 17563356 | |
| 183 | Phosphorylation | ANESATDTGAGNDRR CCCCCCCCCCCCCHH | 25.28 | 24909858 | |
| 211 | Phosphorylation | NNNNQDESDFQTGNG CCCCCCHHHCCCCCC | 52.60 | 22369663 | |
| 215 | Phosphorylation | QDESDFQTGNGSGSN CCHHHCCCCCCCCCC | 32.38 | 22369663 | |
| 219 | Phosphorylation | DFQTGNGSGSNGHGS HCCCCCCCCCCCCCC | 42.94 | 22369663 | |
| 221 | Phosphorylation | QTGNGSGSNGHGSRQ CCCCCCCCCCCCCCC | 41.14 | 22369663 | |
| 226 | Phosphorylation | SGSNGHGSRQGSQFP CCCCCCCCCCCCCCC | 18.76 | 22369663 | |
| 230 | Phosphorylation | GHGSRQGSQFPHFNN CCCCCCCCCCCCCCC | 21.95 | 24961812 | |
| 239 | Phosphorylation | FPHFNNLTYKSGMNS CCCCCCCEECCCCCC | 30.90 | 24961812 | |
| 240 | Phosphorylation | PHFNNLTYKSGMNSD CCCCCCEECCCCCCC | 13.31 | 21440633 | |
| 242 | Phosphorylation | FNNLTYKSGMNSDSD CCCCEECCCCCCCHH | 32.62 | 19795423 | |
| 246 | Phosphorylation | TYKSGMNSDSDFLQG EECCCCCCCHHHHHH | 29.60 | 19779198 | |
| 248 | Phosphorylation | KSGMNSDSDFLQGIN CCCCCCCHHHHHHHC | 30.04 | 21440633 | |
| 258 | Phosphorylation | LQGINEGTDLYAFLF HHHHCCCCCCHHHHH | 19.36 | 19795423 | |
| 261 | Phosphorylation | INEGTDLYAFLFGEK HCCCCCCHHHHHCCC | 9.71 | 19795423 | |
| 271 | Acetylation | LFGEKNPKDNANGNE HHCCCCCCCCCCCCH | 73.36 | 25381059 | |
| 326 | Phosphorylation | PAPFRLRSD------ CCCCCCCCC------ | 52.87 | 21440633 |
| 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 SDS3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SDS3_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 SDS3_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-168, 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-179; THR-181; SER-211;SER-219 AND SER-226, AND MASS SPECTROMETRY. | |
