| UniProt ID | PHO23_YEAST | |
|---|---|---|
| UniProt AC | P50947 | |
| Protein Name | Transcriptional regulatory protein PHO23 | |
| Gene Name | PHO23 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 330 | |
| 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.. | |
| Protein Sequence | MSSPANLFPGLNDITDVLEEFPLATSRYLTLLHEIDAKCVHSMPNLNERIDKFLKKDFNKDHQTQVRLLNNINKIYEELMPSLEEKMHVSSIMLDNLDRLTSRLELAYEVAIKNTEIPRGLRLGVDNHPAMHLHHELMEKIESKSNSKSSQALKSESRREAMAANRRQGEHYSASTHQQDDSKNDANYGGSRHESQDHTGNNTNSRKRANAANTNNADPETKKRKRRVATTAVSPSTISTATAVNNGRIGTSTASRGVSSVGNSNNSRISRPKTNDYGEPLYCYCNQVAYGEMVGCDGADCELEWFHLPCIGLETLPKGKWYCDDCKKKL | |
| 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 |
|---|---|---|---|---|---|
| 60 | Acetylation | FLKKDFNKDHQTQVR HHHHHCCCHHHHHHH | 57.49 | 22865919 | |
| 150 | Phosphorylation | SKSNSKSSQALKSES HHCCCHHHHHHHHHH | 24.18 | 28889911 | |
| 154 | Acetylation | SKSSQALKSESRREA CHHHHHHHHHHHHHH | 56.01 | 22865919 | |
| 155 | Phosphorylation | KSSQALKSESRREAM HHHHHHHHHHHHHHH | 41.47 | 28889911 | |
| 173 | Phosphorylation | RRQGEHYSASTHQQD HHCCCCCCCCCCCCC | 20.04 | 30377154 | |
| 175 | Phosphorylation | QGEHYSASTHQQDDS CCCCCCCCCCCCCCC | 22.08 | 30377154 | |
| 182 | Phosphorylation | STHQQDDSKNDANYG CCCCCCCCCCCCCCC | 41.47 | 30377154 | |
| 183 | Acetylation | THQQDDSKNDANYGG CCCCCCCCCCCCCCC | 66.88 | 22865919 | |
| 195 | Phosphorylation | YGGSRHESQDHTGNN CCCCCCCCCCCCCCC | 34.48 | 30377154 | |
| 222 | Acetylation | NNADPETKKRKRRVA CCCCHHHHHHHHHHE | 49.25 | 25381059 | |
| 230 | Phosphorylation | KRKRRVATTAVSPST HHHHHHEECCCCHHH | 16.66 | 22369663 | |
| 231 | Phosphorylation | RKRRVATTAVSPSTI HHHHHEECCCCHHHH | 18.48 | 22369663 | |
| 234 | Phosphorylation | RVATTAVSPSTISTA HHEECCCCHHHHCCC | 15.63 | 22369663 | |
| 236 | Phosphorylation | ATTAVSPSTISTATA EECCCCHHHHCCCEE | 30.76 | 22369663 | |
| 237 | Phosphorylation | TTAVSPSTISTATAV ECCCCHHHHCCCEEE | 23.49 | 22369663 | |
| 239 | Phosphorylation | AVSPSTISTATAVNN CCCHHHHCCCEEECC | 16.45 | 22369663 | |
| 240 | Phosphorylation | VSPSTISTATAVNNG CCHHHHCCCEEECCC | 24.95 | 22369663 | |
| 242 | Phosphorylation | PSTISTATAVNNGRI HHHHCCCEEECCCCC | 31.09 | 22369663 | |
| 255 | Phosphorylation | RIGTSTASRGVSSVG CCCCCCCCCCCCCCC | 29.65 | 30377154 | |
| 259 | Phosphorylation | STASRGVSSVGNSNN CCCCCCCCCCCCCCC | 23.33 | 22369663 | |
| 260 | Phosphorylation | TASRGVSSVGNSNNS CCCCCCCCCCCCCCC | 31.47 | 22369663 | |
| 264 | Phosphorylation | GVSSVGNSNNSRISR CCCCCCCCCCCCCCC | 31.31 | 22369663 | |
| 267 | Phosphorylation | SVGNSNNSRISRPKT CCCCCCCCCCCCCCC | 34.93 | 22369663 |
| 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 PHO23_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PHO23_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 PHO23_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-234, AND MASSSPECTROMETRY. | |
