| UniProt ID | ESA1_YEAST | |
|---|---|---|
| UniProt AC | Q08649 | |
| Protein Name | Histone acetyltransferase ESA1 | |
| Gene Name | ESA1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 445 | |
| Subcellular Localization | ||
| Protein Description | Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me.. | |
| Protein Sequence | MSHDGKEEPGIAKKINSVDDIIIKCQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVLYPKLKATDEDNKKQKKKKATNTSETPQDSLQDGVDGFSRENTDVMDLDNLNVQGIKDENISHEDEIKKLRTSGSMTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKPPVFTASQLRFAW | |
| 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 |
|---|---|---|---|---|---|
| 6 | Acetylation | --MSHDGKEEPGIAK --CCCCCCCCCCHHH | 66.03 | 24489116 | |
| 13 | Acetylation | KEEPGIAKKINSVDD CCCCCHHHHCCCHHH | 52.87 | 24489116 | |
| 17 | Phosphorylation | GIAKKINSVDDIIIK CHHHHCCCHHHEEEE | 30.32 | 28889911 | |
| 82 | Acetylation | DKEVLYPKLKATDED CHHHHHHHHCCCCCC | 49.41 | 23572591 | |
| 96 | Acetylation | DNKKQKKKKATNTSE CHHHHHHHHCCCCCC | 55.46 | 23572591 | |
| 97 | Acetylation | NKKQKKKKATNTSET HHHHHHHHCCCCCCC | 70.13 | 23572591 | |
| 104 | Phosphorylation | KATNTSETPQDSLQD HCCCCCCCCCHHHHC | 26.47 | 23749301 | |
| 117 | Phosphorylation | QDGVDGFSRENTDVM HCCCCCCCCCCCCCC | 44.19 | 28889911 | |
| 135 | Acetylation | NLNVQGIKDENISHE CCCCCCCCCCCCCCH | 66.85 | 24489116 | |
| 146 | Acetylation | ISHEDEIKKLRTSGS CCCHHHHHHHHHCCC | 43.65 | 24489116 | |
| 150 | Phosphorylation | DEIKKLRTSGSMTQN HHHHHHHHCCCCCCC | 48.12 | 30377154 | |
| 151 | Phosphorylation | EIKKLRTSGSMTQNP HHHHHHHCCCCCCCH | 23.57 | 23749301 | |
| 153 | Phosphorylation | KKLRTSGSMTQNPHE HHHHHCCCCCCCHHH | 20.58 | 23749301 | |
| 155 | Phosphorylation | LRTSGSMTQNPHEVA HHHCCCCCCCHHHHH | 27.22 | 29688323 | |
| 262 | Acetylation | SKLFLDHKTLYYDVD HHHHCCCCCEECCCC | 39.63 | 22020126 | |
| 439 | Phosphorylation | KPPVFTASQLRFAW- CCCCCCHHHHEECC- | 27.04 | 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 ESA1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 262 | K | Acetylation |
| 12110674 |
* 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 ESA1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "MYST protein acetyltransferase activity requires active site lysineautoacetylation."; Yuan H., Rossetto D., Mellert H., Dang W., Srinivasan M., Johnson J.,Hodawadekar S., Ding E.C., Speicher K., Abshiru N., Perry R., Wu J.,Yang C., Zheng Y.G., Speicher D.W., Thibault P., Verreault A.,Johnson F.B., Berger S.L., Sternglanz R., McMahon S.B., Cote J.,Marmorstein R.; EMBO J. 31:58-70(2012). Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 160-435, ACTIVE SITE, ANDACETYLATION AT LYS-262. | |
| 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-17, AND MASSSPECTROMETRY. | |
