| UniProt ID | EAF3_YEAST | |
|---|---|---|
| UniProt AC | Q12432 | |
| Protein Name | Chromatin modification-related protein EAF3 | |
| Gene Name | EAF3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 401 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.. | |
| Protein Sequence | MVDLEQEFALGGRCLAFHGPLMYEAKILKIWDPSSKMYTSIPNDKPGGSSQATKEIKPQKLGEDESIPEEIINGKCFFIHYQGWKSSWDEWVGYDRIRAYNEENIAMKKRLANEAKEAKKSLLEQQKKKKLSTSLGGPSNGGKRKGDSRSNASISKSTSQSFLTSSVSGRKSGRSSANSLHPGSSLRSSSDQNGNDDRRRSSSLSPNMLHHIAGYPTPKISLQIPIKLKSVLVDDWEYVTKDKKICRLPADVTVEMVLNKYEHEVSQELESPGSQSQLSEYCAGLKLYFDKCLGNMLLYRLERLQYDELLKKSSKDQKPLVPIRIYGAIHLLRLISVLPELISSTTMDLQSCQLLIKQTEDFLVWLLMHVDEYFNDKDPNRSDDALYVNTSSQYEGVALGM | |
| 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 |
|---|---|---|---|---|---|
| 45 | Acetylation | YTSIPNDKPGGSSQA EECCCCCCCCCCCCC | 52.80 | 23572591 | |
| 49 | Phosphorylation | PNDKPGGSSQATKEI CCCCCCCCCCCCCCC | 25.78 | 21440633 | |
| 50 | Phosphorylation | NDKPGGSSQATKEIK CCCCCCCCCCCCCCC | 27.40 | 17563356 | |
| 53 | Phosphorylation | PGGSSQATKEIKPQK CCCCCCCCCCCCCCC | 22.90 | 30377154 | |
| 54 | Acetylation | GGSSQATKEIKPQKL CCCCCCCCCCCCCCC | 61.53 | 23572591 | |
| 60 | Acetylation | TKEIKPQKLGEDESI CCCCCCCCCCCCCCC | 67.97 | 24489116 | |
| 120 | Acetylation | NEAKEAKKSLLEQQK HHHHHHHHHHHHHHH | 54.08 | 25381059 | |
| 130 | Acetylation | LEQQKKKKLSTSLGG HHHHHHHCCCCCCCC | 57.46 | 25381059 | |
| 132 | Phosphorylation | QQKKKKLSTSLGGPS HHHHHCCCCCCCCCC | 25.48 | 19779198 | |
| 143 | Acetylation | GGPSNGGKRKGDSRS CCCCCCCCCCCCCCC | 52.95 | 24489116 | |
| 150 | Phosphorylation | KRKGDSRSNASISKS CCCCCCCCCCCCCCC | 40.47 | 28889911 | |
| 153 | Phosphorylation | GDSRSNASISKSTSQ CCCCCCCCCCCCCCC | 31.48 | 27214570 | |
| 156 | Acetylation | RSNASISKSTSQSFL CCCCCCCCCCCCHHH | 56.96 | 22865919 | |
| 157 | Phosphorylation | SNASISKSTSQSFLT CCCCCCCCCCCHHHH | 26.88 | 22369663 | |
| 158 | Phosphorylation | NASISKSTSQSFLTS CCCCCCCCCCHHHHH | 34.22 | 22369663 | |
| 159 | Phosphorylation | ASISKSTSQSFLTSS CCCCCCCCCHHHHHH | 30.80 | 22369663 | |
| 161 | Phosphorylation | ISKSTSQSFLTSSVS CCCCCCCHHHHHHCC | 23.22 | 22369663 | |
| 164 | Phosphorylation | STSQSFLTSSVSGRK CCCCHHHHHHCCCCC | 19.56 | 22369663 | |
| 165 | Phosphorylation | TSQSFLTSSVSGRKS CCCHHHHHHCCCCCC | 30.78 | 22369663 | |
| 166 | Phosphorylation | SQSFLTSSVSGRKSG CCHHHHHHCCCCCCC | 18.31 | 22369663 | |
| 168 | Phosphorylation | SFLTSSVSGRKSGRS HHHHHHCCCCCCCCC | 34.52 | 22369663 | |
| 172 | Phosphorylation | SSVSGRKSGRSSANS HHCCCCCCCCCCCCC | 37.77 | 30377154 | |
| 175 | Phosphorylation | SGRKSGRSSANSLHP CCCCCCCCCCCCCCC | 37.01 | 30377154 | |
| 176 | Phosphorylation | GRKSGRSSANSLHPG CCCCCCCCCCCCCCC | 30.06 | 29136822 | |
| 179 | Phosphorylation | SGRSSANSLHPGSSL CCCCCCCCCCCCCCC | 27.98 | 29136822 | |
| 184 | Phosphorylation | ANSLHPGSSLRSSSD CCCCCCCCCCCCCCC | 30.56 | 30377154 | |
| 201 | Phosphorylation | GNDDRRRSSSLSPNM CCCHHHHHHCCCHHH | 23.59 | 28889911 | |
| 202 | Phosphorylation | NDDRRRSSSLSPNML CCHHHHHHCCCHHHH | 33.22 | 28889911 | |
| 203 | Phosphorylation | DDRRRSSSLSPNMLH CHHHHHHCCCHHHHH | 33.83 | 28152593 | |
| 205 | Phosphorylation | RRRSSSLSPNMLHHI HHHHHCCCHHHHHHH | 19.04 | 19779198 | |
| 271 | Phosphorylation | EVSQELESPGSQSQL HHHHHHCCCCCHHHH | 47.38 | 21551504 |
| 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 EAF3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EAF3_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 EAF3_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-49; SER-50 AND SER-157,AND MASS SPECTROMETRY. | |
| "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-50, AND MASSSPECTROMETRY. | |
