| UniProt ID | AHC1_YEAST | |
|---|---|---|
| UniProt AC | Q12433 | |
| Protein Name | Protein AHC1 | |
| Gene Name | AHC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 566 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Functions as component of the transcription regulatory histone acetylation (HAT) complex ADA. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B. AHC1 is required for the overall structural integrity of the ADA complex.. | |
| Protein Sequence | MMSPAQDKLQHQHHNPNSSSSSSSKMTNVYQVTTPKSPQDLENNMDEPFKMDTATSNPDKDSENTQRLKYECAKGEIQNVLNLHIMLNHKHVRHLRRNVQKVNAKLALLETLHKDTGLLNKIERTYQLKIKQHQQHSVLGGHFHDSTATENTNASNYNLSYPVLSDYNINCQPLSSSSNRNLSTTRIPHHHYHTRSKSNGLLLEPSALRPANSNIIDYRLTGSKSLSEAITKPTPVSLPHSNSDGISSPRSSSISPLDEQPGFQILPFKPSQMHLNHRRNYSSTCLTSNSGIIGKTENNEPIFRRYDGILVIITCSKCDRSGFTSAQGIVNHTRLKHSKLYSSQPLAVLNNQKLLPNDKQDPEILSKFKKLNLDPNKDYLPSDIAIPKPQSPINHSENHTRAPKTVKNTPHLEKLYQNKEDFKKLIDMVNETPDDLNEYLKQREIQLRYQKEQEEESSKSDDEASYVPSPSLSATATTTTTTDPPSPPVLSSSLQRKLLRKRKLSLNSSTPMEDLPLRERLRANPTDKKPRKAALLTNELEGPDPAAKSSSYYNLRSKSRLRGSHT | |
| 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 |
|---|---|---|---|---|---|
| 22 | Phosphorylation | NPNSSSSSSSKMTNV CCCCCCCCCCCCCCE | 40.35 | 30377154 | |
| 23 | Phosphorylation | PNSSSSSSSKMTNVY CCCCCCCCCCCCCEE | 35.61 | 30377154 | |
| 33 | Phosphorylation | MTNVYQVTTPKSPQD CCCEEEECCCCCHHH | 23.12 | 24961812 | |
| 34 | Phosphorylation | TNVYQVTTPKSPQDL CCEEEECCCCCHHHH | 29.84 | 20377248 | |
| 37 | Phosphorylation | YQVTTPKSPQDLENN EEECCCCCHHHHHHC | 29.06 | 21551504 | |
| 105 | Ubiquitination | NVQKVNAKLALLETL HHHHHHHHHHHHHHH | 29.14 | 17644757 | |
| 114 | Ubiquitination | ALLETLHKDTGLLNK HHHHHHHHHCCHHHH | 61.16 | 17644757 | |
| 196 | Phosphorylation | HHHYHTRSKSNGLLL CCCCCCCCCCCCEEE | 41.41 | 28889911 | |
| 198 | Phosphorylation | HYHTRSKSNGLLLEP CCCCCCCCCCEEECH | 37.06 | 22369663 | |
| 224 | Acetylation | DYRLTGSKSLSEAIT EEEECCCCCHHHHCC | 57.68 | 24489116 | |
| 224 | Ubiquitination | DYRLTGSKSLSEAIT EEEECCCCCHHHHCC | 57.68 | 17644757 | |
| 225 | Phosphorylation | YRLTGSKSLSEAITK EEECCCCCHHHHCCC | 38.53 | 27214570 | |
| 232 | Acetylation | SLSEAITKPTPVSLP CHHHHCCCCCCCCCC | 40.56 | 24489116 | |
| 232 | Ubiquitination | SLSEAITKPTPVSLP CHHHHCCCCCCCCCC | 40.56 | 17644757 | |
| 237 | Phosphorylation | ITKPTPVSLPHSNSD CCCCCCCCCCCCCCC | 37.07 | 30377154 | |
| 241 | Phosphorylation | TPVSLPHSNSDGISS CCCCCCCCCCCCCCC | 35.77 | 30377154 | |
| 247 | Phosphorylation | HSNSDGISSPRSSSI CCCCCCCCCCCCCCC | 39.56 | 28889911 | |
| 248 | Phosphorylation | SNSDGISSPRSSSIS CCCCCCCCCCCCCCC | 23.55 | 27214570 | |
| 282 | Phosphorylation | LNHRRNYSSTCLTSN CCCCCCCCCCCEECC | 23.79 | 27214570 | |
| 283 | Phosphorylation | NHRRNYSSTCLTSNS CCCCCCCCCCEECCC | 16.87 | 21440633 | |
| 284 | Phosphorylation | HRRNYSSTCLTSNSG CCCCCCCCCEECCCC | 12.95 | 28889911 | |
| 295 | Ubiquitination | SNSGIIGKTENNEPI CCCCCCCCCCCCCCC | 42.11 | 17644757 | |
| 317 | Ubiquitination | LVIITCSKCDRSGFT EEEEEECCCCCCCCC | 42.15 | 17644757 | |
| 339 | Acetylation | HTRLKHSKLYSSQPL CCCCCCCCCCCCCCE | 51.68 | 24489116 | |
| 339 | Ubiquitination | HTRLKHSKLYSSQPL CCCCCCCCCCCCCCE | 51.68 | 17644757 | |
| 343 | Phosphorylation | KHSKLYSSQPLAVLN CCCCCCCCCCEEECC | 23.43 | 21440633 | |
| 353 | Ubiquitination | LAVLNNQKLLPNDKQ EEECCCCCCCCCCCC | 54.86 | 17644757 | |
| 391 | Phosphorylation | IAIPKPQSPINHSEN CCCCCCCCCCCCCCC | 35.95 | 29136822 | |
| 396 | Phosphorylation | PQSPINHSENHTRAP CCCCCCCCCCCCCCC | 35.29 | 24961812 | |
| 400 | Phosphorylation | INHSENHTRAPKTVK CCCCCCCCCCCCCCC | 39.86 | 24961812 | |
| 457 | Phosphorylation | QKEQEEESSKSDDEA HHHHHHHHCCCCCCH | 46.47 | 21440633 | |
| 458 | Phosphorylation | KEQEEESSKSDDEAS HHHHHHHCCCCCCHH | 39.18 | 20377248 | |
| 505 | Phosphorylation | LLRKRKLSLNSSTPM HHHHCCCCCCCCCCH | 28.65 | 27738172 | |
| 508 | Phosphorylation | KRKLSLNSSTPMEDL HCCCCCCCCCCHHHC | 40.66 | 28132839 | |
| 509 | Phosphorylation | RKLSLNSSTPMEDLP CCCCCCCCCCHHHCC | 35.14 | 28132839 | |
| 510 | Phosphorylation | KLSLNSSTPMEDLPL CCCCCCCCCHHHCCH | 26.86 | 28889911 | |
| 528 | Acetylation | LRANPTDKKPRKAAL HHCCCCCCCCHHHHH | 68.13 | 24489116 | |
| 529 | Acetylation | RANPTDKKPRKAALL HCCCCCCCCHHHHHH | 53.52 | 24489116 | |
| 532 | Ubiquitination | PTDKKPRKAALLTNE CCCCCCHHHHHHHCC | 46.68 | 17644757 | |
| 532 | Acetylation | PTDKKPRKAALLTNE CCCCCCHHHHHHHCC | 46.68 | 24489116 | |
| 548 | Ubiquitination | EGPDPAAKSSSYYNL CCCCCCCCCCCCCCC | 53.64 | 17644757 | |
| 548 | Acetylation | EGPDPAAKSSSYYNL CCCCCCCCCCCCCCC | 53.64 | 24489116 | |
| 549 | Phosphorylation | GPDPAAKSSSYYNLR CCCCCCCCCCCCCCC | 21.57 | 30377154 | |
| 550 | Phosphorylation | PDPAAKSSSYYNLRS CCCCCCCCCCCCCCC | 22.96 | 30377154 | |
| 551 | Phosphorylation | DPAAKSSSYYNLRSK CCCCCCCCCCCCCCC | 38.43 | 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 AHC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AHC1_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 AHC1_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-37; SER-505 AND THR-510,AND MASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, AND MASSSPECTROMETRY. | |
