| UniProt ID | H4_YEAST | |
|---|---|---|
| UniProt AC | P02309 | |
| Protein Name | Histone H4 | |
| Gene Name | HHF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 103 | |
| Subcellular Localization | Nucleus. Chromosome. | |
| Protein Description | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP UAF seems to stimulate basal transcription to a fully activated level.. | |
| Protein Sequence | MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSGRGKGGK ------CCCCCCCCC | 36.88 | 28889911 | |
| 6 | Acetylation | --MSGRGKGGKGLGK --CCCCCCCCCCCCC | 64.23 | 19113941 | |
| 9 | Acetylation | SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH | 60.68 | 19113941 | |
| 9 | Butyrylation | SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH | 60.68 | 19113941 | |
| 13 | Acetylation | KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH | 60.25 | 19113941 | |
| 13 | Butyrylation | KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH | 60.25 | 27105113 | |
| 17 | Acetylation | GLGKGGAKRHRKILR CCCCCHHHHHHHHHH | 52.60 | 11080160 | |
| 17 | Ubiquitination | GLGKGGAKRHRKILR CCCCCHHHHHHHHHH | 52.60 | 22817900 | |
| 21 | Ubiquitination | GGAKRHRKILRDNIQ CHHHHHHHHHHHHCC | 39.71 | 22817900 | |
| 21 | Acetylation | GGAKRHRKILRDNIQ CHHHHHHHHHHHHCC | 39.71 | 17194708 | |
| 32 | Succinylation | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | 22389435 | |
| 32 | Ubiquitination | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | 23749301 | |
| 32 | Acetylation | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | 24489116 | |
| 48 | Phosphorylation | RGGVKRISGLIYEEV CCCCCEECCHHHHHH | 31.42 | 22369663 | |
| 56 | Methylation | GLIYEEVRAVLKSFL CHHHHHHHHHHHHHH | 23.43 | 19113941 | |
| 60 | Acetylation | EEVRAVLKSFLESVI HHHHHHHHHHHHHHH | 32.34 | 24489116 | |
| 60 | Ubiquitination | EEVRAVLKSFLESVI HHHHHHHHHHHHHHH | 32.34 | 23749301 | |
| 61 | Phosphorylation | EVRAVLKSFLESVIR HHHHHHHHHHHHHHH | 30.79 | 22369663 | |
| 65 | Phosphorylation | VLKSFLESVIRDSVT HHHHHHHHHHHHHCC | 25.62 | 22369663 | |
| 70 | Phosphorylation | LESVIRDSVTYTEHA HHHHHHHHCCCCHHH | 13.40 | 22369663 | |
| 72 | Phosphorylation | SVIRDSVTYTEHAKR HHHHHHCCCCHHHCC | 28.78 | 22369663 | |
| 78 | Ubiquitination | VTYTEHAKRKTVTSL CCCCHHHCCCEECHH | 57.23 | 23749301 | |
| 78 | Succinylation | VTYTEHAKRKTVTSL CCCCHHHCCCEECHH | 57.23 | 22389435 | |
| 78 | 2-Hydroxyisobutyrylation | VTYTEHAKRKTVTSL CCCCHHHCCCEECHH | 57.23 | - | |
| 80 | Ubiquitination | YTEHAKRKTVTSLDV CCHHHCCCEECHHHH | 46.79 | 22817900 | |
| 80 | Acetylation | YTEHAKRKTVTSLDV CCHHHCCCEECHHHH | 46.79 | 16768447 | |
| 92 | Ubiquitination | LDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | 23749301 | |
| 92 | Acetylation | LDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | 15808514 | |
| 92 | Glutarylation | LDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | 31542297 | |
| 97 | Phosphorylation | ALKRQGRTLYGFGG- HHHHCCCCEECCCC- | 31.02 | 28889911 |
| 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 H4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 92 | K | Glutarylation |
| 31542297 |
* 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 H4_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-48 AND SER-61, AND MASSSPECTROMETRY. | |
| "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-65, AND MASSSPECTROMETRY. | |
