UniProt ID | H4_DROME | |
---|---|---|
UniProt AC | P84040 | |
Protein Name | Histone H4 | |
Gene Name | His4 | |
Organism | Drosophila melanogaster (Fruit fly). | |
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.. | |
Protein Sequence | MTGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
6 | Acetylation | --MTGRGKGGKGLGK --CCCCCCCCCCCCC | 64.23 | 19608861 | |
9 | Acetylation | TGRGKGGKGLGKGGA CCCCCCCCCCCCCHH | 60.68 | 15188406 | |
13 | Acetylation | KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH | 60.25 | 19608861 | |
17 | Acetylation | GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH | 52.60 | 15188406 | |
32 | Acetylation | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | 21791702 | |
32 | Succinylation | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | 22389435 | |
48 | Phosphorylation | RGGVKRISGLIYEET CCCCCEEECCCHHHH | 31.42 | 19429919 | |
78 | Succinylation | VTYTEHAKRKTVTAM HHCCHHHCCCEECHH | 57.23 | 22389435 | |
80 | Acetylation | YTEHAKRKTVTAMDV CCHHHCCCEECHHHH | 46.79 | 21791702 | |
80 | Succinylation | YTEHAKRKTVTAMDV CCHHHCCCEECHHHH | 46.79 | 22389435 | |
81 | Phosphorylation | TEHAKRKTVTAMDVV CHHHCCCEECHHHHH | 27.41 | 22817900 | |
83 | Phosphorylation | HAKRKTVTAMDVVYA HHCCCEECHHHHHHH | 22.84 | 22817900 | |
92 | Succinylation | MDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | 22389435 |
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_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H4_DROME !! |
* 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_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of H4_DROME !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"A histone code in meiosis: the histone kinase, NHK-1, is required forproper chromosomal architecture in Drosophila oocytes."; Ivanovska I., Khandan T., Ito T., Orr-Weaver T.L.; Genes Dev. 19:2571-2582(2005). Cited for: ACETYLATION AT LYS-6 AND LYS-13. | |
Phosphorylation | |
Reference | PubMed |
"Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81 AND THR-83, AND MASSSPECTROMETRY. |