| UniProt ID | H4_XENLA | |
|---|---|---|
| UniProt AC | P62799 | |
| Protein Name | Histone H4 | |
| Gene Name | ||
| Organism | Xenopus laevis (African clawed frog). | |
| 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 | MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG | |
| 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 | - | |
| 2 | Acetylation | ------MSGRGKGGK ------CCCCCCCCC | 36.88 | - | |
| 4 | Citrullination | ----MSGRGKGGKGL ----CCCCCCCCCCC | 36.02 | - | |
| 4 | Methylation | ----MSGRGKGGKGL ----CCCCCCCCCCC | 36.02 | - | |
| 6 | Glutarylation | --MSGRGKGGKGLGK --CCCCCCCCCCCCC | 64.23 | - | |
| 6 | Acetylation | --MSGRGKGGKGLGK --CCCCCCCCCCCCC | 64.23 | - | |
| 6 | Other | --MSGRGKGGKGLGK --CCCCCCCCCCCCC | 64.23 | - | |
| 6 | Butyrylation | --MSGRGKGGKGLGK --CCCCCCCCCCCCC | 64.23 | - | |
| 6 | Lactoylation | --MSGRGKGGKGLGK --CCCCCCCCCCCCC | 64.23 | - | |
| 9 | Propionylation | SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH | 60.68 | - | |
| 9 | Acetylation | SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH | 60.68 | - | |
| 9 | Lactoylation | SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH | 60.68 | - | |
| 9 | Other | SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH | 60.68 | - | |
| 9 | Butyrylation | SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH | 60.68 | - | |
| 13 | Glutarylation | KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH | 60.25 | - | |
| 13 | Lactoylation | KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH | 60.25 | - | |
| 13 | Methylation | KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH | 60.25 | - | |
| 13 | Butyrylation | KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH | 60.25 | - | |
| 13 | Other | KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH | 60.25 | - | |
| 13 | Acetylation | KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH | 60.25 | - | |
| 17 | Other | GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH | 52.60 | - | |
| 17 | Lactoylation | GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH | 52.60 | - | |
| 17 | Propionylation | GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH | 52.60 | - | |
| 17 | Acetylation | GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH | 52.60 | - | |
| 17 | Butyrylation | GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH | 52.60 | - | |
| 21 | Methylation | GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC | 39.22 | - | |
| 32 | Propionylation | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | - | |
| 32 | Other | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | - | |
| 32 | Glutarylation | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | - | |
| 32 | Succinylation | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | - | |
| 32 | Lactoylation | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | - | |
| 32 | Butyrylation | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | - | |
| 32 | Acetylation | DNIQGITKPAIRRLA HHCCCCCHHHHHHHH | 30.45 | - | |
| 45 | Other | LARRGGVKRISGLIY HHHCCCCCEEECCCH | 47.49 | - | |
| 45 | Butyrylation | LARRGGVKRISGLIY HHHCCCCCEEECCCH | 47.49 | - | |
| 45 | Propionylation | LARRGGVKRISGLIY HHHCCCCCEEECCCH | 47.49 | - | |
| 48 | Phosphorylation | RGGVKRISGLIYEET CCCCCEEECCCHHHH | 31.42 | - | |
| 52 | Phosphorylation | KRISGLIYEETRGVL CEEECCCHHHHHHHH | 16.86 | - | |
| 60 | Other | EETRGVLKVFLENVI HHHHHHHHHHHHHHH | 28.65 | - | |
| 60 | Acetylation | EETRGVLKVFLENVI HHHHHHHHHHHHHHH | 28.65 | - | |
| 60 | Glutarylation | EETRGVLKVFLENVI HHHHHHHHHHHHHHH | 28.65 | - | |
| 78 | Butyrylation | VTYTEHAKRKTVTAM HHCCHHHCCCEECHH | 57.23 | - | |
| 78 | Other | VTYTEHAKRKTVTAM HHCCHHHCCCEECHH | 57.23 | - | |
| 78 | Lactoylation | VTYTEHAKRKTVTAM HHCCHHHCCCEECHH | 57.23 | - | |
| 78 | Glutarylation | VTYTEHAKRKTVTAM HHCCHHHCCCEECHH | 57.23 | - | |
| 78 | Succinylation | VTYTEHAKRKTVTAM HHCCHHHCCCEECHH | 57.23 | - | |
| 78 | Propionylation | VTYTEHAKRKTVTAM HHCCHHHCCCEECHH | 57.23 | - | |
| 80 | Propionylation | YTEHAKRKTVTAMDV CCHHHCCCEECHHHH | 46.79 | - | |
| 80 | Acetylation | YTEHAKRKTVTAMDV CCHHHCCCEECHHHH | 46.79 | - | |
| 80 | Other | YTEHAKRKTVTAMDV CCHHHCCCEECHHHH | 46.79 | - | |
| 80 | Butyrylation | YTEHAKRKTVTAMDV CCHHHCCCEECHHHH | 46.79 | - | |
| 80 | Glutarylation | YTEHAKRKTVTAMDV CCHHHCCCEECHHHH | 46.79 | - | |
| 89 | Phosphorylation | VTAMDVVYALKRQGR ECHHHHHHHHHHCCC | 13.18 | - | |
| 92 | Acetylation | MDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | - | |
| 92 | Succinylation | MDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | - | |
| 92 | Propionylation | MDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | - | |
| 92 | Other | MDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | - | |
| 92 | Lactoylation | MDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | - | |
| 92 | Glutarylation | MDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | - | |
| 92 | Butyrylation | MDVVYALKRQGRTLY HHHHHHHHHCCCCEE | 34.21 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 48 | S | Phosphorylation | Kinase | PAK2 | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H4_XENLA !! | ||||||
* 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_XENLA !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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