| UniProt ID | H2B11_XENLA | |
|---|---|---|
| UniProt AC | P02281 | |
| Protein Name | Histone H2B 1.1 | |
| Gene Name | ||
| Organism | Xenopus laevis (African clawed frog). | |
| Sequence Length | 126 | |
| 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 | MPEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKSRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK | |
| 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 |
|---|---|---|---|---|---|
| 6 | Acetylation | --MPEPAKSAPAPKK --CCCCCCCCCCCCC | 58.84 | - | |
| 13 | Acetylation | KSAPAPKKGSKKAVT CCCCCCCCCCCCCCC | 68.32 | - | |
| 15 | Phosphorylation | APAPKKGSKKAVTKT CCCCCCCCCCCCCHH | 39.60 | 12757711 | |
| 16 | Acetylation | PAPKKGSKKAVTKTQ CCCCCCCCCCCCHHC | 54.11 | - | |
| 21 | Acetylation | GSKKAVTKTQKKDGK CCCCCCCHHCCCCCC | 42.22 | - | |
| 113 | O-linked_Glycosylation | ELAKHAVSEGTKAVT HHHHHHHHHHCHHHH | 30.96 | - |
| 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 H2B11_XENLA !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H2B11_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 H2B11_XENLA !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of H2B11_XENLA !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Apoptotic phosphorylation of histone H2B is mediated by mammaliansterile twenty kinase."; Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A.,Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.; Cell 113:507-517(2003). Cited for: PHOSPHORYLATION AT SER-15. | |