| UniProt ID | H2B1_CHICK | |
|---|---|---|
| UniProt AC | P0C1H3 | |
| Protein Name | Histone H2B 1/2/3/4/6 | |
| Gene Name | H2B-I | |
| Organism | Gallus gallus (Chicken). | |
| 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.; Has broad-spectrum antibacterial activity. May be important in the antimicrobial defenses of chick reproductive system during follicle development in the ovary and egg formation in the oviduct.. | |
| Protein Sequence | MPEPAKSAPAPKKGSKKAVTKTQKKGDKKRKKSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | |
| 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 | 12865423 | |
| 13 | Acetylation | KSAPAPKKGSKKAVT CCCCCCCCCCCCCCH | 68.32 | 12865423 | |
| 15 | Phosphorylation | APAPKKGSKKAVTKT CCCCCCCCCCCCHHH | 39.60 | 12757711 | |
| 16 | Acetylation | PAPKKGSKKAVTKTQ CCCCCCCCCCCHHHH | 54.11 | 12865423 | |
| 21 | Acetylation | GSKKAVTKTQKKGDK CCCCCCHHHHHCCCH | 42.22 | 12865423 | |
| 121 | Ubiquitination | EGTKAVTKYTSSK-- HHHHHHHHHCCCC-- | 39.67 | 2713375 |
| 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 H2B1_CHICK !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H2B1_CHICK !! | ||||||
* 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 H2B1_CHICK !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Acetylation of histone H2B mirrors that of H4 and H3 at the chickenbeta-globin locus but not at housekeeping genes."; Myers F.A., Chong W., Evans D.R., Thorne A.W., Crane-Robinson C.; J. Biol. Chem. 278:36315-36322(2003). Cited for: ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21. | |
| 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. | |