| UniProt ID | H2AX_XENLA | |
|---|---|---|
| UniProt AC | Q6GM86 | |
| Protein Name | Histone H2AX | |
| Gene Name | h2afx | |
| Organism | Xenopus laevis (African clawed frog). | |
| Sequence Length | 139 | |
| Subcellular Localization | Nucleus. Chromosome. | |
| Protein Description | Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation (By similarity).. | |
| Protein Sequence | MSGRGKAVSKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAHRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKSRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKSSGGVSTSGKKSSQQSQEY | |
| 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 | Acetylation | ------MSGRGKAVS ------CCCCCCHHH | 36.88 | - | |
| 2 | Phosphorylation | ------MSGRGKAVS ------CCCCCCHHH | 36.88 | - | |
| 10 | Lactoylation | GRGKAVSKTRAKAKT CCCCHHHHHHHHHHH | 35.12 | - | |
| 136 | Phosphorylation | GKKSSQQSQEY---- CCCCCCCCCCC---- | 19.83 | 10477747 | |
| 139 | Phosphorylation | SSQQSQEY------- CCCCCCCC------- | 19.06 | 19092802 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 139 | Y | Phosphorylation | Kinase | WSTF | A8DZJ1 | Uniprot |
| 139 | Y | Phosphorylation | Kinase | BAZ1B | - | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H2AX_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 H2AX_XENLA !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of H2AX_XENLA !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Megabase chromatin domains involved in DNA double-strand breaks invivo."; Rogakou E.P., Boon C., Redon C., Bonner W.M.; J. Cell Biol. 146:905-916(1999). Cited for: PHOSPHORYLATION AT SER-136. | |
| "WSTF regulates the H2A.X DNA damage response via a novel tyrosinekinase activity."; Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A.,Erdjument-Bromage H., Ishibe-Murakami S., Wang B., Tempst P.,Hofmann K., Patel D.J., Elledge S.J., Allis C.D.; Nature 457:57-62(2009). Cited for: PHOSPHORYLATION AT TYR-139. | |