| UniProt ID | H2A_DROME | |
|---|---|---|
| UniProt AC | P84051 | |
| Protein Name | Histone H2A | |
| Gene Name | His2A | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 124 | |
| 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 | MSGRGKGGKVKGKAKSRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLSGVTIAQGGVLPNIQAVLLPKKTEKKA | |
| 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 | ------MSGRGKGGK ------CCCCCCCCC | 36.88 | - | |
| 2 | Phosphorylation | ------MSGRGKGGK ------CCCCCCCCC | 36.88 | 15133681 | |
| 6 | Acetylation | --MSGRGKGGKVKGK --CCCCCCCCCCCCC | 64.23 | 21791702 | |
| 9 | Acetylation | SGRGKGGKVKGKAKS CCCCCCCCCCCCCCC | 49.82 | 21791702 | |
| 36 | Succinylation | RIHRLLRKGNYAERV HHHHHHHCCCHHHHH | 52.02 | 22389435 | |
| 104 | Methylation | LSGVTIAQGGVLPNI HHCCEEECCCCCCCC | 45.37 | - | |
| 118 | Ubiquitination | IQAVLLPKKTEKKA- CEEEECCCCCCCCC- | 72.76 | 31113955 | |
| 119 | Ubiquitination | QAVLLPKKTEKKA-- EEEECCCCCCCCC-- | 61.04 | 15386022 | |
| 120 | Phosphorylation | AVLLPKKTEKKA--- EEECCCCCCCCC--- | 60.20 | 16230526 |
| 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 H2A_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H2A_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 H2A_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of H2A_DROME !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| 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: PHOSPHORYLATION AT THR-120. | |
| "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 duringmitosis in the early Drosophila embryo."; Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N.,Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.; Genes Dev. 18:877-888(2004). Cited for: PROTEIN SEQUENCE OF 96-122, AND PHOSPHORYLATION AT THR-120. | |
