| UniProt ID | H2B6_ARATH | |
|---|---|---|
| UniProt AC | O23629 | |
| Protein Name | Histone H2B.6 | |
| Gene Name | H2B | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 150 | |
| 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 | MAPRAEKKPAEKKPAAEKPVEEKSKAEKAPAEKKPKAGKKLPKEAGAGGDKKKKMKKKSVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLASESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS | |
| 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 | Methylation | ------MAPRAEKKP ------CCCHHHCCC | 11.42 | 17691833 | |
| 2 | "N,N-dimethylalanine" | ------MAPRAEKKP ------CCCHHHCCC | 11.42 | - | |
| 7 | Acetylation | -MAPRAEKKPAEKKP -CCCHHHCCCCCCCC | 64.17 | 17691833 | |
| 12 | Acetylation | AEKKPAEKKPAAEKP HHCCCCCCCCCCCCC | 67.19 | 17691833 | |
| 13 | "N6,N6-dimethyllysine" | EKKPAEKKPAAEKPV HCCCCCCCCCCCCCH | 31.24 | - | |
| 13 | Methylation | EKKPAEKKPAAEKPV HCCCCCCCCCCCCCH | 31.24 | - | |
| 28 | Acetylation | EEKSKAEKAPAEKKP HHHHHHHCCCHHHCC | 65.61 | 17691833 | |
| 33 | Acetylation | AEKAPAEKKPKAGKK HHCCCHHHCCCCCCC | 76.20 | 17691833 | |
| 34 | Acetylation | EKAPAEKKPKAGKKL HCCCHHHCCCCCCCC | 43.16 | 21311031 | |
| 39 | Acetylation | EKKPKAGKKLPKEAG HHCCCCCCCCCHHHC | 56.87 | 17691833 | |
| 40 | Acetylation | KKPKAGKKLPKEAGA HCCCCCCCCCHHHCC | 69.93 | 17691833 | |
| 72 | Methylation | IYIFKVLKQVHPDIG HHHHHHHHHHCCCCC | 53.94 | 23161681 | |
| 81 | Phosphorylation | VHPDIGISSKAMGIM HCCCCCCCHHHHHHH | 22.15 | 25561503 | |
| 82 | Phosphorylation | HPDIGISSKAMGIMN CCCCCCCHHHHHHHH | 23.63 | 25561503 | |
| 83 | Methylation | PDIGISSKAMGIMNS CCCCCCHHHHHHHHH | 35.29 | 23161681 | |
| 116 | Phosphorylation | YNKKPTITSREIQTA HCCCCCCCHHHHHHH | 24.98 | 25561503 | |
| 117 | Phosphorylation | NKKPTITSREIQTAV CCCCCCCHHHHHHHH | 24.86 | 25561503 | |
| 134 | Methylation | VLPGELAKHAVSEGT HCCHHHHHHHHHHHC | 44.73 | 23161681 | |
| 138 | Phosphorylation | ELAKHAVSEGTKAVT HHHHHHHHHHCHHHH | 30.96 | 25561503 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H2B6_ARATH !! | ||||||
* 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 H2B6_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of H2B6_ARATH !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Characterization of post-translational modifications of histone H2B-variants isolated from Arabidopsis thaliana."; Bergmueller E., Gehrig P.M., Gruissem W.; J. Proteome Res. 6:3655-3668(2007). Cited for: ACETYLATION AT LYS-7; LYS-12; LYS-28; LYS-33; LYS-39 AND LYS-40,METHYLATION AT ALA-2, UBIQUITINATION AT LYS-146, AND MASSSPECTROMETRY. | |
| Methylation | |
| Reference | PubMed |
| "Characterization of post-translational modifications of histone H2B-variants isolated from Arabidopsis thaliana."; Bergmueller E., Gehrig P.M., Gruissem W.; J. Proteome Res. 6:3655-3668(2007). Cited for: ACETYLATION AT LYS-7; LYS-12; LYS-28; LYS-33; LYS-39 AND LYS-40,METHYLATION AT ALA-2, UBIQUITINATION AT LYS-146, AND MASSSPECTROMETRY. | |