|Ref Sequence ID
|Protein Existence Status
|H2A.J promotes inflammatory gene expression in senescence.required for the production of SASP (senescent-associated secretory proteins)factors.
|The specific C-terminus of H2A.J is important for its function in promoting inflammatory gene expression in senescence.H2A.J differs from canonical H2A by only five amino acids involving a substitution of Val for Ala at position 11 in the N-terminal tail, and a unique C terminus containing a potentially phosphorylatable SQ motif.Conserved Val11 and Ser-123 are functionally important for H2A.J transcriptional activity.
|Acetylation, Isopeptide bond formation, Methylation, Phosphorylation, Ubl conjugation
| Site(s) of PTM(s)
|>sp|Q3ZBX9|H2AJ_BOVIN Histone H2A.J OS=Bos taurus OX=9913 GN=H2AJ PE=2 SV=1 MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKK T*121ESQKTKSK
|Predicted Disorder Regions
|TM Helix Prediction
|No TM helices
|Significance of PTMs
|phosphorylation of H2A.J on Ser-123 which is important for DNA-nucleosome interaction.Phosphorylation of the SQ motif plays a role in DNA-damage responses.Monoubiquitination of Lys-120 gives a specific tag for epigenetic transcriptional repression.Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties.Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription
|1.Contrepois, K., Coudereau, C., Benayoun, B. et al. Histone variant H2A.J accumulates in senescent cells and promotes inflammatory gene expression. Nat Commun 8, 14995 (2017). https://doi.org/10.1038/ncomms14995 2.Foster ER, Downs JA. Histone H2A phosphorylation in DNA double-strand break repair. FEBS J. 2005 Jul;272(13):3231-40. doi: 10.1111/j.1742-4658.2005.04741.x. PMID: 15978030.