Primary Information |
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| BoMiProt ID | Bomi6287 |
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| Protein Name | Histone H2A.J |
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| Organism | Bos taurus |
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| Uniprot ID | Q3ZBX9 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001071557.1 |
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| Aminoacid Length | 129 |
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| Molecular Weight | 14019 |
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| FASTA Sequence |
Download |
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| Gene Name | H2AJ |
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| Gene ID | 618489 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| Protein Function | H2A.J promotes inflammatory gene expression in senescence.required for the production of SASP (senescent-associated secretory proteins)factors. |
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| Biochemical Properties | 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. |
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| PTMs | Acetylation, Isopeptide bond formation, Methylation, Phosphorylation, Ubl conjugation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q3ZBX9|H2AJ_BOVIN Histone H2A.J OS=Bos taurus OX=9913 GN=H2AJ PE=2 SV=1
MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT
AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKK
T*121ESQKTKSK |
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| Predicted Disorder Regions | 1-33, 114-129 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| 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 |
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| Bibliography | 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. |
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