Primary Information |
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BoMiProt ID | Bomi6290 |
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Protein Name | Histone H3.1 |
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Organism | Bos taurus |
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Uniprot ID | P68432 |
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Milk Fraction | Whey |
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Ref Sequence ID | XP_002697506.1 |
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Aminoacid Length | 136 |
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Molecular Weight | 15404 |
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FASTA Sequence |
Download |
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Gene ID | 107131750 |
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Protein Existence Status | Reviewed |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | testis |
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Protein Function | Citrullination of extracellular histone H3.1 reduces antibacterial activity and exacerbates its proteolytic degradation |
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PTMs | Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Methylation, Phosphoprotein, Ubl conjugation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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Predicted Disorder Regions | 1-55, 114-136 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.Citrullination at Arg-9 and 18 by PADI4 impairs methylation and represses transcription.Phosphorylation at Thr-12 by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. |
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Bibliography | 1.Tanner L, Bhongir RKV, Karlsson CAQ, Le S, Ljungberg JK, Andersson P, Andersson C, Malmström J, Egesten A, Single AB. Citrullination of extracellular histone H3.1 reduces antibacterial activity and exacerbates its proteolytic degradation. J Cyst Fibros. 2021 Mar;20(2):346-355. doi: 10.1016/j.jcf.2020.07.010. Epub 2020 Jul 26. PMID: 32727663. |