Primary Information |
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BoMiProt ID | Bomi6292 |
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Protein Name | Histone H4/H4.1 |
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Organism | Bos taurus |
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Uniprot ID | P62803 |
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Milk Fraction | Whey,Casein |
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Ref Sequence ID | NP_001093194.1 |
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Aminoacid Length | 103 |
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Molecular Weight | 11367 |
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FASTA Sequence |
Download |
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Gene ID | 280691
526789
527645
530773
617875 |
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Protein Existence Status | Reviewed |
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Secondary Information |
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Protein Function | Core component of nucleosome. |
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PTMs | Acetylation, Citrullination, Hydroxylation, Isopeptide bond formation, Methylation, Phosphorylation, Ubl conjugation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P62803|H4_BOVIN Histone H4 OS=Bos taurus OX=9913 PE=1 SV=2
MS*2GRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRIS*48GLIY*52EETRGVLK
VFLENVIRDAVTYTEHAKRKT*81VTAMDVVY*89ALKRQGRTLYGFGG |
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Predicted Disorder Regions | 1-42, 101-103 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | Methylation of H4-Lys-20 generally correlates with transcriptional repression.H4K16 is the first lysine to be acetylated after replication which is important for recruiting Suv39h1 and G9a to the histone tails.H4K79 methylation is associated with gene silencing.Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4. |
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Bibliography | 1.Robin, P., Fritsch, L., Philipot, O. et al. Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a. Genome Biol 8, R270 (2007). https://doi.org/10.1186/gb-2007-8-12-r270 |