Primary Information |
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| BoMiProt ID | Bomi6291 |
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| Protein Name | Histone H3.2 |
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| Organism | Bos taurus |
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| Uniprot ID | P84227 |
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| Milk Fraction | Whey,Casein |
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| Ref Sequence ID | NP_001160041.1 |
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| Aminoacid Length | 136 |
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| Molecular Weight | 15388 |
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| FASTA Sequence |
Download |
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| Gene Name | N/A |
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| Gene ID | 504599
788077 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | Core component of nucleosome which play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. H3.2 are expressed only in S-phase. |
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| PTMs | Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Lipidation, Methylation, Palmitoylation, Phosphorylation, 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, 115-136 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).Mono methylation on Lys of TK4QTAR which is imp for transcriptional activation.andMono,Di and Tri-methylation K9STGGKAPR which is imp for transcriptional silencing.Acetylation on Lys of KSTGGK14APR which is imp for transcriptional activation.H3.2 is enriched in Lys27 di- and trimethylation. These generally repressive marks have been associated with gene silencing and the formation of facultative heterochromatin. |
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| Bibliography | 1.Hake SB, Garcia BA, Duncan EM, Kauer M, Dellaire G, Shabanowitz J, Bazett-Jones DP, Allis CD, Hunt DF. Expression patterns and post-translational modifications associated with mammalian histone H3 variants. J Biol Chem. 2006 Jan 6;281(1):559-68. doi: 10.1074/jbc.M509266200. Epub 2005 Nov 2. PMID: 16267050. |
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