Histone H2B type 1-K

Also known as: HIRA-interacting protein 1, H2BC12, O60814

Histone H2B type 1-K (H2BC12, O60814) is a core component of the nucleosome, the fundamental structural unit of chromatin. As a histone protein, it pairs with H2A to form the H2A-H2B dimer, which assembles with histones H3 and H4 to create the nucleosome core particle. This structure wraps approximately 147 base pairs of DNA, compacting it into chromatin and regulating DNA accessibility for processes such as transcription, replication, and repair. Post-translational modifications of H2B, including ubiquitination and acetylation, modulate chromatin dynamics and gene expression, though specific functional roles for this variant remain to be fully characterized. Current research on Histone H2B type 1-K is classified as experimental, with no indexed PubMed references available. This indicates a lack of published, peer-reviewed studies specifically investigating this histone variant’s unique properties or functions. Given the high sequence similarity among H2B subtypes, its role is presumed to align with general nucleosome functions, but variant-specific interactions (e.g., with HIRA in histone chaperone complexes) or tissue-specific expression patterns have not been experimentally validated. Clinically, histones are implicated in cancer, autoimmune disorders, and epigenetic dysregulation, but no direct clinical relevance has been established for Histone H2B type 1-K. Its experimental status and absence of research data preclude any therapeutic or diagnostic applications at this time. Further studies are needed to elucidate its specific contributions to chromatin biology and disease. For research purposes only — not medical advice.

Key data

Mechanism of action

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling

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