Histone H2B type 1-C/E/F/G/I (UniProt: P62807; also known as Histone H2B.1 A, Histone H2B.a, H2B/a, Histone H2B.g, H2B/g, Histone H2B.h, H2B/h, Histone H2B.k, H2B/k, Histone H2B.l, H2B/l) is encoded by the HIST1H2BC (also known as H2BFL, HIST1H2BE, H2BFH, HIST1H2BF, H2BFG, HIST1H2BG, H2BFA, HIST1H2BI, H2BFK) gene (Gene ID: 3017, 9339, 8343, 8344, 8346, 8347) in human. Histones are basic nuclear proteins that are responsible for the nucleosome structure of chromatin in eukaryotes. They undergo a number of post-translational modifications (PTM) at their N- and C-terminal tails which can influence chromatin structure and stability; and consequently, transcription, and DNA replication and repair. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which DNA is wrapped in repeating units, called nucleosomes, which limits 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. Histone H2B is one of the main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N terminal tail, H2B is involved with the structure of the nucleosomes of the ′beads on a string′ structure. Histone H2B can be monoubiquitinated on Lysine123 by RAD6/UBC2-BRE1 complex to form H2BK123Ub1 complex that gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. H2BK123ub1 is reported to modulates the formation of double-strand breaks during meiosis and is a required for DNA-damage checkpoint activation. Methylation of N-terminus Proline 1 of histone H2B (Pme) by NTMT (CG1675) is one of the rare modification that has been addressed. Heat shock or arsenite treatment is shown to increase methylation on proline 1 in Drosophila cells. (Ref.: Villar-Garea, A., et al. (2012). Nucl. Acid Res. 40(4); 1536 1549; Desrosiers, R., and Tanguay, RM. (1998). J. Biol. Chem. 263(10):4686-4692).，官网链接：https://www.sigmaaldrich.cn/product/mm/abe1464 默克 科研、开发、生产。 作为生命科学行业的全球领先供应商，我们致力于为科研、生物技术开发和生产，以及制药药物疗法开发和生产提供各类解决方案和服务。

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