Alternative titles; symbols
HGNC Approved Gene Symbol: H3C2
Cytogenetic location: 6p22.2 Genomic coordinates (GRCh38): 6:26,031,589-26,032,099 (from NCBI)
For background information on histones, histone gene clusters, and the H3 histone family, see HIST1H3A (602810).
Zhong et al. (1983) identified a gene encoding a member of the H3 class of histones. Albig and Doenecke (1997) designated this gene H3/l.
By genomic sequence analysis, Marzluff et al. (2002) identified the mouse and human HIST1H3B genes. They noted that all H3 genes in histone gene cluster-1 (HIST1), including HIST1H3B, encode the same protein, designated H3.1. H3.1 differs from H3.2, which is encoded by HIST2H3C (142780), at only 1 residue, and from histone H3.3, which is encoded by both H3F3A (601128) and H3F3B (601058), at a few residues.
By analysis of a YAC contig, Albig et al. (1997) mapped the H3/l gene to 6p21.3, within a cluster of 35 histone genes.
By genomic sequence analysis, Marzluff et al. (2002) determined that the histone gene cluster on chromosome 6p22-p21, which they called HIST1, contains 55 histone genes, including HIST1H3B.
See HIST1H3A (602810) for functional information on H3.1 and the H3 histone family.
Wu et al. (2012) reported that a K27M mutation occurring in either H3F3A or HIST1H3B was observed in 78% of diffuse intrinsic pontine gliomas (DIPGs) and 22% of non-brain-stem gliomas.
Lewis et al. (2013) reported that human (DIPGs) containing the K27M mutation in either histone H3.3 (H3F3A) or H3.1 (HIST1H3B) display significantly lower overall amounts of H3 with trimethylated lysine-27 (H3K27me3) and that histone H3K27M transgenes are sufficient to reduce the amounts of H3K27me3 in vitro and in vivo. Lewis et al. (2013) found that H3K27M inhibits the enzymatic activity of the Polycomb repressive complex-2 (PRC2) through interaction with the EZH2 (601573) subunit. In addition, transgenes containing lysine-to-methionine substitutions at other known methylated lysines (H3K9 and H3K36) are sufficient to cause specific reduction in methylation through inhibition of SET domain enzymes. Lewis et al. (2013) proposed that K-to-M substitutions may represent a mechanism to alter epigenetic states in a variety of pathologies.
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Albig, W., Kioschis, P., Poustka, A., Meergans, K., Doenecke, D. Human histone gene organization: nonregular arrangement within a large cluster. Genomics 40: 314-322, 1997. [PubMed: 9119399] [Full Text: https://doi.org/10.1006/geno.1996.4592]
Lewis, P. W., Muller, M. M., Koletsky, M. S., Cordero, F., Lin, S., Banaszynski, L. A., Garcia, B. A., Muir, T. W., Becher, O. J., Allis, C. D. Inhibition of PRC2 activity by a gain-of-function H3 mutation found in pediatric glioblastoma. Science 340: 857-861, 2013. [PubMed: 23539183] [Full Text: https://doi.org/10.1126/science.1232245]
Marzluff, W. F., Gongidi, P., Woods, K. R., Jin, J., Maltais, L. J. The human and mouse replication-dependent histone genes. Genomics 80: 487-498, 2002. [PubMed: 12408966]
Wu, G., Broniscer, A., McEachron, T. A., Lu, C., Paugh, B. S., Becksfort, J., Qu, C., Ding, L., Huether, R., Parker, M., Zhang, J., Gajjar, A., and 9 others. Somatic histone H3 alterations in pediatric diffuse intrinsic pontine gliomas and non-brainstem glioblastomas. Nature Genet. 44: 251-253, 2012. [PubMed: 22286216] [Full Text: https://doi.org/10.1038/ng.1102]
Zhong, R., Roeder, R. G., Heintz, N. The primary structure and expression of four cloned human histone genes. Nucleic Acids Res. 11: 7409-7425, 1983. [PubMed: 6647026] [Full Text: https://doi.org/10.1093/nar/11.21.7409]