HIST1H2BH

Histone cluster 1, H2bh
PDB rendering based on 1aoi.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1aoi​, 1eqz​, 1f66​, 1hio​, 1hq3​, 1kx3​, 1kx4​, 1kx5​, 1m18​, 1m19​, 1m1a​, 1p34​, 1p3a​, 1p3b​, 1p3f​, 1p3g​, 1p3i​, 1p3k​, 1p3l​, 1p3m​, 1p3o​, 1p3p​, 1s32​, 1tzy​, 1u35​, 1zbb​, 1zla​, 2aro​, 2cv5​, 2f8n​, 2fj7​, 2hio​, 2nzd​
Identifiers
Symbols	HIST1H2BH ; H2B/j; H2BFJ
External IDs	OMIM: 602806 HomoloGene: 134772 GeneCards: HIST1H2BH Gene
Gene ontology Molecular function • DNA binding • protein heterodimerization activity Cellular component • nucleosome • nucleus • nucleoplasm • extracellular exosome Biological process • chromatin organization • nucleosome assembly Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8345	665596
Ensembl	ENSG00000275713	ENSMUSG00000069307
UniProt	Q93079	Q64478
RefSeq (mRNA)	NM_003524	NM_001097979
RefSeq (protein)	NP_003515	NP_001091448
Location (UCSC)	Chr 6: 26.25 – 26.25 Mb	Chr 13: 21.81 – 21.81 Mb
PubMed search

Histone H2B type 1-H is a protein that in humans is encoded by the HIST1H2BH gene.^[1][2][3]

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2B family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.^[3]

References

1. Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D (Apr 1997). "Human histone gene organization: nonregular arrangement within a large cluster". Genomics 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
2. Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
3. "Entrez Gene: HIST1H2BH histone cluster 1, H2bh".

Further reading

• Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus.". Hum. Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656.
• El Kharroubi A, Piras G, Zensen R, Martin MA (1998). "Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter.". Mol. Cell. Biol. 18 (5): 2535–44. PMC 110633. PMID 9566873.
• Deng L, de la Fuente C, Fu P, et al. (2001). "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones.". Virology 277 (2): 278–95. doi:10.1006/viro.2000.0593. PMID 11080476.
• Deng L, Wang D, de la Fuente C, et al. (2001). "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA.". Virology 289 (2): 312–26. doi:10.1006/viro.2001.1129. PMID 11689053.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Cheung WL, Ajiro K, Samejima K, et al. (2003). "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase.". Cell 113 (4): 507–17. doi:10.1016/S0092-8674(03)00355-6. PMID 12757711.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
• Lusic M, Marcello A, Cereseto A, Giacca M (2004). "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter.". EMBO J. 22 (24): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
• Golebiowski F, Kasprzak KS (2007). "Inhibition of core histones acetylation by carcinogenic nickel(II).". Mol. Cell. Biochem. 279 (1-2): 133–9. doi:10.1007/s11010-005-8285-1. PMID 16283522.
• Zhu B, Zheng Y, Pham AD, et al. (2006). "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation.". Mol. Cell 20 (4): 601–11. doi:10.1016/j.molcel.2005.09.025. PMID 16307923.
• Bonenfant D, Coulot M, Towbin H, et al. (2006). "Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry.". Mol. Cell Proteomics 5 (3): 541–52. doi:10.1074/mcp.M500288-MCP200. PMID 16319397.
• Siuti N, Roth MJ, Mizzen CA, et al. (2006). "Gene-specific characterization of human histone H2B by electron capture dissociation.". J. Proteome Res. 5 (2): 233–9. doi:10.1021/pr050268v. PMID 16457587.
• Beck HC, Nielsen EC, Matthiesen R, et al. (2006). "Quantitative proteomic analysis of post-translational modifications of human histones.". Mol. Cell Proteomics 5 (7): 1314–25. doi:10.1074/mcp.M600007-MCP200. PMID 16627869.
• Pavri R, Zhu B, Li G, et al. (2006). "Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II.". Cell 125 (4): 703–17. doi:10.1016/j.cell.2006.04.029. PMID 16713563.
• Kim SC, Sprung R, Chen Y, et al. (2006). "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.". Mol. Cell 23 (4): 607–18. doi:10.1016/j.molcel.2006.06.026. PMID 16916647.