HIST1H2BD

H2BC5
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 5KGF
Identifiers
Aliases	H2BC5, H2B.1B, H2B/b, H2BFB, HIRIP2, dJ221C16.6, histone cluster 1, H2bd, histone cluster 1 H2B family member d, H2BFG, H2BFL, H2B/k, H2B/l, H2B/h, H2BFK, HIST1H2BE, HIST1H2BC, HIST1H2BG, HIST1H2BI, H2BFA, H2BFH, H2B/a, H2B/g, HIST1H2BF, HIST1H2BD, H2B clustered histone 5
External IDs	OMIM: 602799 MGI: 1925553 HomoloGene: 134740 GeneCards: H2BC5
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.2 Start 26,158,122 bp End 26,171,349 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 B1.3 Start 58,839,746 bp End 58,840,359 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube Achilles tendon pylorus prostate right lobe of liver right ventricle ganglionic eminence kidney islet of Langerhans anterior pituitary Top expressed in medial ganglionic eminence lens spermatid cerebellar cortex trigeminal ganglion spermatocyte visual cortex olfactory bulb superior frontal gyrus cerebellar vermis More reference expression data BioGPS n/a
Gene ontology Molecular function protein heterodimerization activity DNA binding molecular function protein binding identical protein binding Cellular component chromosome nucleosome extracellular exosome nucleoplasm nucleus cytosol extracellular space Biological process nucleosome assembly protein ubiquitination innate immune response in mucosa defense response to bacterium antimicrobial humoral immune response mediated by antimicrobial peptide Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3017 78303 Ensembl ENSG00000158373 ENSMUSG00000056895 UniProt P58876 P62807 Q9D2U9 RefSeq (mRNA) NM_021063 NM_138720 NM_030082 RefSeq (protein) NP_066407 NP_619790 NP_003517 NP_001368918 NP_084358 Location (UCSC) Chr 6: 26.16 – 26.17 Mb Chr 11: 58.84 – 58.84 Mb PubMed search
Wikidata
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Histone H2B type 1-D is a protein that in humans is encoded by the HIST1H2BD gene.

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryote. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H2B family. Two transcripts that encode the same protein have been identified for this gene, which is found in the large histone gene cluster on chromosome 6p22-p21.3.

Further reading

• Albig W, Kioschis P, Poustka A, et al. (1997). "Human histone gene organization: nonregular arrangement within a large cluster". Genomics. 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
• 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. S2CID 38539096.
• 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. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
• Lorain S, Quivy JP, Monier-Gavelle F, et al. (1998). "Core Histones and HIRIP3, a Novel Histone-Binding Protein, Directly Interact with WD Repeat Protein HIRA". Mol. Cell. Biol. 18 (9): 5546–56. doi:10.1128/MCB.18.9.5546. PMC 109139. PMID 9710638.
• 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. Bibcode:2002PNAS...9916899M. 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. S2CID 21854.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. 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.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
• 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. S2CID 25071586.
• 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. S2CID 2614680.