HIST1H2BH

H2BC9
Identifiers
Aliases	H2BC9 , H2B/j, H2BFJ, histone cluster 1, H2bh, histone cluster 1 H2B family member h, HIST1H2BH, H2B clustered histone 9
External IDs	OMIM: 602806 MGI: 3710645 HomoloGene: 134772 GeneCards: H2BC9
Gene location (Human) Chr. Chromosome 6 (human) [1] Band 6p22.2 Start 26,251,614 bp [1] End 26,252,075 bp [1]
Gene location (Mouse) Chr. Chromosome 13 (mouse) [2] Band 13|13 A3.1 Start 22,017,913 bp [2] End 22,021,700 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow cells monocyte jejunal mucosa right ventricle thymus bronchial epithelial cell embryo right uterine tube cavity of mouth blood Top expressed in bone marrow mesencephalon esophagus ileum conceptus placenta heart yolk sac jejunum urinary bladder More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding protein heterodimerization activity protein binding enzyme binding ubiquitin-like protein ligase binding STAT family protein binding Cellular component chromosome nucleosome extracellular exosome nucleus nucleoplasm cytosol protein-containing complex Biological process nucleosome assembly protein ubiquitination Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8345 665622 Ensembl ENSG00000275713 ENSMUSG00000069303 UniProt Q93079 P10853 RefSeq (mRNA) NM_003524 NM_001110555 NM_001313878 RefSeq (protein) NP_003515 NP_835505 NP_001091448 NP_001300809 NP_001104025 NP_001300807 NP_835502 NP_835506 NP_835508 Location (UCSC) Chr 6: 26.25 – 26.25 Mb Chr 13: 22.02 – 22.02 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Histone H2B type 1-H is a protein that in humans is encoded by the HIST1H2BH gene. ^{[5] [6] [7]}

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000275713 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000069303 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "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. 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.
• 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.
• 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.
• 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.