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H2BC14
Identifiers
Aliases	H2BC14, H2B/e, H2BFE, dJ160A22.3, histone cluster 1, H2bm, histone cluster 1 H2B family member m, HIST1H2BM, H2B clustered histone 14
External IDs	OMIM: 602802; MGI: 2448407; HomoloGene: 136772; GeneCards: H2BC14; OMA:H2BC14 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.1 Start 27,815,022 bp End 27,815,489 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A3.1 Start 21,938,293 bp End 21,938,673 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow cells ventricular zone epithelium of colon tonsil thymus ganglionic eminence mucosa of transverse colon blood lymph node corpus callosum Top expressed in genital tubercle uterus spermatid bone marrow embryo embryo spermatocyte primary oocyte tail of embryo thymus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein heterodimerization activity DNA binding Cellular component nucleosome nucleus chromosome extracellular exosome nucleoplasm cytosol Biological process nucleosome assembly protein ubiquitination Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8342 319187 Ensembl ENSG00000273703 ENSMUSG00000095217 UniProt Q99879 P10853 RefSeq (mRNA) NM_003521 NM_178201 RefSeq (protein) NP_003512 NP_835505 NP_001091448 NP_001300809 NP_001104025 NP_001300807 NP_835502 NP_835506 NP_835508 Location (UCSC) Chr 6: 27.82 – 27.82 Mb Chr 13: 21.94 – 21.94 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Histone H2B type 1-M is a protein that in humans is encoded by the HIST1H2BM gene.

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 small histone gene cluster on chromosome 6p22-p21.3.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000273703 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000095217 – 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, Doenecke D (Feb 1998). "The human histone gene cluster at the D6S105 locus". Hum Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656. S2CID 38539096.
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: HIST1H2BM histone cluster 1, H2bm".

Further reading

• 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.
• Albig W, Trappe R, Kardalinou E, et al. (1999). "The human H2A and H2B histone gene complement". Biol. Chem. 380 (1): 7–18. doi:10.1515/BC.1999.002. PMID 10064132. S2CID 12807248.
• 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.
• 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.
• 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.

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