HIST2H2BF

H2BC18
Identifiers
Aliases	H2BC18, histone cluster 2 H2B family member f, H2B clustered histone 18, HIST2H2BF
External IDs	MGI: 2448413 HomoloGene: 136264 GeneCards: H2BC18
Gene location (Human) Chr. Chromosome 1 (human) Band 1q21.2 Start 149,782,689 bp End 149,812,373 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 F2.1 Start 96,177,068 bp End 96,177,448 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow cells blood corpus callosum right uterine tube prostate thymus vagina cervix Achilles tendon stomach Top expressed in uterus bone marrow morula yolk sac mesencephalon spermatocyte thymus secondary oocyte spermatid blastocyst More reference expression data BioGPS n/a
Gene ontology Molecular function protein heterodimerization activity DNA binding molecular function Cellular component chromosome nucleosome extracellular exosome nucleus nucleoplasm cytosol Biological process nucleosome assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 440689 319189 Ensembl ENSG00000203814 ENSMUSG00000105827 UniProt Q5QNW6 Q64525 RefSeq (mRNA) NM_001024599 NM_001161334 NM_175666 RefSeq (protein) NP_001019770 NP_001154806 NP_783597 Location (UCSC) Chr 1: 149.78 – 149.81 Mb Chr 3: 96.18 – 96.18 Mb PubMed search
Wikidata
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Histone H2B type 2-F is a protein that in humans is encoded by the HIST2H2BF gene.

Further reading

• 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.
• 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.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
• 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.