H2BFS

H2B histone family, member S (pseudogene)
Identifiers
Symbol	H2BFS
External IDs	GeneCards: H2BFS Gene
Gene ontology Molecular function • DNA binding • protein heterodimerization activity Cellular component • nucleosome • extracellular space • nucleus Biological process • innate immune response in mucosa • antibacterial humoral response • substantia nigra development • defense response to Gram-positive bacterium Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	54145	n/a
Ensembl	n/a	n/a
UniProt	P57053	n/a
RefSeq (mRNA)	NM_017445	n/a
RefSeq (protein)	NP_059141	n/a
Location (UCSC)	n/a	n/a
PubMed search		n/a

Histone H2B type F-S is a protein that in humans is encoded by the H2BFS gene.^[1]

References

1. "Entrez Gene: H2BFS H2B histone family, member S".

Further reading

• Frohm M, Gunne H, Bergman AC, et al. (1996). "Biochemical and antibacterial analysis of human wound and blister fluid.". Eur. J. Biochem. 237 (1): 86–92. doi:10.1111/j.1432-1033.1996.0086n.x. PMID 8620898.
• 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.
• Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21.". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
• 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.
• Kim HS, Cho JH, Park HW, et al. (2002). "Endotoxin-neutralizing antimicrobial proteins of the human placenta.". J. Immunol. 168 (5): 2356–64. doi:10.4049/jimmunol.168.5.2356. PMID 11859126.
• 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.
• Tollin M, Bergman P, Svenberg T, et al. (2004). "Antimicrobial peptides in the first line defence of human colon mucosa.". Peptides 24 (4): 523–30. doi:10.1016/S0196-9781(03)00114-1. PMID 12860195.
• 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.
• Howell SJ, Wilk D, Yadav SP, Bevins CL (2004). "Antimicrobial polypeptides of the human colonic epithelium.". Peptides 24 (11): 1763–70. doi:10.1016/j.peptides.2003.07.028. PMID 15019208.
• 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.
• 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.
• 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.