HIST3H2BB

From Wikipedia, the free encyclopedia

Histone cluster 3, H2bb

PDB rendering based on 1aoi.

Available structures: 1aoi, 1eqz, 1f66, 1hio, 1hq3, 1kx3, 1kx4, 1kx5, 1m18, 1m19, 1m1a, 1p34, 1p3a, 1p3b, 1p3f, 1p3g, 1p3i, 1p3k, 1p3l, 1p3m, 1p3o, 1p3p, 1s32, 1tzy, 1u35, 1zbb, 1zla, 2aro, 2cv5, 2f8n, 2fj7, 2hio, 2nzd

Identifiers

Symbol(s)

HIST3H2BB;

External IDs

MGI: 1922442 HomoloGene: 75941

Gene ontology
Molecular Function:	• DNA binding
Cellular Component:	• nucleosome • nucleus • chromosome
Biological Process:	• nucleosome assembly • chromosome organization and biogenesis (sensu Eukaryota)

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_175055 (mRNA)
NP_778225 (protein)

NM_206882 (mRNA)
NP_996765 (protein)

Location

Chr 1: 226.71 - 226.71 Mb

Chr 11: 58.77 - 58.77 Mb

Pubmed search

[1]

[2]

Histone cluster 3, H2bb, also known as HIST3H2BB, is a human gene.^[1]

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. 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. Transcripts from this gene contain a palindromic termination element.^[1]

[edit] References

^ ^a ^b Entrez Gene: HIST3H2BB histone cluster 3, H2bb.

[edit] Further reading

Borowski P, Heiland M, Oehlmann K, et al. (1996). "Non-structural protein 3 of hepatitis C virus inhibits phosphorylation mediated by cAMP-dependent protein kinase.". Eur. J. Biochem. 237 (3): 611–8. PMID 8647104.
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. PMID 9566873.
Borowski P, Kühl R, Laufs R, et al. (1999). "Identification and characterization of a histone binding site of the non-structural protein 3 of hepatitis C virus.". J. Clin. Virol. 13 (1-2): 61–9. PMID 10405893.
Thomson S, Clayton AL, Hazzalin CA, et al. (1999). "The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase.". EMBO J. 18 (17): 4779–93. doi:10.1093/emboj/18.17.4779. PMID 10469656.
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.
Marzluff WF, Gongidi P, Woods KR, et al. (2003). "The human and mouse replication-dependent histone genes.". Genomics 80 (5): 487–98. PMID 12408966.
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. 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. PMID 12757711.
Coleman MA, Miller KA, Beernink PT, et al. (2004). "Identification of chromatin-related protein interactions using protein microarrays.". Proteomics 3 (11): 2101–7. doi:10.1002/pmic.200300593. PMID 14595808.
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. PMID 14657027.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Kanno T, Kanno Y, Siegel RM, et al. (2004). "Selective recognition of acetylated histones by bromodomain proteins visualized in living cells.". Mol. Cell 13 (1): 33–43. PMID 14731392.
Zhang Y, Griffin K, Mondal N, Parvin JD (2004). "Phosphorylation of histone H2A inhibits transcription on chromatin templates.". J. Biol. Chem. 279 (21): 21866–72. doi:10.1074/jbc.M400099200. PMID 15010469.
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. 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.
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.
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.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.