HIST1H2BB

From Wikipedia, the free encyclopedia

Histone cluster 1, 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)

HIST1H2BB; H2B.1; H2B/f; H2BFF; MGC119804

External IDs

OMIM: 602803 MGI: 2448377 HomoloGene: 86898

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_021062 (mRNA)
NP_066406 (protein)

NM_175664 (mRNA)
NP_783595 (protein)

Location

Chr 6: 26.15 - 26.15 Mb

Chr 13: 23.75 - 23.75 Mb

Pubmed search

[1]

[2]

Histone cluster 1, H2bb, also known as HIST1H2BB, 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 lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.^[1]

[edit] References

^ ^a ^b Entrez Gene: HIST1H2BB histone cluster 1, H2bb.

[edit] Further reading

Albig W, Kardalinou E, Drabent B, et al. (1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes.". Genomics 10 (4): 940–8. PMID 1916825.
Kardalinou E, Eick S, Albig W, Doenecke D (1993). "Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones.". J. Cell. Biochem. 52 (4): 375–83. doi:10.1002/jcb.240520402. PMID 8227173.
Albig W, Kioschis P, Poustka A, et al. (1997). "Human histone gene organization: nonregular arrangement within a large cluster.". Genomics 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus.". Hum. Genet. 101 (3): 284–94. PMID 9439656.
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.
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.
Galasinski SC, Louie DF, Gloor KK, et al. (2002). "Global regulation of post-translational modifications on core histones.". J. Biol. Chem. 277 (4): 2579–88. doi:10.1074/jbc.M107894200. PMID 11709551.
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.
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.
Citterio E, Papait R, Nicassio F, et al. (2004). "Np95 is a histone-binding protein endowed with ubiquitin ligase activity.". Mol. Cell. Biol. 24 (6): 2526–35. PMID 14993289.
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.
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.