HIST1H2BB

Histone cluster 1, H2bb, also known as HIST1H2BB, is a human gene.cite web | title = Entrez Gene: HIST1H2BB histone cluster 1, H2bb| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3018| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: HIST1H2BB histone cluster 1, H2bb| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3018| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Albig W, Kardalinou E, Drabent B, "et al." |title=Isolation and characterization of two human H1 histone genes within clusters of core histone genes. |journal=Genomics |volume=10 |issue= 4 |pages= 940–8 |year= 1991 |pmid= 1916825 |doi=
*cite journal | author=Kardalinou E, Eick S, Albig W, Doenecke D |title=Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones. |journal=J. Cell. Biochem. |volume=52 |issue= 4 |pages= 375–83 |year= 1993 |pmid= 8227173 |doi= 10.1002/jcb.240520402
*cite journal | author=Albig W, Kioschis P, Poustka A, "et al." |title=Human histone gene organization: nonregular arrangement within a large cluster. |journal=Genomics |volume=40 |issue= 2 |pages= 314–22 |year= 1997 |pmid= 9119399 |doi= 10.1006/geno.1996.4592
*cite journal | author=Albig W, Doenecke D |title=The human histone gene cluster at the D6S105 locus. |journal=Hum. Genet. |volume=101 |issue= 3 |pages= 284–94 |year= 1998 |pmid= 9439656 |doi=
*cite journal | author=El Kharroubi A, Piras G, Zensen R, Martin MA |title=Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2535–44 |year= 1998 |pmid= 9566873 |doi=
*cite journal | author=Deng L, de la Fuente C, Fu P, "et al." |title=Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. |journal=Virology |volume=277 |issue= 2 |pages= 278–95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593
*cite journal | author=Deng L, Wang D, de la Fuente C, "et al." |title=Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA. |journal=Virology |volume=289 |issue= 2 |pages= 312–26 |year= 2001 |pmid= 11689053 |doi= 10.1006/viro.2001.1129
*cite journal | author=Galasinski SC, Louie DF, Gloor KK, "et al." |title=Global regulation of post-translational modifications on core histones. |journal=J. Biol. Chem. |volume=277 |issue= 4 |pages= 2579–88 |year= 2002 |pmid= 11709551 |doi= 10.1074/jbc.M107894200
*cite journal | author=Marzluff WF, Gongidi P, Woods KR, "et al." |title=The human and mouse replication-dependent histone genes. |journal=Genomics |volume=80 |issue= 5 |pages= 487–98 |year= 2003 |pmid= 12408966 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Cheung WL, Ajiro K, Samejima K, "et al." |title=Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase. |journal=Cell |volume=113 |issue= 4 |pages= 507–17 |year= 2003 |pmid= 12757711 |doi=
*cite journal | author=Lusic M, Marcello A, Cereseto A, Giacca M |title=Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6550–61 |year= 2004 |pmid= 14657027 |doi= 10.1093/emboj/cdg631
*cite journal | author=Citterio E, Papait R, Nicassio F, "et al." |title=Np95 is a histone-binding protein endowed with ubiquitin ligase activity. |journal=Mol. Cell. Biol. |volume=24 |issue= 6 |pages= 2526–35 |year= 2004 |pmid= 14993289 |doi=
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Golebiowski F, Kasprzak KS |title=Inhibition of core histones acetylation by carcinogenic nickel(II). |journal=Mol. Cell. Biochem. |volume=279 |issue= 1-2 |pages= 133–9 |year= 2007 |pmid= 16283522 |doi= 10.1007/s11010-005-8285-1
*cite journal | author=Zhu B, Zheng Y, Pham AD, "et al." |title=Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation. |journal=Mol. Cell |volume=20 |issue= 4 |pages= 601–11 |year= 2006 |pmid= 16307923 |doi= 10.1016/j.molcel.2005.09.025
*cite journal | author=Bonenfant D, Coulot M, Towbin H, "et al." |title=Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry. |journal=Mol. Cell Proteomics |volume=5 |issue= 3 |pages= 541–52 |year= 2006 |pmid= 16319397 |doi= 10.1074/mcp.M500288-MCP200
*cite journal | author=Pavri R, Zhu B, Li G, "et al." |title=Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. |journal=Cell |volume=125 |issue= 4 |pages= 703–17 |year= 2006 |pmid= 16713563 |doi= 10.1016/j.cell.2006.04.029
*cite journal | author=Kim SC, Sprung R, Chen Y, "et al." |title=Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. |journal=Mol. Cell |volume=23 |issue= 4 |pages= 607–18 |year= 2006 |pmid= 16916647 |doi= 10.1016/j.molcel.2006.06.026

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