HIST3H2BB
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
Histone H2B type 3-B is a protein that in humans is encoded by the HIST3H2BB gene.{{cite journal |vauthors=Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ | title = The human and mouse replication-dependent histone genes | journal = Genomics | volume = 80 | issue = 5 | pages = 487–98 |date=Oct 2002 | pmid = 12408966 | doi =10.1016/S0888-7543(02)96850-3 }}{{cite web | title = Entrez Gene: HIST3H2BB histone cluster 3, H2bb| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=128312}}
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 base pairs (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.
References
{{reflist}}
Further reading
{{refbegin | 2}}
- {{cite journal |vauthors=Borowski P, Heiland M, Oehlmann K, etal |title=Non-structural protein 3 of hepatitis C virus inhibits phosphorylation mediated by cAMP-dependent protein kinase. |journal=Eur. J. Biochem. |volume=237 |issue= 3 |pages= 611–8 |year= 1996 |pmid= 8647104 |doi=10.1111/j.1432-1033.1996.0611p.x |doi-access=free }}
- {{cite journal |vauthors=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= 10.1128/mcb.18.5.2535| pmc=110633 }}
- {{cite journal |vauthors=Borowski P, Kühl R, Laufs R, etal |title=Identification and characterization of a histone binding site of the non-structural protein 3 of hepatitis C virus. |journal=J. Clin. Virol. |volume=13 |issue= 1–2 |pages= 61–9 |year= 1999 |pmid= 10405893 |doi=10.1016/S1386-6532(99)00007-4 }}
- {{cite journal |vauthors=Thomson S, Clayton AL, Hazzalin CA, etal |title=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. |journal=EMBO J. |volume=18 |issue= 17 |pages= 4779–93 |year= 1999 |pmid= 10469656 |doi= 10.1093/emboj/18.17.4779 | pmc=1171550 }}
- {{cite journal |vauthors=Deng L, de la Fuente C, Fu P, etal |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 |doi-access= free }}
- {{cite journal |vauthors=Deng L, Wang D, de la Fuente C, etal |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 |doi-access= free }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
- {{cite journal |vauthors=Cheung WL, Ajiro K, Samejima K, etal |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=10.1016/S0092-8674(03)00355-6 |s2cid=21854 |doi-access=free }}
- {{cite journal |vauthors=Coleman MA, Miller KA, Beernink PT, etal |title=Identification of chromatin-related protein interactions using protein microarrays. |journal=Proteomics |volume=3 |issue= 11 |pages= 2101–7 |year= 2004 |pmid= 14595808 |doi= 10.1002/pmic.200300593 |s2cid=23471253 }}
- {{cite journal |vauthors=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 | pmc=291826 }}
- {{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |doi-access= free }}
- {{cite journal |vauthors=Kanno T, Kanno Y, Siegel RM, etal |title=Selective recognition of acetylated histones by bromodomain proteins visualized in living cells. |journal=Mol. Cell |volume=13 |issue= 1 |pages= 33–43 |year= 2004 |pmid= 14731392 |doi=10.1016/S1097-2765(03)00482-9 |doi-access=free }}
- {{cite journal |vauthors=Zhang Y, Griffin K, Mondal N, Parvin JD |title=Phosphorylation of histone H2A inhibits transcription on chromatin templates. |journal=J. Biol. Chem. |volume=279 |issue= 21 |pages= 21866–72 |year= 2004 |pmid= 15010469 |doi= 10.1074/jbc.M400099200 |doi-access= free }}
- {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 | pmc=528928 }}
- {{cite journal |vauthors=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 |s2cid=25071586 |url=https://zenodo.org/record/1232822 }}
- {{cite journal |vauthors=Zhu B, Zheng Y, Pham AD, etal |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 |doi-access= free }}
- {{cite journal |vauthors=Bonenfant D, Coulot M, Towbin H, etal |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 |doi-access= free }}
- {{cite journal |vauthors=Beck HC, Nielsen EC, Matthiesen R, etal |title=Quantitative proteomic analysis of post-translational modifications of human histones. |journal=Mol. Cell. Proteomics |volume=5 |issue= 7 |pages= 1314–25 |year= 2006 |pmid= 16627869 |doi= 10.1074/mcp.M600007-MCP200 |doi-access= free }}
- {{cite journal |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |bibcode=2006Natur.441..315G |doi-access= free }}
{{refend}}
{{PDB Gallery|geneid=128312}}
{{gene-1-stub}}