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| | '''Histone H2B type 3-B''' is a [[protein]] that in humans is encoded by the ''HIST3H2BB'' [[gene]].<ref name="pmid12408966">{{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 | pmc = | doi =10.1016/S0888-7543(02)96850-3 }}</ref><ref name="entrez">{{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| accessdate = }}</ref> | ||
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| 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 contain a palindromic termination element.<ref name="entrez" | | 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 contain a palindromic termination element.<ref name="entrez"/> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
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| citations = | | citations = | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | | *{{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 | *{{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 | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | | *{{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 | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | | *{{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 }} | ||
*{{cite journal | *{{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 | | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{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 }} | |||
*{{cite journal | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=128312}} | |||
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Latest revision as of 13:43, 31 August 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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Location (UCSC) | n/a | n/a | |||||
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Histone H2B type 3-B is a protein that in humans is encoded by the HIST3H2BB gene.[1][2]
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.[2]
References
- ↑ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
- ↑ 2.0 2.1 "Entrez Gene: HIST3H2BB histone cluster 3, H2bb".
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. doi:10.1111/j.1432-1033.1996.0611p.x. 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. doi:10.1128/mcb.18.5.2535. PMC 110633. 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. doi:10.1016/S1386-6532(99)00007-4. 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. PMC 1171550. 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.
- 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.
- 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. PMC 291826. 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. doi:10.1016/S1097-2765(03)00482-9. 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. 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.
- 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.
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