HIST3H2BB: Difference between revisions

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{{Underlinked|date=March 2014}}
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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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{{GNF_Protein_box
| image = PBB_Protein_HIST3H2BB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aoi.
| PDB = {{PDB2|1aoi}}, {{PDB2|1eqz}}, {{PDB2|1f66}}, {{PDB2|1hio}}, {{PDB2|1hq3}}, {{PDB2|1kx3}}, {{PDB2|1kx4}}, {{PDB2|1kx5}}, {{PDB2|1m18}}, {{PDB2|1m19}}, {{PDB2|1m1a}}, {{PDB2|1p34}}, {{PDB2|1p3a}}, {{PDB2|1p3b}}, {{PDB2|1p3f}}, {{PDB2|1p3g}}, {{PDB2|1p3i}}, {{PDB2|1p3k}}, {{PDB2|1p3l}}, {{PDB2|1p3m}}, {{PDB2|1p3o}}, {{PDB2|1p3p}}, {{PDB2|1s32}}, {{PDB2|1tzy}}, {{PDB2|1u35}}, {{PDB2|1zbb}}, {{PDB2|1zla}}, {{PDB2|2aro}}, {{PDB2|2cv5}}, {{PDB2|2f8n}}, {{PDB2|2fj7}}, {{PDB2|2hio}}, {{PDB2|2nzd}}
| Name = Histone cluster 3, H2bb
| HGNCid = 20514
| Symbol = HIST3H2BB
| AltSymbols =;
| OMIM =
| ECnumber =
| Homologene = 75941
| MGIid = 1922442
  | GeneAtlas_image1 = PBB_GE_HIST3H2BB_gnf1h11064_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_HIST3H2BB_gnf1h11065_at_tn.png
| GeneAtlas_image3 = PBB_GE_HIST3H2BB_gnf1h11068_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}}
| Component = {{GNF_GO|id=GO:0000786 |text = nucleosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
| Process = {{GNF_GO|id=GO:0006334 |text = nucleosome assembly}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 128312
    | Hs_Ensembl = ENSG00000197435
    | Hs_RefseqProtein = NP_778225
    | Hs_RefseqmRNA = NM_175055
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 226712431
    | Hs_GenLoc_end = 226714794
    | Hs_Uniprot = Q8N257
    | Mm_EntrezGene = 382522
    | Mm_Ensembl = ENSMUSG00000069311
    | Mm_RefseqmRNA = NM_206882
    | Mm_RefseqProtein = NP_996765
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 58770243
    | Mm_GenLoc_end = 58770707
    | Mm_Uniprot = Q8CGP0
  }}
}}
'''Histone cluster 3, H2bb''', also known as '''HIST3H2BB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST3H2BB histone cluster 3, H2bb| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=128312| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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 contain a palindromic termination element.<ref name="entrez">{{cite web | title = Entrez Gene: HIST3H2BB histone cluster 3, H2bb| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=128312| accessdate = }}</ref>
| 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|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Borowski P, Heiland M, Oehlmann K, ''et al.'' |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=  }}
*{{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  | 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  |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 | author=Borowski P, Kühl R, Laufs R, ''et al.'' |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=  }}
*{{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 | author=Thomson S, Clayton AL, Hazzalin CA, ''et al.'' |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 }}
*{{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 | 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   |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 | 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   |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 | 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   |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 | 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   |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 | 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   |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  | author=Coleman MA, Miller KA, Beernink PT, ''et al.'' |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  |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 | 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   |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 | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |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   |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  | author=Kanno T, Kanno Y, Siegel RM, ''et al.'' |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= }}
*{{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 | author=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   |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  | 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  |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 | 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   |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 | 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   |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 | 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   |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  | author=Beck HC, Nielsen EC, Matthiesen R, ''et al.'' |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 | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |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 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=128312}}
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Latest revision as of 13:43, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ 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. ↑ 2.0 2.1 "Entrez Gene: HIST3H2BB histone cluster 3, H2bb".

Further reading



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