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{{Infobox_gene}}
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'''Histone H2B type 1-B''' is a [[protein]] that in humans is encoded by the ''HIST1H2BB'' [[gene]].<ref name="pmid8227173">{{cite journal |vauthors=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 |date=Dec 1993 | pmid = 8227173 | pmc =  | doi = 10.1002/jcb.240520402 }}</ref><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: HIST1H2BB histone cluster 1, H2bb| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3018| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_HIST1H2BB_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 1, H2bb
| HGNCid = 4751
| Symbol = HIST1H2BB
| AltSymbols =; H2B.1; H2B/f; H2BFF; MGC119804
| OMIM = 602803
| ECnumber =
| Homologene = 86898
| MGIid = 2448377
  | GeneAtlas_image1 = PBB_GE_HIST1H2BB_208547_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 = 3018
    | Hs_Ensembl = ENSG00000196226
    | Hs_RefseqProtein = NP_066406
    | Hs_RefseqmRNA = NM_021062
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 26151484
    | Hs_GenLoc_end = 26151864
    | Hs_Uniprot = P33778
    | Mm_EntrezGene = 319178
    | Mm_Ensembl = ENSMUSG00000075031
    | Mm_RefseqmRNA = NM_175664
    | Mm_RefseqProtein = NP_783595
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 23754259
    | Mm_GenLoc_end = 23754989
    | Mm_Uniprot = Q14AF8
  }}
}}
'''Histone cluster 1, H2bb''', also known as '''HIST1H2BB''', is a human [[gene]].<ref name="entrez">{{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 = }}</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 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.<ref name="entrez">{{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 = }}</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 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.<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=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   |vauthors=Albig W, Kardalinou E, Drabent B, etal |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=10.1016/0888-7543(91)90183-F  }}
*{{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   |vauthors=Albig W, Kioschis P, Poustka A, etal |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, 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  |vauthors=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=10.1007/s004390050630 }}
*{{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  |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=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=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, 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, 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=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=Galasinski SC, Louie DF, Gloor KK, etal |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=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   |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=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=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=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=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=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=Citterio E, Papait R, Nicassio F, etal |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=10.1128/MCB.24.6.2526-2535.2004  | pmc=355858 }}
*{{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=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=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  |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=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=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=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=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=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=Pavri R, Zhu B, Li G, etal |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=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=Kim SC, Sprung R, Chen Y, etal |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 }}
*{{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 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3018}}
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Latest revision as of 13:39, 31 August 2017

VALUE_ERROR (nil)
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 1-B is a protein that in humans is encoded by the HIST1H2BB gene.[1][2][3]

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.[3]

References

  1. ↑ Kardalinou E, Eick S, Albig W, Doenecke D (Dec 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: HIST1H2BB histone cluster 1, H2bb".

Further reading



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