Protein-coding gene in the species Homo sapiens
H2BC3 Identifiers Aliases H2BC3 , H2B.1, H2B/f, H2BFF, histone cluster 1, H2bb, histone cluster 1 H2B family member b, HIST1H2BB, H2B clustered histone 3External IDs OMIM : 602803 ; MGI : 2448377 ; HomoloGene : 137348 ; GeneCards : H2BC3 ; OMA :H2BC3 - orthologs Gene location (Mouse ) Chr. Chromosome 13 (mouse) Band 13|13 A3.1 Start 23,930,717 bp End 23,931,224 bp
Wikidata
Histone H2B type 1-B is a protein that in humans is encoded by the HIST1H2BB gene .
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.
References
^ GRCh38: Ensembl release 89: ENSG00000276410 – Ensembl , May 2017
^ GRCm38: Ensembl release 89: ENSMUSG00000075031 – Ensembl , May 2017
"Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine ."Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .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 . S2CID 42454232 .
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 .
^ "Entrez Gene: HIST1H2BB histone cluster 1, H2bb" .
Further reading
Albig W, Kardalinou E, Drabent B, et al. (1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics . 10 (4): 940–8. doi :10.1016/0888-7543(91)90183-F . PMID 1916825 . Albig W, Kioschis P, Poustka A, et al. (1997). "Human histone gene organization: nonregular arrangement within a large cluster". Genomics . 40 (2): 314–22. doi :10.1006/geno.1996.4592 . PMID 9119399 . Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet . 101 (3): 284–94. doi :10.1007/s004390050630 . PMID 9439656 . S2CID 38539096 . 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 . 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 . Galasinski SC, Louie DF, Gloor KK, et al. (2002). "Global regulation of post-translational modifications on core histones" . J. Biol. Chem . 277 (4): 2579–88. doi :10.1074/jbc.M107894200 . PMID 11709551 . 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. Bibcode :2002PNAS...9916899M . 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 . S2CID 21854 . 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 . Citterio E, Papait R, Nicassio F, et al. (2004). "Np95 is a histone-binding protein endowed with ubiquitin ligase activity" . Mol. Cell. Biol . 24 (6): 2526–35. doi :10.1128/MCB.24.6.2526-2535.2004 . PMC 355858 . PMID 14993289 . 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 . S2CID 25071586 . 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 . Pavri R, Zhu B, Li G, et al. (2006). "Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II" . Cell . 125 (4): 703–17. doi :10.1016/j.cell.2006.04.029 . PMID 16713563 . S2CID 2614680 . Kim SC, Sprung R, Chen Y, et al. (2006). "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey" . Mol. Cell . 23 (4): 607–18. doi :10.1016/j.molcel.2006.06.026 . PMID 16916647 . PDB gallery
1aoi : COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT
1eqz : X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.5 A RESOLUTION
1f66 : 2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z
1hq3 : CRYSTAL STRUCTURE OF THE HISTONE-CORE-OCTAMER IN KCL/PHOSPHATE
1kx3 : X-Ray Structure of the Nucleosome Core Particle, NCP146, at 2.0 A Resolution
1kx4 : X-Ray Structure of the Nucleosome Core Particle, NCP146b, at 2.6 A Resolution
1kx5 : X-Ray Structure of the Nucleosome Core Particle, NCP147, at 1.9 A Resolution
1m18 : LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
1m19 : LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
1m1a : LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
1p34 : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3a : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3b : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3f : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3g : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3i : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3k : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3l : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3m : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3o : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3p : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1s32 : Molecular Recognition of the Nucleosomal 'Supergroove'
1tzy : Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution
1u35 : Crystal structure of the nucleosome core particle containing the histone domain of macroH2A
1zbb : Structure of the 4_601_167 Tetranucleosome
1zla : X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core
2aro : Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione
2cv5 : Crystal structure of human nucleosome core particle
2f8n : 2.9 Angstrom X-ray structure of hybrid macroH2A nucleosomes
2fj7 : Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element
2hio : HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN
2nzd : Nucleosome core particle containing 145 bp of DNA
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