HIST1H2BB

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H2BC3

Protein HIST1H2BB PDB 1aoi.png

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
3X1S, 3X1U

Identifiers

H2BC3, H2B.1, H2B/f, H2BFF, histone cluster 1, H2bb, histone cluster 1 H2B family member b, HIST1H2BB, H2B clustered histone 3

External IDs

OMIM: 602803 MGI: 2448377 HomoloGene: 137348 GeneCards: H2BC3

Gene location (Human)

Chr.	Chromosome 6 (human)^[1]

Band	6p22.2	Start	26,043,227 bp^[1]
Band	6p22.2	End	26,043,713 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 13 (mouse)^[2]

Band	13\|13 A3.1	Start	23,930,717 bp^[2]
Band	13\|13 A3.1	End	23,931,224 bp^[2]

RNA expression pattern

Top expressed in
stomach lung kidney colon heart Achilles tendon muscle tissue corpus callosum
More reference expression data


More reference expression data

Gene ontology
Molecular function	protein heterodimerization activity DNA binding GO:0001948 protein binding
Cellular component	nucleosome nucleus chromosome nucleoplasm cytosol
Biological process	nucleosome assembly protein ubiquitination
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse


3018


319178

Ensembl


ENSG00000276410


ENSMUSG00000075031


P33778


Q64475

RefSeq (mRNA)


NM_021062


NM_175664

RefSeq (protein)


NP_066406


NP_783595

Location (UCSC)

Chr 6: 26.04 – 26.04 Mb

Chr 13: 23.93 – 23.93 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Histone H2B type 1-B is a protein that in humans is encoded by the HIST1H2BB gene.^[5]^[6]^[7]

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.^[7]

References[]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000276410 - Ensembl, May 2017
^ ^a ^b ^c 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.
^ ^a ^b "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. 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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