HIST1H2BN

H2BC15
Identifiers
Aliases	H2BC15 , H2B/d, H2BFD, histone cluster 1, H2bn, histone cluster 1 H2B family member n, H2B clustered histone 15, HIST1H2BN
External IDs	OMIM: 602801 MGI: 2448404 HomoloGene: 135961 GeneCards: H2BC15
Gene location (Human) Chr. Chromosome 6 (human) [1] Band 6p22.1 Start 27,838,545 bp [1] End 27,855,709 bp [1]
Gene location (Mouse) Chr. Chromosome 13 (mouse) [2] Band 13|13 A3.1 Start 21,906,214 bp [2] End 21,906,737 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow cells monocyte Achilles tendon stromal cell of endometrium thymus striated muscle tissue skeletal muscle tissue popliteal artery blood ventricle Top expressed in spermatid spermatocyte uterus bone marrow morula mesencephalon secondary oocyte thymus yolk sac blastocyst More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding protein heterodimerization activity Cellular component chromosome nucleosome extracellular exosome nucleus nucleoplasm cytosol Biological process nucleosome assembly protein ubiquitination Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8341 319186 Ensembl ENSG00000233822 ENSMUSG00000114279 UniProt Q99877 P10854 RefSeq (mRNA) NM_003520 NM_178200 RefSeq (protein) NP_003511 NP_835507 Location (UCSC) Chr 6: 27.84 – 27.86 Mb Chr 13: 21.91 – 21.91 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Histone H2B type 1-N is a protein that in humans is encoded by the HIST1H2BN gene. ^{[5] [6] [7]}

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2B family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000233822 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000114279 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Albig W, Doenecke D (Feb 1998). "The human histone gene cluster at the D6S105 locus". Hum Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID   9439656. S2CID   38539096.
6. 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.
7. "Entrez Gene: HIST1H2BN histone cluster 1, H2bn".

Further reading

• 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.
• Albig W, Trappe R, Kardalinou E, et al. (1999). "The human H2A and H2B histone gene complement". Biol. Chem. 380 (1): 7–18. doi:10.1515/BC.1999.002. PMID   10064132. S2CID   12807248.
• 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. 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.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi: 10.1038/nature02055 . PMID   14574404.
• 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.
• 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.
• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID   15635413. S2CID   4344740.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• 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.
• 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.
• 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.