HIST1H2BA

From Wikipedia, the free encyclopedia

Histone cluster 1, H2ba

PDB rendering based on 1hio.

Available structures: 1hio

Identifiers

Symbol(s)

HIST1H2BA; H2BFU; STBP; TSH2B; bA317E16.3

External IDs

OMIM: 609904 MGI: 2448375 HomoloGene: 69356

Gene ontology
Molecular Function:	• DNA binding
Cellular Component:	• nucleosome • nucleus • chromosome
Biological Process:	• nucleosome assembly • chromosome organization and biogenesis (sensu Eukaryota)

Orthologs

Human

Mouse

Refseq

NM_170610 (mRNA)
NP_733759 (protein)

NM_175663 (mRNA)
NP_783594 (protein)

Location

Chr 6: 25.84 - 25.84 Mb

Chr 13: 23.94 - 23.94 Mb

Pubmed search

[1]

[2]

Histone cluster 1, H2ba, also known as HIST1H2BA, is a human gene.^[1]

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 testis/sperm-specific member of the histone H2B family. Transcripts from this gene contain a palindromic termination element.^[1]

[edit] References

^ ^a ^b Entrez Gene: HIST1H2BA histone cluster 1, H2ba.

[edit] 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. 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.
Zalensky AO, Siino JS, Gineitis AA, et al. (2003). "Human testis/sperm-specific histone H2B (hTSH2B). Molecular cloning and characterization.". J. Biol. Chem. 277 (45): 43474-80. doi:10.1074/jbc.M206065200. PMID 12213818.
Marzluff WF, Gongidi P, Woods KR, et al. (2003). "The human and mouse replication-dependent histone genes.". Genomics 80 (5): 487-98. PMID 12408966.
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. PMID 12477932.
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. 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. PMID 15489334.
Li A, Maffey AH, Abbott WD, et al. (2005). "Characterization of nucleosomes consisting of the human testis/sperm-specific histone H2B variant (hTSH2B).". Biochemistry 44 (7): 2529-35. doi:10.1021/bi048061n. PMID 15709765.
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.
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.
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.
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.