Biology:HIST1H2AB
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Histone H2A type 1-B/E is a protein that in humans is encoded by the HIST1H2AB gene.[1][2][3][4]
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an 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 H2A 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.[4]
References
- ↑ "The human histone gene cluster at the D6S105 locus". Hum Genet 101 (3): 284–94. Feb 1998. doi:10.1007/s004390050630. PMID 9439656.
- ↑ "Human histone gene organization: nonregular arrangement within a large cluster". Genomics 40 (2): 314–22. Apr 1997. doi:10.1006/geno.1996.4592. PMID 9119399.
- ↑ "The human and mouse replication-dependent histone genes". Genomics 80 (5): 487–98. Oct 2002. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
- ↑ 4.0 4.1 "Entrez Gene: HIST1H2AB histone cluster 1, H2ab". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8335.
Further reading
- "The primary structure and expression of four cloned human histone genes.". Nucleic Acids Res. 11 (21): 7409–25. 1984. doi:10.1093/nar/11.21.7409. PMID 6647026.
- "Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter.". Mol. Cell. Biol. 18 (5): 2535–44. 1998. doi:10.1128/mcb.18.5.2535. PMID 9566873.
- "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. 2001. doi:10.1006/viro.2000.0593. PMID 11080476.
- "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA.". Virology 289 (2): 312–26. 2001. doi:10.1006/viro.2001.1129. PMID 11689053.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter.". EMBO J. 22 (24): 6550–61. 2004. doi:10.1093/emboj/cdg631. PMID 14657027.
- "Np95 is a histone-binding protein endowed with ubiquitin ligase activity.". Mol. Cell. Biol. 24 (6): 2526–35. 2004. doi:10.1128/MCB.24.6.2526-2535.2004. PMID 14993289.
- "Phosphorylation of histone H2A inhibits transcription on chromatin templates.". J. Biol. Chem. 279 (21): 21866–72. 2004. doi:10.1074/jbc.M400099200. PMID 15010469.
- "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo.". Genes Dev. 18 (8): 877–88. 2004. doi:10.1101/gad.1184604. PMID 15078818.
- "Role of histone H2A ubiquitination in Polycomb silencing.". Nature 431 (7010): 873–8. 2004. doi:10.1038/nature02985. PMID 15386022. Bibcode: 2004Natur.431..873W.
- "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. 2005. doi:10.1038/nature03207. PMID 15635413. Bibcode: 2005Natur.433...77A.
- "Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes.". Biochemistry 44 (15): 5827–34. 2005. doi:10.1021/bi047505c. PMID 15823041.
- "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.". Mol. Cell 20 (6): 845–54. 2006. doi:10.1016/j.molcel.2005.12.002. PMID 16359901.
- "DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A.". Genes Dev. 20 (10): 1343–52. 2006. doi:10.1101/gad.373706. PMID 16702407.