H1FX
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H1 histone family, member X, also known as H1FX, 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 encodes a member of the histone H1 family.[1]
References
Further reading
- Ohsumi K, Katagiri C (1991). "Occurrence of H1 subtypes specific to pronuclei and cleavage-stage cell nuclei of anuran amphibians". Dev. Biol. 147 (1): 110–20. PMID 1879604.
- Yamamoto T, Horikoshi M (1996). "Cloning of the cDNA encoding a novel subtype of histone H1". Gene. 173 (2): 281–5. PMID 8964515.
- Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–94. PMID 9439656.
- 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.
- Sulimova GE, Kutsenko AS, Rakhmanaliev ER; et al. (2003). "Human chromosome 3: integration of 60 NotI clones into a physical and gene map". Cytogenet. Genome Res. 98 (2–3): 177–83. doi:10.1159/000069814. PMID 12698000.
- Beausoleil SA, Jedrychowski M, Schwartz D; et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.
- 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.
- Garcia BA, Busby SA, Barber CM; et al. (2005). "Characterization of phosphorylation sites on histone H1 isoforms by tandem mass spectrometry". J. Proteome Res. 3 (6): 1219–27. doi:10.1021/pr0498887. PMID 15595731.
- Andersen JS, Lam YW, Leung AK; et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Happel N, Schulze E, Doenecke D (2005). "Characterisation of human histone H1x". Biol. Chem. 386 (6): 541–51. doi:10.1515/BC.2005.064. PMID 16006241.
- Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Takata H, Matsunaga S, Morimoto A; et al. (2007). "H1.X with different properties from other linker histones is required for mitotic progression". FEBS Lett. 581 (20): 3783–8. doi:10.1016/j.febslet.2007.06.076. PMID 17632103.