H1FX
From Wikipedia, the free encyclopedia
H1 histone family, member X
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Identifiers | ||||||||||||||
Symbol(s) | H1FX; H1X; MGC15959; MGC8350 | |||||||||||||
External IDs | OMIM: 602785 MGI: 2685307 HomoloGene: 4397 | |||||||||||||
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RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 8971 | 243529 | ||||||||||||
Ensembl | ENSG00000184897 | ENSMUSG00000044927 | ||||||||||||
Uniprot | Q92522 | n/a | ||||||||||||
Refseq | NM_006026 (mRNA) NP_006017 (protein) |
XM_981507 (mRNA) XP_986601 (protein) |
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Location | Chr 3: 130.52 - 130.52 Mb | Chr 6: 87.95 - 87.95 Mb | ||||||||||||
Pubmed search | [1] | [2] |
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]
[edit] References
[edit] 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: . 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: . 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: . 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: . 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: . PMID 15595731.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77-83. doi: . PMID 15635413.
- Happel N, Schulze E, Doenecke D (2005). "Characterisation of human histone H1x.". Biol. Chem. 386 (6): 541-51. doi: . 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: . 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: . PMID 17632103.