H1FX

H1-10
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2LSO
Identifiers
Aliases	H1-10 , H1X, H1.10, H1 histone family member X, H1FX, H1.10 linker histone
External IDs	OMIM: 602785 MGI: 2685307 HomoloGene: 4397 GeneCards: H1-10
Gene location (Human) Chr. Chromosome 3 (human) [1] Band 3q21.3 Start 129,314,771 bp [1] End 129,316,286 bp [1]
Gene location (Mouse) Chr. Chromosome 6 (mouse) [2] Band 6|6 D1 Start 87,957,403 bp [2] End 87,958,619 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence thymus skin of abdomen right uterine tube left uterine tube canal of the cervix right lung anterior pituitary monocyte tibial nerve Top expressed in adrenal medulla ganglionic eminence white adipose tissue mirror testicle neural tube superior frontal gyrus bone marrow hippocampus proper mesencephalon More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding RNA binding cadherin binding double-stranded DNA binding protein binding nucleosomal DNA binding Cellular component nucleosome nucleolus nucleus chromosome Biological process nucleosome assembly regulation of transcription, DNA-templated chromosome condensation negative regulation of DNA recombination Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8971 243529 Ensembl ENSG00000184897 ENSMUSG00000044927 UniProt Q92522 Q80ZM5 RefSeq (mRNA) NM_006026 NM_198622 RefSeq (protein) NP_006017 NP_941024 Location (UCSC) Chr 3: 129.31 – 129.32 Mb Chr 6: 87.96 – 87.96 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Histone H1x is a protein that in humans is encoded by the H1FX gene. ^{[5] [6] [7]}

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000184897 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000044927 - 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. Yamamoto T, Horikoshi M (Dec 1996). "Cloning of the cDNA encoding a novel subtype of histone H1". Gene. 173 (2): 281–285. doi:10.1016/0378-1119(96)00020-0. PMID   8964515.
6. Albig W, Doenecke D (Feb 1998). "The human histone gene cluster at the D6S105 locus". Hum Genet. 101 (3): 284–294. doi:10.1007/s004390050630. PMID   9439656. S2CID   38539096.
7. "Entrez Gene: H1FX H1 histone family, member X".

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): 110–120. doi:10.1016/S0012-1606(05)80011-9. PMID   1879604.
• 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): 16899–16903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . 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): 177–183. doi:10.1159/000069814. PMID   12698000. S2CID   41010053.
• 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): 12130–12135. Bibcode:2004PNAS..10112130B. doi: 10.1073/pnas.0404720101 . PMC   514446 . 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): 2121–2127. doi:10.1101/gr.2596504. PMC   528928 . 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): 1219–1227. doi:10.1021/pr0498887. PMID   15595731.
• 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.
• Happel N, Schulze E, Doenecke D (2005). "Characterisation of human histone H1x". Biol. Chem. 386 (6): 541–551. doi:10.1515/BC.2005.064. PMID   16006241. S2CID   39956199.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi: 10.1016/j.cell.2006.09.026 . PMID   17081983. S2CID   7827573.
• 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): 3783–3788. doi: 10.1016/j.febslet.2007.06.076 . PMID   17632103. S2CID   45800557.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Histone H1x