HIST2H3A

{{Short description|Protein-coding gene in the species Homo sapiens}} {{Infobox_gene}}

'''Histone cluster 2 H3 family member a''' is a protein that in humans is encoded by the HIST2H3A gene.<ref name="entrez"> {{cite web | title = Entrez Gene: Histone cluster 2 H3 family member a | url = https://www.ncbi.nlm.nih.gov/gene/333932 | access-date = 2018-08-05 }}</ref>

==Function==

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 replication-dependent histone that is a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in a histone cluster on human chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the centromeric copy. [provided by RefSeq, Aug 2015].

== References ==

== Further reading ==

{{refbegin | 30em}} *{{cite journal |vauthors=Ruthenburg AJ, Wang W, Graybosch DM, Li H, Allis CD, Patel DJ, Verdine GL |title=Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex |journal=Nat. Struct. Mol. Biol. |volume=13 |issue=8 |pages=704–12 |date=August 2006 |pmid=16829959 |pmc=4698793 |doi=10.1038/nsmb1119 }} *{{cite journal |vauthors=Couture JF, Collazo E, Trievel RC |title=Molecular recognition of histone H3 by the WD40 protein WDR5 |journal=Nat. Struct. Mol. Biol. |volume=13 |issue=8 |pages=698–703 |date=August 2006 |pmid=16829960 |doi=10.1038/nsmb1116 |s2cid=26165068 }} *{{cite journal |vauthors=Rodriguez-Collazo P, Snyder SK, Chiffer RC, Zlatanova J, Leuba SH, Smith CL |title=cAMP signaling induces rapid loss of histone H3 phosphorylation in mammary adenocarcinoma-derived cell lines |journal=Exp. Cell Res. |volume=314 |issue=1 |pages=1–10 |date=January 2008 |pmid=17950276 |pmc=4426871 |doi=10.1016/j.yexcr.2007.09.011 }} *{{cite journal |vauthors=Ho CC, Cheng CC, Liu YH, Pei RJ, Hsu YH, Yeh KT, Ho LC, Tsai MC, Lai YS |title=Possible relation between histone 3 and cytokeratin 18 in human hepatocellular carcinoma |journal=In Vivo |volume=22 |issue=4 |pages=457–62 |date=2008 |pmid=18712172 }} *{{cite journal |vauthors=Song JJ, Kingston RE |title=WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket |journal=J. Biol. Chem. |volume=283 |issue=50 |pages=35258–64 |date=December 2008 |pmid=18840606 |pmc=2596411 |doi=10.1074/jbc.M806900200 |doi-access=free }} *{{cite journal |vauthors=Xie W, Song C, Young NL, Sperling AS, Xu F, Sridharan R, Conway AE, Garcia BA, Plath K, Clark AT, Grunstein M |title=Histone h3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells |journal=Mol. Cell |volume=33 |issue=4 |pages=417–27 |date=February 2009 |pmid=19250903 |pmc=2671231 |doi=10.1016/j.molcel.2009.02.004 }} *{{cite journal |vauthors=Loomis RJ, Naoe Y, Parker JB, Savic V, Bozovsky MR, Macfarlan T, Manley JL, Chakravarti D |title=Chromatin binding of SRp20 and ASF/SF2 and dissociation from mitotic chromosomes is modulated by histone H3 serine 10 phosphorylation |journal=Mol. Cell |volume=33 |issue=4 |pages=450–61 |date=February 2009 |pmid=19250906 |pmc=2667802 |doi=10.1016/j.molcel.2009.02.003 }} *{{cite journal |vauthors=Suphioglu C, Sadli N, Coonan D, Kumar L, De Mel D, Lesheim J, Sinclair AJ, Ackland L |title=Zinc and DHA have opposing effects on the expression levels of histones H3 and H4 in human neuronal cells |journal=Br. J. Nutr. |volume=103 |issue=3 |pages=344–51 |date=February 2010 |pmid=19747413 |doi=10.1017/S0007114509991826 |doi-access=free |hdl=10536/DRO/DU:30023162 |hdl-access=free }}