HIST2H3A

Histone cluster 2 H3 family member a is a protein that in humans is encoded by the HIST2H3A gene.

H3C15
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2IIJ, 2X4W, 2X4X, 2X4Y, 3AV1, 3DB3, 3MO8, 3R93, 4MZF, 4MZG, 4MZH, 4OUC, 5BO0, 2HIO, 5B0Z, 2ARO, 1EQZ, 1HQ3, 4KGC, 1TZY, 4UUZ, 2F8N, 5B0Y, 4LD9, 5B40, 5CIU
Identifiers
Aliases	H3C15, H3/n, H3/o, histone cluster 2, H3a, histone cluster 2 H3 family member a, HIST2H3A, H3 clustered histone 15, H3C14, H3C13
External IDs	MGI: 2448329 HomoloGene: 133885 GeneCards: H3C15
Gene location (Human) Chr. Chromosome 1 (human) Band 1q21.2 Start 149,852,608 bp End 149,853,125 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13 A3.1|13 9.78 cM Start 23,728,222 bp End 23,729,482 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow cells ganglionic eminence corpus callosum islet of Langerhans Achilles tendon blood prefrontal cortex monocyte left ventricle cerebellar cortex Top expressed in spermatocyte secondary oocyte maxillary prominence primitive streak morula medial ganglionic eminence yolk sac extraocular muscle digastric muscle abdominal wall More reference expression data BioGPS n/a
Gene ontology Molecular function protein heterodimerization activity DNA binding histone binding protein binding chromatin binding nucleosomal DNA binding Cellular component extracellular exosome extracellular region nucleoplasm chromosome nucleosome nucleus chromatin Biological process epigenetic maintenance of chromatin in transcription-competent conformation blood coagulation rDNA heterochromatin assembly nucleosome assembly negative regulation of gene expression, epigenetic negative regulation of transcription by RNA polymerase II chromatin organization regulation of gene silencing by miRNA interleukin-7-mediated signaling pathway regulation of megakaryocyte differentiation regulation of hematopoietic stem cell differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 333932 260423 Ensembl ENSG00000203852 ENSMUSG00000100210 UniProt Q71DI3 P84228 RefSeq (mRNA) NM_001005464 NM_013548 RefSeq (protein) NP_066403 NP_001116847 NP_473386 NP_835734 NP_783584 NP_835510 NP_835587 NP_038576 NP_835511 NP_835512 Location (UCSC) Chr 1: 149.85 – 149.85 Mb Chr 13: 23.73 – 23.73 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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].

Further reading

• Ruthenburg AJ, Wang W, Graybosch DM, Li H, Allis CD, Patel DJ, Verdine GL (August 2006). "Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex". Nat. Struct. Mol. Biol. 13 (8): 704–12. doi:10.1038/nsmb1119. PMC 4698793. PMID 16829959.
• Couture JF, Collazo E, Trievel RC (August 2006). "Molecular recognition of histone H3 by the WD40 protein WDR5". Nat. Struct. Mol. Biol. 13 (8): 698–703. doi:10.1038/nsmb1116. PMID 16829960. S2CID 26165068.
• Rodriguez-Collazo P, Snyder SK, Chiffer RC, Zlatanova J, Leuba SH, Smith CL (January 2008). "cAMP signaling induces rapid loss of histone H3 phosphorylation in mammary adenocarcinoma-derived cell lines". Exp. Cell Res. 314 (1): 1–10. doi:10.1016/j.yexcr.2007.09.011. PMC 4426871. PMID 17950276.
• Ho CC, Cheng CC, Liu YH, Pei RJ, Hsu YH, Yeh KT, Ho LC, Tsai MC, Lai YS (2008). "Possible relation between histone 3 and cytokeratin 18 in human hepatocellular carcinoma". In Vivo. 22 (4): 457–62. PMID 18712172.
• Song JJ, Kingston RE (December 2008). "WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket". J. Biol. Chem. 283 (50): 35258–64. doi:10.1074/jbc.M806900200. PMC 2596411. PMID 18840606.
• Xie W, Song C, Young NL, Sperling AS, Xu F, Sridharan R, Conway AE, Garcia BA, Plath K, Clark AT, Grunstein M (February 2009). "Histone h3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells". Mol. Cell. 33 (4): 417–27. doi:10.1016/j.molcel.2009.02.004. PMC 2671231. PMID 19250903.
• Loomis RJ, Naoe Y, Parker JB, Savic V, Bozovsky MR, Macfarlan T, Manley JL, Chakravarti D (February 2009). "Chromatin binding of SRp20 and ASF/SF2 and dissociation from mitotic chromosomes is modulated by histone H3 serine 10 phosphorylation". Mol. Cell. 33 (4): 450–61. doi:10.1016/j.molcel.2009.02.003. PMC 2667802. PMID 19250906.
• Suphioglu C, Sadli N, Coonan D, Kumar L, De Mel D, Lesheim J, Sinclair AJ, Ackland L (February 2010). "Zinc and DHA have opposing effects on the expression levels of histones H3 and H4 in human neuronal cells". Br. J. Nutr. 103 (3): 344–51. doi:10.1017/S0007114509991826. hdl:10536/DRO/DU:30023162. PMID 19747413.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.