HIST1H2AC

H2AC6
Identifiers
Aliases	H2AC6, H2A/l, H2AFL, dJ221C16.4, histone cluster 1, H2ac, histone cluster 1 H2A family member c, HIST1H2AC, H2A clustered histone 6
External IDs	OMIM: 602794; MGI: 2448302; HomoloGene: 130459; GeneCards: H2AC6; OMA:H2AC6 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.2 Start 26,124,145 bp End 26,139,116 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A3.1 Start 21,994,635 bp End 21,995,114 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte blood buccal mucosa cell pericardium jejunal mucosa mucosa of transverse colon optic nerve granulocyte bone marrow C1 segment Top expressed in embryo embryo neural tube blastocyst urinary bladder morula tail of embryo granulocyte bone marrow mesencephalon More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein heterodimerization activity DNA binding molecular function Cellular component nucleosome nucleus chromosome extracellular exosome nucleoplasm Biological process negative regulation of cell population proliferation chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8334 665433 Ensembl ENSG00000180573 ENSMUSG00000094248 UniProt Q93077 C0HKE2 B2RVF0 C0HKE1 C0HKE3 C0HKE4 C0HKE5 C0HKE6 C0HKE7 C0HKE8 C0HKE9 RefSeq (mRNA) NM_003512 NM_001177544 RefSeq (protein) NP_003503 NP_835496 NP_835495 NP_835494 NP_835491 NP_835489 NP_783591 NP_835493 NP_835496 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835489 NP_001171015 NP_835496 NP_835491 NP_835493 NP_835494 NP_835495 NP_835492 NP_783591 NP_835494 NP_835489 NP_835495 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835495 NP_835489 NP_835494 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835492 NP_835491 NP_835489 NP_835495 NP_835494 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835491 NP_835489 NP_835495 NP_835494 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_783591 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_001171015 NP_835493 NP_835496 NP_783591 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_001171015 NP_835493 NP_835496 Location (UCSC) Chr 6: 26.12 – 26.14 Mb Chr 13: 21.99 – 22 Mb PubMed search
Wikidata
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Histone H2A type 1-C is a protein that in humans is encoded by the HIST1H2AC gene.

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes.

The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.

Cancer

HIST1H2AC gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. For this reason, HIST1H2AC is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.

Further reading

• Ruddy DA, Kronmal GS, Lee VK, et al. (1997). "A 1.1-Mb transcript map of the hereditary hemochromatosis locus". Genome Res. 7 (5): 441–56. doi:10.1101/gr.7.5.441. PMID 9149941.
• Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656. S2CID 38539096.
• El Kharroubi A, Piras G, Zensen R, Martin MA (1998). "Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter". Mol. Cell. Biol. 18 (5): 2535–44. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
• Deng L, de la Fuente C, Fu P, et al. (2001). "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones". Virology. 277 (2): 278–95. doi:10.1006/viro.2000.0593. PMID 11080476.
• Deng L, Wang D, de la Fuente C, et al. (2001). "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA". Virology. 289 (2): 312–26. doi:10.1006/viro.2001.1129. PMID 11689053.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Lusic M, Marcello A, Cereseto A, Giacca M (2004). "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter". EMBO J. 22 (24): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
• Zhang Y, Griffin K, Mondal N, Parvin JD (2004). "Phosphorylation of histone H2A inhibits transcription on chromatin templates". J. Biol. Chem. 279 (21): 21866–72. doi:10.1074/jbc.M400099200. PMID 15010469.
• Aihara H, Nakagawa T, Yasui K, et al. (2004). "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo". Genes Dev. 18 (8): 877–88. doi:10.1101/gad.1184604. PMC 395847. PMID 15078818.
• Wang H, Wang L, Erdjument-Bromage H, et al. (2004). "Role of histone H2A ubiquitination in Polycomb silencing". Nature. 431 (7010): 873–8. Bibcode:2004Natur.431..873W. doi:10.1038/nature02985. PMID 15386022. S2CID 4344378.
• 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. PMC 528928. PMID 15489334.
• 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.
• Hagiwara T, Hidaka Y, Yamada M (2005). "Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes". Biochemistry. 44 (15): 5827–34. doi:10.1021/bi047505c. PMID 15823041.
• Bonenfant D, Coulot M, Towbin H, et al. (2006). "Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry". Mol. Cell. Proteomics. 5 (3): 541–52. doi:10.1074/mcp.M500288-MCP200. PMID 16319397.
• Cao R, Tsukada Y, Zhang Y (2006). "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing". Mol. Cell. 20 (6): 845–54. doi:10.1016/j.molcel.2005.12.002. PMID 16359901.
• Boyne MT, Pesavento JJ, Mizzen CA, Kelleher NL (2006). "Precise characterization of human histones in the H2A gene family by top down mass spectrometry". J. Proteome Res. 5 (2): 248–53. doi:10.1021/pr050269n. PMID 16457589.
• Bergink S, Salomons FA, Hoogstraten D, et al. (2006). "DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A". Genes Dev. 20 (10): 1343–52. doi:10.1101/gad.373706. PMC 1472908. PMID 16702407.