H2AC8 Gene

Name H2A clustered histone 8
Description 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 is intronless and encodes a replication-dependent histone that is a member of the histone H2A family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3. [provided by RefSeq, Aug 2015]
Summary
{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Histone H2AC8 belongs to the family of core H2A proteins that are integral to nucleosome assembly and chromatin organization. Like other canonical H2A variants, H2AC8 is presumed to play a central role in packaging DNA into nucleosomes, thereby governing accessibility for transcription, replication, and repair. Recent studies on distinct H2A family members have shown that subtle differences in sequence or post‐translational modification can alter nucleosome stability and affect gene expression programs that control key cellular processes. For example, variants such as H2A.J have been implicated in promoting the inflammatory secretory phenotype of senescent cells, suggesting that changes in H2A composition contribute to age‐associated chromatin remodeling and altered signalling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " Similarly, investigations of H2A.Z have demonstrated that its acetylation status and incorporation into nucleosomes can modulate nucleosome conformation and stability, underscoring the role of H2A variants in fine‐tuning chromatin dynamics."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " In addition, studies addressing histone interactions with key DNA repair proteins show that core histones, including members of the H2A family, may facilitate the efficient recognition and repair of DNA lesions, further contributing to genomic stability."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " Moreover, altered expression of H2A variants has been reported in response to stress conditions such as burn injury, where changes in histone mRNA and protein levels indicate a rapid reorganization of chromatin structure during tissue injury and repair."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": " Developmental studies have also revealed that differential expression of H2A isoforms accompanies the transition from undifferentiated embryonic states to mature tissues, suggesting a role in epigenetic reprogramming during differentiation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " Finally, shifts in the balance of H2A variants in neoplastic tissues have been linked with oncogenic transformation and proliferation, implying that the proper regulation of these histones is vital for maintaining cellular homeostasis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": " Together, these findings support the view that H2AC8, as a member of the canonical H2A group, is essential for preserving chromatin architecture and modulating the transcriptional and DNA repair landscapes—functions that are critical for cell survival, differentiation, and the response to both intrinsic and environmental challenges.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Kévin Contrepois, Clément Coudereau, Bérénice A Benayoun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Histone variant H2A.J accumulates in senescent cells and promotes inflammatory gene expression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncomms14995"}], "href": "https://doi.org/10.1038/ncomms14995"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28489069"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28489069"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Toyotaka Ishibashi, Deanna Dryhurst, Kristie L Rose, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Acetylation of vertebrate H2A.Z and its effect on the structure of the nucleosome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi900196c"}], "href": "https://doi.org/10.1021/bi900196c"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19385636"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19385636"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Suryakant K Niture, Catalin E Doneanu, Chinavenmeni S Velu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteomic analysis of human O6-methylguanine-DNA methyltransferase by affinity chromatography and tandem mass spectrometry."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2005.09.177"}], "href": "https://doi.org/10.1016/j.bbrc.2005.09.177"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16226712"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16226712"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Jayoung Jeong, Lee K Adamson, David G Greenhalgh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Injury-associated differential regulation of histone expression and modification in the thymus of mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Biol Med (Maywood) (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1177/153537020422900407"}], "href": "https://doi.org/10.1177/153537020422900407"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15044716"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15044716"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Monica Tyagi, Bharat Khade, Shafqat A Khan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expression of histone variant, H2A.1 is associated with the undifferentiated state of hepatocyte."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Biol Med (Maywood) (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1177/1535370214531869"}], "href": "https://doi.org/10.1177/1535370214531869"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24764240"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24764240"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Satyajeet P Khare, Ajitkumar Sharma, Kedar K Deodhar, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Overexpression of histone variant H2A.1 and cellular transformation are related in N-nitrosodiethylamine-induced sequential hepatocarcinogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Biol Med (Maywood) (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1258/ebm.2010.010140"}], "href": "https://doi.org/10.1258/ebm.2010.010140"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21239733"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21239733"}]}]}]}
NCBI Gene ID 3012
API
Download Associations
Predicted Functions View H2AC8's ARCHS4 Predicted Functions.
Co-expressed Genes View H2AC8's ARCHS4 Predicted Functions.
Expression in Tissues and Cell Lines View H2AC8's ARCHS4 Predicted Functions.

Functional Associations

H2AC8 has 895 functional associations with biological entities spanning 5 categories (disease, phenotype or trait, chemical, functional term, phrase or reference, cell line, cell type or tissue, gene, protein or microRNA) extracted from 12 datasets.

Click the + buttons to view associations for H2AC8 from the datasets below.

If available, associations are ranked by standardized value

Dataset Summary
Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles tissue samples with high or low expression of H2AC8 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
CellMarker Gene-Cell Type Associations cell types associated with H2AC8 gene from the CellMarker Gene-Cell Type Associations dataset.
CM4AI KOLF21J CRISPRi Gene Perturbation Atlas gene perturbations changing expression of H2AC8 gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
DISEASES Experimental Gene-Disease Association Evidence Scores 2025 diseases associated with H2AC8 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.
DISEASES Text-mining Gene-Disease Association Evidence Scores 2025 diseases co-occuring with H2AC8 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
GTEx Tissue Gene Expression Profiles 2023 tissues with high or low expression of H2AC8 gene relative to other tissues from the GTEx Tissue Gene Expression Profiles 2023 dataset.
IMPC Knockout Mouse Phenotypes phenotypes of mice caused by H2AC8 gene knockout from the IMPC Knockout Mouse Phenotypes dataset.
LINCS L1000 CMAP Chemical Perturbation Consensus Signatures small molecule perturbations changing expression of H2AC8 gene from the LINCS L1000 CMAP Chemical Perturbations Consensus Signatures dataset.
PFOCR Pathway Figure Associations 2024 pathways involving H2AC8 protein from the Wikipathways PFOCR 2024 dataset.
Replogle et al., Cell, 2022 K562 Essential Perturb-seq Gene Perturbation Signatures gene perturbations changing expression of H2AC8 gene from the Replogle et al., Cell, 2022 K562 Essential Perturb-seq Gene Perturbation Signatures dataset.
Rummagene Transcription Factor Associations 2026 transcription factors regulating expression of H2AC8 gene from the Rummagene Transcription Factor Associations 2026 dataset.
WikiPathways Pathways 2024 pathways involving H2AC8 protein from the WikiPathways Pathways 2024 dataset.