Histones are a complex family of highly conserved basic proteins responsible for packaging chromosomal DNA into nucleosomes. There are subtype diversities: H1, H2A, H2B and H3 or H4. It has become more and more evident that histone modifications are key players in the regulation of chromatin states and dynamics as well as in gene expression. Therefore, histone modifications and the enzymatic machineries that set them are crucial regulators that can control cellular proliferation, differentiation, plasticity, and malignancy processes. However, extracellular histones are a double-edged sword because they also damage host tissue and may cause death. Histones bound to platelets, induced calcium influx, and recruited plasma adhesion proteins such as fibrinogen to induce platelet aggregation. Histone cluster 3, H2a also known as histone H2A (HIST3H2A) is a member of histones. Covalent modification of histones is important in regulating chromatin dynamics and transcription. One example of such modification is ubiquitination, which mainly occurs on histones H2A and H2B. E3 ubiquitin ligase complex is specific for histone H2A (HIST3H2A). Reducing the expression of Ring2 results in a dramatic decrease in the level of ubiquitinated H2A in HeLa cells. DNA damage induces monoubiquitylation of histone H2A (HIST3H2A) in the vicinity of DNA lesions.
HIST3H2A ELISA Pair sets
HIST3H2A cDNA Clones
- HIST3H2A cDNA Clone / ORF Clone, Cat No:HG10926-M
- HIST3H2A cDNA Clone / ORF Clone, Cat No: MG51011-G
Entrez Gene summary for HIST3H2A:
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 member of the histone H2A family. Transcripts from this gene contain a palindromic termination element.
OMIM - description for HIST3H2A:
By genomic sequence analysis, Marzluff et al. (2002) determined that the HIST1 cluster on chromosome 6p22-p21 contains 55 histone genes, including 12 H2A genes. The HIST1H2AA gene is the most telomeric H2A gene within the HIST1 cluster. The HIST1 cluster spans over 2 Mb and includes 2 large gaps (over 250 kb each) where there are no histone genes, but many other genes. The organization of histone genes in the mouse Hist1 cluster on chromosome 13A2-A3 is essentially identical to that in human HIST1. The HIST2 cluster on chromosome 1q21 contains 6 histone genes, including 3 H2A genes (e.g., HIST2H2AA3; 142720), and the HIST3 cluster on chromosome 1q42 contains 3 histone genes, including 1 H2A gene (HIST3H2A). Hist2 and Hist3 are located on mouse chromosomes 3F1-F2 and 11B2, respectively. Marzluff et al. (2002) noted that all 3 histone clusters in human and mouse contain pairs of H2A and H2B genes. These paired H2A and H2B genes are transcribed from opposite strands, with their 5-prime ends separated by an intergenic region of less than 300 nucleotides. A similar organization of H2a and H2b genes is found in yeast, Drosophila, C. elegans, and sea urchin.
Wikipedia summary for HIST3H2A:
Histone H2A type 3 is a protein that in humans is encoded by the HIST3H2A gene.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 member of the histone H2A family. Transcripts from this gene contain a palindromic termination element.
Recommended name: Histone H2A type 3
Belongs to the histone H2A family.
The chromatin-associated form is phosphorylated on Thr-121 during mitosis Probable. Ref.6 Ref.7 Deiminated on Arg-4 in granulocytes upon calcium entry. Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3. Monoubiquitination of Lys-120 by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Monoubiquitination and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events. Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
|Subcellular location:||Nucleus. Chromosome.|
General information above from UniProt
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.