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Data show that Omomyc protein co-localized with proto-oncogene (show RAB1A Proteins) protein c-myc (c-Myc (show MYC Proteins)), protein arginine methyltransferase 5 (PRMT5 (show PRMT5 Proteins)) and histone H4 H4R3me2s-enriched chromatin domains.
H4K12ac is regulated by estrogen receptor-alpha (show ESR1 Proteins) and is associated with BRD4 (show BRD4 Proteins) function and inducible transcription
Systemic lupus erythematosus appears to be associated with an imbalance in histone acetyltransferases and histone deacetylase (show HDAC1 Proteins) enzymes favoring pathologic H4 acetylation.
Data indicate that MEP50 (show WDR77 Proteins) WD repeat protein (show DCAF7 Proteins) is essential for methylation of histones H4 and H2A by PRMT5 (show PRMT5 Proteins) arginine methyltransferase.
Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions.
Acetylation at lysine 5 of histone H4 associated with lytic gene promoters during reactivation of Kaposi's sarcoma-associated herpesvirus.
An increase in histone H4 acetylation caused by hypoxia in human neuroblastoma (show ARHGEF16 Proteins) cell lines corresponds to increased levels of N-myc (show MYCN Proteins) transcription factor in these cells.
Human PIH1 domain-containing protein 1 (PIH1) interacts directly with histone H4 and recruits the Brg1 (show SMARCA4 Proteins)-SWI (show SMARCA1 Proteins)/SNF (show SNRPA Proteins) complex via SNF5 (show SMARCB1 Proteins) to human rRNA genes.
Data indicate that G1-phase histone assembly is restricted to CENP-A (show CENPA Proteins) and H4.
SRP68/72 heterodimers as major nuclear proteins whose binding of histone H4 tail is inhibited by H4R3 methylation.
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 H4 family. Transcripts from this gene lack polyA tails\\\\; instead, they contain a palindromic termination element.
, histone 4, H4