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ata show that PP32 and SET/TAF-Ibeta proteins block HAT1-mediated H4 acetylation.
Data suggest post-translational modifications of histones, trimethylation of lysine 36 in H3 (H3K36me3) and acetylation of lysine 16 in H4 (H4K16ac), have roles in DNA damage repair; H3K36me3 stimulates H4K16ac upon DNA double-strand break; SETD2, LEDGF (show PSIP1 Proteins), and KAT5 (show KAT5 Proteins) are required for these epigenetic changes. (SETD2 = SET domain containing 2; LEDGF (show PSIP1 Proteins) = lens epithelium-derived growth factor (show PSIP1 Proteins); KAT5 (show KAT5 Proteins) = lysine acetyltransferase 5 (show KAT5 Proteins))
Data suggest that O-GlcNAc (show OGT Proteins) transferase 1 (OGT1) specifically binds to, O-GlcNAcylates, and stabilizes nonspecific lethal protein3 (NSL3 (show KANSL3 Proteins)); stabilization of NSL3 (show KANSL3 Proteins) by OGT1 up-regulates global acetylation levels of histone 4 at Lys-5 (show AASDHPPT Proteins), Lys (show LYZ Proteins)-8, and Lys (show LYZ Proteins)-16.
Data show that Omomyc protein co-localized with proto-oncogene (show RAB1A Proteins) protein c (show PROC Proteins)-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.
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