| Function | Chromatin reader protein that specifically recognizes and binds histone H4 acetylated at 'Lys-5' and 'Lys-12' (H4K5ac and H4K12ac, respectively), thereby controlling gene expression and remodeling chromatin structures. Recruits transcription factors and coactivators to target gene sites, and activates RNA polymerase II machinery for transcriptional elongation. Plays a key role in genome compartmentalization via its association with CTCF and cohesin: recruited to chromatin by CTCF and promotes formation of topologically associating domains (TADs) via its ability to bind acetylated histones, contributing to CTCF boundary formation and enhancer insulation. Also recognizes and binds acetylated non-histone proteins, such as STAT3. Involved in inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17: recognizes and binds STAT3 acetylated at 'Lys-87', promoting STAT3 recruitment to chromatin. In addition to acetylated lysines, also recognizes and binds lysine residues on histones that are both methylated and acetylated on the same side chain to form N6-acetyl-N6-methyllysine (Kacme), an epigenetic mark of active chromatin associated with increased transcriptional initiation. Specifically binds histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively). |
| Protein Name | Bromodomain-Containing Protein 2O27.1.1 |
| Database Links | Reactome: R-HSA-8951936 |
| Cellular Localisation | NucleusChromosomeDetected On Chromatin And Nucleosomes |
| Alternative Protein Names | Bromodomain-Containing Protein 2 proteinO27.1.1 proteinBRD2 proteinKIAA9001 proteinRING3 protein |
Information sourced from Uniprot.org
