Brd4 Rabbit Polyclonal Antibody (ER1901-02)

UNIPROT #

O60885

PROTEIN NAME

Brd4

SYNONYMS

Brd4 antibody;BRD4-NUT FUSION antibody;BRD4-NUT fusion oncoprotein antibody;BRD4_HUMAN antibody;Bromodomain containing 4 antibody;bromodomain containing protein 4 antibody;Bromodomain-containing protein 4 antibody;CAP antibody;chromosome associated protein antibody;HUNK1 antibody;HUNKI antibody;MCAP antibody;Mitotic chromosome-associated protein antibody;Protein HUNK1 antibody

TISSUE SPECIFICITY

Ubiquitously expressed.

POST-TRANSLATIONAL MODIFICATION

Phosphorylation by CK2 disrupt the intramolecular binding between the bromo domain 2 and the NPS region and promotes binding between the NPS and the BID regions, leading to activate the protein and promote binding to acetylated histones. In absence of phosphorylation, BRD4 does not localize to p53/TP53 target gene promoters, phosphorylation promoting recruitment to p53/TP53 target promoters.

SUBCELLULAR LOCATION

Nucleus.

FUNCTION

Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters: BRD4 is required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II. Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II. According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B. Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters.