AlphaFold predicted structure
BRD4 · O60885
Mean pLDDT
55.3/ 100
Low
1,362 residues
Confidence breakdown
- Very high(≥ 90)18%
- Confident(70–90)12%
- Low(50–70)10%
- Very low(< 50)61%
Open interactive 3D viewer
AlphaFold (Jumper et al., 2021) · CC BY 4.0
BRD4
Chr 19p13.12bromodomain containing 4
- Aliases:
- HUNKI, MCAP, CAP, HUNK1, FSHRG4
- MANE:
- ENST00000679869.1
Annotations refreshed 1 month ago.
Predicted protein structure
Clinical relevance (Genomics England PanelApp)
Diagnostic Grade (Green)
DDG2P
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknownFetal anomalies
MONOALLELIC, autosomal or pseudoautosomal, NOT imprintedIntellectual disability
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknownSevere microcephaly
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Disease associations (Open Targets)
Cornelia de Lange syndrome 6
0.69Cornelia de Lange syndrome
0.50neoplasm
0.49syndromic intellectual disability
0.453q26 microduplication syndrome
0.45hereditary disease
0.41esophageal squamous cell carcinoma
0.40nut midline carcinoma
0.39colon adenocarcinoma
0.37cutaneous melanoma
0.37
Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.
Protein function (UniProt)
Bromodomain-containing protein 4
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 (PubMed:20871596, PubMed:23086925, PubMed:23317504, PubMed:29176719, PubMed:29379197). 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 (PubMed:22334664, PubMed:23317504, PubMed:23589332). 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 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). BRD4 and JMJD6 are 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 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (By similarity). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:23086925). 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 (PubMed:19103749). Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (PubMed:23317504)
Diseases associated with BRD4
Curated MONDO disease pages that list BRD4 among their top associated genes.