The domain within your query sequence starts at position and ends at position ; the E-value for the BTP domain shown below is < 1e-12.
BTPBromodomain transcription factors and PHD domain containing proteins
|SMART accession number:||SM00576|
|Description:||subdomain of archael histone-like transcription factors|
|Interpro abstract (IPR006565):|
This bromodomain is found in eukaryotic transcription factors and PHD domain containing proteins (IPR001965). The tandem PHD finger-bromodomain is found in many chromatin-associated proteins. It is involved in gene silencing by the human co-repressor KRAB-associated protein 1 (KAP1). The tandem PHD finger-bromodomain of KAP1 has a distinct structure that joins the two protein modules. The first helix, alpha(Z), of an atypical bromodomain forms the central hydrophobic core that anchors the other three helices of the bromodomain on one side and the zinc binding PHD finger on the other [(PUBMED:18488044)].
The Rap1 GTPase-activating protein, Sipa1, is modulated by the cellular bromodomain protein, Brd4. Brd4 belongs to the BET family and is a multifunctional protein involved in transcription, replication, the signal transduction pathway, and cell cycle progression. All of these functions are linked to its association with acetylated chromatin. It has tandem bromodomains [(PUBMED:18500820)]. The dysregulation of the Brd4-associated pathways may play an important role in breast cancer progression [(PUBMED:18427120)]. Bovine papillomavirus type 1 E2 also binds to chromosomes in a complex with Brd4. Interaction with Brd4 is additionally important for E2-mediated transcriptional regulation [(PUBMED:18495759), (PUBMED:18513937)].
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