Summary: Bromodomain extra-terminal - transcription regulation
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Bromodomain extra-terminal - transcription regulation Provide feedback
The BET, or bromodomain extra-terminal domain, is found on bromodomain proteins that play key roles in development, cancer progression and virus-host pathogenesis. It interacts with NSD3, JMJD6, CHD4, GLTSCR1, and ATAD5 all of which are shown to impart a pTEFb-independent transcriptional activation function on the bromodomain proteins [1].
Literature references
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Rahman S, Sowa ME, Ottinger M, Smith JA, Shi Y, Harper JW, Howley PM;, Mol Cell Biol. 2011;31:2641-2652.: The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3. PUBMED:21555454 EPMC:21555454
Internal database links
SCOOP: | MIC19_MIC25 |
Similarity to PfamA using HHSearch: | AHD |
This tab holds annotation information from the InterPro database.
InterPro entry IPR027353
The bromodomain and extraterminal (BET) proteins are a class of transcriptional regulators whose members can be found in animals, plants and fungi. BET proteins are involved in diverse cellular phenomena such as meiosis, cell-cycle control, and homeosis and have been suggested to modulate chromatin structure and affect transcription via a sequence-independent mechanism. BET proteins are defined as having one (plants) or two (animals/yeast) bromodomains and an Extra Terminal (ET) domain. The ET domain consists of three separate regions, only one of which, the N-terminal ET (NET) domain is conserved in all BET proteins. The function of the NET domain is assumed to be protein binding [ PUBMED:7816623 , PUBMED:11487468 , PUBMED:12969431 , PUBMED:18815416 ].
The structure of the NET domain comprises three alpha-helices and a characteristic loop region of an irregular but well-defined structure. The NET structure has an acidic patch that forms a continuous ridge with a hydrophobic cleft. which may interact with other proteins and/or DNA [ PUBMED:18815416 ].
Some proteins known to contain a NET domain include:
- Human RING3 (now designated Brd2)
- Murine MCAP (now designated Brd4)
- Drosophila Fsh
- Yeast Bdf1 and Bdf2
- Arabidopsis imbibition-inducible (IMB1), whichplays a role in abscisic acid (ABA) and phytochrome A (phyA) mediated responses of seed germination.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
Alignments
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Seed (155) |
Full (6516) |
Representative proteomes | UniProt (10001) |
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RP15 (977) |
RP35 (2804) |
RP55 (4959) |
RP75 (6760) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (155) |
Full (6516) |
Representative proteomes | UniProt (10001) |
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RP15 (977) |
RP35 (2804) |
RP55 (4959) |
RP75 (6760) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | [1] |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Coggill P |
Number in seed: | 155 |
Number in full: | 6516 |
Average length of the domain: | 64.2 aa |
Average identity of full alignment: | 36 % |
Average coverage of the sequence by the domain: | 9.21 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 64 | ||||||||||||
Family (HMM) version: | 8 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the BET domain has been found. There are 15 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.