Summary: BTB/POZ domain
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BTB/POZ domain Edit Wikipedia article
| BTB/POZ domain | |||||||||
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Structure of the BTB domain from PLZF.[1]
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| Identifiers | |||||||||
| Symbol | BTB | ||||||||
| Pfam | PF00651 | ||||||||
| InterPro | IPR013069 | ||||||||
| PROSITE | PS50097 | ||||||||
| SCOP | 1buo | ||||||||
| SUPERFAMILY | 1buo | ||||||||
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The BTB/POZ domain is a common structural domain contained within some proteins.
The BTB (for BR-C, ttk and bab)[2] or POZ (for Pox virus and Zinc finger)[3] domain is present near the N-terminus of a fraction of zinc finger proteins and in proteins that contain the Kelch motif and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerisation and in some instances heteromeric dimerisation.[3] The structure of the dimerised PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule.[1] BTB/POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT.[4][5][6] The POZ or BTB domain is also known as BR-C/Ttk or ZiN.
References
- ^ a b Ahmad KF, Engel CK, Privé GG (October 1998). "Crystal structure of the BTB domain from PLZF". Proc. Natl. Acad. Sci. U.S.A. 95 (21): 12123–8. doi:10.1073/pnas.95.21.12123. PMC 22795
. PMID 9770450. - ^ Zollman S, Godt D, Privé GG, Couderc JL, Laski FA (October 1994). "The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila". Proc. Natl. Acad. Sci. U.S.A. 91 (22): 10717–21. doi:10.1073/pnas.91.22.10717. PMC 45093. PMID 7938017.
- ^ a b Bardwell VJ, Treisman R (July 1994). "The POZ domain: a conserved protein-protein interaction motif". Genes Dev. 8 (14): 1664–77. doi:10.1101/gad.8.14.1664. PMID 7958847.
- ^ Deweindt C, Albagli O, Bernardin F, Dhordain P, Quief S, Lantoine D, Kerckaert JP, Leprince D (December 1995). "The LAZ3/BCL6 oncogene encodes a sequence-specific transcriptional inhibitor: a novel function for the BTB/POZ domain as an autonomous repressing domain". Cell Growth Differ. 6 (12): 1495–503. PMID 9019154.
- ^ Huynh KD, Bardwell VJ (November 1998). "The BCL-6 POZ domain and other POZ domains interact with the co-repressors N-CoR and SMRT". Oncogene. 17 (19): 2473–84. doi:10.1038/sj.onc.1202197. PMID 9824158.
- ^ Wong CW, Privalsky ML (October 1998). "Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6". J. Biol. Chem. 273 (42): 27695–702. doi:10.1074/jbc.273.42.27695. PMID 9765306.
This article incorporates text from the public domain Pfam and InterPro IPR013069
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
BTB/POZ domain Provide feedback
The BTB (for BR-C, ttk and bab) [1] or POZ (for Pox virus and Zinc finger) [2] domain is present near the N-terminus of a fraction of zinc finger (PF00096) proteins and in proteins that contain the PF01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerisation and in some instances heteromeric dimerisation [2]. The structure of the dimerised PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule [3]. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT [4,5,6]. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.
Literature references
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Zollman S, Godt D, Prive GG, Couderc JL, Laski FA; , Proc Natl Acad Sci U S A 1994;91:10717-10721.: The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila. PUBMED:7938017 EPMC:7938017
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Bardwell VJ, Treisman R; , Genes Dev 1994;8:1664-1677.: The POZ domain: a conserved protein-protein interaction motif. PUBMED:7958847 EPMC:7958847
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Ahmad KF, Engel CK, Prive GG; , Proc Natl Acad Sci U S A 1998;95:12123-12128.: Crystal structure of the BTB domain from PLZF. PUBMED:9770450 EPMC:9770450
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Deweindt C, Albagli O, Bernardin F, Dhordain P, Quief S, Lantoine D, Kerckaert JP, Leprince D; , Cell Growth Differ 1995;6:1495-1503.: The LAZ3/BCL6 oncogene encodes a sequence-specific transcriptional inhibitor: a novel function for the BTB/POZ domain as an autonomous repressing domain. PUBMED:9019154 EPMC:9019154
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Huynh KD, Bardwell VJ; , Oncogene 1998;17:2473-2484.: The BCL-6 POZ domain and other POZ domains interact with the co-repressors N-CoR and SMRT. PUBMED:9824158 EPMC:9824158
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Wong CW, Privalsky ML; , J Biol Chem 1998;273:27695-27702.: Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6. PUBMED:9765306 EPMC:9765306
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Stogios PJ, Downs GS, Jauhal JJ, Nandra SK, Prive GG; , Genome Biol. 2005;6:R82.: Sequence and structural analysis of BTB domain proteins. PUBMED:16207353 EPMC:16207353
Internal database links
| SCOOP: | BACK BTB_2 BTB_3 DUF3342 Skp1_POZ zf-C2H2 |
| Similarity to PfamA using HHSearch: | BTB_2 Skp1_POZ BTB_3 |
External database links
| PROSITE profile: | PS50097 |
| SCOP: | 1buo |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000210
The BTB domain (Broad-Complex, Tramtrack and Bric a brac) is also known as the POZ domain (POxvirus and Zinc finger). It is a homodimerization domain occurring at the N terminus of proteins containing multiple copies of either zinc fingers of the C2H2 type or Kelch repeats [ PUBMED:7938017 , PUBMED:7958847 ]. Many BTB proteins are transcriptional regulators that are thought to act through the control of chromatin structure.
The structure of the BTB domain of the promyelocytic leukemia zinc finger (PLZF) protein has been determined by X-ray crystallography and reveals a tightly intertwined dimer with an extensive hydrophobic interface [ PUBMED:9770450 ]. A surface-exposed groove lined with conserved amino acids is formed at the dimer interface, suggesting a peptide-binding site.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | protein binding (GO:0005515) |
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
This family is a member of clan POZ (CL0033), which has the following description:
The POZ domain is found in a variety of transcription factors. POZ domains are also found in the tetramerisation domain of voltage gated K+ channels. In general these domains mediate homo-oligomerisation.
The clan contains the following 6 members:
BACK BTB BTB_2 BTB_3 DUF3342 Skp1_POZAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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| Seed (83) |
Full (87659) |
Representative proteomes | UniProt (152057) |
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| RP15 (17617) |
RP35 (40077) |
RP55 (75228) |
RP75 (98011) |
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| PP/heatmap | 1 | ||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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| Seed (83) |
Full (87659) |
Representative proteomes | UniProt (152057) |
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|---|---|---|---|---|---|---|---|
| RP15 (17617) |
RP35 (40077) |
RP55 (75228) |
RP75 (98011) |
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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
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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: | Prosite |
| Previous IDs: | none |
| Type: | Domain |
| Sequence Ontology: | SO:0000417 |
| Author: |
Bateman A  , Bardwell VJ
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| Number in seed: | 83 |
| Number in full: | 87659 |
| Average length of the domain: | 106.10 aa |
| Average identity of full alignment: | 19 % |
| Average coverage of the sequence by the domain: | 20.62 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 111 | ||||||||||||
| Family (HMM) version: | 33 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Colour assignments
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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 BTB domain has been found. There are 186 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.
