Summary: Basic region leucine zipper
This is the Wikipedia entry entitled "BZIP domain". More...
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BZIP domain Edit Wikipedia article
|bZIP transcription factor|
The Basic Leucine Zipper Domain (bZIP domain) is found in many DNA binding eukaryotic proteins. One part of the domain contains a region that mediates sequence specific DNA binding properties and the leucine zipper that is required to hold together (dimerize) two DNA binding regions. The DNA binding region comprises a number of basic amino acids such as arginine and lysine. Proteins containing this domain are transcription factors.
bZIP transcription factors
bZIP transcription factors are found in all organisms. A recent evolutionary study revealed that 4 bZIP genes were encoded by the genome of the most recent common ancestor of all plants. Interactions between bZIP transcription factors play important roles in cancer development in epithelial tissues, steroid hormone synthesis by cells of endocrine tissues, factors affecting reproductive functions, and several other phenomena that affect human health.
bZIP domain containing proteins
- AP-1 fos/jun heterodimer that forms a transcription factor
- Jun-B transcription factor
- CREB cAMP response element transcription factor
- OPAQUE2 (O2) transcription factor of the 22-kD zein gene that encodes a class of storage proteins in the endosperm of maize (Zea Mays) kernels
- NFE2L2 or Nrf2
- Bzip Maf transcription factors
Human proteins containing this domain
ATF1; ATF2; ATF4; ATF5; ATF6; ATF7; BACH1; BACH2; BATF; BATF2; CREB1; CREB3; CREB3L1; CREB3L2; CREB3L3; CREB3L4; CREB5; CREBL1; CREM; E4BP4; FOSL1; FOSL2; JUN; JUNB; JUND; MAFA; MAFB; NFE2; NFE2L2; NFE2L3; SNFT; XBP1
- bZIP domain entry in the SMART database
- bZIP family at PlantTFDB: Plant Transcription Factor Database
- Plant bZIP transcription factors
- Ellenberger T (1994). "Getting a grip in DNA recognition: structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains.". Curr. Opin. Struct. Biol. 4 (1): 12–21. doi:10.1016/S0959-440X(94)90054-X.
- Hurst HC (1995). "Transcription factors 1: bZIP proteins". Protein Profile 2 (2): 101–68. PMID 7780801.
- Corrêa LGG, Riaño-Pachón DM, Schrago CG, dos Santos RV, Mueller-Roeber B, Vincentz M. (2008). "The Role of bZIP Transcription Factors in Green Plant Evolution: Adaptive Features Emerging from Four Founder Genes". In Shiu, Shin-Han. PLoS ONE 3 (8): e2944. doi:10.1371/journal.pone.0002944. PMC 2492810. PMID 18698409.
- Vlahopoulos SA, Logotheti S, Mikas D, Giarika A, Gorgoulis V, Zoumpourlis V (April 2008). "The role of ATF-2 in oncogenesis". BioEssays 30 (4): 314–27. doi:10.1002/bies.20734. PMID 18348191.
- Manna PR, Dyson MT, Eubank DW, Clark BJ, Lalli E, Sassone-Corsi P, Zeleznik AJ, Stocco DM (January 2002). "Regulation of steroidogenesis and the steroidogenic acute regulatory protein by a member of the cAMP response-element binding protein family". Mol. Endocrinol. 16 (1): 184–99. doi:10.1210/me.16.1.184. PMID 11773448.
- Hoare S, Copland JA, Wood TG, Jeng YJ, Izban MG, Soloff MS (May 1999). "Identification of a GABP alpha/beta binding site involved in the induction of oxytocin receptor gene expression in human breast cells, potentiation by c-Fos/c-Jun". Endocrinology 140 (5): 2268–79. doi:10.1210/en.140.5.2268. PMID 10218980.
Basic region leucine zipper Provide feedback
No Pfam abstract.
Internal database links
|Similarity to PfamA using HHSearch:||bZIP_Maf bZIP_1|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR011700
The basic-leucine zipper (bZIP) transcription factors [PUBMED:7780801, PUBMED:] of eukaryotes are proteins that contain a basic region mediating sequence-specific DNA-binding, followed by a leucine zipper region (see INTERPRO), which is required for dimerization.
|Molecular function||sequence-specific DNA binding (GO:0043565)|
|sequence-specific DNA binding transcription factor activity (GO:0003700)|
|protein dimerization activity (GO:0046983)|
|Biological process||regulation of transcription, DNA-dependent (GO:0006355)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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Curation and family details
|Seed source:||PfamB-200; Release 14.0;|
|Number in seed:||48|
|Number in full:||1966|
|Average length of the domain:||53.70 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||17.49 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 bZIP_2 domain has been found. There are 25 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 seqence.
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