spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR004827 Basic-leucine zipper (bZIP) transcription factor

Protein matchesHelp
UniProtKB
Matches:
4445 proteins
AccessionHelp IPR004827 TF_bZIP
SecondaryHelp IPR001871
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR004826 Maf transcription factor
IPR011616 bZIP transcription factor, bZIP-1
IPR011700 Basic leucine zipper
Contains IPR008917 Eukaryotic transcription factor, Skn-1-like, DNA-binding
GO Term annotationHelp
Process GO:0006355 regulation of transcription, DNA-dependent
Function GO:0003700 transcription factor activity
GO:0043565 sequence-specific DNA binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The basic-leucine zipper (bZIP) transcription factors [1, 2] of eukaryotic are proteins that contain a basic region mediating sequence-specific DNA-binding followed by a leucine zipper region (see IPR002158) required for dimerization.

Structural linksHelp
PDB - click here
Database linksHelp
PDBe-motif: PS00036
PROSITE doc: PDOC00036
Blocks: IPB004827
InteractionsHelp
This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR004827 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A8MPH9 Transcription factor kayak, isoforms D/sro

O14867 Transcription regulator protein BACH1

O54790 Transcription factor MafG

P03069 General control protein GCN4

P34707 Protein skinhead-1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013089 Kelch related
IPR013069 BTB/POZ
IPR011333 BTB/POZ fold
IPR000837 Fos transforming protein
IPR000210 BTB/POZ-like
IPR004827 Basic-leucine zipper (bZIP) transcription factor
IPR008917 Eukaryotic transcription factor, Skn-1-like, DNA-binding
IPR004826 Maf transcription factor
IPR011616 bZIP transcription factor, bZIP-1
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Hurst HC.
Transcription factors 1: bZIP proteins.
2 101-68 1995 [PubMed: 7780801]
2. Ellenberger T.
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 12-21 1994

Additional ReadingHelp
Deng Y, Liu J, Zheng Q, Li Q, Kallenbach NR, Lu M.
A heterospecific leucine zipper tetramer.
Chem. Biol. 15 2008 908-19 [PubMed: 18804028]
http://dx.doi.org/10.1016/j.chembiol.2008.07.008
Datta S, Johansson H, Hettiarachchi C, Irigoyen ML, Desai M, Rubio V, Holm M.
LZF1/SALT TOLERANCE HOMOLOG3, an Arabidopsis B-box protein involved in light-dependent development and gene expression, undergoes COP1-mediated ubiquitination.
Plant Cell 20 2008 2324-38 [PubMed: 18796637]
http://dx.doi.org/10.1105/tpc.108.061747
Kuras L, Cherest H, Surdin-Kerjan Y, Thomas D.
A heteromeric complex containing the centromere binding factor 1 and two basic leucine zipper factors, Met4 and Met28, mediates the transcription activation of yeast sulfur metabolism.
EMBO J. 15 1996 2519-29 [PubMed: 8665859]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=8665859&action=stream&blobtype=pdf
Brown JH, Yang Y, Reshetnikova L, Gourinath S, Suveges D, Kardos J, Hobor F, Reutzel R, Nyitray L, Cohen C.
An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins.
J. Mol. Biol. 375 2008 1434-43 [PubMed: 18155233]
http://dx.doi.org/10.1016/j.jmb.2007.11.071
Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Muller CW.
Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein.
Mol. Cell 21 2006 565-72 [PubMed: 16483937]
http://dx.doi.org/10.1016/j.molcel.2006.01.006
Baranger AM.
Accessory factor-bZIP-DNA interactions.
2 1998 18-23 [PubMed: 9667910]
http://dx.doi.org/10.1016/S1367-5931(98)80031-8
Liu J, Zheng Q, Deng Y, Cheng CS, Kallenbach NR, Lu M.
A seven-helix coiled coil.
Proc. Natl. Acad. Sci. U.S.A. 103 2006 15457-62 [PubMed: 17030805]
http://dx.doi.org/10.1073/pnas.0604871103
Ellenberger TE, Brandl CJ, Struhl K, Harrison SC.
The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex.
Cell 71 1992 1223-37 [PubMed: 1473154]
http://dx.doi.org/10.1016/S0092-8674(05)80070-4
Yadav MK, Leman LJ, Price DJ, Brooks CL 3rd, Stout CD, Ghadiri MR.
Coiled coils at the edge of configurational heterogeneity. Structural analyses of parallel and antiparallel homotetrameric coiled coils reveal configurational sensitivity to a single solvent-exposed amino acid substitution.
Biochemistry 45 2006 4463-73 [PubMed: 16584182]
http://dx.doi.org/10.1021/bi060092q
spacer
spacer
InterPro 23.1