|PROSITE documentation PDOC00924 [for PROSITE entry PS50254]|
Various studies (reviewed in [1,2,3,4,5]) have allowed the characterization of a family of eukaryotic transcription factors with basic impact on oncogenesis, embryonic development and differentiation including immune response and acute phase reaction. Most of these transcription factors bind as dimers to the consensus DNA sequence motif 5'-GGGRNNYYCC-3' termed kappa-B according the first described factor-binding sequence motif located in the immunoglobulin kappa light chain enhancer region.
Proteins of this family appear to be regulated, at least in part, by subcellular localization whereby the inactive cytoplasmic forms become active transcriptional control proteins by translocation to the nucleus. Members of the Rel family share a highly conserved 300 amino acids domain termed Rel homology domain (RHD) which is located towards the amino terminus. The unique C-terminal is thought to be involved in gene activation and cytoplasmic anchoring functions.
Proteins known to contain a RHD domain are listed below:
For several proteins it has been demonstrated ( and references therein) that the Rel homology domain includes:
(1) a DNA-binding domain, which binds to the consensus DNA sequence motif 5'-GGGRNNYYCC-3' (except for dorsal, which recognizes the related motif 5'-GRGAAAANCC-3'); (2) a dimerization domain, which is located in the C-terminal part of the RHD; (3) a PKA phosphorylation site (see <PDOC00004>) (except in RelB); (4) a nuclear localization signal (NLS), which consists of a stretch of four or five basic residues.
As a signature for this family we selected a region that is located at the N-terminal of the RHD. This region includes a conserved cysteine that seems to be essential for DNA-binding in p50 . We also developed a profile that spans completly the RHD.Last update:
December 2001 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Kabrun N., Enrietto P.J.|
|Title||The Rel family of proteins in oncogenesis and differentiation.|
|Source||Semin. Cancer Biol. 5:103-112(1994).|
|2||Authors||Blank V., Kourilsky P., Israel A.|
|Title||NF-kappa B and related proteins: Rel/dorsal homologies meet ankyrin-like repeats.|
|Source||Trends Biochem. Sci. 17:135-140(1992).|
|Source||Current Biol. 1:103-105(1991).|
|Title||Malignant transformation by mutant Rel proteins.|
|Source||Trends Genet. 7:318-322(1991).|
|Title||NF-kappa B, KBF1, dorsal, and related matters.|
|6||Authors||Mitomo K., Nakayama K., Fujimoto K., Sun X., Seki S., Yamamoto K.-I.|
|Title||Two different cellular redox systems regulate the DNA-binding activity of the p50 subunit of NF-kappa B in vitro.|