The Rel homology domain (RHD) is a protein domain found in a family of eukaryotic transcription factors, [2] including both NF-κB and NFAT, among others. Some of these transcription factors appear to form multi-protein DNA -bound complexes. [3] Phosphorylation of the RHD appears to play a role in the regulation of some of these transcription factors, acting to modulate the expression of their …
Members of the NF-κB/Rel family of transcription factors share an approximately 300 amino acid-long N-terminal region, called the Rel-homology domain (Baeuerle and Henkel 1994, Siebenlist et al. 1994). Many of the major functions of the family members reside in this region, like DNA binding, dimerization, nuclear localization, and interactions with an inhibitory molecule, IκB. Some of the …
The Rel homology domain (RHD) is a protein domain found in a family of eukaryotic transcription factors, including both NF-κB and NFAT, among others. Some of these transcription factors appear to form multi-protein DNA-bound complexes. Phosphorylation of the RHD appears to play a role in the regulation of some of these transcription factors, acting to modulate the expression of their target …
Rel homology domain phylogeny and domain architecture of Rel homology domain-containing proteins in NF-κB and NFAT families. Only SH-aLRT and nonparametric bootstrap support values above 80 and 60, respectively, are shown. Fully supported bipartitions are indicated with filled circles. Sequences are color-coded according to taxonomic group: red, Metazoa; yellow, Choanoflagellatea; orange …
The Nuclear Factor Kappa B (NF-κB) transcription factor family consists of five members: RelA (p65), RelB, c-Rel, p50 (p105/NF-κB1), and p52 (p100/NF-κB2). This family is considered a master regulator of classical biochemical pathways such as inflammation, immunity, cell proliferation, and cell death. The proteins in this family have a conserved Rel homology domain (RHD) with the following …
Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See
Courtois G, Gilmore TD (2006) Mutations in the NF-κB signaling pathway: implications for human disease. Oncogene 25:6831-6843 Article CAS PubMed Google Scholar Ghosh S (ed) (2006) Handbook of transcription factor NF-kappaB. CRC Press LLC, Boca Raton, p 232 Google Scholar Gilmore TD (2006) The NF-κB signal transduction pathway: pathways, players, perspectives. Oncogene 18:6842-6844 …
A conserved DNA-binding domain (~300 aa), first identified in the product of the rel oncogene, a transcription factor, and subsequently found to be characteristic of eukaryotic transcription factors such as NFκB and NFAT. Phosphorylation of the domain may regulate activity of the factors.
The protein product, proto-oncogene c-Rel, contains a Rel homology domainand DNA-binding domain, and functions as a transcriptional activator in the nucleus and nucleoplasm. It is expressed at high levels in the hematopoietic system, gastrointestinal tract, and skin, matching its prominent roles in immune and tissue-specific regulatory programs.