| Description | The relA gene encodes a protein composed 551 amino acids with an approximately molecular weight of 65 kDa. The N-terminal region of RelA contains a Rel homology domain (RHD) followed by a nuclear localization signal. The C-terminal region of RelA contains a putative leucine zipper domain and a transactivation domain that is important for the NF-kB-mediated gene transactivation. A number of protein kinases can phosphorylate RelA and consequently potentiate the transcriptional activity of NF-kB complexes. These kinases include IKKb, PKA, and possibly GSK3 and MAP kinase p38. The phosphorylation of the transactivation domain of RelA was considered as an important event for the recruitment and/or interaction with co-factors and general transcriptional machinery subunits such as p300 and TFIIB. |
| Expression | wide. |
| Localisation | cytosol, nuclei after activation. |
| Function | regulation of the genes involved in cell-to-cell interaction, intercellular communication, cell recruitment or transmigration, amplification or spreading of primary pathogenic signals, cell apoptosis, and initiation or acceleration of tumorigenesis. The p50/RelA complex is the most abundant NF-kB complex in all type tissues or cells. Interaction with: members of IkB family and Rel family; GR; HDAC3; CREB; p300; Sp1, Egr1; AES; TFIIB. |
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