| Primary Identifier | IPR030495 | Type | Family |
| Short Name | RelA |
| description | This entry represents RelA, also known as nuclear factor NF-kappa-B p65 subunit. RelA and p50 is the mostly commonly found heterodimer complex among NF-kappaB homodimers and heterodimers, and is the functional component participating in nuclear transclocation and activation of NF-kappaB [].NF-kappaB is a pleiotropic transcription factor present in almost all cell types. It is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappaB is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RelA/p65, RelB, NFKB1/p50, c-Rel and NFKB2/p52 []. Each individual NF-kappaB subunit, and perhaps each dimer, carries out unique functions in regulating transcription. Dimer-specific functions can be conferred by selective protein-protein interactions with other transcription factors, coregulatory proteins, and chromatin proteins [].The prototypical NF-kB complex is a p50/RelA heterodimer. NF-kB is largely sequestered in the cytoplasm through its association with an IkB inhibitor []. Cytoplasmic events culminating in the phosphorylation of IkB-alpha lead to its polyubiquitylation and proteasome-mediated degradation. The liberated NF-kB complex translocates to the nucleus. In the nucleus, site-specific acetylation and phosphorylation of RelA regulates the actions of the NF-kB complex [, ]. |
