| Primary Identifier | IPR030503 | Type | Family |
| Short Name | NF-kB_p105 |
| description | This entry represents the NF-kappaB subunit precursor p105, which can undergo cotranslational processing by the 26S proteasome to produce a 50kDa protein (p50). p50 is a DNA binding subunit of the NF-kappaB (NF-kappaB) protein complex [].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 [].NF-kB1 and NF-kB2 are synthesised as large precursors, called p105 and p100, which undergo processing to generate the NF-kB subunits p50 and p52, respectively []. The processing of p105 and p100 is mediated by the ubiquitin/proteasome pathway, and involves selective degradation of their C-terminal regions containing ankyrin repeats []. Unlike RelA, RelB and c-Rel, p50 and p52 do not contain transactivation domains in their C-termini. Nevertheless, they play critical roles in modulating the specificity of NF-kB function []. |
