Anti-RELA

Enables several functions, including DNA-binding transcription factor activity, RNA polymerase II-specific, actinin binding activity, and ankyrin repeat binding activity. Involved in several processes, including negative regulation of protein sumoylation, postsynapse to nucleus signaling pathway, and regulation of transcription, DNA-templated. Acts upstream of or within several processes, including cellular response to hepatocyte growth factor stimulus, cellular response to lipopolysaccharide, and positive regulation of interleukin-12 production. Located in several cellular components, including chromatin, cytosol, and glutamatergic synapse. Is expressed in several structures, including alimentary system, early conceptus, genitourinary system, musculature, and skin. Human ortholog(s) of this gene implicated in ductal carcinoma in situ, lung non-small cell carcinoma, lymphoma, and renal cell carcinoma. Orthologous to human RELA (RELA proto-oncogene, NF-kB subunit). Protein function: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and 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-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain- containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric RELA-NFKB1 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. The NF-kappa-B heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function as transcriptional activators. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I- kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The inhibitory effect of I- kappa-B on NF-kappa-B through retention in the cytoplasm is exerted primarily through the interaction with RELA. RELA shows a weak DNA- binding site which could contribute directly to DNA binding in the NF- kappa-B complex. Beside its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression (PubMed:29813070). Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells. The NF-kappa-B homodimeric RELA- RELA complex appears to be involved in invasin-mediated activation of IL-8 expression. [The UniProt Consortium]