Phospho-NF-kB p65 (S529) Recombinant Rabbit Monoclonal Antibody [SP07-00] - BSA and Azide free

Function

Proteins encoded by the v-Rel viral oncogene and its cellular homolog, c-Rel, are members of a family of transcription factors that include the two subunits of the transcription factor NκB (p50 and p65) and the Drosophila maternal morphogen, dorsal. Both proteins specifically bind to DNA sequences that are the same or slight variations of the 10 bp κB sequence in the immunoglobulin κ light chain enhancer. This same sequence is also present in a number of other cellular and viral enhancers. The DNA binding activity of NFκB is activated and NFκB is subsequently transported from the cytoplasm to the nucleus in cells exposed to mitogens or growth factors. cDNAs encoding precursors for two distinct proteins of the same size have been described, designated p105 and p100. The p105 precursor contains p50 at its N-terminus and a C-terminal region that when expressed as a separate molecule, designated pdI, binds to p50 and regulates its activity.

Background References

1. Yang K et al. Effect of PLCe gene silencing on inhibiting the cancerous transformation of ulcerative colitis. Exp Ther Med 12:422-426 (2016).

2. Jeon M et al. Elevated IL-1 expression induces invasiveness of triple negative breast cancer cells and is suppressed by zerumbone. Chem Biol Interact 258:126-33 (2016).

Post-translational Modification

Ubiquitinated by RNF182, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response.; Monomethylated at Lys-310 by SETD6. Monomethylation at Lys-310 is recognized by the ANK repeats of EHMT1 and promotes the formation of repressed chromatin at target genes, leading to down-regulation of NF-kappa-B transcription factor activity. Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes (By similarity).; Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity (By similarity). Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities.; Reversibly acetylated; the acetylation seems to be mediated by CBP, the deacetylation by HDAC3 and SIRT2. Acetylation at Lys-122 enhances DNA binding and impairs association with NFKBIA. Acetylation at Lys-310 is required for full transcriptional activity in the absence of effects on DNA binding and NFKBIA association. Acetylation at Lys-310 promotes interaction with BRD4. Acetylation can also lower DNA-binding and results in nuclear export. Interaction with BRMS1 promotes deacetylation of Lys-310. Lys-310 is deacetylated by SIRT2.; S-nitrosylation of Cys-38 inactivates the enzyme activity.; Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity.; Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B.; Proteolytically cleaved within a conserved N-terminus region required for base-specific contact with DNA in a CPEN1-mediated manner, and hence inhibits NF-kappa-B transcriptional activity.

Subcellular Location

Nucleus, Cytoplasm.

UNIPROT

SwissProt: Q04206 Human

Synonyms