NF-kappa B p65; nuclear factor NF-kappa-B p65 subunit (RELA, NFKB3)
Jump to navigation
Jump to search
Function
- p65 subunit of NF-kappa B
- component of the NF-kappa-B p65-p50 complex
- component of the NF-kappa-B p65-c-Rel complex
- component of the NF- kappa-B p65-p65 complex
- component of the NF-kappa-B p65-p52 complex
- NF-kappa-B heterodimeric p65-p50 & p65-c-Rel complexes are transcriptional activators
- NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression
- inhibitory effect of I-kappa-B upon NF-kappa-B in the cytoplasm is exerted primarily through interaction with p65
- NF-kappa-B p65 binds to IKB, inhibiting transcriptional activity of NF-kappa B by retaining it in the cytoplasm
- activation of NF-kappa B with translocation to the nucleus appears to require phosphorylation-dependent proteolysis of IKB
- p65 shows a weak DNA-binding site which may contribute to DNA binding in the NF-kappa-B complex
- may interact with ETHE1
- binds AES & TLE1
- interacts with TP53BP2
- binds to & is phosphorylated by the activated form of either RPS6KA4 or RPS6KA5
- interacts with ING4; interaction may be indirect
- interacts with CARM1, USP48 & UNC5CL
- interacts with IRAK1BP1 (putative)
- interacts with IKBNS (putative)
- interacts with NFKBIA
- interacts with GSK3B
- interacts with NFKBIB (putative)
- interacts with NFKBIE
- interacts with NFKBIZ (putative)
- part of a 70-90 kD complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, IKBKAP & MAP3K14
- interacts with HDAC3; HDAC3 mediates the deacetylation of RELA
- interacts with HDAC1; interaction requires non-phosphorylated RELA
- interacts with CBP; interaction requires phosphorylated RELA
- interacts (phosphorylated at Thr-254) with PIN1; interaction inhibits p65 binding to NFKBIA
- interacts with SOCS1
- interacts with UXT
- ubiquitinated, leading to its proteosomal degradation
- degradation is required for termination of NF-kappa-B response
- phosphorylation on Ser-536 stimulates acetylation on Lys-310 & interaction with CBP; the phosphorylated & acetylated forms show enhanced transcriptional activity
- reversibly acetylated; the acetylation seems to be mediated by CBP, the deacetylation by HDAC3
- acetylation at Lys-122 enhances DNA binding & impairs association with NFKBIA
- acetylation at Lys-310 is required for full transcriptional activity in the absence of effects on DNA binding & NFKBIA association
- acetylation can also lower DNA-binding & results in nuclear export
Structure
Compartment
- nucleus, cytoplasm
- nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B)
Alternative splicing
named isoforms=4
More general terms
References
- ↑ Ruben SM, Dillon PJ, Schreck R, Henkel T, Chen CH, Maher M, Baeuerle PA, Rosen CA. Isolation of a rel-related human cDNA that potentially encodes the 65-kD subunit of NF-kappa B. Science. 1991 Oct 4;254(5028):11. PMID: https://www.ncbi.nlm.nih.gov/pubmed/1925549
Ruben SM, Dillon PJ, Schreck R, Henkel T, Chen CH, Maher M, Baeuerle PA, Rosen CA. Isolation of a rel-related human cDNA that potentially encodes the 65-kD subunit of NF-kappa B. Science. 1991 Mar 22;251(5000):1490-3. Erratum in: Science. 1991 Oct 4;254(5028):11. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2006423 - ↑ Brown K, Gerstberger S, Carlson L, Franzoso G, Siebenlist U. Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation. Science. 1995 Mar 10;267(5203):1485-8. PMID: https://www.ncbi.nlm.nih.gov/pubmed/7878466
- ↑ Entrez Gene http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=5970
- ↑ UniProt http://www.uniprot.org/uniprot/Q04206.html
- ↑ Atlas of genetics & cytogenetics in oncology & haematology http://atlasgeneticsoncology.org/genes/RELAID325.html
- ↑ SeattleSNPs http://pga.gs.washington.edu/data/rela/