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Protein NFKB2 PDB 1a3q.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases NFKB2, CVID10, H2TF1, LYT-10, LYT10, NF-kB2, p105, p52, p100, p49/p100, nuclear factor kappa B subunit 2
External IDs MGI: 1099800 HomoloGene: 1873 GeneCards: 4791
RNA expression pattern
PBB GE NFKB2 207535 s at tn.png

PBB GE NFKB2 209636 at tn.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)


RefSeq (protein)



Location (UCSC) Chr 10: 102.39 – 102.4 Mb Chr 19: 46.3 – 46.31 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Nuclear factor NF-kappa-B p100 subunit is a protein that in humans is encoded by the NFKB2 gene.[1]


NFKB has been detected in numerous cell types that express cytokines, chemokines, growth factors, cell adhesion molecules, and some acute phase proteins in health and in various disease states. NFKB is activated by a wide variety of stimuli such as cytokines, oxidant-free radicals, inhaled particles, ultraviolet irradiation, and bacterial or viral products. Inappropriate activation of NF-kappa-B has been linked to inflammatory events associated with autoimmune arthritis, asthma, septic shock, lung fibrosis, glomerulonephritis, atherosclerosis, and AIDS. In contrast, complete and persistent inhibition of NF-kappa-B has been linked directly to apoptosis, inappropriate immune cell development, and delayed cell growth. For reviews, see Chen et al. (1999) and Baldwin (1996).[supplied by OMIM][2]

Clinical significance[edit]

Mutation of the NFKB2 gene has been linked to Common variable immunodeficiency (CVID) as the cause of the disease. Other genes might also be responsible. The frequency of NFKB2 mutation in CVID population is yet to be established.[3]


NFKB2 has been shown to interact with:

See also[edit]


  1. ^ Schmid RM, Perkins ND, Duckett CS, Andrews PC, Nabel GJ (Aug 1991). "Cloning of an NF-kappa B subunit which stimulates HIV transcription in synergy with p65". Nature 352 (6337): 733–6. doi:10.1038/352733a0. PMID 1876189. 
  2. ^ "Entrez Gene: NFKB2 nuclear factor of kappa light polypeptide gene enhancer in B-cells 2 (p49/p100)". 
  3. ^ Chen K, Coonrod EM, Kumánovics A, Franks ZF, Durtschi JD, Margraf RL, Wu W, Heikal NM, Augustine NH, Ridge PG, Hill HR, Jorde LB, Weyrich AS, Zimmerman GA, Gundlapalli AV, Bohnsack JF, Voelkerding KV (Nov 2013). "Germline mutations in NFKB2 implicate the noncanonical NF-κB pathway in the pathogenesis of common variable immunodeficiency". American Journal of Human Genetics 93 (5): 812–24. doi:10.1016/j.ajhg.2013.09.009. PMID 24140114. 
  4. ^ a b Thornburg NJ, Pathmanathan R, Raab-Traub N (Dec 2003). "Activation of nuclear factor-kappaB p50 homodimer/Bcl-3 complexes in nasopharyngeal carcinoma". Cancer Research 63 (23): 8293–301. PMID 14678988. 
  5. ^ Bours V, Franzoso G, Azarenko V, Park S, Kanno T, Brown K, Siebenlist U (Mar 1993). "The oncoprotein Bcl-3 directly transactivates through kappa B motifs via association with DNA-binding p50B homodimers". Cell 72 (5): 729–39. doi:10.1016/0092-8674(93)90401-b. PMID 8453667. 
  6. ^ Fong A, Sun SC (Jun 2002). "Genetic evidence for the essential role of beta-transducin repeat-containing protein in the inducible processing of NF-kappa B2/p100". The Journal of Biological Chemistry 277 (25): 22111–4. doi:10.1074/jbc.C200151200. PMID 11994270. 
  7. ^ Vatsyayan J, Qing G, Xiao G, Hu J (Sep 2008). "SUMO1 modification of NF-kappaB2/p100 is essential for stimuli-induced p100 phosphorylation and processing". EMBO Reports 9 (9): 885–90. doi:10.1038/embor.2008.122. PMC 2529344. PMID 18617892. 
  8. ^ a b c d e Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (Feb 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. 
  9. ^ Li Z, Nabel GJ (Oct 1997). "A new member of the I kappaB protein family, I kappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription". Molecular and Cellular Biology 17 (10): 6184–90. doi:10.1128/mcb.17.10.6184. PMC 232469. PMID 9315679. 
  10. ^ a b Scheinman RI, Beg AA, Baldwin AS (Oct 1993). "NF-kappa B p100 (Lyt-10) is a component of H2TF1 and can function as an I kappa B-like molecule". Molecular and Cellular Biology 13 (10): 6089–101. doi:10.1128/mcb.13.10.6089. PMC 364669. PMID 8413211. 
  11. ^ Ayroldi E, Migliorati G, Bruscoli S, Marchetti C, Zollo O, Cannarile L, D'Adamio F, Riccardi C (Aug 2001). "Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappaB". Blood 98 (3): 743–53. doi:10.1182/blood.v98.3.743. PMID 11468175. 

Further reading[edit]

  • Schreck R, Albermann K, Baeuerle PA (1993). "Nuclear factor kappa B: an oxidative stress-responsive transcription factor of eukaryotic cells (a review)". Free Radical Research Communications 17 (4): 221–37. doi:10.3109/10715769209079515. PMID 1473734. 
  • Baldwin AS (1996). "The NF-kappa B and I kappa B proteins: new discoveries and insights". Annual Review of Immunology 14 (1): 649–83. doi:10.1146/annurev.immunol.14.1.649. PMID 8717528. 
  • Chen F, Castranova V, Shi X, Demers LM (Jan 1999). "New insights into the role of nuclear factor-kappaB, a ubiquitous transcription factor in the initiation of diseases". Clinical Chemistry 45 (1): 7–17. PMID 9895331. 
  • Bottex-Gauthier C, Pollet S, Favier A, Vidal DR (Apr 2002). "[The Rel/NF-kappa-B transcription factors: complex role in cell regulation]". Pathologie-Biologie 50 (3): 204–11. doi:10.1016/s0369-8114(02)00289-4. PMID 11980335. 
  • Garg A, Aggarwal BB (Jun 2002). "Nuclear transcription factor-kappaB as a target for cancer drug development". Leukemia 16 (6): 1053–68. doi:10.1038/sj.leu.2402482. PMID 12040437. 

External links[edit]