NFKB1

NFKB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1MDI, 1MDJ, 1MDK, 1NFI, 1SVC, 2DBF, 2O61, 3GUT
Identifiers
Aliases	NFKB1 , EBP-1, KBF1, NF-kB1, NF-kappa-B, NF-kappaB, NFKB-p105, NFKB-p50, NFkappaB, p105, p50, CVID12, nuclear factor kappa B subunit 1, NF-kappa-B1, NF-kB, NF-kappabeta
External IDs	OMIM: 164011 MGI: 97312 HomoloGene: 2971 GeneCards: NFKB1
Gene location (Human) Chr. Chromosome 4 (human) [1] Band 4q24 Start 102,501,331 bp [1] End 102,617,302 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3 G3|3 62.82 cM Start 135,290,416 bp [2] End 135,397,308 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon monocyte appendix gallbladder bone marrow cells rectum middle frontal gyrus blood lymph node upper lobe of left lung Top expressed in spleen thymus lymph node lip right lung saccule bone marrow corneal stroma left lung otic placode More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA-binding transcription factor activity RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor binding DNA-binding transcription activator activity, RNA polymerase II-specific DNA-binding transcription repressor activity, RNA polymerase II-specific RNA polymerase II cis-regulatory region sequence-specific DNA binding protein homodimerization activity chromatin binding protein binding DNA binding sequence-specific DNA binding actinin binding identical protein binding transcription cis-regulatory region binding protein heterodimerization activity DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component cytoplasm mitochondrion nucleus I-kappaB/NF-kappaB complex nucleoplasm extracellular region cytosol secretory granule lumen specific granule lumen Biological process cellular response to interleukin-6 positive regulation of canonical Wnt signaling pathway regulation of transcription by RNA polymerase II transcription by RNA polymerase II negative regulation of vitamin D biosynthetic process Fc-epsilon receptor signaling pathway cellular response to mechanical stimulus NIK/NF-kappaB signaling stress-activated MAPK cascade negative regulation of inflammatory response apoptotic process response to muscle stretch regulation of transcription, DNA-templated stimulatory C-type lectin receptor signaling pathway transcription, DNA-templated positive regulation of transcription, DNA-templated negative regulation of calcidiol 1-monooxygenase activity positive regulation of hyaluronan biosynthetic process membrane protein intracellular domain proteolysis inflammatory response I-kappaB kinase/NF-kappaB signaling positive regulation of miRNA metabolic process cellular response to nicotine negative regulation of transcription by RNA polymerase II positive regulation of macrophage derived foam cell differentiation positive regulation of NF-kappaB transcription factor activity negative regulation of cholesterol transport negative regulation of transcription, DNA-templated negative regulation of cytokine production positive regulation of lipid storage cellular response to dsRNA T cell receptor signaling pathway positive regulation of type I interferon production positive regulation of transcription by RNA polymerase II signal transduction cellular response to lipopolysaccharide cellular response to interleukin-1 innate immune response negative regulation of apoptotic process negative regulation of gene expression neutrophil degranulation cellular response to tumor necrosis factor cellular response to angiotensin interleukin-1-mediated signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4790 18033 Ensembl ENSG00000109320 ENSMUSG00000028163 UniProt P19838 P25799 RefSeq (mRNA) NM_001165412 NM_003998 NM_001319226 NM_001382625 NM_001382626 NM_001382627 NM_001382628 NM_008689 RefSeq (protein) NP_001158884 NP_001306155 NP_003989 NP_001369554 NP_001369555 NP_001369556 NP_001369557 NP_001158884.1 NP_001306155.1 NP_032715 Location (UCSC) Chr 4: 102.5 – 102.62 Mb Chr 3: 135.29 – 135.4 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Nuclear factor NF-kappa-B p105 subunit is a protein that in humans is encoded by the NFKB1 gene. ^[5]

This gene encodes a 105 kD protein which can undergo cotranslational processing by the 26S proteasome to produce a 50 kD protein. The 105 kD protein is a Rel protein-specific transcription inhibitor and the 50 kD protein is a DNA binding subunit of the NF-kappaB (NF-κB) protein complex. NF-κB is a transcription factor that is activated by various intra- and extra-cellular stimuli such as cytokines, oxidant-free radicals, ultraviolet irradiation, and bacterial or viral products. Activated NF-κB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions; over 200 known genes are targets of NF-κB in various cell types, under specific conditions. Inappropriate activation of NF-κB has been associated with a number of inflammatory diseases while persistent inhibition of NF-κB leads to inappropriate immune cell development or delayed cell growth. ^[6]

Model organisms

Nfkb1 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Normal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Abnormal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal [7]
Clinical chemistry	Abnormal [8]
Plasma immunoglobulins	Abnormal
Haematology	Abnormal [9]
Peripheral blood lymphocytes	Abnormal [10]
Micronucleus test	Normal
Heart weight	Normal
Tail epidermis wholemount	Normal
Skin Histopathology	Normal
Brain histopathology	Normal
Salmonella infection	Abnormal [11]
All tests and analysis from [12] [13]

Model organisms have been used in the study of NFKB1 function. A conditional knockout mouse line, called Nfkb1^{tm1a(KOMP)Wtsi [14] [15]} was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists. ^{[16] [17] [18]}

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. ^{[12] [19]} Twenty five tests were carried out on mutant mice and six significant abnormalities were observed. ^[12] Female homozygotes had a decreased respiratory quotient, increased circulating alkaline phosphatase level and increased leukocyte cell number. Male homozygotes showed an increased susceptibility to Salmonella infection, while homozygotes of both sex had decreased IgG1 and decreased regulatory T cell and NK cell numbers. ^[12]

Interactions

NFKB1 has been shown to interact with:

• BCL3, ^{[20] [21] [22]}
• C22orf25,
• HDAC1, ^[23]
• HMGA2 ^[24]
• IKK2, ^{[20] [25]}
• ITGB3BP, ^[26]
• IκBα, ^{[27] [28]}
• LYL1, ^[29]
• MAP3K7IP2, ^[30]
• MAP3K8, ^{[31] [32]}
• MEN1, ^[33]
• NFKB2, ^[31]
• NFKBIE, ^[34]
• NOTCH1, ^{[35] [36]}
• Nuclear receptor coactivator 1, ^{[37] [38]}
• RELA, ^{[31] [39]}
• RELB, ^[31]
• STAT3, ^[40]
• STAT6, ^[41] and
• TSC22D3. ^[42]

References

1. GRCh38: Ensembl release 89: ENSG00000109320 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028163 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Meyer R, Hatada EN, Hohmann HP, Haiker M, Bartsch C, Röthlisberger U, Lahm HW, Schlaeger EJ, van Loon AP, Scheidereit C (March 1991). "Cloning of the DNA-binding subunit of human nuclear factor kappa B: the level of its mRNA is strongly regulated by phorbol ester or tumor necrosis factor alpha". Proc Natl Acad Sci U S A. 88 (3): 966–70. Bibcode:1991PNAS...88..966M. doi: 10.1073/pnas.88.3.966 . PMC   50935 . PMID   1992489.
6. "Entrez Gene: NF-κB nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 (p105)".
7. "Eye morphology data for Nfkb1". Wellcome Trust Sanger Institute.
8. "Clinical chemistry data for Nfkb1". Wellcome Trust Sanger Institute.
9. "Haematology data for Nfkb1". Wellcome Trust Sanger Institute.
10. "Peripheral blood lymphocytes data for Nfkb1". Wellcome Trust Sanger Institute.
11. "Salmonella infection data for Nfkb1". Wellcome Trust Sanger Institute.
12. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. S2CID   85911512.
13. Mouse Resources Portal, Wellcome Trust Sanger Institute.
14. "International Knockout Mouse Consortium".
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22. Naumann M, Wulczyn FG, Scheidereit C (January 1993). "The NF-kappa B precursor p105 and the proto-oncogene product Bcl-3 are I kappa B molecules and control nuclear translocation of NF-kappa B". EMBO J. 12 (1): 213–22. doi:10.1002/j.1460-2075.1993.tb05647.x. PMC   413194 . PMID   8428580.
23. Zhong H, May MJ, Jimi E, Ghosh S (March 2002). "The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1". Mol. Cell. 9 (3): 625–36. doi: 10.1016/s1097-2765(02)00477-x . PMID   11931769.
24. Noro B, Licheri B, Sgarra R, Rustighi A, Tessari MA, Chau KY, Ono SJ, Giancotti V, Manfioletti G (April 2003). "Molecular dissection of the architectural transcription factor HMGA2". Biochemistry. 42 (15): 4569–77. doi:10.1021/bi026605k. PMID   12693954. S2CID   39605320.
25. Heissmeyer V, Krappmann D, Hatada EN, Scheidereit C (February 2001). "Shared pathways of IkappaB kinase-induced SCF(betaTrCP)-mediated ubiquitination and degradation for the NF-kappaB precursor p105 and IkappaBalpha". Mol. Cell. Biol. 21 (4): 1024–35. doi:10.1128/MCB.21.4.1024-1035.2001. PMC   99557 . PMID   11158290.
26. Besta F, Massberg S, Brand K, Müller E, Page S, Grüner S, Lorenz M, Sadoul K, Kolanus W, Lengyel E, Gawaz M (October 2002). "Role of beta(3)-endonexin in the regulation of NF-kappaB-dependent expression of urokinase-type plasminogen activator receptor". J. Cell Sci. 115 (Pt 20): 3879–88. doi: 10.1242/jcs.00081 . PMID   12244126.
27. Hay DC, Kemp GD, Dargemont C, Hay RT (May 2001). "Interaction between hnRNPA1 and IkappaBalpha is required for maximal activation of NF-kappaB-dependent transcription". Mol. Cell. Biol. 21 (10): 3482–90. doi:10.1128/MCB.21.10.3482-3490.2001. PMC   100270 . PMID   11313474.
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29. Ferrier R, Nougarede R, Doucet S, Kahn-Perles B, Imbert J, Mathieu-Mahul D (January 1999). "Physical interaction of the bHLH LYL1 protein and NF-kappaB1 p105". Oncogene. 18 (4): 995–1005. doi: 10.1038/sj.onc.1202374 . PMID   10023675.
30. Baek SH, Ohgi KA, Rose DW, Koo EH, Glass CK, Rosenfeld MG (July 2002). "Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein". Cell. 110 (1): 55–67. doi: 10.1016/S0092-8674(02)00809-7 . PMID   12150997. S2CID   17679498.
31. 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 (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID   14743216. S2CID   11683986.
32. Belich MP, Salmerón A, Johnston LH, Ley SC (January 1999). "TPL-2 kinase regulates the proteolysis of the NF-kappaB-inhibitory protein NF-kappaB1 p105". Nature. 397 (6717): 363–8. Bibcode:1999Natur.397..363B. doi:10.1038/16946. PMID   9950430. S2CID   4391108.
33. Heppner C, Bilimoria KY, Agarwal SK, Kester M, Whitty LJ, Guru SC, Chandrasekharappa SC, Collins FS, Spiegel AM, Marx SJ, Burns AL (August 2001). "The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation". Oncogene. 20 (36): 4917–25. doi: 10.1038/sj.onc.1204529 . PMID   11526476.
34. Li Z, Nabel GJ (October 1997). "A new member of the I kappaB protein family, I kappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription". Mol. Cell. Biol. 17 (10): 6184–90. doi:10.1128/mcb.17.10.6184. PMC   232469 . PMID   9315679.
35. Guan E, Wang J, Laborda J, Norcross M, Baeuerle PA, Hoffman T (May 1996). "T cell leukemia-associated human Notch/translocation-associated Notch homologue has I kappa B-like activity and physically interacts with nuclear factor-kappa B proteins in T cells". J. Exp. Med. 183 (5): 2025–32. doi:10.1084/jem.183.5.2025. PMC   2192574 . PMID   8642313.
36. Wang J, Shelly L, Miele L, Boykins R, Norcross MA, Guan E (July 2001). "Human Notch-1 inhibits NF-kappa B activity in the nucleus through a direct interaction involving a novel domain". J. Immunol. 167 (1): 289–95. doi: 10.4049/jimmunol.167.1.289 . PMID   11418662.
37. Lee SK, Na SY, Jung SY, Choi JE, Jhun BH, Cheong J, Meltzer PS, Lee YC, Lee JW (June 2000). "Activating protein-1, nuclear factor-kappaB, and serum response factor as novel target molecules of the cancer-amplified transcription coactivator ASC-2". Mol. Endocrinol. 14 (6): 915–25. doi: 10.1210/mend.14.6.0471 . PMID   10847592.
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39. Palvimo JJ, Reinikainen P, Ikonen T, Kallio PJ, Moilanen A, Jänne OA (September 1996). "Mutual transcriptional interference between RelA and androgen receptor". J. Biol. Chem. 271 (39): 24151–6. doi: 10.1074/jbc.271.39.24151 . PMID   8798655.
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42. Ayroldi E, Migliorati G, Bruscoli S, Marchetti C, Zollo O, Cannarile L, D'Adamio F, Riccardi C (August 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

• Baldwin AS (1996). "The NF-kappa B and I kappa B proteins: new discoveries and insights". Annu. Rev. Immunol. 14: 649–83. doi:10.1146/annurev.immunol.14.1.649. PMID   8717528.
• Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease". Folia Biol. (Praha). 42 (5): 227–30. doi:10.1007/BF02818986. PMID   8997639. S2CID   7617882.
• Chen F, Castranova V, Shi X, Demers LM (1999). "New insights into the role of nuclear factor-kappaB, a ubiquitous transcription factor in the initiation of diseases". Clin. Chem. 45 (1): 7–17. doi: 10.1093/clinchem/45.1.7 . PMID   9895331.
• Bottex-Gauthier C, Pollet S, Favier A, Vidal DR (2002). "[The Rel/NF-kappa-B transcription factors: complex role in cell regulation]". Pathol. Biol. 50 (3): 204–11. doi:10.1016/s0369-8114(02)00289-4. PMID   11980335.
• Garg A, Aggarwal BB (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.
• Sun Z, Andersson R (2003). "NF-kappaB activation and inhibition: a review". Shock. 18 (2): 99–106. doi: 10.1097/00024382-200208000-00001 . PMID   12166787.
• Mercurio AM (2003). "Invasive skin carcinoma--Ras and alpha6beta4 integrin lead the way". Cancer Cell. 3 (3): 201–2. doi: 10.1016/S1535-6108(03)00049-7 . PMID   12676577.
• Sun SC, Xiao G (2004). "Deregulation of NF-kappaB and its upstream kinases in cancer". Cancer Metastasis Rev. 22 (4): 405–22. doi:10.1023/A:1023733231406. PMID   12884915. S2CID   44227245.
• Kucharczak J, Simmons MJ, Fan Y, Gélinas C (2004). "To be, or not to be: NF-kappaB is the answer--role of Rel/NF-kappaB in the regulation of apoptosis". Oncogene. 22 (56): 8961–82. doi: 10.1038/sj.onc.1207230 . PMID   14663476.
• Suh J, Rabson AB (2004). "NF-kappaB activation in human prostate cancer: important mediator or epiphenomenon?". J. Cell. Biochem. 91 (1): 100–17. doi:10.1002/jcb.10729. PMID   14689584. S2CID   84116960.
• Muthumani K, Desai BM, Hwang DS, Choo AY, Laddy DJ, Thieu KP, Rao RG, Weiner DB (2004). "HIV-1 Vpr and anti-inflammatory activity". DNA Cell Biol. 23 (4): 239–47. doi:10.1089/104454904773819824. PMID   15142381.
• Schmitz ML, Mattioli I, Buss H, Kracht M (2005). "NF-kappaB: a multifaceted transcription factor regulated at several levels". ChemBioChem. 5 (10): 1348–58. doi:10.1002/cbic.200400144. PMID   15457532. S2CID   85775279.
• Pise-Masison CA, Brady JN (2006). "Setting the stage for transformation: HTLV-1 Tax inhibition of p53 function". Front. Biosci. 10 (1–3): 919–30. doi:10.2741/1586. PMID   15569630. S2CID   35215552.
• Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection". Curr. HIV Res. 3 (1): 87–94. doi:10.2174/1570162052773013. PMID   15638726.
• Le Rouzic E, Benichou S (2006). "The Vpr protein from HIV-1: distinct roles along the viral life cycle". Retrovirology. 2: 11. doi: 10.1186/1742-4690-2-11 . PMC   554975 . PMID   15725353.
• Zhao RY, Elder RT (2005). "Viral infections and cell cycle G2/M regulation". Cell Res. 15 (3): 143–9. doi: 10.1038/sj.cr.7290279 . PMID   15780175.
• Zhao RY, Bukrinsky M, Elder RT (2005). "HIV-1 viral protein R (Vpr) & host cellular responses". Indian J. Med. Res. 121 (4): 270–86. PMID   15817944.
• Muthumani K, Choo AY, Hwang DS, Ugen KE, Weiner DB (2006). "HIV-1 Vpr: enhancing sensitivity of tumors to apoptosis". Current Drug Delivery. 1 (4): 335–44. doi:10.2174/1567201043334614. PMID   16305395.
• Courtois G, Smahi A (2006). "NF-kappaB-related genetic diseases". Cell Death Differ. 13 (5): 843–51. doi: 10.1038/sj.cdd.4401841 . PMID   16397577.
• Mattson MP, Meffert MK (2006). "Roles for NF-kappaB in nerve cell survival, plasticity, and disease". Cell Death Differ. 13 (5): 852–60. doi: 10.1038/sj.cdd.4401837 . PMID   16397579.
• Schmitz ML, Krappmann D (2006). "Controlling NF-kappaB activation in T cells by costimulatory receptors". Cell Death Differ. 13 (5): 834–42. doi: 10.1038/sj.cdd.4401845 . PMID   16410801.
• Janssens S, Tschopp J (2006). "Signals from within: the DNA-damage-induced NF-kappaB response". Cell Death Differ. 13 (5): 773–84. doi: 10.1038/sj.cdd.4401843 . PMID   16410802.
• Perkins ND, Gilmore TD (2006). "Good cop, bad cop: the different faces of NF-kappaB". Cell Death Differ. 13 (5): 759–72. doi: 10.1038/sj.cdd.4401838 . PMID   16410803.
• Weil R, Israël A (2006). "Deciphering the pathway from the TCR to NF-kappaB". Cell Death Differ. 13 (5): 826–33. doi: 10.1038/sj.cdd.4401856 . PMID   16439988.
• Kim HJ, Hawke N, Baldwin AS (2006). "NF-kappaB and IKK as therapeutic targets in cancer". Cell Death Differ. 13 (5): 738–47. doi: 10.1038/sj.cdd.4401877 . PMID   16485028.
• Braun T, Carvalho G, Fabre C, Grosjean J, Fenaux P, Kroemer G (2006). "Targeting NF-kappaB in hematologic malignancies". Cell Death Differ. 13 (5): 748–58. doi: 10.1038/sj.cdd.4401874 . PMID   16498458.
• Bottero V, Withoff S, Verma IM (2006). "NF-kappaB and the regulation of hematopoiesis". Cell Death Differ. 13 (5): 785–97. doi: 10.1038/sj.cdd.4401888 . PMID   16528384.
• Xiao G (2007). "Autophagy and NF-κB fight for fate". Cytokine Growth Factor Rev. 18 (3–4): 233–43. doi:10.1016/j.cytogfr.2007.04.006. PMC   2810660 . PMID   17485237.

External links

• NFKB1+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• FactorBook NFKB

This article incorporates text from the United States National Library of Medicine, which is in the public domain.