Biology:NFKB1
 Generic protein structure example |
Nuclear factor NF-kappa-B p105 subunit is a protein that in humans is encoded by the NFKB1 gene.[1]
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.[2]
Interactions
NFKB1 has been shown to interact with:
- BCL3,[3][4][5]
- C22orf25,
- HDAC1,[6]
- HMGA2[7]
- IKK2,[3][8]
- ITGB3BP,[9]
- IκBα,[10][11]
- LYL1,[12]
- MAP3K7IP2,[13]
- MAP3K8,[14][15]
- MEN1,[16]
- NFKB2,[14]
- NFKBIE,[17]
- NOTCH1,[18][19]
- Nuclear receptor coactivator 1,[20][21]
- RELA,[14][22]
- RELB,[14]
- STAT3,[23]
- STAT6,[24] and
- TSC22D3.[25]
References
- ↑ "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. March 1991. doi:10.1073/pnas.88.3.966. PMID 1992489. Bibcode: 1991PNAS...88..966M.
- ↑ "Entrez Gene: NF-κB nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 (p105)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4790.
- ↑ 3.0 3.1 "NF-kappaB p105 is a target of IkappaB kinases and controls signal induction of Bcl-3-p50 complexes". EMBO J. 18 (17): 4766–78. September 1999. doi:10.1093/emboj/18.17.4766. PMID 10469655.
- ↑ "Activation of nuclear factor-kappaB p50 homodimer/Bcl-3 complexes in nasopharyngeal carcinoma". Cancer Res. 63 (23): 8293–301. December 2003. PMID 14678988.
- ↑ "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. January 1993. doi:10.1002/j.1460-2075.1993.tb05647.x. PMID 8428580.
- ↑ "The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1". Mol. Cell 9 (3): 625–36. March 2002. doi:10.1016/s1097-2765(02)00477-x. PMID 11931769.
- ↑ "Molecular dissection of the architectural transcription factor HMGA2". Biochemistry 42 (15): 4569–77. April 2003. doi:10.1021/bi026605k. PMID 12693954.
- ↑ "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. February 2001. doi:10.1128/MCB.21.4.1024-1035.2001. PMID 11158290.
- ↑ "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. October 2002. doi:10.1242/jcs.00081. PMID 12244126.
- ↑ "Interaction between hnRNPA1 and IkappaBalpha is required for maximal activation of NF-kappaB-dependent transcription". Mol. Cell. Biol. 21 (10): 3482–90. May 2001. doi:10.1128/MCB.21.10.3482-3490.2001. PMID 11313474.
- ↑ "Ikappa Balpha functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-kappaB". J. Biol. Chem. 273 (39): 25427–35. September 1998. doi:10.1074/jbc.273.39.25427. PMID 9738011.
- ↑ "Physical interaction of the bHLH LYL1 protein and NF-kappaB1 p105". Oncogene 18 (4): 995–1005. January 1999. doi:10.1038/sj.onc.1202374. PMID 10023675.
- ↑ "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. July 2002. doi:10.1016/S0092-8674(02)00809-7. PMID 12150997.
- ↑ 14.0 14.1 14.2 14.3 "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. February 2004. doi:10.1038/ncb1086. PMID 14743216.
- ↑ "TPL-2 kinase regulates the proteolysis of the NF-kappaB-inhibitory protein NF-kappaB1 p105". Nature 397 (6717): 363–8. January 1999. doi:10.1038/16946. PMID 9950430. Bibcode: 1999Natur.397..363B.
- ↑ "The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation". Oncogene 20 (36): 4917–25. August 2001. doi:10.1038/sj.onc.1204529. PMID 11526476.
- ↑ "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. October 1997. doi:10.1128/mcb.17.10.6184. PMID 9315679.
- ↑ "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. May 1996. doi:10.1084/jem.183.5.2025. PMID 8642313.
- ↑ "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. July 2001. doi:10.4049/jimmunol.167.1.289. PMID 11418662.
- ↑ "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. June 2000. doi:10.1210/mend.14.6.0471. PMID 10847592.
- ↑ "Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappaB-mediated transactivations". J. Biol. Chem. 273 (18): 10831–4. May 1998. doi:10.1074/jbc.273.18.10831. PMID 9556555.
- ↑ "Mutual transcriptional interference between RelA and androgen receptor". J. Biol. Chem. 271 (39): 24151–6. September 1996. doi:10.1074/jbc.271.39.24151. PMID 8798655.
- ↑ "Signal transducers and activators of transcription 3 (STAT3) inhibits transcription of the inducible nitric oxide synthase gene by interacting with nuclear factor kappaB". Biochem. J. 367 (Pt 1): 97–105. October 2002. doi:10.1042/BJ20020588. PMID 12057007.
- ↑ "Interaction of stat6 and NF-kappaB: direct association and synergistic activation of interleukin-4-induced transcription". Mol. Cell. Biol. 18 (6): 3395–404. June 1998. doi:10.1128/mcb.18.6.3395. PMID 9584180.
- ↑ "Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappaB". Blood 98 (3): 743–53. August 2001. doi:10.1182/blood.v98.3.743. PMID 11468175.
Further reading
- "The NF-kappa B and I kappa B proteins: new discoveries and insights". Annu. Rev. Immunol. 14: 649–83. 1996. doi:10.1146/annurev.immunol.14.1.649. PMID 8717528. https://cdr.lib.unc.edu/record/uuid:ac4a905e-d22c-42a3-a3fa-656535b1143a.
- "The cleavage of host cell proteins by HIV-1 protease". Folia Biol. (Praha) 42 (5): 227–30. 1997. doi:10.1007/BF02818986. PMID 8997639.
- "New insights into the role of nuclear factor-kappaB, a ubiquitous transcription factor in the initiation of diseases". Clin. Chem. 45 (1): 7–17. 1999. doi:10.1093/clinchem/45.1.7. PMID 9895331.
- "[The Rel/NF-kappa-B transcription factors: complex role in cell regulation]". Pathol. Biol. 50 (3): 204–11. 2002. doi:10.1016/s0369-8114(02)00289-4. PMID 11980335.
- "Nuclear transcription factor-kappaB as a target for cancer drug development". Leukemia 16 (6): 1053–68. 2002. doi:10.1038/sj.leu.2402482. PMID 12040437.
- "NF-kappaB activation and inhibition: a review". Shock 18 (2): 99–106. 2003. doi:10.1097/00024382-200208000-00001. PMID 12166787.
- "Invasive skin carcinoma--Ras and alpha6beta4 integrin lead the way". Cancer Cell 3 (3): 201–2. 2003. doi:10.1016/S1535-6108(03)00049-7. PMID 12676577.
- "Deregulation of NF-kappaB and its upstream kinases in cancer". Cancer Metastasis Rev. 22 (4): 405–22. 2004. doi:10.1023/A:1023733231406. PMID 12884915.
- "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. 2004. doi:10.1038/sj.onc.1207230. PMID 14663476.
- "NF-kappaB activation in human prostate cancer: important mediator or epiphenomenon?". J. Cell. Biochem. 91 (1): 100–17. 2004. doi:10.1002/jcb.10729. PMID 14689584.
- "HIV-1 Vpr and anti-inflammatory activity". DNA Cell Biol. 23 (4): 239–47. 2004. doi:10.1089/104454904773819824. PMID 15142381.
- "NF-kappaB: a multifaceted transcription factor regulated at several levels". ChemBioChem 5 (10): 1348–58. 2005. doi:10.1002/cbic.200400144. PMID 15457532.
- "Setting the stage for transformation: HTLV-1 Tax inhibition of p53 function". Front. Biosci. 10 (1–3): 919–30. 2006. doi:10.2741/1586. PMID 15569630.
- "Nef: "necessary and enforcing factor" in HIV infection". Curr. HIV Res. 3 (1): 87–94. 2005. doi:10.2174/1570162052773013. PMID 15638726.
- "The Vpr protein from HIV-1: distinct roles along the viral life cycle". Retrovirology 2: 11. 2006. doi:10.1186/1742-4690-2-11. PMID 15725353.
- "Viral infections and cell cycle G2/M regulation". Cell Res. 15 (3): 143–9. 2005. doi:10.1038/sj.cr.7290279. PMID 15780175.
- "HIV-1 viral protein R (Vpr) & host cellular responses". Indian J. Med. Res. 121 (4): 270–86. 2005. PMID 15817944.
- "HIV-1 Vpr: enhancing sensitivity of tumors to apoptosis". Current Drug Delivery 1 (4): 335–44. 2006. doi:10.2174/1567201043334614. PMID 16305395.
- "NF-kappaB-related genetic diseases". Cell Death Differ. 13 (5): 843–51. 2006. doi:10.1038/sj.cdd.4401841. PMID 16397577.
- "Roles for NF-kappaB in nerve cell survival, plasticity, and disease". Cell Death Differ. 13 (5): 852–60. 2006. doi:10.1038/sj.cdd.4401837. PMID 16397579.
- "Controlling NF-kappaB activation in T cells by costimulatory receptors". Cell Death Differ. 13 (5): 834–42. 2006. doi:10.1038/sj.cdd.4401845. PMID 16410801.
- "Signals from within: the DNA-damage-induced NF-kappaB response". Cell Death Differ. 13 (5): 773–84. 2006. doi:10.1038/sj.cdd.4401843. PMID 16410802.
- "Good cop, bad cop: the different faces of NF-kappaB". Cell Death Differ. 13 (5): 759–72. 2006. doi:10.1038/sj.cdd.4401838. PMID 16410803.
- "Deciphering the pathway from the TCR to NF-kappaB". Cell Death Differ. 13 (5): 826–33. 2006. doi:10.1038/sj.cdd.4401856. PMID 16439988.
- "NF-kappaB and IKK as therapeutic targets in cancer". Cell Death Differ. 13 (5): 738–47. 2006. doi:10.1038/sj.cdd.4401877. PMID 16485028.
- "Targeting NF-kappaB in hematologic malignancies". Cell Death Differ. 13 (5): 748–58. 2006. doi:10.1038/sj.cdd.4401874. PMID 16498458.
- "NF-kappaB and the regulation of hematopoiesis". Cell Death Differ. 13 (5): 785–97. 2006. doi:10.1038/sj.cdd.4401888. PMID 16528384.
- "Autophagy and NF-κB fight for fate". Cytokine Growth Factor Rev. 18 (3–4): 233–43. 2007. doi:10.1016/j.cytogfr.2007.04.006. PMID 17485237.
External links
- NFKB1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
- FactorBook NFKB
PDB gallery | |
|---|---|
|
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
 |  |
