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NFKB1

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
NFKB1
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

1MDI,1MDJ,1MDK,1NFI,1SVC,2DBF,2O61,3GUT

Identifiers
AliasesNFKB1, 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 IDsOMIM:164011;MGI:97312;HomoloGene:2971;GeneCards:NFKB1;OMA:NFKB1 - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for NFKB1
Genomic location for NFKB1
Band4q24Start102,501,331bp[1]
End102,617,302bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for NFKB1
Genomic location for NFKB1
Band3 G3|3 62.82 cMStart135,290,416bp[2]
End135,397,308bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • cartilage tissue

  • Achilles tendon

  • monocyte

  • appendix

  • epithelium of colon

  • gallbladder

  • bone marrow cells

  • rectum

  • middle frontal gyrus

  • blood
Top expressed in
  • granulocyte

  • spleen

  • thymus

  • lactiferous gland

  • lymph node

  • lip

  • otic vesicle

  • Ileal epithelium

  • right lung

  • gastrula
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
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 MbChr 3: 135.29 – 135.4 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Nuclear factor NF-kappa-B p105 subunit is aprotein that in humans is encoded by theNFKB1gene.[5]

This gene encodes a 105 kDprotein which can undergo cotranslational processing by the 26Sproteasome 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 atranscription factor that is activated by various intra- and extra-cellular stimuli such ascytokines, 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]

Interactions

[edit]

NFKB1 has been shown tointeract with:

References

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  1. ^abcGRCh38: Ensembl release 89: ENSG00000109320Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000028163Ensembl, 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. ^abHeissmeyer V, Krappmann D, Wulczyn FG, Scheidereit C (September 1999)."NF-kappaB p105 is a target of IkappaB kinases and controls signal induction of Bcl-3-p50 complexes".EMBO J.18 (17):4766–78.doi:10.1093/emboj/18.17.4766.PMC 1171549.PMID 10469655.
  8. ^Thornburg NJ, Pathmanathan R, Raab-Traub N (December 2003). "Activation of nuclear factor-kappaB p50 homodimer/Bcl-3 complexes in nasopharyngeal carcinoma".Cancer Res.63 (23):8293–301.PMID 14678988.
  9. ^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.
  10. ^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.
  11. ^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.
  12. ^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.
  13. ^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.
  14. ^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.
  15. ^Malek S, Huxford T, Ghosh G (September 1998)."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.doi:10.1074/jbc.273.39.25427.PMID 9738011.
  16. ^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.
  17. ^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.
  18. ^abcdBouwmeester 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.
  19. ^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.
  20. ^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.
  21. ^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.
  22. ^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.
  23. ^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.
  24. ^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.
  25. ^Na SY, Lee SK, Han SJ, Choi HS, Im SY, Lee JW (May 1998)."Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappaB-mediated transactivations".J. Biol. Chem.273 (18):10831–4.doi:10.1074/jbc.273.18.10831.PMID 9556555.
  26. ^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.
  27. ^Yu Z, Zhang W, Kone BC (October 2002)."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.doi:10.1042/BJ20020588.PMC 1222853.PMID 12057007.
  28. ^Shen CH, Stavnezer J (June 1998)."Interaction of stat6 and NF-kappaB: direct association and synergistic activation of interleukin-4-induced transcription".Mol. Cell. Biol.18 (6):3395–404.doi:10.1128/mcb.18.6.3395.PMC 108921.PMID 9584180.
  29. ^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

[edit]

External links

[edit]
PDB gallery
  • 1bfs: STRUCTURE OF NF-KB P50 HOMODIMER BOUND TO A KB SITE
    1bfs: STRUCTURE OF NF-KB P50 HOMODIMER BOUND TO A KB SITE
  • 1ikn: IKAPPABALPHA/NF-KAPPAB COMPLEX
    1ikn: IKAPPABALPHA/NF-KAPPAB COMPLEX
  • 1le5: Crystal structure of a NF-kB heterodimer bound to an IFNb-kB
    1le5: Crystal structure of a NF-kB heterodimer bound to an IFNb-kB
  • 1le9: Crystal structure of a NF-kB heterodimer bound to the Ig/HIV-kB siti
    1le9: Crystal structure of a NF-kB heterodimer bound to the Ig/HIV-kB siti
  • 1lei: The kB DNA sequence from the HLV-LTR functions as an allosteric regulator of HIV transcription
    1lei: The kB DNA sequence from the HLV-LTR functions as an allosteric regulator of HIV transcription
  • 1nfi: I-KAPPA-B-ALPHA/NF-KAPPA-B COMPLEX
    1nfi: I-KAPPA-B-ALPHA/NF-KAPPA-B COMPLEX
  • 1nfk: STRUCTURE OF THE NUCLEAR FACTOR KAPPA-B (NF-KB) P50 HOMODIMER
    1nfk: STRUCTURE OF THE NUCLEAR FACTOR KAPPA-B (NF-KB) P50 HOMODIMER
  • 1ooa: CRYSTAL STRUCTURE OF NF-kB(p50)2 COMPLEXED TO A HIGH-AFFINITY RNA APTAMER
    1ooa: CRYSTAL STRUCTURE OF NF-kB(p50)2 COMPLEXED TO A HIGH-AFFINITY RNA APTAMER
  • 1svc: NFKB P50 HOMODIMER BOUND TO DNA
    1svc: NFKB P50 HOMODIMER BOUND TO DNA
  • 1u36: Crystal structure of WLAC mutant of dimerisation domain of NF-kB p50 transcription factor
    1u36: Crystal structure of WLAC mutant of dimerisation domain of NF-kB p50 transcription factor
  • 1u3j: Crystal structure of MLAV mutant of dimerisation domain of NF-kB p50 transcription factor
    1u3j: Crystal structure of MLAV mutant of dimerisation domain of NF-kB p50 transcription factor
  • 1u3y: Crystal structure of ILAC mutant of dimerisation domain of NF-kB p50 transcription factor
    1u3y: Crystal structure of ILAC mutant of dimerisation domain of NF-kB p50 transcription factor
  • 1u3z: Crystal structure of MLAC mutant of dimerisation domain of NF-kB p50 transcription factor
    1u3z: Crystal structure of MLAC mutant of dimerisation domain of NF-kB p50 transcription factor
  • 1u41: Crystal structure of YLGV mutant of dimerisation domain of NF-kB p50 transcription factor
    1u41: Crystal structure of YLGV mutant of dimerisation domain of NF-kB p50 transcription factor
  • 1u42: Crystal structure of MLAM mutant of dimerisation domain of NF-kB p50 transcription factor
    1u42: Crystal structure of MLAM mutant of dimerisation domain of NF-kB p50 transcription factor
  • 1vkx: CRYSTAL STRUCTURE OF THE NFKB P50/P65 HETERODIMER COMPLEXED TO THE IMMUNOGLOBULIN KB DNA
    1vkx: CRYSTAL STRUCTURE OF THE NFKB P50/P65 HETERODIMER COMPLEXED TO THE IMMUNOGLOBULIN KB DNA
  • 2dbf: Solution structure of the Death domain in human Nuclear factor NF-kappa-B p105 subunit
    2dbf: Solution structure of the Death domain in human Nuclear factor NF-kappa-B p105 subunit
  • 2i9t: Structure of NF-kB p65-p50 heterodimer bound to PRDII element of B-interferon promoter
    2i9t: Structure of NF-kB p65-p50 heterodimer bound to PRDII element of B-interferon promoter
(1) Basic domains
(1.1) Basicleucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3)bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2)Zinc finger DNA-binding domains
(2.1)Nuclear receptor(Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3.1)Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3)Fork head /winged helix
(3.4)Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4)β-Scaffold factors with minor groove contacts
(4.1)Rel homology region
(4.2)STAT
(4.3) p53-like
(4.4)MADS box
(4.6)TATA-binding proteins
(4.7)High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3)Pocket domain
(0.5)AP-2/EREBP-related factors
(0.6) Miscellaneous

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.

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