NFKB1: Difference between revisions

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{{Infobox_gene}}
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'''Nuclear factor NF-kappa-B p105 subunit''' is a [[protein]] that in humans is encoded by the ''NFKB1'' [[gene]].<ref name="pmid1992489">{{cite journal | vauthors = Meyer R, Hatada EN, Hohmann HP, Haiker M, Bartsch C, Röthlisberger U, Lahm HW, Schlaeger EJ, van Loon AP, Scheidereit C | title = 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 | journal = Proc Natl Acad Sci U S A | volume = 88 | issue = 3 | pages = 966–70 | date = March 1991 | pmid = 1992489 | pmc = 50935 | doi = 10.1073/pnas.88.3.966 }}</ref>
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'''Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 (p105)''', also known as '''NFKB1''', is a human [[gene]].
<!-- This infobox is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NFKB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bfs.
| PDB = {{PDB2|1bfs}}, {{PDB2|1ikn}}, {{PDB2|1le5}}, {{PDB2|1le9}}, {{PDB2|1lei}}, {{PDB2|1nfi}}, {{PDB2|1nfk}}, {{PDB2|1ooa}}, {{PDB2|1svc}}, {{PDB2|1u36}}, {{PDB2|1u3j}}, {{PDB2|1u3y}}, {{PDB2|1u3z}}, {{PDB2|1u41}}, {{PDB2|1u42}}, {{PDB2|1vkx}}, {{PDB2|2dbf}}, {{PDB2|2i9t}}
| Name = Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 (p105)
| HGNCid = 7794
| Symbol = NFKB1
| AltSymbols =; DKFZp686C01211; EBP-1; KBF1; MGC54151; NF-kappa-B; NFKB-p105; NFKB-p50
| OMIM = 164011
| ECnumber = 
| Homologene = 2971
| MGIid = 97312
| GeneAtlas_image1 = PBB_GE_NFKB1_209239_at.png
<!-- The Following entry is a time stamp of the last bot update.  It is typically hidden data -->
| DateOfBotUpdate = 17:29, 11 September 2007 (UTC)
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016566 |text = specific transcriptional repressor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0019733 |text = antibacterial humoral response}} {{GNF_GO|id=GO:0045083 |text = negative regulation of interleukin-12 biosynthetic process}} {{GNF_GO|id=GO:0045892 |text = negative regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4790
    | Hs_Ensembl = ENSG00000109320
    | Hs_RefseqProtein = NP_003989
    | Hs_RefseqmRNA = NM_003998
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 103641518
    | Hs_GenLoc_end = 103757506
    | Hs_Uniprot = P19838
    | Mm_EntrezGene = 18033
    | Mm_Ensembl = ENSMUSG00000028163
    | Mm_RefseqmRNA = NM_008689
    | Mm_RefseqProtein = NP_032715
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 135292997
    | Mm_GenLoc_end = 135605172
    | Mm_Uniprot = P25799
  }}
}}
<!-- This summary is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =  
| summary_text = 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-kappa-B (NFKB) protein complex. NFKB is a transcription regulator that is activated by various intra- and extra-cellular stimuli such as cytokines, oxidant-free radicals, ultraviolet irradiation, and bacterial or viral products. Activated NFKB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions. Inappropriate activation of NFKB has been associated with a number of inflammatory diseases while persistent inhibition of NFKB leads to inappropriate immune cell development or delayed cell growth.<ref>{{cite web | title = Entrez Gene: NFKB1 nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 (p105)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4790| accessdate = }}</ref>
}}


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 [[cytokine]]s, 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.<ref>{{cite web | title = Entrez Gene: NF-κB nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 (p105)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4790| accessdate = }}</ref>


==References==
==Model organisms==
{{reflist|2}}
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" |
==Further reading==
|+ ''Nfkb1'' knockout mouse phenotype
|-
! Characteristic!! Phenotype
|-
| [[Homozygote]] viability || bgcolor="#488ED3"|Normal
|-
| Fertility || bgcolor="#488ED3"|Normal
|-
| Body weight || bgcolor="#488ED3"|Normal
|-
| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal
|-
| Neurological assessment || bgcolor="#488ED3"|Normal
|-
| Grip strength || bgcolor="#488ED3"|Normal
|-
| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal
|-
| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
|-
| [[Indirect calorimetry]] || bgcolor="#C40000"|Abnormal
|-
| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
|-
| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
|-
| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
|-
| [[Radiography]] || bgcolor="#488ED3"|Normal
|-
| Body temperature || bgcolor="#488ED3"|Normal
|-
| Eye morphology || bgcolor="#488ED3"|Normal<ref name="Eye morphology">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAHS/eye-morphology/ |title=Eye morphology data for Nfkb1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Clinical chemistry]] || bgcolor="#C40000"|Abnormal<ref name="Clinical chemistry">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAHS/plasma-chemistry/ |title=Clinical chemistry data for Nfkb1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Blood plasma|Plasma]] [[immunoglobulin]]s || bgcolor="#C40000"|Abnormal
|-
| [[Haematology]] || bgcolor="#C40000"|Abnormal<ref name="Haematology">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAHS/haematology-cbc/ |title=Haematology data for Nfkb1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Peripheral blood lymphocyte]]s || bgcolor="#C40000"|Abnormal<ref name="Peripheral blood lymphocytes">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAHS/peripheral-blood-lymphocytes/ |title=Peripheral blood lymphocytes data for Nfkb1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Micronucleus test]] || bgcolor="#488ED3"|Normal
|-
| Heart weight || bgcolor="#488ED3"|Normal
|-
| Tail epidermis wholemount || bgcolor="#488ED3"|Normal
|-
| Skin Histopathology || bgcolor="#488ED3"|Normal
|-
| Brain histopathology || bgcolor="#488ED3"|Normal
|-
| ''[[Salmonella]]'' infection || bgcolor="#C40000"|Abnormal<ref name="''Salmonella'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAHS/salmonella-challenge/ |title=''Salmonella'' infection data for Nfkb1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal | doi = 10.1111/j.1755-3768.2010.4142.x | title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice | year = 2010 | author = Gerdin AK | journal = Acta Ophthalmologica | volume = 88 | pages =  925–7 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref>
|}
[[Model organism]]s have been used in the study of NFKB1 function. A conditional [[knockout mouse]] line, called ''Nfkb1<sup>tm1a(KOMP)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Nfkb1 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4363738 |title=Mouse Genome Informatics}}</ref> 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.<ref name="pmid21677750">{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–342 | year = 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | year = 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A Mouse for All Reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | year = 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref>


{{refbegin | 2}}
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism. | journal = Genome Biol | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}</ref> Twenty five tests were carried out on [[mutant]] mice and six significant abnormalities were observed.<ref name="mgp_reference" /> 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.<ref name="mgp_reference" />
{{PBB_Further_reading
 
| citations =  
== Interactions ==
*{{cite journal | author=Baldwin AS |title=The NF-kappa B and I kappa B proteins: new discoveries and insights. |journal=Annu. Rev. Immunol. |volume=14 |issue= |pages= 649-83 |year= 1996 |pmid= 8717528 |doi= 10.1146/annurev.immunol.14.1.649 }}
 
*{{cite journal  | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227-30 |year= 1997 |pmid= 8997639 |doi= }}
NFKB1 has been shown to [[Protein-protein interaction|interact]] with:
*{{cite journal  | author=Chen F, Castranova V, Shi X, Demers LM |title=New insights into the role of nuclear factor-kappaB, a ubiquitous transcription factor in the initiation of diseases. |journal=Clin. Chem. |volume=45 |issue= 1 |pages= 7-17 |year= 1999 |pmid= 9895331 |doi=  }}
{{div col|colwidth=20em}}
*{{cite journal | author=Bottex-Gauthier C, Pollet S, Favier A, Vidal DR |title=[The Rel/NF-kappa-B transcription factors: complex role in cell regulation] |journal=Pathol. Biol. |volume=50 |issue= 3 |pages= 204-11 |year= 2002 |pmid= 11980335 |doi=  }}
* [[BCL3]],<ref name = pmid10469655/><ref name = pmid14678988>{{cite journal | vauthors = Thornburg NJ, Pathmanathan R, Raab-Traub N | title = Activation of nuclear factor-kappaB p50 homodimer/Bcl-3 complexes in nasopharyngeal carcinoma | journal = Cancer Res. | volume = 63 | issue = 23 | pages = 8293–301 | date = December 2003 | pmid = 14678988 | doi =  }}</ref><ref name = pmid8428580>{{cite journal | vauthors = Naumann M, Wulczyn FG, Scheidereit C | title = 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 | journal = EMBO J. | volume = 12 | issue = 1 | pages = 213–22 | date = January 1993 | pmid = 8428580 | pmc = 413194 | doi =  }}</ref>
*{{cite journal | author=Garg A, Aggarwal BB |title=Nuclear transcription factor-kappaB as a target for cancer drug development. |journal=Leukemia |volume=16 |issue= 6 |pages= 1053-68 |year= 2002 |pmid= 12040437 |doi= 10.1038/sj.leu.2402482 }}
* [[C22orf25]],
*{{cite journal | author=Sun Z, Andersson R |title=NF-kappaB activation and inhibition: a review. |journal=Shock |volume=18 |issue= 2 |pages= 99-106 |year= 2003 |pmid= 12166787 |doi= }}
* [[HDAC1]],<ref name = pmid11931769>{{cite journal | vauthors = Zhong H, May MJ, Jimi E, Ghosh S | title = The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1 | journal = Mol. Cell | volume = 9 | issue = 3 | pages = 625–36 | date = March 2002 | pmid = 11931769 | doi = 10.1016/s1097-2765(02)00477-x}}</ref>
*{{cite journal | author=Mercurio AM |title=Invasive skin carcinoma--Ras and alpha6beta4 integrin lead the way. |journal=Cancer Cell |volume=3 |issue= 3 |pages= 201-2 |year= 2003 |pmid= 12676577 |doi= }}
* [[HMGA2]]<ref name = pmid12693954>{{cite journal | vauthors = Noro B, Licheri B, Sgarra R, Rustighi A, Tessari MA, Chau KY, Ono SJ, Giancotti V, Manfioletti G | title = Molecular dissection of the architectural transcription factor HMGA2 | journal = Biochemistry | volume = 42 | issue = 15 | pages = 4569–77 | date = April 2003 | pmid = 12693954 | doi = 10.1021/bi026605k }}</ref>
*{{cite journal | author=Sun SC, Xiao G |title=Deregulation of NF-kappaB and its upstream kinases in cancer. |journal=Cancer Metastasis Rev. |volume=22 |issue= 4 |pages= 405-22 |year= 2004 |pmid= 12884915 |doi= }}
* [[IKK2]],<ref name = pmid10469655>{{cite journal | vauthors = Heissmeyer V, Krappmann D, Wulczyn FG, Scheidereit C | title = NF-kappaB p105 is a target of IkappaB kinases and controls signal induction of Bcl-3-p50 complexes | journal = EMBO J. | volume = 18 | issue = 17 | pages = 4766–78 | date = September 1999 | pmid = 10469655 | pmc = 1171549 | doi = 10.1093/emboj/18.17.4766 }}</ref><ref name = pmid11158290>{{cite journal | vauthors = Heissmeyer V, Krappmann D, Hatada EN, Scheidereit C | title = Shared pathways of IkappaB kinase-induced SCF(betaTrCP)-mediated ubiquitination and degradation for the NF-kappaB precursor p105 and IkappaBalpha | journal = Mol. Cell. Biol. | volume = 21 | issue = 4 | pages = 1024–35 | date = February 2001 | pmid = 11158290 | pmc = 99557 | doi = 10.1128/MCB.21.4.1024-1035.2001 }}</ref>
*{{cite journal | author=Kucharczak J, Simmons MJ, Fan Y, Gélinas C |title=To be, or not to be: NF-kappaB is the answer--role of Rel/NF-kappaB in the regulation of apoptosis. |journal=Oncogene |volume=22 |issue= 56 |pages= 8961-82 |year= 2004 |pmid= 14663476 |doi= 10.1038/sj.onc.1207230 }}
* [[ITGB3BP]],<ref name = pmid12244126>{{cite journal | vauthors = Besta F, Massberg S, Brand K, Müller E, Page S, Grüner S, Lorenz M, Sadoul K, Kolanus W, Lengyel E, Gawaz M | title = Role of beta(3)-endonexin in the regulation of NF-kappaB-dependent expression of urokinase-type plasminogen activator receptor | journal = J. Cell Sci. | volume = 115 | issue = Pt 20 | pages = 3879–88 | date = October 2002 | pmid = 12244126 | doi = 10.1242/jcs.00081}}</ref>
*{{cite journal | author=Suh J, Rabson AB |title=NF-kappaB activation in human prostate cancer: important mediator or epiphenomenon? |journal=J. Cell. Biochem. |volume=91 |issue= 1 |pages= 100-17 |year= 2004 |pmid= 14689584 |doi= 10.1002/jcb.10729 }}
* [[IκBα]],<ref name = pmid11313474>{{cite journal | vauthors = Hay DC, Kemp GD, Dargemont C, Hay RT | title = Interaction between hnRNPA1 and IkappaBalpha is required for maximal activation of NF-kappaB-dependent transcription | journal = Mol. Cell. Biol. | volume = 21 | issue = 10 | pages = 3482–90 | date = May 2001 | pmid = 11313474 | pmc = 100270 | doi = 10.1128/MCB.21.10.3482-3490.2001 }}</ref><ref name = pmid9738011>{{cite journal | vauthors = Malek S, Huxford T, Ghosh G | title = Ikappa Balpha functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-kappaB | journal = J. Biol. Chem. | volume = 273 | issue = 39 | pages = 25427–35 | date = September 1998 | pmid = 9738011 | doi = 10.1074/jbc.273.39.25427}}</ref>
*{{cite journal | author=Muthumani K, Desai BM, Hwang DS, ''et al.'' |title=HIV-1 Vpr and anti-inflammatory activity. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 239-47 |year= 2004 |pmid= 15142381 |doi= 10.1089/104454904773819824 }}
* [[LYL1]],<ref name = pmid10023675>{{cite journal | vauthors = Ferrier R, Nougarede R, Doucet S, Kahn-Perles B, Imbert J, Mathieu-Mahul D | title = Physical interaction of the bHLH LYL1 protein and NF-kappaB1 p105 | journal = Oncogene | volume = 18 | issue = 4 | pages = 995–1005 | date = January 1999 | pmid = 10023675 | doi = 10.1038/sj.onc.1202374 }}</ref>
*{{cite journal | author=Schmitz ML, Mattioli I, Buss H, Kracht M |title=NF-kappaB: a multifaceted transcription factor regulated at several levels. |journal=Chembiochem |volume=5 |issue= 10 |pages= 1348-58 |year= 2005 |pmid= 15457532 |doi= 10.1002/cbic.200400144 }}
* [[MAP3K7IP2]],<ref name = pmid12150997>{{cite journal | vauthors = Baek SH, Ohgi KA, Rose DW, Koo EH, Glass CK, Rosenfeld MG | title = Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein | journal = Cell | volume = 110 | issue = 1 | pages = 55–67 | date = July 2002 | pmid = 12150997 | doi =  10.1016/S0092-8674(02)00809-7}}</ref>
*{{cite journal | author=Pise-Masison CA, Brady JN |title=Setting the stage for transformation: HTLV-1 Tax inhibition of p53 function. |journal=Front. Biosci. |volume=10 |issue= |pages= 919-30 |year= 2006 |pmid= 15569630 |doi=  }}
* [[MAP3K8]],<ref name = pmid14743216/><ref name = pmid9950430>{{cite journal | vauthors = Belich MP, Salmerón A, Johnston LH, Ley SC | title = TPL-2 kinase regulates the proteolysis of the NF-kappaB-inhibitory protein NF-kappaB1 p105 | journal = Nature | volume = 397 | issue = 6717 | pages = 363–8 | date = January 1999 | pmid = 9950430 | doi = 10.1038/16946 }}</ref>
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
* [[MEN1]],<ref name = pmid11526476>{{cite journal | vauthors = Heppner C, Bilimoria KY, Agarwal SK, Kester M, Whitty LJ, Guru SC, Chandrasekharappa SC, Collins FS, Spiegel AM, Marx SJ, Burns AL | title = The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation | journal = Oncogene | volume = 20 | issue = 36 | pages = 4917–25 | date = August 2001 | pmid = 11526476 | doi = 10.1038/sj.onc.1204529 }}</ref>
*{{cite journal | author=Le Rouzic E, Benichou S |title=The Vpr protein from HIV-1: distinct roles along the viral life cycle. |journal=Retrovirology |volume=2 |issue= |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11 }}
* [[NFKB2]],<ref name = pmid14743216>{{cite journal | vauthors = 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 | title = A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway | journal = Nat. Cell Biol. | volume = 6 | issue = 2 | pages = 97–105 | date = February 2004 | pmid = 14743216 | doi = 10.1038/ncb1086 }}</ref>
*{{cite journal | author=Zhao RY, Elder RT |title=Viral infections and cell cycle G2/M regulation. |journal=Cell Res. |volume=15 |issue= 3 |pages= 143-9 |year= 2005 |pmid= 15780175 |doi= 10.1038/sj.cr.7290279 }}
* [[NFKBIE]],<ref name = pmid9315679>{{cite journal | vauthors = Li Z, Nabel GJ | title = A new member of the I kappaB protein family, I kappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription | journal = Mol. Cell. Biol. | volume = 17 | issue = 10 | pages = 6184–90 | date = October 1997 | pmid = 9315679 | pmc = 232469 | doi =  10.1128/mcb.17.10.6184}}</ref>
*{{cite journal | author=Zhao RY, Bukrinsky M, Elder RT |title=HIV-1 viral protein R (Vpr) & host cellular responses. |journal=Indian J. Med. Res. |volume=121 |issue= 4 |pages= 270-86 |year= 2005 |pmid= 15817944 |doi=  }}
* [[NOTCH1]],<ref name = pmid8642313>{{cite journal | vauthors = Guan E, Wang J, Laborda J, Norcross M, Baeuerle PA, Hoffman T | title = 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 | journal = J. Exp. Med. | volume = 183 | issue = 5 | pages = 2025–32 | date = May 1996 | pmid = 8642313 | pmc = 2192574 | doi =  10.1084/jem.183.5.2025}}</ref><ref name = pmid11418662>{{cite journal | vauthors = Wang J, Shelly L, Miele L, Boykins R, Norcross MA, Guan E | title = Human Notch-1 inhibits NF-kappa B activity in the nucleus through a direct interaction involving a novel domain | journal = J. Immunol. | volume = 167 | issue = 1 | pages = 289–95 | date = July 2001 | pmid = 11418662 | doi = 10.4049/jimmunol.167.1.289}}</ref>
*{{cite journal | author=Muthumani K, Choo AY, Hwang DS, ''et al.'' |title=HIV-1 Vpr: enhancing sensitivity of tumors to apoptosis. |journal=Current drug delivery |volume=1 |issue= 4 |pages= 335-44 |year= 2006 |pmid= 16305395 |doi=  }}
* [[Nuclear receptor coactivator 1]],<ref name = pmid10847592>{{cite journal | vauthors = Lee SK, Na SY, Jung SY, Choi JE, Jhun BH, Cheong J, Meltzer PS, Lee YC, Lee JW | title = Activating protein-1, nuclear factor-kappaB, and serum response factor as novel target molecules of the cancer-amplified transcription coactivator ASC-2 | journal = Mol. Endocrinol. | volume = 14 | issue = 6 | pages = 915–25 | date = June 2000 | pmid = 10847592 | doi = 10.1210/mend.14.6.0471 }}</ref><ref name = pmid9556555>{{cite journal | vauthors = Na SY, Lee SK, Han SJ, Choi HS, Im SY, Lee JW | title = Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappaB-mediated transactivations | journal = J. Biol. Chem. | volume = 273 | issue = 18 | pages = 10831–4 | date = May 1998 | pmid = 9556555 | doi = 10.1074/jbc.273.18.10831}}</ref>
*{{cite journal | author=Courtois G, Smahi A |title=NF-kappaB-related genetic diseases. |journal=Cell Death Differ. |volume=13 |issue= 5 |pages= 843-51 |year= 2006 |pmid= 16397577 |doi= 10.1038/sj.cdd.4401841 }}
* [[RELA]],<ref name = pmid14743216/><ref name = pmid8798655>{{cite journal | vauthors = Palvimo JJ, Reinikainen P, Ikonen T, Kallio PJ, Moilanen A, Jänne OA | title = Mutual transcriptional interference between RelA and androgen receptor | journal = J. Biol. Chem. | volume = 271 | issue = 39 | pages = 24151–6 | date = September 1996 | pmid = 8798655 | doi = 10.1074/jbc.271.39.24151}}</ref>
*{{cite journal | author=Mattson MP, Meffert MK |title=Roles for NF-kappaB in nerve cell survival, plasticity, and disease. |journal=Cell Death Differ. |volume=13 |issue= 5 |pages= 852-60 |year= 2006 |pmid= 16397579 |doi= 10.1038/sj.cdd.4401837 }}
* [[RELB]],<ref name = pmid14743216/>
*{{cite journal | author=Schmitz ML, Krappmann D |title=Controlling NF-kappaB activation in T cells by costimulatory receptors. |journal=Cell Death Differ. |volume=13 |issue= 5 |pages= 834-42 |year= 2006 |pmid= 16410801 |doi= 10.1038/sj.cdd.4401845 }}
* [[STAT3]],<ref name = pmid12057007>{{cite journal | vauthors = Yu Z, Zhang W, Kone BC | title = Signal transducers and activators of transcription 3 (STAT3) inhibits transcription of the inducible nitric oxide synthase gene by interacting with nuclear factor kappaB | journal = Biochem. J. | volume = 367 | issue = Pt 1 | pages = 97–105 | date = October 2002 | pmid = 12057007 | pmc = 1222853 | doi = 10.1042/BJ20020588 }}</ref>
*{{cite journal | author=Janssens S, Tschopp J |title=Signals from within: the DNA-damage-induced NF-kappaB response. |journal=Cell Death Differ. |volume=13 |issue= 5 |pages= 773-84 |year= 2006 |pmid= 16410802 |doi= 10.1038/sj.cdd.4401843 }}
* [[STAT6]],<ref name = pmid9584180>{{cite journal | vauthors = Shen CH, Stavnezer J | title = Interaction of stat6 and NF-kappaB: direct association and synergistic activation of interleukin-4-induced transcription | journal = Mol. Cell. Biol. | volume = 18 | issue = 6 | pages = 3395–404 | date = June 1998 | pmid = 9584180 | pmc = 108921 | doi = 10.1128/mcb.18.6.3395}}</ref>  and
*{{cite journal | author=Perkins ND, Gilmore TD |title=Good cop, bad cop: the different faces of NF-kappaB. |journal=Cell Death Differ. |volume=13 |issue= 5 |pages= 759-72 |year= 2006 |pmid= 16410803 |doi= 10.1038/sj.cdd.4401838 }}
* [[TSC22D3]].<ref name = pmid11468175>{{cite journal | vauthors = Ayroldi E, Migliorati G, Bruscoli S, Marchetti C, Zollo O, Cannarile L, D'Adamio F, Riccardi C | title = Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappaB | journal = Blood | volume = 98 | issue = 3 | pages = 743–53 | date = August 2001 | pmid = 11468175 | doi = 10.1182/blood.v98.3.743}}</ref>
*{{cite journal | author=Weil R, Israël A |title=Deciphering the pathway from the TCR to NF-kappaB. |journal=Cell Death Differ. |volume=13 |issue= 5 |pages= 826-33 |year= 2006 |pmid= 16439988 |doi= 10.1038/sj.cdd.4401856 }}
{{Div col end}}
*{{cite journal | author=Kim HJ, Hawke N, Baldwin AS |title=NF-kappaB and IKK as therapeutic targets in cancer. |journal=Cell Death Differ. |volume=13 |issue= 5 |pages= 738-47 |year= 2006 |pmid= 16485028 |doi= 10.1038/sj.cdd.4401877 }}
{{Clear}}
*{{cite journal  | author=Braun T, Carvalho G, Fabre C, ''et al.'' |title=Targeting NF-kappaB in hematologic malignancies. |journal=Cell Death Differ. |volume=13 |issue= 5 |pages= 748-58 |year= 2006 |pmid= 16498458 |doi= 10.1038/sj.cdd.4401874 }}
 
*{{cite journal | author=Bottero V, Withoff S, Verma IM |title=NF-kappaB and the regulation of hematopoiesis. |journal=Cell Death Differ. |volume=13 |issue= 5 |pages= 785-97 |year= 2006 |pmid= 16528384 |doi= 10.1038/sj.cdd.4401888 }}
== References ==
*{{cite journal  | author=Xiao G |title=Autophagy and NF-kappaB: fight for fate. |journal=Cytokine Growth Factor Rev. |volume=18 |issue= 3-4 |pages= 233-43 |year= 2007 |pmid= 17485237 |doi= 10.1016/j.cytogfr.2007.04.006 }}
{{Reflist|35em}}
}}
 
== Further reading ==
{{refbegin|35em}}
* {{cite journal | vauthors = Baldwin AS | title = The NF-kappa B and I kappa B proteins: new discoveries and insights | journal = Annu. Rev. Immunol. | volume = 14 | issue =  | pages = 649–83 | year = 1996 | pmid = 8717528 | doi = 10.1146/annurev.immunol.14.1.649 }}
* {{cite journal | vauthors = Snásel J, Pichová I | title = The cleavage of host cell proteins by HIV-1 protease | journal = Folia Biol. (Praha) | volume = 42 | issue = 5 | pages = 227–30 | year = 1997 | pmid = 8997639 | doi = 10.1007/BF02818986 }}
* {{cite journal | vauthors = Chen F, Castranova V, Shi X, Demers LM | title = New insights into the role of nuclear factor-kappaB, a ubiquitous transcription factor in the initiation of diseases | journal = Clin. Chem. | volume = 45 | issue = 1 | pages = 7–17 | year = 1999 | pmid = 9895331 | doi =  }}
* {{cite journal | vauthors = Bottex-Gauthier C, Pollet S, Favier A, Vidal DR | title = [The Rel/NF-kappa-B transcription factors: complex role in cell regulation] | journal = Pathol. Biol. | volume = 50 | issue = 3 | pages = 204–11 | year = 2002 | pmid = 11980335 | doi = 10.1016/s0369-8114(02)00289-4 }}
* {{cite journal | vauthors = Garg A, Aggarwal BB | title = Nuclear transcription factor-kappaB as a target for cancer drug development | journal = Leukemia | volume = 16 | issue = 6 | pages = 1053–68 | year = 2002 | pmid = 12040437 | doi = 10.1038/sj.leu.2402482 }}
* {{cite journal | vauthors = Sun Z, Andersson R | title = NF-kappaB activation and inhibition: a review | journal = Shock | volume = 18 | issue = 2 | pages = 99–106 | year = 2003 | pmid = 12166787 | doi = 10.1097/00024382-200208000-00001 }}
* {{cite journal | vauthors = Mercurio AM | title = Invasive skin carcinoma--Ras and alpha6beta4 integrin lead the way | journal = Cancer Cell | volume = 3 | issue = 3 | pages = 201–2 | year = 2003 | pmid = 12676577 | doi = 10.1016/S1535-6108(03)00049-7 }}
* {{cite journal | vauthors = Sun SC, Xiao G | title = Deregulation of NF-kappaB and its upstream kinases in cancer | journal = Cancer Metastasis Rev. | volume = 22 | issue = 4 | pages = 405–22 | year = 2004 | pmid = 12884915 | doi = 10.1023/A:1023733231406 }}
* {{cite journal | vauthors = Kucharczak J, Simmons MJ, Fan Y, Gélinas C | title = To be, or not to be: NF-kappaB is the answer--role of Rel/NF-kappaB in the regulation of apoptosis | journal = Oncogene | volume = 22 | issue = 56 | pages = 8961–82 | year = 2004 | pmid = 14663476 | doi = 10.1038/sj.onc.1207230 }}
* {{cite journal | vauthors = Suh J, Rabson AB | title = NF-kappaB activation in human prostate cancer: important mediator or epiphenomenon? | journal = J. Cell. Biochem. | volume = 91 | issue = 1 | pages = 100–17 | year = 2004 | pmid = 14689584 | doi = 10.1002/jcb.10729 }}
* {{cite journal | vauthors = Muthumani K, Desai BM, Hwang DS, Choo AY, Laddy DJ, Thieu KP, Rao RG, Weiner DB | title = HIV-1 Vpr and anti-inflammatory activity | journal = DNA Cell Biol. | volume = 23 | issue = 4 | pages = 239–47 | year = 2004 | pmid = 15142381 | doi = 10.1089/104454904773819824 }}
* {{cite journal | vauthors = Schmitz ML, Mattioli I, Buss H, Kracht M | title = NF-kappaB: a multifaceted transcription factor regulated at several levels | journal = Chembiochem | volume = 5 | issue = 10 | pages = 1348–58 | year = 2005 | pmid = 15457532 | doi = 10.1002/cbic.200400144 }}
* {{cite journal | vauthors = Pise-Masison CA, Brady JN | title = Setting the stage for transformation: HTLV-1 Tax inhibition of p53 function | journal = Front. Biosci. | volume = 10 | issue =  | pages = 919–30 | year = 2006 | pmid = 15569630 | doi = 10.2741/1586 }}
* {{cite journal | vauthors = Joseph AM, Kumar M, Mitra D | title = Nef: "necessary and enforcing factor" in HIV infection | journal = Curr. HIV Res. | volume = 3 | issue = 1 | pages = 87–94 | year = 2005 | pmid = 15638726 | doi = 10.2174/1570162052773013 }}
* {{cite journal | vauthors = Le Rouzic E, Benichou S | title = The Vpr protein from HIV-1: distinct roles along the viral life cycle | journal = Retrovirology | volume = 2 | issue =  | pages = 11 | year = 2006 | pmid = 15725353 | pmc = 554975 | doi = 10.1186/1742-4690-2-11 }}
* {{cite journal | vauthors = Zhao RY, Elder RT | title = Viral infections and cell cycle G2/M regulation | journal = Cell Res. | volume = 15 | issue = 3 | pages = 143–9 | year = 2005 | pmid = 15780175 | doi = 10.1038/sj.cr.7290279 }}
* {{cite journal | vauthors = Zhao RY, Bukrinsky M, Elder RT | title = HIV-1 viral protein R (Vpr) & host cellular responses | journal = Indian J. Med. Res. | volume = 121 | issue = 4 | pages = 270–86 | year = 2005 | pmid = 15817944 | doi =  }}
* {{cite journal | vauthors = Muthumani K, Choo AY, Hwang DS, Ugen KE, Weiner DB | title = HIV-1 Vpr: enhancing sensitivity of tumors to apoptosis | journal = Current drug delivery | volume = 1 | issue = 4 | pages = 335–44 | year = 2006 | pmid = 16305395 | doi = 10.2174/1567201043334614 }}
* {{cite journal | vauthors = Courtois G, Smahi A | title = NF-kappaB-related genetic diseases | journal = Cell Death Differ. | volume = 13 | issue = 5 | pages = 843–51 | year = 2006 | pmid = 16397577 | doi = 10.1038/sj.cdd.4401841 }}
* {{cite journal | vauthors = Mattson MP, Meffert MK | title = Roles for NF-kappaB in nerve cell survival, plasticity, and disease | journal = Cell Death Differ. | volume = 13 | issue = 5 | pages = 852–60 | year = 2006 | pmid = 16397579 | doi = 10.1038/sj.cdd.4401837 }}
* {{cite journal | vauthors = Schmitz ML, Krappmann D | title = Controlling NF-kappaB activation in T cells by costimulatory receptors | journal = Cell Death Differ. | volume = 13 | issue = 5 | pages = 834–42 | year = 2006 | pmid = 16410801 | doi = 10.1038/sj.cdd.4401845 }}
* {{cite journal | vauthors = Janssens S, Tschopp J | title = Signals from within: the DNA-damage-induced NF-kappaB response | journal = Cell Death Differ. | volume = 13 | issue = 5 | pages = 773–84 | year = 2006 | pmid = 16410802 | doi = 10.1038/sj.cdd.4401843 }}
* {{cite journal | vauthors = Perkins ND, Gilmore TD | title = Good cop, bad cop: the different faces of NF-kappaB | journal = Cell Death Differ. | volume = 13 | issue = 5 | pages = 759–72 | year = 2006 | pmid = 16410803 | doi = 10.1038/sj.cdd.4401838 }}
* {{cite journal | vauthors = Weil R, Israël A | title = Deciphering the pathway from the TCR to NF-kappaB | journal = Cell Death Differ. | volume = 13 | issue = 5 | pages = 826–33 | year = 2006 | pmid = 16439988 | doi = 10.1038/sj.cdd.4401856 }}
* {{cite journal | vauthors = Kim HJ, Hawke N, Baldwin AS | title = NF-kappaB and IKK as therapeutic targets in cancer | journal = Cell Death Differ. | volume = 13 | issue = 5 | pages = 738–47 | year = 2006 | pmid = 16485028 | doi = 10.1038/sj.cdd.4401877 }}
* {{cite journal | vauthors = Braun T, Carvalho G, Fabre C, Grosjean J, Fenaux P, Kroemer G | title = Targeting NF-kappaB in hematologic malignancies | journal = Cell Death Differ. | volume = 13 | issue = 5 | pages = 748–58 | year = 2006 | pmid = 16498458 | doi = 10.1038/sj.cdd.4401874 }}
* {{cite journal | vauthors = Bottero V, Withoff S, Verma IM | title = NF-kappaB and the regulation of hematopoiesis | journal = Cell Death Differ. | volume = 13 | issue = 5 | pages = 785–97 | year = 2006 | pmid = 16528384 | doi = 10.1038/sj.cdd.4401888 }}
* {{cite journal | vauthors = Xiao G | title = Autophagy and NF-κB fight for fate | journal = Cytokine Growth Factor Rev. | volume = 18 | issue = 3–4 | pages = 233–43 | year = 2007 | pmid = 17485237 | pmc = 2810660 | doi = 10.1016/j.cytogfr.2007.04.006 }}
{{refend}}
{{refend}}


{{Protein-stub}}
== External links ==
{{WikiDoc Sources}}
* {{MeshName|NFKB1+protein,+human}}
* {{FactorBook|NFKB}}
 
{{PDB Gallery|geneid=4790}}
{{Transcription factors|g4}}
{{NLM content}}
 
[[Category:Transcription factors]]
[[Category:Genes mutated in mice]]

Latest revision as of 20:26, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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RefSeq (mRNA)

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View/Edit Human

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]

Model organisms

Model organisms have been used in the study of NFKB1 function. A conditional knockout mouse line, called Nfkb1tm1a(KOMP)Wtsi[10][11] 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.[12][13][14]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[8][15] Twenty five tests were carried out on mutant mice and six significant abnormalities were observed.[8] 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.[8]

Interactions

NFKB1 has been shown to interact with:

References

  1. ↑ 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. doi:10.1073/pnas.88.3.966. PMC 50935. PMID 1992489.
  2. ↑ "Entrez Gene: NF-κB nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 (p105)".
  3. ↑ "Eye morphology data for Nfkb1". Wellcome Trust Sanger Institute.
  4. ↑ "Clinical chemistry data for Nfkb1". Wellcome Trust Sanger Institute.
  5. ↑ "Haematology data for Nfkb1". Wellcome Trust Sanger Institute.
  6. ↑ "Peripheral blood lymphocytes data for Nfkb1". Wellcome Trust Sanger Institute.
  7. ↑ "Salmonella infection data for Nfkb1". Wellcome Trust Sanger Institute.
  8. ↑ 8.0 8.1 8.2 8.3 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.
  9. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  10. ↑ "International Knockout Mouse Consortium".
  11. ↑ "Mouse Genome Informatics".
  12. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  13. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  14. ↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  15. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  16. ↑ 16.0 16.1 Heissmeyer 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.
  17. ↑ 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.
  18. ↑ 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. PMC 413194. PMID 8428580.
  19. ↑ 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.
  20. ↑ 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.
  21. ↑ 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.
  22. ↑ 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.
  23. ↑ 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.
  24. ↑ 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.
  25. ↑ 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.
  26. ↑ 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.
  27. ↑ 27.0 27.1 27.2 27.3 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.
  28. ↑ 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. doi:10.1038/16946. PMID 9950430.
  29. ↑ 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.
  30. ↑ 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.
  31. ↑ 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.
  32. ↑ 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.
  33. ↑ 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.
  34. ↑ 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.
  35. ↑ 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.
  36. ↑ 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.
  37. ↑ 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.
  38. ↑ 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

External links

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

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