Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]

 NFKB1_HUMAN             Reviewed;         968 AA.
P19838; A8K5Y5; B3KVE8; Q68D84; Q86V43; Q8N4X7; Q9NZC0;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
20-JUN-2002, sequence version 2.
27-SEP-2017, entry version 225.
RecName: Full=Nuclear factor NF-kappa-B p105 subunit;
AltName: Full=DNA-binding factor KBF1;
AltName: Full=EBP-1;
AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1;
Contains:
RecName: Full=Nuclear factor NF-kappa-B p50 subunit;
Name=NFKB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
PubMed=2203531; DOI=10.1016/0092-8674(90)90275-J;
Kieran M., Blank V., Logeat F., Vandekerckhove J., Lottspeich F.,
le Bail O., Urban M.B., Kourilsky P., Baeuerle P.A., Israel A.;
"The DNA binding subunit of NF-kappa B is identical to factor KBF1 and
homologous to the rel oncogene product.";
Cell 62:1007-1018(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2234062; DOI=10.1038/348076a0;
Bours V., Villalobos J., Burd P.R., Kelly K., Siebenlist U.;
"Cloning of a mitogen-inducible gene encoding a kappa B DNA-binding
protein with homology to the rel oncogene and to cell-cycle motifs.";
Nature 348:76-80(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
PubMed=1992489; DOI=10.1073/pnas.88.3.966;
Meyer R., Hatada E.N., Hohmann H.-P., Haiker M., Bartsch C.,
Roethlisberger U., Lahm H.-W., Schlaeger E.J., van Loon A.P.G.M.,
Scheidereit C.;
"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. 88:966-970(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8825636; DOI=10.1006/geno.1995.1270;
Heron E., Deloukas P., van Loon A.P.G.M.;
"The complete exon-intron structure of the 156-kb human gene NFKB1,
which encodes the p105 and p50 proteins of transcription factors NF-
kappa B and I kappa B-gamma: implications for NF-kappa B-mediated
signal transduction.";
Genomics 30:493-505(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Chang H.-M., Tsai S.-F.;
"Genome sequencing of the chromosome 4q region implicated in human
hepatocellular carcinoma pathogenesis.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain, and Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Rectum tumor;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-489; VAL-506;
ILE-566; LYS-578; GLN-711 AND THR-901.
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Muscle, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX.
PubMed=1740106;
Hansen S.K., Nerlov C., Zabel U., Verde P., Johnsen M., Baeuerle P.A.,
Blasi F.;
"A novel complex between the p65 subunit of NF-kappa B and c-Rel binds
to a DNA element involved in the phorbol ester induction of the human
urokinase gene.";
EMBO J. 11:205-213(1992).
[11]
UBIQUITINATION.
PubMed=8087845; DOI=10.1016/S0092-8674(94)90482-0;
Palombella V.J., Rando O.J., Goldberg A.L., Maniatis T.;
"The ubiquitin-proteasome pathway is required for processing the NF-
kappa B1 precursor protein and the activation of NF-kappa B.";
Cell 78:773-785(1994).
[12]
IDENTIFICATION IN THE NF-KAPPA-B P50-C-REL COMPLEX.
PubMed=8152812;
Beg A.A., Baldwin A.S. Jr.;
"Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor
necrosis factor.";
Oncogene 9:1487-1492(1994).
[13]
PROTEOLYTIC PROCESSING OF P105, AND GENERATION OF P50 AND P105.
PubMed=8628291; DOI=10.1128/MCB.16.5.2248;
Lin L., Ghosh S.;
"A glycine-rich region in NF-kappaB p105 functions as a processing
signal for the generation of the p50 subunit.";
Mol. Cell. Biol. 16:2248-2254(1996).
[14]
S-NITROSYLATION AT CYS-61, MUTAGENESIS OF CYS-61, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=8710491; DOI=10.1093/nar/24.12.2236;
Matthews J.R., Botting C.H., Panico M., Morris H.R., Hay R.T.;
"Inhibition of NF-kappaB DNA binding by nitric oxide.";
Nucleic Acids Res. 24:2236-2242(1996).
[15]
INTERACTION WITH NFKBIE.
PubMed=9315679; DOI=10.1128/MCB.17.10.6184;
Li Z., Nabel G.J.;
"A new member of the IkappaB protein family, IkappaB epsilon, inhibits
RelA (p65)-mediated NF-kappaB transcription.";
Mol. Cell. Biol. 17:6184-6190(1997).
[16]
COTRANSLATIONAL FOLDING/PROCESSING OF P105, AND GENERATION OF
P50/P105.
PubMed=9529257; DOI=10.1016/S0092-8674(00)81409-9;
Lin L., DeMartino G.N., Greene W.C.;
"Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome.";
Cell 92:819-828(1998).
[17]
IDENTIFICATION IN A COMPLEX WITH BCL3, AND MUTAGENESIS OF SER-921;
SER-923 AND SER-932.
PubMed=10469655; DOI=10.1093/emboj/18.17.4766;
Heissmeyer V., Krappmann D., Wulczyn F.G., Scheidereit C.;
"NF-kappaB p105 is a target of IkappaB kinases and controls signal
induction of Bcl-3-p50 complexes.";
EMBO J. 18:4766-4778(1999).
[18]
INTERACTION WITH MAP3K8.
PubMed=9950430; DOI=10.1038/16946;
Belich M.P., Salmeron A., Johnston L.H., Ley S.C.;
"TPL-2 kinase regulates the proteolysis of the NF-kappaB-inhibitory
protein NF-kappaB1 p105.";
Nature 397:363-368(1999).
[19]
COTRANSLATIONAL FOLDING/PROCESSING OF P105, GENERATION OF P50/P105,
AND P50-P105 TRANSIENT HETERODIMER FORMATION.
PubMed=10970863; DOI=10.1093/emboj/19.17.4712;
Lin L., DeMartino G.N., Greene W.C.;
"Cotranslational dimerization of the Rel homology domain of NF-kappaB1
generates p50-p105 heterodimers and is required for effective p50
production.";
EMBO J. 19:4712-4722(2000).
[20]
INTERACTION WITH NCOA3.
PubMed=11094166; DOI=10.1016/S0014-5793(00)02223-7;
Werbajh S., Nojek I., Lanz R., Costas M.A.;
"RAC-3 is a NF-kappa B coactivator.";
FEBS Lett. 485:195-199(2000).
[21]
S-NITROSYLATION.
PubMed=11327828; DOI=10.1021/bi002239y;
Marshall H.E., Stamler J.S.;
"Inhibition of NF-kappaB by S-nitrosylation.";
Biochemistry 40:1688-1693(2001).
[22]
INTERACTION WITH DSIPI.
PubMed=11468175; DOI=10.1182/blood.V98.3.743;
Ayroldi E., Migliorati G., Bruscoli S., Marchetti C., Zollo O.,
Cannarile L., D'Adamio F., Riccardi C.;
"Modulation of T-cell activation by the glucocorticoid-induced leucine
zipper factor via inhibition of nuclear factor kappa B.";
Blood 98:743-753(2001).
[23]
LIPIDATION AT CYS-61, AND MUTAGENESIS OF CYS-61.
PubMed=11466314; DOI=10.1074/jbc.M104518200;
Cernuda-Morollon E., Pineda-Molina E., Canada F.J., Perez-Sala D.;
"15-Deoxy-Delta 12,14-prostaglandin J2 inhibition of NF-kappaB-DNA
binding through covalent modification of the p50 subunit.";
J. Biol. Chem. 276:35530-35536(2001).
[24]
PHOSPHORYLATION AT SER-927.
PubMed=11297557; DOI=10.1074/jbc.M101754200;
Salmeron A., Janzen J., Soneji Y., Bump N., Kamens J., Allen H.,
Ley S.C.;
"Direct phosphorylation of NF-kappa B1 p105 by the Ikappa B kinase
complex on serine 927 is essential for signal-induced p105
proteolysis.";
J. Biol. Chem. 276:22215-22222(2001).
[25]
INTERACTION WITH MEN1.
PubMed=11526476; DOI=10.1038/sj.onc.1204529;
Heppner C., Bilimoria K.Y., Agarwal S.K., Kester M., Whitty L.J.,
Guru S.C., Chandrasekharappa S.C., Collins F.S., Spiegel A.M.,
Marx S.J., Burns A.L.;
"The tumor suppressor protein menin interacts with NF-kappaB proteins
and inhibits NF-kappaB-mediated transactivation.";
Oncogene 20:4917-4925(2001).
[26]
INTERACTION WITH CFLAR.
PubMed=13679070; DOI=10.1016/j.bbrc.2003.08.104;
Li Z., Zhang J., Chen D., Shu H.B.;
"Casper/c-FLIP is physically and functionally associated with NF-
kappaB1 p105.";
Biochem. Biophys. Res. Commun. 309:980-985(2003).
[27]
ACETYLATION AT LYS-431; LYS-440 AND LYS-441.
PubMed=11739381; DOI=10.1074/jbc.M107848200;
Furia B., Deng L., Wu K., Baylor S., Kehn K., Li H., Donnelly R.,
Coleman T., Kashanchi F.;
"Enhancement of nuclear factor-kappa B acetylation by coactivator p300
and HIV-1 Tat proteins.";
J. Biol. Chem. 277:4973-4980(2002).
[28]
INTERACTION WITH DSIPI.
PubMed=12393603; DOI=10.1182/blood-2002-02-0538;
Berrebi D., Bruscoli S., Cohen N., Foussat A., Migliorati G.,
Bouchet-Delbos L., Maillot M.-C., Portier A., Couderc J., Galanaud P.,
Peuchmaur M., Riccardi C., Emilie D.;
"Synthesis of glucocorticoid-induced leucine zipper (GILZ) by
macrophages: an anti-inflammatory and immunosuppressive mechanism
shared by glucocorticoids and IL-10.";
Blood 101:729-738(2003).
[29]
ACETYLATION.
PubMed=12471036; DOI=10.1074/jbc.M209286200;
Deng W.G., Zhu Y., Wu K.K.;
"Up-regulation of p300 binding and p50 acetylation in tumor necrosis
factor-alpha-induced cyclooxygenase-2 promoter activation.";
J. Biol. Chem. 278:4770-4777(2003).
[30]
INTERACTION WITH GSK3B, PHOSPHORYLATION AT SER-903 AND SER-907, AND
MUTAGENESIS OF SER-903 AND SER-907.
PubMed=12871932; DOI=10.1074/jbc.M305676200;
Demarchi F., Bertoli C., Sandy P., Schneider C.;
"Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105
stability.";
J. Biol. Chem. 278:39583-39590(2003).
[31]
PHOSPHORYLATION AT SER-927 AND SER-932.
PubMed=12482991; DOI=10.1128/MCB.23.1.402-413.2003;
Lang V., Janzen J., Fischer G.Z., Soneji Y., Beinke S., Salmeron A.,
Allen H., Hay R.T., Ben-Neriah Y., Ley S.C.;
"betaTrCP-mediated proteolysis of NF-kappaB1 p105 requires
phosphorylation of p105 serines 927 and 932.";
Mol. Cell. Biol. 23:402-413(2003).
[32]
INTERACTION WITH UNC5CL.
PubMed=14769797; DOI=10.1074/jbc.M310737200;
Zhang J., Xu L.-G., Han K.-J., Shu H.-B.;
"Identification of a ZU5 and death domain-containing inhibitor of NF-
kappaB.";
J. Biol. Chem. 279:17819-17825(2004).
[33]
INTERACTION WITH MAP3K8 AND TNIP2.
PubMed=15169888; DOI=10.1128/MCB.24.12.5235-5248.2004;
Lang V., Symons A., Watton S.J., Janzen J., Soneji Y., Beinke S.,
Howell S., Ley S.C.;
"ABIN-2 forms a ternary complex with TPL-2 and NF-kappa B1 p105 and is
essential for TPL-2 protein stability.";
Mol. Cell. Biol. 24:5235-5248(2004).
[34]
IDENTIFICATION IN THE NF-KAPPA-B P50-C-REL COMPLEX.
PubMed=15102766; DOI=10.1128/IAI.72.5.2582-2589.2004;
Guizani-Tabbane L., Ben-Aissa K., Belghith M., Sassi A., Dellagi K.;
"Leishmania major amastigotes induce p50/c-Rel NF-kappa B
transcription factor in human macrophages: involvement in cytokine
synthesis.";
Infect. Immun. 72:2582-2589(2004).
[35]
FUNCTION, AND INTERACTION WITH MAP3K8.
PubMed=15485931; DOI=10.1128/MCB.24.21.9658-9667.2004;
Beinke S., Robinson M.J., Hugunin M., Ley S.C.;
"Lipopolysaccharide activation of the TPL-2/MEK/extracellular signal-
regulated kinase mitogen-activated protein kinase cascade is regulated
by IkappaB kinase-induced proteolysis of NF-kappaB1 p105.";
Mol. Cell. Biol. 24:9658-9667(2004).
[36]
INTERACTION WITH SPAG9.
PubMed=14743216; DOI=10.1038/ncb1086;
Bouwmeester T., Bauch A., Ruffner H., Angrand P.-O., Bergamini G.,
Croughton K., Cruciat C., Eberhard D., Gagneur J., Ghidelli S.,
Hopf C., Huhse B., Mangano R., Michon A.-M., Schirle M., Schlegl J.,
Schwab M., Stein M.A., Bauer A., Casari G., Drewes G., Gavin A.-C.,
Jackson D.B., Joberty G., Neubauer G., Rick J., Kuster B.,
Superti-Furga G.;
"A physical and functional map of the human TNF-alpha/NF-kappa B
signal transduction pathway.";
Nat. Cell Biol. 6:97-105(2004).
[37]
INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-678, AND MUTAGENESIS OF
ASN-678.
PubMed=17003112; DOI=10.1073/pnas.0606877103;
Cockman M.E., Lancaster D.E., Stolze I.P., Hewitson K.S.,
McDonough M.A., Coleman M.L., Coles C.H., Yu X., Hay R.T., Ley S.C.,
Pugh C.W., Oldham N.J., Masson N., Schofield C.J., Ratcliffe P.J.;
"Posttranslational hydroxylation of ankyrin repeats in IkappaB
proteins by the hypoxia-inducible factor (HIF) asparaginyl
hydroxylase, factor inhibiting HIF (FIH).";
Proc. Natl. Acad. Sci. U.S.A. 103:14767-14772(2006).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-937, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903 AND SER-907, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-892, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[43]
INVOLVEMENT IN CVID12.
PubMed=26279205; DOI=10.1016/j.ajhg.2015.07.008;
Fliegauf M., Bryant V.L., Frede N., Slade C., Woon S.T., Lehnert K.,
Winzer S., Bulashevska A., Scerri T., Leung E., Jordan A., Keller B.,
de Vries E., Cao H., Yang F., Schaeffer A.A., Warnatz K., Browett P.,
Douglass J., Ameratunga R.V., van der Meer J.W., Grimbacher B.;
"Haploinsufficiency of the NF-kappaB1 Subunit p50 in Common Variable
Immunodeficiency.";
Am. J. Hum. Genet. 97:389-403(2015).
[44]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-325, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[45]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-365.
PubMed=7830764; DOI=10.1038/373311a0;
Mueller C.W., Rey F.A., Sodeoka M., Verdine G.L., Harrison S.C.;
"Structure of the NF-kappa B p50 homodimer bound to DNA.";
Nature 373:311-317(1995).
[46]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 248-354.
PubMed=9865693; DOI=10.1016/S0092-8674(00)81698-0;
Jacobs M.D., Harrison S.C.;
"Structure of an IkappaBalpha/NF-kappaB complex.";
Cell 95:749-758(1998).
[47]
STRUCTURE BY NMR OF 804-893.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the death domain in human nuclear factor NF-
kappa-B p105 subunit.";
Submitted (DEC-2006) to the PDB data bank.
-!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor present
in almost all cell types and is the endpoint of a series of signal
transduction events that are initiated by a vast array of stimuli
related to many biological processes such as inflammation,
immunity, differentiation, cell growth, tumorigenesis and
apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed
by the Rel-like domain-containing proteins RELA/p65, RELB,
NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric
p65-p50 complex appears to be most abundant one. The dimers bind
at kappa-B sites in the DNA of their target genes and the
individual dimers have distinct preferences for different kappa-B
sites that they can bind with distinguishable affinity and
specificity. Different dimer combinations act as transcriptional
activators or repressors, respectively. NF-kappa-B is controlled
by various mechanisms of post-translational modification and
subcellular compartmentalization as well as by interactions with
other cofactors or corepressors. NF-kappa-B complexes are held in
the cytoplasm in an inactive state complexed with members of the
NF-kappa-B inhibitor (I-kappa-B) family. In a conventional
activation pathway, I-kappa-B is phosphorylated by I-kappa-B
kinases (IKKs) in response to different activators, subsequently
degraded thus liberating the active NF-kappa-B complex which
translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and
RelB-p50 complexes are transcriptional activators. The NF-kappa-B
p50-p50 homodimer is a transcriptional repressor, but can act as a
transcriptional activator when associated with BCL3. NFKB1 appears
to have dual functions such as cytoplasmic retention of attached
NF-kappa-B proteins by p105 and generation of p50 by a
cotranslational processing. The proteasome-mediated process
ensures the production of both p50 and p105 and preserves their
independent function, although processing of NFKB1/p105 also
appears to occur post-translationally. p50 binds to the kappa-B
consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region
of genes involved in immune response and acute phase reactions. In
a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK
signaling; active MAP3K8 is released by proteasome-dependent
degradation of NFKB1/p105. {ECO:0000269|PubMed:15485931}.
-!- SUBUNIT: Component of the NF-kappa-B p65-p50 complex. Component of
the NF-kappa-B p65-p50 complex. Homodimer; component of the NF-
kappa-B p50-p50 complex. Component of the NF-kappa-B p105-p50
complex. Component of the NF-kappa-B p50-c-Rel complex. Component
of a complex consisting of the NF-kappa-B p50-p50 homodimer and
BCL3. Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts
with NCOA3 coactivator, which may coactivate NF-kappa-B dependent
expression via its histone acetyltransferase activity. Interacts
with DSIPI; this interaction prevents nuclear translocation and
DNA-binding. Interacts with SPAG9 and UNC5CL. NFKB1/p105 interacts
with CFLAR; the interaction inhibits p105 processing into p50.
NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2.
Interacts with GSK3B; the interaction prevents processing of p105
to p50. NFKB1/p50 interacts with NFKBIE. NFKB1/p50 interacts with
NFKBIZ. Nuclear factor NF-kappa-B p50 subunit interacts with
NFKBID (By similarity). Directly interacts with MEN1. Interacts
with HIF1AN. {ECO:0000250, ECO:0000269|PubMed:10469655,
ECO:0000269|PubMed:11094166, ECO:0000269|PubMed:11468175,
ECO:0000269|PubMed:11526476, ECO:0000269|PubMed:12393603,
ECO:0000269|PubMed:12871932, ECO:0000269|PubMed:13679070,
ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:14769797,
ECO:0000269|PubMed:15102766, ECO:0000269|PubMed:15169888,
ECO:0000269|PubMed:15485931, ECO:0000269|PubMed:17003112,
ECO:0000269|PubMed:1740106, ECO:0000269|PubMed:8152812,
ECO:0000269|PubMed:9315679, ECO:0000269|PubMed:9950430}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-300010, EBI-300010;
Q92887:ABCC2; NbExp=3; IntAct=EBI-300010, EBI-3916193;
O15111:CHUK; NbExp=3; IntAct=EBI-300010, EBI-81249;
P35606:COPB2; NbExp=3; IntAct=EBI-300010, EBI-1056534;
P35222:CTNNB1; NbExp=3; IntAct=EBI-300010, EBI-491549;
P03372:ESR1; NbExp=3; IntAct=EBI-697771, EBI-78473;
Q13547:HDAC1; NbExp=5; IntAct=EBI-300010, EBI-301834;
P08238:HSP90AB1; NbExp=3; IntAct=EBI-300010, EBI-352572;
P34931:HSPA1L; NbExp=3; IntAct=EBI-300010, EBI-354912;
O14920:IKBKB; NbExp=3; IntAct=EBI-300010, EBI-81266;
P41279:MAP3K8; NbExp=13; IntAct=EBI-300010, EBI-354900;
O00255:MEN1; NbExp=2; IntAct=EBI-697771, EBI-592789;
O00255-2:MEN1; NbExp=4; IntAct=EBI-697771, EBI-9869387;
Q00653:NFKB2; NbExp=8; IntAct=EBI-300010, EBI-307326;
P25963:NFKBIA; NbExp=5; IntAct=EBI-300010, EBI-307386;
P46531:NOTCH1; NbExp=2; IntAct=EBI-300010, EBI-636374;
Q14690:PDCD11; NbExp=2; IntAct=EBI-300010, EBI-300028;
Q8IZL8:PELP1; NbExp=2; IntAct=EBI-300010, EBI-716449;
Q8IV08:PLD3; NbExp=2; IntAct=EBI-300010, EBI-2689908;
Q04864:REL; NbExp=7; IntAct=EBI-300010, EBI-307352;
Q04206:RELA; NbExp=13; IntAct=EBI-300010, EBI-73886;
Q01201:RELB; NbExp=5; IntAct=EBI-300010, EBI-357837;
P23396:RPS3; NbExp=5; IntAct=EBI-300010, EBI-351193;
O60271:SPAG9; NbExp=2; IntAct=EBI-300010, EBI-1023301;
Q15025:TNIP1; NbExp=4; IntAct=EBI-300010, EBI-357849;
Q8NFZ5:TNIP2; NbExp=8; IntAct=EBI-1452239, EBI-359372;
P10226:UL42 (xeno); NbExp=4; IntAct=EBI-300010, EBI-1029310;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, but also
found in the cytoplasm in an inactive form complexed to an
inhibitor (I-kappa-B).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P19838-1; Sequence=Displayed;
Name=2;
IsoId=P19838-2; Sequence=VSP_021025;
Name=3;
IsoId=P19838-3; Sequence=VSP_042869, VSP_042870;
Note=No experimental confirmation available.;
-!- INDUCTION: By phorbol ester and TNF.
-!- DOMAIN: The C-terminus of p105 might be involved in cytoplasmic
retention, inhibition of DNA-binding, and transcription
activation.
-!- DOMAIN: Glycine-rich region (GRR) appears to be a critical element
in the generation of p50.
-!- PTM: While translation occurs, the particular unfolded structure
after the GRR repeat promotes the generation of p50 making it an
acceptable substrate for the proteasome. This process is known as
cotranslational processing. The processed form is active and the
unprocessed form acts as an inhibitor (I kappa B-like), being able
to form cytosolic complexes with NF-kappa B, trapping it in the
cytoplasm. Complete folding of the region downstream of the GRR
repeat precludes processing. {ECO:0000269|PubMed:8628291}.
-!- PTM: Phosphorylation at 'Ser-903' and 'Ser-907' primes p105 for
proteolytic processing in response to TNF-alpha stimulation.
Phosphorylation at 'Ser-927' and 'Ser-932' are required for
BTRC/BTRCP-mediated proteolysis. {ECO:0000269|PubMed:11297557,
ECO:0000269|PubMed:12482991, ECO:0000269|PubMed:12871932,
ECO:0000269|PubMed:8628291}.
-!- PTM: Polyubiquitination seems to allow p105 processing.
{ECO:0000269|PubMed:8087845, ECO:0000269|PubMed:8628291}.
-!- PTM: S-nitrosylation of Cys-61 affects DNA binding.
{ECO:0000269|PubMed:11327828, ECO:0000269|PubMed:8710491}.
-!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-
prostaglandin-J2 is autocatalytic and reversible. It may occur as
an alternative to other cysteine modifications, such as S-
nitrosylation and S-palmitoylation.
-!- DISEASE: Immunodeficiency, common variable, 12 (CVID12)
[MIM:616576]: A primary immunodeficiency characterized by antibody
deficiency, hypogammaglobulinemia, recurrent bacterial infections
and an inability to mount an antibody response to antigen.
{ECO:0000269|PubMed:26279205}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NFKB1ID323.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/nfkb1/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M55643; AAA36361.1; -; mRNA.
EMBL; M58603; AAA36360.1; -; mRNA.
EMBL; Z47748; CAB94757.1; -; Genomic_DNA.
EMBL; Z47749; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47750; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47751; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47752; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47753; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47754; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47755; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47734; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47735; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47736; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47737; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47738; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47739; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47740; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47741; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47742; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47743; CAB94757.1; JOINED; Genomic_DNA.
EMBL; Z47744; CAB94757.1; JOINED; Genomic_DNA.
EMBL; AF213884; AAF35232.1; -; Genomic_DNA.
EMBL; AK122850; BAG53760.1; -; mRNA.
EMBL; AK291450; BAF84139.1; -; mRNA.
EMBL; CR749522; CAH18336.1; -; mRNA.
EMBL; AY223820; AAO30127.1; -; Genomic_DNA.
EMBL; BC033210; AAH33210.1; -; mRNA.
EMBL; BC051765; AAH51765.1; -; mRNA.
CCDS; CCDS3657.1; -. [P19838-2]
CCDS; CCDS54783.1; -. [P19838-1]
PIR; A37867; A37867.
RefSeq; NP_001158884.1; NM_001165412.1. [P19838-1]
RefSeq; NP_001306155.1; NM_001319226.1. [P19838-1]
RefSeq; NP_003989.2; NM_003998.3. [P19838-2]
UniGene; Hs.618430; -.
PDB; 1MDI; NMR; -; B=55-67.
PDB; 1MDJ; NMR; -; B=55-67.
PDB; 1MDK; NMR; -; B=55-67.
PDB; 1NFI; X-ray; 2.70 A; B/D=248-354.
PDB; 1SVC; X-ray; 2.60 A; P=2-365.
PDB; 2DBF; NMR; -; A=806-893.
PDB; 2O61; X-ray; 2.80 A; B=40-352.
PDB; 3GUT; X-ray; 3.59 A; B/D/F/H=41-352.
PDBsum; 1MDI; -.
PDBsum; 1MDJ; -.
PDBsum; 1MDK; -.
PDBsum; 1NFI; -.
PDBsum; 1SVC; -.
PDBsum; 2DBF; -.
PDBsum; 2O61; -.
PDBsum; 3GUT; -.
ProteinModelPortal; P19838; -.
SMR; P19838; -.
BioGrid; 110857; 150.
CORUM; P19838; -.
DIP; DIP-106N; -.
ELM; P19838; -.
IntAct; P19838; 481.
MINT; MINT-85658; -.
STRING; 9606.ENSP00000226574; -.
BindingDB; P19838; -.
ChEMBL; CHEMBL3251; -.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB05487; CC-8490.
DrugBank; DB05212; HE3286.
DrugBank; DB05767; HMPL-004.
DrugBank; DB05464; NOX-700.
DrugBank; DB05451; P54.
DrugBank; DB01411; Pranlukast.
DrugBank; DB05471; SGN-30.
DrugBank; DB01041; Thalidomide.
DrugBank; DB08814; Triflusal.
iPTMnet; P19838; -.
PhosphoSitePlus; P19838; -.
BioMuta; NFKB1; -.
DMDM; 21542418; -.
EPD; P19838; -.
MaxQB; P19838; -.
PaxDb; P19838; -.
PeptideAtlas; P19838; -.
PRIDE; P19838; -.
DNASU; 4790; -.
Ensembl; ENST00000226574; ENSP00000226574; ENSG00000109320. [P19838-2]
Ensembl; ENST00000394820; ENSP00000378297; ENSG00000109320. [P19838-1]
Ensembl; ENST00000505458; ENSP00000424790; ENSG00000109320. [P19838-1]
Ensembl; ENST00000600343; ENSP00000469340; ENSG00000109320. [P19838-3]
GeneID; 4790; -.
KEGG; hsa:4790; -.
UCSC; uc011cep.2; human. [P19838-1]
CTD; 4790; -.
DisGeNET; 4790; -.
EuPathDB; HostDB:ENSG00000109320.11; -.
GeneCards; NFKB1; -.
HGNC; HGNC:7794; NFKB1.
HPA; CAB004031; -.
HPA; HPA027305; -.
MalaCards; NFKB1; -.
MIM; 164011; gene.
MIM; 616576; phenotype.
neXtProt; NX_P19838; -.
OpenTargets; ENSG00000109320; -.
PharmGKB; PA248; -.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00500000044765; -.
HOGENOM; HOG000004822; -.
HOVERGEN; HBG052613; -.
InParanoid; P19838; -.
KO; K02580; -.
OMA; PFRYKPR; -.
OrthoDB; EOG091G03PF; -.
PhylomeDB; P19838; -.
TreeFam; TF325632; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-193692; Regulated proteolysis of p75NTR.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-209560; NF-kB is activated and signals survival.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-448706; Interleukin-1 processing.
Reactome; R-HSA-5603027; IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
Reactome; R-HSA-5603029; IkBA variant leads to EDA-ID.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5660668; CLEC7A/inflammasome pathway.
Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
SignaLink; P19838; -.
SIGNOR; P19838; -.
ChiTaRS; NFKB1; human.
EvolutionaryTrace; P19838; -.
GeneWiki; NFKB1; -.
GenomeRNAi; 4790; -.
PMAP-CutDB; P19838; -.
PRO; PR:P19838; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109320; -.
CleanEx; HS_NFKB1; -.
ExpressionAtlas; P19838; baseline and differential.
Genevisible; P19838; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0033256; C:I-kappaB/NF-kappaB complex; TAS:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0042805; F:actinin binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0000975; F:regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071359; P:cellular response to dsRNA; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:BHF-UCL.
GO; GO:0071354; P:cellular response to interleukin-6; IMP:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0071316; P:cellular response to nicotine; IMP:BHF-UCL.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IMP:BHF-UCL.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0010956; P:negative regulation of calcidiol 1-monooxygenase activity; IDA:BHF-UCL.
GO; GO:0032269; P:negative regulation of cellular protein metabolic process; IC:BHF-UCL.
GO; GO:0032375; P:negative regulation of cholesterol transport; IC:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0045083; P:negative regulation of interleukin-12 biosynthetic process; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0010957; P:negative regulation of vitamin D biosynthetic process; IC:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; IDA:UniProtKB.
GO; GO:0010884; P:positive regulation of lipid storage; IC:BHF-UCL.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
GO; GO:2000630; P:positive regulation of miRNA metabolic process; IMP:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:UniProtKB.
CDD; cd00204; ANK; 1.
CDD; cd01177; IPT_NFkappaB; 1.
Gene3D; 1.25.40.20; -; 3.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR000488; Death_domain.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT.
InterPro; IPR033926; IPT_NFkappaB.
InterPro; IPR030503; NF-kB_p105.
InterPro; IPR000451; NFkB/Dor.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR030492; RHD_CS.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
PANTHER; PTHR24169; PTHR24169; 1.
PANTHER; PTHR24169:SF26; PTHR24169:SF26; 1.
Pfam; PF00023; Ank; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00531; Death; 1.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR01415; ANKYRIN.
PRINTS; PR00057; NFKBTNSCPFCT.
SMART; SM00248; ANK; 6.
SMART; SM00005; DEATH; 1.
SMART; SM00429; IPT; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS01204; REL_1; 1.
PROSITE; PS50254; REL_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
ANK repeat; Apoptosis; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Hydroxylation;
Isopeptide bond; Lipoprotein; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; S-nitrosylation; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 968 Nuclear factor NF-kappa-B p105 subunit.
/FTId=PRO_0000030310.
CHAIN 1 433 Nuclear factor NF-kappa-B p50 subunit.
/FTId=PRO_0000030311.
DOMAIN 42 367 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
REPEAT 542 571 ANK 1.
REPEAT 581 610 ANK 2.
REPEAT 614 643 ANK 3.
REPEAT 650 679 ANK 4.
REPEAT 684 714 ANK 5.
REPEAT 718 747 ANK 6.
REPEAT 771 801 ANK 7.
DOMAIN 805 892 Death.
REGION 372 394 GRR.
REGION 435 968 Interaction with CFLAR.
{ECO:0000269|PubMed:13679070}.
REGION 650 684 Essential for interaction with HIF1AN.
{ECO:0000269|PubMed:17003112}.
MOTIF 360 365 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 375 433 Gly-rich.
SITE 433 434 Cleavage (when cotranslationally
processed).
MOD_RES 61 61 S-nitrosocysteine; alternate.
{ECO:0000269|PubMed:8710491}.
MOD_RES 337 337 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 431 431 N6-acetyllysine; by EP300.
{ECO:0000305|PubMed:11739381}.
MOD_RES 440 440 N6-acetyllysine; by EP300.
{ECO:0000305|PubMed:11739381}.
MOD_RES 441 441 N6-acetyllysine; by EP300.
{ECO:0000305|PubMed:11739381}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000250|UniProtKB:P25799}.
MOD_RES 678 678 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:17003112}.
MOD_RES 759 759 Phosphoserine.
{ECO:0000250|UniProtKB:Q63369}.
MOD_RES 892 892 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 903 903 Phosphoserine; by GSK3-beta; in vitro.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12871932}.
MOD_RES 907 907 Phosphoserine; by GSK3-beta; in vitro.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12871932}.
MOD_RES 927 927 Phosphoserine; by IKKB.
{ECO:0000269|PubMed:11297557,
ECO:0000269|PubMed:12482991}.
MOD_RES 932 932 Phosphoserine; by IKKB.
{ECO:0000269|PubMed:12482991}.
MOD_RES 937 937 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 943 943 Phosphothreonine.
{ECO:0000250|UniProtKB:P25799}.
LIPID 61 61 S-(15-deoxy-Delta12,14-prostaglandin J2-
9-yl)cysteine; alternate.
{ECO:0000269|PubMed:11466314}.
CROSSLNK 325 325 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 180 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042869.
VAR_SEQ 39 39 T -> TA (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2203531}.
/FTId=VSP_021025.
VAR_SEQ 181 189 EGGGDRQLG -> MNGLCCMAL (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042870.
VARIANT 489 489 T -> I (in dbSNP:rs4648065).
{ECO:0000269|Ref.8}.
/FTId=VAR_016268.
VARIANT 506 506 M -> V (in dbSNP:rs4648072).
{ECO:0000269|Ref.8}.
/FTId=VAR_016269.
VARIANT 566 566 T -> I (in dbSNP:rs4648085).
{ECO:0000269|Ref.8}.
/FTId=VAR_016270.
VARIANT 578 578 R -> K (in dbSNP:rs4648086).
{ECO:0000269|Ref.8}.
/FTId=VAR_016271.
VARIANT 711 711 H -> Q (in dbSNP:rs4648099).
{ECO:0000269|Ref.8}.
/FTId=VAR_016272.
VARIANT 901 901 A -> T (in dbSNP:rs4648118).
{ECO:0000269|Ref.8}.
/FTId=VAR_016273.
MUTAGEN 61 61 C->S: Suppresses S-nitrosylation-induced
inhibition of DNA-binding activity. Loss
of S-(15-deoxy-Delta12,14-prostaglandin
J2-9-yl)cysteine-induced inhibition of
DNA-binding activity.
{ECO:0000269|PubMed:11466314,
ECO:0000269|PubMed:8710491}.
MUTAGEN 678 678 N->A: Fails to promote HIF1AN-dependent
2-oxoglutarate decarboxylation.
{ECO:0000269|PubMed:17003112}.
MUTAGEN 903 903 S->A: Prevents p105 proteolysis in
response to TNF-alpha.
{ECO:0000269|PubMed:12871932}.
MUTAGEN 907 907 S->A: Prevents p105 proteolysis in
response to TNF-alpha.
{ECO:0000269|PubMed:12871932}.
MUTAGEN 921 921 S->A: Decrease in stimuli-induced
phosphorylation. Loss of phosphorylation;
when associated with A-923 and A-932.
{ECO:0000269|PubMed:10469655}.
MUTAGEN 923 923 S->A: Decrease in stimuli-induced
phosphorylation. Loss of phosphorylation;
when associated with A-921 and A-932.
{ECO:0000269|PubMed:10469655}.
MUTAGEN 932 932 S->A: Decrease in stimuli-induced
phosphorylation. Loss of phosphorylation;
when associated with A-921 and A-923.
{ECO:0000269|PubMed:10469655}.
CONFLICT 243 243 K -> SE (in Ref. 4; CAB94757).
{ECO:0000305}.
CONFLICT 361 361 R -> G (in Ref. 7; CAH18336).
{ECO:0000305}.
CONFLICT 551 552 II -> SS (in Ref. 4; CAB94757).
{ECO:0000305}.
CONFLICT 573 573 D -> G (in Ref. 6; BAF84139).
{ECO:0000305}.
CONFLICT 726 726 A -> V (in Ref. 4; CAB94757).
{ECO:0000305}.
CONFLICT 825 825 I -> T (in Ref. 7; CAH18336).
{ECO:0000305}.
CONFLICT 869 869 V -> I (in Ref. 4; CAB94757).
{ECO:0000305}.
CONFLICT 927 927 S -> T (in Ref. 1; AAA36361, 3; AAA36360
and 4; CAB94757). {ECO:0000305}.
STRAND 43 48 {ECO:0000244|PDB:1SVC}.
STRAND 52 54 {ECO:0000244|PDB:1SVC}.
HELIX 60 62 {ECO:0000244|PDB:1SVC}.
STRAND 83 88 {ECO:0000244|PDB:1SVC}.
STRAND 94 100 {ECO:0000244|PDB:1SVC}.
STRAND 103 105 {ECO:0000244|PDB:1SVC}.
STRAND 110 115 {ECO:0000244|PDB:1SVC}.
STRAND 122 126 {ECO:0000244|PDB:1SVC}.
STRAND 133 135 {ECO:0000244|PDB:1SVC}.
STRAND 138 143 {ECO:0000244|PDB:1SVC}.
HELIX 146 148 {ECO:0000244|PDB:1SVC}.
HELIX 149 163 {ECO:0000244|PDB:1SVC}.
HELIX 167 170 {ECO:0000244|PDB:1SVC}.
HELIX 173 178 {ECO:0000244|PDB:1SVC}.
STRAND 180 182 {ECO:0000244|PDB:2O61}.
TURN 184 187 {ECO:0000244|PDB:1SVC}.
HELIX 190 204 {ECO:0000244|PDB:1SVC}.
STRAND 211 221 {ECO:0000244|PDB:1SVC}.
STRAND 223 225 {ECO:0000244|PDB:1SVC}.
STRAND 227 230 {ECO:0000244|PDB:1SVC}.
STRAND 234 240 {ECO:0000244|PDB:1SVC}.
HELIX 245 247 {ECO:0000244|PDB:1SVC}.
STRAND 252 256 {ECO:0000244|PDB:1SVC}.
STRAND 258 261 {ECO:0000244|PDB:1SVC}.
STRAND 267 274 {ECO:0000244|PDB:1SVC}.
HELIX 277 279 {ECO:0000244|PDB:1SVC}.
STRAND 281 288 {ECO:0000244|PDB:1SVC}.
TURN 289 291 {ECO:0000244|PDB:1SVC}.
STRAND 292 297 {ECO:0000244|PDB:1SVC}.
HELIX 302 304 {ECO:0000244|PDB:1SVC}.
TURN 307 309 {ECO:0000244|PDB:1SVC}.
STRAND 310 314 {ECO:0000244|PDB:1SVC}.
STRAND 319 322 {ECO:0000244|PDB:2O61}.
STRAND 327 334 {ECO:0000244|PDB:1SVC}.
TURN 336 338 {ECO:0000244|PDB:1SVC}.
STRAND 345 350 {ECO:0000244|PDB:1SVC}.
HELIX 813 823 {ECO:0000244|PDB:2DBF}.
HELIX 832 839 {ECO:0000244|PDB:2DBF}.
HELIX 842 844 {ECO:0000244|PDB:2DBF}.
HELIX 845 850 {ECO:0000244|PDB:2DBF}.
HELIX 854 864 {ECO:0000244|PDB:2DBF}.
HELIX 869 879 {ECO:0000244|PDB:2DBF}.
HELIX 883 892 {ECO:0000244|PDB:2DBF}.
SEQUENCE 968 AA; 105356 MW; 2A7C8FF86A10D1A8 CRC64;
MAEDDPYLGR PEQMFHLDPS LTHTIFNPEV FQPQMALPTD GPYLQILEQP KQRGFRFRYV
CEGPSHGGLP GASSEKNKKS YPQVKICNYV GPAKVIVQLV TNGKNIHLHA HSLVGKHCED
GICTVTAGPK DMVVGFANLG ILHVTKKKVF ETLEARMTEA CIRGYNPGLL VHPDLAYLQA
EGGGDRQLGD REKELIRQAA LQQTKEMDLS VVRLMFTAFL PDSTGSFTRR LEPVVSDAIY
DSKAPNASNL KIVRMDRTAG CVTGGEEIYL LCDKVQKDDI QIRFYEEEEN GGVWEGFGDF
SPTDVHRQFA IVFKTPKYKD INITKPASVF VQLRRKSDLE TSEPKPFLYY PEIKDKEEVQ
RKRQKLMPNF SDSFGGGSGA GAGGGGMFGS GGGGGGTGST GPGYSFPHYG FPTYGGITFH
PGTTKSNAGM KHGTMDTESK KDPEGCDKSD DKNTVNLFGK VIETTEQDQE PSEATVGNGE
VTLTYATGTK EESAGVQDNL FLEKAMQLAK RHANALFDYA VTGDVKMLLA VQRHLTAVQD
ENGDSVLHLA IIHLHSQLVR DLLEVTSGLI SDDIINMRND LYQTPLHLAV ITKQEDVVED
LLRAGADLSL LDRLGNSVLH LAAKEGHDKV LSILLKHKKA ALLLDHPNGD GLNAIHLAMM
SNSLPCLLLL VAAGADVNAQ EQKSGRTALH LAVEHDNISL AGCLLLEGDA HVDSTTYDGT
TPLHIAAGRG STRLAALLKA AGADPLVENF EPLYDLDDSW ENAGEDEGVV PGTTPLDMAT
SWQVFDILNG KPYEPEFTSD DLLAQGDMKQ LAEDVKLQLY KLLEIPDPDK NWATLAQKLG
LGILNNAFRL SPAPSKTLMD NYEVSGGTVR ELVEALRQMG YTEAIEVIQA ASSPVKTTSQ
AHSLPLSPAS TRQQIDELRD SDSVCDSGVE TSFRKLSFTE SLTSGASLLT LNKMPHDYGQ
EGPLEGKI


Related products :

Catalog number Product name Quantity
U1824m CLIA DNA-binding factor KBF1,EBP-1,Mouse,Mus musculus,NF-kappa-B1 p84_NF-kappa-B1 p98,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
E1824m ELISA DNA-binding factor KBF1,EBP-1,Mouse,Mus musculus,NF-kappa-B1 p84_NF-kappa-B1 p98,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
U1824m CLIA kit DNA-binding factor KBF1,EBP-1,Mouse,Mus musculus,NF-kappa-B1 p84_NF-kappa-B1 p98,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cel 96T
E1824m ELISA kit DNA-binding factor KBF1,EBP-1,Mouse,Mus musculus,NF-kappa-B1 p84_NF-kappa-B1 p98,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-ce 96T
U1824r CLIA kit DNA-binding factor KBF1,EBP-1,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1,Rat,Rattus norvegicus 96T
U1824r CLIA DNA-binding factor KBF1,EBP-1,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1,Rat,Rattus norvegicus 96T
E1824r ELISA DNA-binding factor KBF1,EBP-1,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1,Rat,Rattus norvegicus 96T
E1824r ELISA kit DNA-binding factor KBF1,EBP-1,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1,Rat,Rattus norvegicus 96T
U1824h CLIA DNA-binding factor KBF1,EBP-1,Homo sapiens,Human,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
E1824h ELISA DNA-binding factor KBF1,EBP-1,Homo sapiens,Human,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
U1824h CLIA kit DNA-binding factor KBF1,EBP-1,Homo sapiens,Human,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
E1824h ELISA kit DNA-binding factor KBF1,EBP-1,Homo sapiens,Human,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
EIAAB27078 Chicken,DNA-binding factor KBF2,Gallus gallus,Lyt-10,NFKB2,Nuclear factor NF-kappa-B p100 subunit,Nuclear factor NF-kappa-B p97 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cel
EIAAB27080 DNA-binding factor KBF2,Mouse,Mus musculus,Nfkb2,Nuclear factor NF-kappa-B p100 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2
E1824c ELISA kit Chicken,Gallus gallus,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
U1824c CLIA kit Chicken,Gallus gallus,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
E1824c ELISA Chicken,Gallus gallus,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
U1824c CLIA Chicken,Gallus gallus,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
U0616m CLIA Mouse,Mus musculus,Nfkb3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,Rela,Transcription factor p65 96T
E0616m ELISA kit Mouse,Mus musculus,Nfkb3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,Rela,Transcription factor p65 96T
E0616m ELISA Mouse,Mus musculus,Nfkb3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,Rela,Transcription factor p65 96T
E0616h ELISA Homo sapiens,Human,NFKB3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,RELA,Transcription factor p65 96T
U0616h CLIA Homo sapiens,Human,NFKB3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,RELA,Transcription factor p65 96T
E0616h ELISA kit Homo sapiens,Human,NFKB3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,RELA,Transcription factor p65 96T
E1824c ELISA Canis familiaris,Canis lupus familiaris,Dog,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur