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Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (H2TF1) (Lymphocyte translocation chromosome 10 protein) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) (Oncogene Lyt-10) (Lyt10) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]

 NFKB2_HUMAN             Reviewed;         900 AA.
Q00653; A8K9D9; D3DR83; Q04860; Q9BU75; Q9H471; Q9H472;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 4.
25-OCT-2017, entry version 216.
RecName: Full=Nuclear factor NF-kappa-B p100 subunit;
AltName: Full=DNA-binding factor KBF2;
AltName: Full=H2TF1;
AltName: Full=Lymphocyte translocation chromosome 10 protein;
AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2;
AltName: Full=Oncogene Lyt-10;
Short=Lyt10;
Contains:
RecName: Full=Nuclear factor NF-kappa-B p52 subunit;
Name=NFKB2; Synonyms=LYT10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
TISSUE=Leukemia;
PubMed=1876189; DOI=10.1038/352733a0;
Schmid R.M., Perkins N.D., Duckett C.S., Andrews P.C., Nabel G.J.;
"Cloning of an NF-kappa B subunit which stimulates HIV transcription
in synergy with p65.";
Nature 352:733-736(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1531086; DOI=10.1128/MCB.12.2.685;
Bours V., Burd P.R., Brown K., Villalobos J., Park S., Ryseck R.P.,
Bravo R., Kelly K., Siebenlist U.;
"A novel mitogen-inducible gene product related to p50/p105-NF-kappa B
participates in transactivation through a kappa B site.";
Mol. Cell. Biol. 12:685-695(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION, AND P80HT
GENERATION.
PubMed=8036016;
Thakur S., Lin H.C., Tseng W.T., Kumar S., Bravo R., Foss F.,
Gelinas C., Rabson A.B.;
"Rearrangement and altered expression of the NFKB-2 gene in human
cutaneous T-lymphoma cells.";
Oncogene 9:2335-2344(1994).
[4]
SEQUENCE REVISION.
Rabson A.B.;
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Thymus;
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 [GENOMIC DNA], AND VARIANTS LYS-14; ARG-351 AND
ARG-452.
NIEHS SNPs program;
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Lymph;
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).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-220.
PubMed=7969113; DOI=10.1128/MCB.14.12.7695;
Liptay S., Schmid R.M., Nabel E.G., Nabel G.J.;
"Transcriptional regulation of NF-kappa B2: evidence for kappa B-
mediated positive and negative autoregulation.";
Mol. Cell. Biol. 14:7695-7703(1994).
[12]
PROTEIN SEQUENCE OF 459-470; 580-597 AND 636-647 (ISOFORM 1).
PubMed=8360178;
Potter D.A., Larson C.J., Eckes P., Schmid R.M., Nabel G.J.,
Verdine G.L., Sharp P.A.;
"Purification of the major histocompatibility complex class I
transcription factor H2TF1. The full-length product of the nfkb2
gene.";
J. Biol. Chem. 268:18882-18890(1993).
[13]
IDENTIFICATION IN A COMPLEX WITH BCL3.
PubMed=8453667; DOI=10.1016/0092-8674(93)90401-B;
Bours V., Franzoso G., Azarenko V., Park S., Kanno T., Brown K.,
Siebenlist U.;
"The oncoprotein Bcl-3 directly transactivates through kappa B motifs
via association with DNA-binding p50B homodimers.";
Cell 72:729-739(1993).
[14]
FUNCTION, AND IDENTIFICATION IN THE NF-KAPPA-B RELB-P52 COMPLEX.
PubMed=7925301;
Dobrzanski P., Ryseck R.P., Bravo R.;
"Differential interactions of Rel-NF-kappa B complexes with I kappa B
alpha determine pools of constitutive and inducible NF-kappa B
activity.";
EMBO J. 13:4608-4616(1994).
[15]
IDENTIFICATION IN THE NF-KAPPA-B P52-C-REL COMPLEX, AND IDENTIFICATION
IN THE NF-KAPPA-B P65-P52 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).
[16]
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).
[17]
COTRANSLATIONAL FOLDING/PROCESSING OF P100, AND GENERATION OF
P52/P100.
PubMed=10597218; DOI=10.1038/sj.onc.1203022;
Heusch M., Lin L., Geleziunas R., Greene W.C.;
"The generation of nfkb2 p52: mechanism and efficiency.";
Oncogene 18:6201-6208(1999).
[18]
PHOSPHORYLATION AT SER-713; SER-715 AND SER-717, MUTAGENESIS,
DIMERIZATION, AND PROTEOLYTIC PROCESSING OF P100.
PubMed=8887665; DOI=10.1128/MCB.16.11.6363;
Betts J.C., Nabel G.J.;
"Differential regulation of NF-kappaB2(p100) processing and control by
amino-terminal sequences.";
Mol. Cell. Biol. 16:6363-6371(1996).
[19]
PHOSPHORYLATION AT SER-866 AND SER-870, MUTAGENESIS OF SER-866 AND
SER-870, AND PROTEOLYTIC PROCESSING OF P100.
PubMed=11239468; DOI=10.1016/S1097-2765(01)00187-3;
Xiao G., Harhaj E.W., Sun S.-C.;
"NF-kappaB-inducing kinase regulates the processing of NF-kappaB2
p100.";
Mol. Cell 7:401-409(2001).
[20]
CHROMOSOMAL TRANSLOCATION WITH IGHA1.
PubMed=1760839; DOI=10.1016/0092-8674(91)90285-7;
Neri A., Chang C.C., Lombardi L., Salina M., Corradini P.,
Maiolo A.T., Chaganti R.S., Dalla-Favera R.;
"B cell lymphoma-associated chromosomal translocation involves
candidate oncogene lyt-10, homologous to NF-kappa B p50.";
Cell 67:1075-1087(1991).
[21]
CHROMOSOMAL ABERRATIONS, AND GENERATION OF LB40 AND EB308.
PubMed=7949142;
Migliazza A., Lombardi L., Rocchi M., Trecca D., Chang C.-C.,
Antonacci R., Fracchiolla N.S., Ciana P., Maiolo A.T., Neri A.;
"Heterogeneous chromosomal aberrations generate 3' truncations of the
NFKB2/lyt-10 gene in lymphoid malignancies.";
Blood 84:3850-3860(1994).
[22]
CHARACTERIZATION OF THE TWO PROMOTER REGIONS.
PubMed=7541912; DOI=10.1093/nar/23.12.2328;
Lombardi L., Ciana P., Cappellini C., Trecca D., Guerrini L.,
Migliazza A., Maiolo A.T., Neri A.;
"Structural and functional characterization of the promoter regions of
the NFKB2 gene.";
Nucleic Acids Res. 23:2328-2336(1995).
[23]
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).
[24]
UBIQUITINATION AT LYS-855.
PubMed=14676825; DOI=10.1038/sj.onc.1207366;
Amir R.E., Haecker H., Karin M., Ciechanover A.;
"Mechanism of processing of the NF-kappa B2 p100 precursor:
identification of the specific polyubiquitin chain-anchoring lysine
residue and analysis of the role of NEDD8-modification on the
SCF(beta-TrCP) ubiquitin ligase.";
Oncogene 23:2540-2547(2004).
[25]
IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
PubMed=16477006; DOI=10.1073/pnas.0511096103;
Song Y.J., Jen K.Y., Soni V., Kieff E., Cahir-McFarland E.;
"IL-1 receptor-associated kinase 1 is critical for latent membrane
protein 1-induced p65/RelA serine 536 phosphorylation and NF-kappaB
activation.";
Proc. Natl. Acad. Sci. U.S.A. 103:2689-2694(2006).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429, AND 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).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[28]
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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-161 AND SER-812,
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).
[30]
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).
[31]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 37-327.
PubMed=9384586; DOI=10.1093/emboj/16.23.7078;
Cramer P., Larson C.J., Verdine G.L., Mueller C.W.;
"Structure of the human NF-kappaB p52 homodimer-DNA complex at 2.1-A
resolution.";
EMBO J. 16:7078-7090(1997).
[32]
STRUCTURE BY NMR OF 764-859.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the death domain of nuclear factor NF-kappa-B
p100.";
Submitted (DEC-2006) to the PDB data bank.
[33]
INVOLVEMENT IN CVID10.
PubMed=24140114; DOI=10.1016/j.ajhg.2013.09.009;
Chen K., Coonrod E.M., Kumanovics A., Franks Z.F., Durtschi J.D.,
Margraf R.L., Wu W., Heikal N.M., Augustine N.H., Ridge P.G.,
Hill H.R., Jorde L.B., Weyrich A.S., Zimmerman G.A., Gundlapalli A.V.,
Bohnsack J.F., Voelkerding K.V.;
"Germline mutations in NFKB2 implicate the noncanonical NF-kappaB
pathway in the pathogenesis of common variable immunodeficiency.";
Am. J. Hum. Genet. 93:812-824(2013).
[34]
VARIANTS CVID10 GLY-865 AND VAL-867.
PubMed=25524009; DOI=10.1186/s12881-014-0139-9;
Brue T., Quentien M.H., Khetchoumian K., Bensa M., Capo-Chichi J.M.,
Delemer B., Balsalobre A., Nassif C., Papadimitriou D.T., Pagnier A.,
Hasselmann C., Patry L., Schwartzentruber J., Souchon P.F.,
Takayasu S., Enjalbert A., Van Vliet G., Majewski J., Drouin J.,
Samuels M.E.;
"Mutations in NFKB2 and potential genetic heterogeneity in patients
with DAVID syndrome, having variable endocrine and immune
deficiencies.";
BMC Med. Genet. 15:139-139(2014).
-!- 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. 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. In a non-canonical activation pathway, the MAP3K14-
activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated
with RelB, inducing its proteolytic processing to NFKB2/p52 and
the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B
heterodimeric RelB-p52 complex is a transcriptional activator. The
NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2
appears to have dual functions such as cytoplasmic retention of
attached NF-kappa-B proteins by p100 and generation of p52 by a
cotranslational processing. The proteasome-mediated process
ensures the production of both p52 and p100 and preserves their
independent function. p52 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. p52 and p100 are
respectively the minor and major form; the processing of p100
being relatively poor. Isoform p49 is a subunit of the NF-kappa-B
protein complex, which stimulates the HIV enhancer in synergy with
p65. In concert with RELB, regulates the circadian clock by
repressing the transcriptional activator activity of the CLOCK-
ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:7925301}.
-!- SUBUNIT: Component of the NF-kappa-B RelB-p52 complex. Homodimer;
component of the NF-kappa-B p52-p52 complex. Component of the NF-
kappa-B p65-p52 complex. Component of the NF-kappa-B p52-c-Rel
complex. NFKB2/p52 interacts with NFKBIE. Component of a complex
consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Directly
interacts with MEN1. {ECO:0000269|PubMed:11526476,
ECO:0000269|PubMed:16477006, ECO:0000269|PubMed:7925301,
ECO:0000269|PubMed:8152812, ECO:0000269|PubMed:8453667,
ECO:0000269|PubMed:9315679}.
-!- INTERACTION:
P41279:MAP3K8; NbExp=2; IntAct=EBI-307326, EBI-354900;
O00255-2:MEN1; NbExp=3; IntAct=EBI-9869360, EBI-9869387;
P19838:NFKB1; NbExp=8; IntAct=EBI-307326, EBI-300010;
Q04864:REL; NbExp=3; IntAct=EBI-307326, EBI-307352;
Q01201:RELB; NbExp=3; IntAct=EBI-307326, EBI-357837;
P63165:SUMO1; NbExp=2; IntAct=EBI-307326, EBI-80140;
-!- 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; Synonyms=p100;
IsoId=Q00653-1; Sequence=Displayed;
Name=3; Synonyms=p49;
IsoId=Q00653-3; Sequence=VSP_040082, VSP_040083;
Note=Ref.1 (CAA43716.1) sequence(s) differ(s) from that shown
due to frameshifts in positions 407, 414.;
Name=4;
IsoId=Q00653-4; Sequence=VSP_040084;
-!- DOMAIN: The C-terminus of p100 might be involved in cytoplasmic
retention, inhibition of DNA-binding by p52 homodimers, and/or
transcription activation. {ECO:0000250}.
-!- DOMAIN: The glycine-rich region (GRR) appears to be a critical
element in the generation of p52.
-!- PTM: While translation occurs, the particular unfolded structure
after the GRR repeat promotes the generation of p52 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.
-!- PTM: Subsequent to MAP3K14-dependent serine phosphorylation, p100
polyubiquitination occurs then triggering its proteasome-dependent
processing. {ECO:0000269|PubMed:11239468,
ECO:0000269|PubMed:14676825, ECO:0000269|PubMed:8887665}.
-!- PTM: Constitutive processing is tightly suppressed by its C-
terminal processing inhibitory domain, named PID, which contains
the death domain.
-!- DISEASE: Note=A chromosomal aberration involving NFKB2 is found in
a case of B-cell non Hodgkin lymphoma (B-NHL). Translocation
t(10;14)(q24;q32) with IGHA1. The resulting oncogene is also
called Lyt-10C alpha variant.
-!- DISEASE: Note=A chromosomal aberration involving NFKB2 is found in
a cutaneous T-cell leukemia (C-TCL) cell line. This rearrangement
produces the p80HT gene which codes for a truncated 80 kDa protein
(p80HT).
-!- DISEASE: Note=In B-cell leukemia (B-CLL) cell line, LB40 and
EB308, can be found after heterogeneous chromosomal aberrations,
such as internal deletions.
-!- DISEASE: Immunodeficiency, common variable, 10 (CVID10)
[MIM:615577]: A primary immunodeficiency characterized by
childhood-onset of recurrent infections, hypogammaglobulinemia,
and decreased numbers of memory and marginal zone B-cells. Some
patients may develop autoimmune features and have circulating
autoantibodies. An unusual feature is central adrenal
insufficiency. {ECO:0000269|PubMed:24140114,
ECO:0000269|PubMed:25524009}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=CAA43715.1; Type=Frameshift; Positions=456, 458, 470, 900; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NFKB2ID362.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/nfkb2/";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X61498; CAA43715.1; ALT_FRAME; mRNA.
EMBL; X61499; CAA43716.1; ALT_FRAME; mRNA.
EMBL; S76638; AAB21124.1; -; mRNA.
EMBL; U09609; AAA21462.2; -; mRNA.
EMBL; BT009769; AAP88771.1; -; mRNA.
EMBL; AK292654; BAF85343.1; -; mRNA.
EMBL; AY865619; AAW56071.1; -; Genomic_DNA.
EMBL; AL121928; CAC08399.1; -; Genomic_DNA.
EMBL; CH471066; EAW49700.1; -; Genomic_DNA.
EMBL; CH471066; EAW49701.1; -; Genomic_DNA.
EMBL; CH471066; EAW49702.1; -; Genomic_DNA.
EMBL; CH471066; EAW49704.1; -; Genomic_DNA.
EMBL; CH471066; EAW49706.1; -; Genomic_DNA.
EMBL; BC002844; AAH02844.1; -; mRNA.
EMBL; U20816; AAA68171.1; -; Genomic_DNA.
CCDS; CCDS41564.1; -. [Q00653-1]
CCDS; CCDS41565.1; -. [Q00653-4]
PIR; A42024; A42024.
PIR; A57034; A57034.
PIR; I38609; I38609.
PIR; S17233; S17233.
RefSeq; NP_001070962.1; NM_001077494.3. [Q00653-1]
RefSeq; NP_001248332.1; NM_001261403.2. [Q00653-4]
RefSeq; NP_001275653.1; NM_001288724.1. [Q00653-4]
RefSeq; NP_001309863.1; NM_001322934.1. [Q00653-1]
RefSeq; NP_001309864.1; NM_001322935.1.
RefSeq; NP_002493.3; NM_002502.5. [Q00653-4]
UniGene; Hs.73090; -.
PDB; 1A3Q; X-ray; 2.10 A; A/B=37-327.
PDB; 2D96; NMR; -; A=766-859.
PDB; 3DO7; X-ray; 3.05 A; B=37-329.
PDB; 4OT9; X-ray; 3.35 A; A=407-765.
PDBsum; 1A3Q; -.
PDBsum; 2D96; -.
PDBsum; 3DO7; -.
PDBsum; 4OT9; -.
ProteinModelPortal; Q00653; -.
SMR; Q00653; -.
BioGrid; 110858; 53.
CORUM; Q00653; -.
DIP; DIP-24239N; -.
DIP; DIP-27535N; -.
IntAct; Q00653; 39.
MINT; MINT-7944680; -.
STRING; 9606.ENSP00000358983; -.
ChEMBL; CHEMBL3003; -.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB05487; CC-8490.
DrugBank; DB01296; Glucosamine.
DrugBank; DB05212; HE3286.
DrugBank; DB05767; HMPL-004.
DrugBank; DB05464; NOX-700.
DrugBank; DB05451; P54.
DrugBank; DB05471; SGN-30.
iPTMnet; Q00653; -.
PhosphoSitePlus; Q00653; -.
SwissPalm; Q00653; -.
DMDM; 116242678; -.
EPD; Q00653; -.
MaxQB; Q00653; -.
PaxDb; Q00653; -.
PeptideAtlas; Q00653; -.
PRIDE; Q00653; -.
DNASU; 4791; -.
Ensembl; ENST00000189444; ENSP00000189444; ENSG00000077150. [Q00653-4]
Ensembl; ENST00000369966; ENSP00000358983; ENSG00000077150. [Q00653-1]
Ensembl; ENST00000428099; ENSP00000410256; ENSG00000077150. [Q00653-4]
GeneID; 4791; -.
KEGG; hsa:4791; -.
UCSC; uc001kva.4; human. [Q00653-1]
CTD; 4791; -.
DisGeNET; 4791; -.
EuPathDB; HostDB:ENSG00000077150.17; -.
GeneCards; NFKB2; -.
HGNC; HGNC:7795; NFKB2.
HPA; CAB022098; -.
HPA; HPA008422; -.
HPA; HPA023900; -.
MalaCards; NFKB2; -.
MIM; 164012; gene.
MIM; 615577; phenotype.
neXtProt; NX_Q00653; -.
OpenTargets; ENSG00000077150; -.
Orphanet; 1572; Common variable immunodeficiency.
PharmGKB; PA31600; -.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00500000044765; -.
HOGENOM; HOG000004822; -.
HOVERGEN; HBG052613; -.
InParanoid; Q00653; -.
KO; K04469; -.
OMA; FRGHTPL; -.
OrthoDB; EOG091G03PF; -.
PhylomeDB; Q00653; -.
TreeFam; TF325632; -.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
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-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
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-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
SIGNOR; Q00653; -.
ChiTaRS; NFKB2; human.
EvolutionaryTrace; Q00653; -.
GeneWiki; NFKB2; -.
GenomeRNAi; 4791; -.
PMAP-CutDB; Q00653; -.
PRO; PR:Q00653; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000077150; -.
CleanEx; HS_NFKB2; -.
ExpressionAtlas; Q00653; baseline and differential.
Genevisible; Q00653; HS.
GO; GO:0033257; C:Bcl3/NF-kappaB2 complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0002268; P:follicular dendritic cell differentiation; IEA:Ensembl.
GO; GO:0002467; P:germinal center formation; IEA:Ensembl.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
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:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
CDD; cd00204; ANK; 2.
CDD; cd01177; IPT_NFkappaB; 1.
Gene3D; 1.25.40.20; -; 2.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; IPR000451; NFkB/Dor.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR030492; RHD_CS.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
InterPro; IPR037059; RHD_DNA_bind_dom_sf.
PANTHER; PTHR24169; PTHR24169; 1.
Pfam; PF12796; Ank_2; 2.
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; Activator; Alternative splicing; ANK repeat;
Biological rhythms; Chromosomal rearrangement; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 900 Nuclear factor NF-kappa-B p100 subunit.
/FTId=PRO_0000030321.
CHAIN 1 454 Nuclear factor NF-kappa-B p52 subunit.
/FTId=PRO_0000030322.
DOMAIN 38 343 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
REPEAT 487 519 ANK 1.
REPEAT 526 555 ANK 2.
REPEAT 559 591 ANK 3.
REPEAT 599 628 ANK 4.
REPEAT 633 663 ANK 5.
REPEAT 667 696 ANK 6.
REPEAT 729 758 ANK 7.
DOMAIN 764 851 Death.
REGION 346 377 GRR.
MOTIF 337 341 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 350 400 Gly-rich.
SITE 454 455 Cleavage (when cotranslationally
processed).
SITE 490 491 Breakpoint for translocation to form
NFKB2-IGHA1 oncogene.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 429 429 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 713 713 Phosphoserine.
{ECO:0000269|PubMed:8887665}.
MOD_RES 715 715 Phosphoserine.
{ECO:0000269|PubMed:8887665}.
MOD_RES 717 717 Phosphoserine.
{ECO:0000269|PubMed:8887665}.
MOD_RES 812 812 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 866 866 Phosphoserine; by MAP3K14.
{ECO:0000269|PubMed:11239468}.
MOD_RES 870 870 Phosphoserine; by MAP3K14.
{ECO:0000269|PubMed:11239468}.
CROSSLNK 855 855 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:14676825}.
VAR_SEQ 374 428 GSLGFFPSSLAYSPYQSGAGPMGCYPGGGGGAQMAATVPSR
DSGEEAAEPSAPSR -> EGVLMEGGVKVREAVEEKNLGEA
GRGLHACNPALWEAKAGRLPEIRSSRPAWPTA (in
isoform 3). {ECO:0000303|PubMed:1876189}.
/FTId=VSP_040082.
VAR_SEQ 429 900 Missing (in isoform 3).
{ECO:0000303|PubMed:1876189}.
/FTId=VSP_040083.
VAR_SEQ 860 860 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1876189,
ECO:0000303|Ref.5}.
/FTId=VSP_040084.
VARIANT 14 14 E -> K (in dbSNP:rs45581936).
{ECO:0000269|Ref.7}.
/FTId=VAR_022223.
VARIANT 351 351 G -> R (in dbSNP:rs45580031).
{ECO:0000269|Ref.7}.
/FTId=VAR_022224.
VARIANT 392 392 A -> G (in dbSNP:rs11574848).
/FTId=VAR_051781.
VARIANT 452 452 G -> R (in dbSNP:rs45471103).
{ECO:0000269|Ref.7}.
/FTId=VAR_022225.
VARIANT 618 900 Missing (in truncated form EB308).
/FTId=VAR_018452.
VARIANT 667 669 AGN -> SAS (in truncated form p80HT).
/FTId=VAR_006909.
VARIANT 670 900 Missing (in truncated form p80HT).
/FTId=VAR_006910.
VARIANT 703 900 Missing (in truncated form LB40).
/FTId=VAR_018453.
VARIANT 865 865 D -> G (in CVID10; unknown pathological
significance; de novo mutation;
dbSNP:rs727502787).
{ECO:0000269|PubMed:25524009}.
/FTId=VAR_074035.
VARIANT 867 867 A -> V (in CVID10; unknown pathological
significance; de novo mutation;
dbSNP:rs727502788).
{ECO:0000269|PubMed:25524009}.
/FTId=VAR_074036.
MUTAGEN 247 249 YLL->AAA: Two-fold reduction in
heterodimerization with RelA.
{ECO:0000269|PubMed:8887665}.
MUTAGEN 399 399 P->A: No change in cleavage rate or
products. {ECO:0000269|PubMed:8887665}.
MUTAGEN 404 404 G->A: No change in cleavage rate or
products. {ECO:0000269|PubMed:8887665}.
MUTAGEN 405 405 A->P: No change in cleavage rate or
products. {ECO:0000269|PubMed:8887665}.
MUTAGEN 406 406 Q->N: No change in cleavage rate or
products. {ECO:0000269|PubMed:8887665}.
MUTAGEN 713 713 S->G: Loss of phosphorylation; when
associated with A-715 and A-717.
{ECO:0000269|PubMed:8887665}.
MUTAGEN 715 715 S->A: Loss of phosphorylation; when
associated with G-713 and A-717.
{ECO:0000269|PubMed:8887665}.
MUTAGEN 717 717 S->A: Loss of phosphorylation; when
associated with G-713 and A-715.
{ECO:0000269|PubMed:8887665}.
MUTAGEN 866 866 S->A: Decrease in MAP3K14-induced
phosphorylation; no inducible processing
occurs; when associated with A-869.
{ECO:0000269|PubMed:11239468}.
MUTAGEN 870 870 S->A: Decrease in MAP3K14-induced
phosphorylation; no inducible processing
occurs; when associated with A-865.
{ECO:0000269|PubMed:11239468}.
CONFLICT 144 144 K -> E (in Ref. 2; AAB21124).
{ECO:0000305}.
CONFLICT 213 213 I -> T (in Ref. 1; CAA43715/CAA43716 and
11; AAA68171). {ECO:0000305}.
CONFLICT 396 396 G -> R (in Ref. 1; CAA43715).
{ECO:0000305}.
CONFLICT 433 434 EP -> DA (in Ref. 2; AAB21124).
{ECO:0000305}.
CONFLICT 459 459 R -> K (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 465 465 G -> C (in Ref. 1; CAA43715).
{ECO:0000305}.
CONFLICT 470 470 A -> R (in Ref. 1; CAA43715 and 2;
AAB21124). {ECO:0000305}.
CONFLICT 741 741 K -> L (in Ref. 1; CAA43715).
{ECO:0000305}.
CONFLICT 860 860 A -> T (in Ref. 2; AAB21124).
{ECO:0000305}.
CONFLICT 876 876 E -> K (in Ref. 2; AAB21124).
{ECO:0000305}.
CONFLICT 891 891 C -> S (in Ref. 1; CAA43715).
{ECO:0000305}.
STRAND 39 44 {ECO:0000244|PDB:1A3Q}.
STRAND 48 51 {ECO:0000244|PDB:1A3Q}.
TURN 56 58 {ECO:0000244|PDB:1A3Q}.
STRAND 79 83 {ECO:0000244|PDB:1A3Q}.
STRAND 87 96 {ECO:0000244|PDB:1A3Q}.
STRAND 98 101 {ECO:0000244|PDB:1A3Q}.
STRAND 106 111 {ECO:0000244|PDB:1A3Q}.
STRAND 116 118 {ECO:0000244|PDB:3DO7}.
STRAND 120 124 {ECO:0000244|PDB:1A3Q}.
STRAND 130 132 {ECO:0000244|PDB:1A3Q}.
STRAND 136 140 {ECO:0000244|PDB:1A3Q}.
TURN 143 145 {ECO:0000244|PDB:1A3Q}.
HELIX 146 158 {ECO:0000244|PDB:1A3Q}.
TURN 159 161 {ECO:0000244|PDB:1A3Q}.
HELIX 168 182 {ECO:0000244|PDB:1A3Q}.
STRAND 189 198 {ECO:0000244|PDB:1A3Q}.
STRAND 205 207 {ECO:0000244|PDB:3DO7}.
STRAND 217 219 {ECO:0000244|PDB:1A3Q}.
STRAND 220 222 {ECO:0000244|PDB:3DO7}.
TURN 223 225 {ECO:0000244|PDB:1A3Q}.
STRAND 230 234 {ECO:0000244|PDB:1A3Q}.
STRAND 236 239 {ECO:0000244|PDB:1A3Q}.
STRAND 240 242 {ECO:0000244|PDB:3DO7}.
STRAND 245 252 {ECO:0000244|PDB:1A3Q}.
TURN 255 257 {ECO:0000244|PDB:1A3Q}.
STRAND 258 264 {ECO:0000244|PDB:1A3Q}.
STRAND 266 268 {ECO:0000244|PDB:1A3Q}.
STRAND 270 273 {ECO:0000244|PDB:1A3Q}.
HELIX 278 280 {ECO:0000244|PDB:1A3Q}.
TURN 283 285 {ECO:0000244|PDB:1A3Q}.
STRAND 286 290 {ECO:0000244|PDB:1A3Q}.
STRAND 303 311 {ECO:0000244|PDB:1A3Q}.
TURN 312 314 {ECO:0000244|PDB:1A3Q}.
STRAND 321 326 {ECO:0000244|PDB:1A3Q}.
HELIX 439 467 {ECO:0000244|PDB:4OT9}.
HELIX 470 475 {ECO:0000244|PDB:4OT9}.
HELIX 476 480 {ECO:0000244|PDB:4OT9}.
HELIX 491 497 {ECO:0000244|PDB:4OT9}.
HELIX 501 512 {ECO:0000244|PDB:4OT9}.
TURN 513 515 {ECO:0000244|PDB:4OT9}.
HELIX 519 521 {ECO:0000244|PDB:4OT9}.
HELIX 530 536 {ECO:0000244|PDB:4OT9}.
HELIX 540 548 {ECO:0000244|PDB:4OT9}.
HELIX 563 567 {ECO:0000244|PDB:4OT9}.
HELIX 575 582 {ECO:0000244|PDB:4OT9}.
HELIX 586 588 {ECO:0000244|PDB:4OT9}.
TURN 589 593 {ECO:0000244|PDB:4OT9}.
TURN 597 599 {ECO:0000244|PDB:4OT9}.
HELIX 603 609 {ECO:0000244|PDB:4OT9}.
HELIX 613 621 {ECO:0000244|PDB:4OT9}.
TURN 631 633 {ECO:0000244|PDB:4OT9}.
HELIX 637 643 {ECO:0000244|PDB:4OT9}.
HELIX 647 654 {ECO:0000244|PDB:4OT9}.
TURN 655 657 {ECO:0000244|PDB:4OT9}.
HELIX 671 678 {ECO:0000244|PDB:4OT9}.
HELIX 681 689 {ECO:0000244|PDB:4OT9}.
TURN 733 735 {ECO:0000244|PDB:4OT9}.
HELIX 740 751 {ECO:0000244|PDB:4OT9}.
STRAND 752 754 {ECO:0000244|PDB:4OT9}.
HELIX 772 782 {ECO:0000244|PDB:2D96}.
STRAND 783 786 {ECO:0000244|PDB:2D96}.
HELIX 791 798 {ECO:0000244|PDB:2D96}.
HELIX 801 808 {ECO:0000244|PDB:2D96}.
HELIX 813 823 {ECO:0000244|PDB:2D96}.
HELIX 828 838 {ECO:0000244|PDB:2D96}.
HELIX 841 848 {ECO:0000244|PDB:2D96}.
SEQUENCE 900 AA; 96749 MW; 6BAD7038834783CA CRC64;
MESCYNPGLD GIIEYDDFKL NSSIVEPKEP APETADGPYL VIVEQPKQRG FRFRYGCEGP
SHGGLPGASS EKGRKTYPTV KICNYEGPAK IEVDLVTHSD PPRAHAHSLV GKQCSELGIC
AVSVGPKDMT AQFNNLGVLH VTKKNMMGTM IQKLQRQRLR SRPQGLTEAE QRELEQEAKE
LKKVMDLSIV RLRFSAFLRA SDGSFSLPLK PVISQPIHDS KSPGASNLKI SRMDKTAGSV
RGGDEVYLLC DKVQKDDIEV RFYEDDENGW QAFGDFSPTD VHKQYAIVFR TPPYHKMKIE
RPVTVFLQLK RKRGGDVSDS KQFTYYPLVE DKEEVQRKRR KALPTFSQPF GGGSHMGGGS
GGAAGGYGGA GGGGSLGFFP SSLAYSPYQS GAGPMGCYPG GGGGAQMAAT VPSRDSGEEA
AEPSAPSRTP QCEPQAPEML QRAREYNARL FGLAQRSARA LLDYGVTADA RALLAGQRHL
LTAQDENGDT PLHLAIIHGQ TSVIEQIVYV IHHAQDLGVV NLTNHLHQTP LHLAVITGQT
SVVSFLLRVG ADPALLDRHG DSAMHLALRA GAGAPELLRA LLQSGAPAVP QLLHMPDFEG
LYPVHLAVRA RSPECLDLLV DSGAEVEATE RQGGRTALHL ATEMEELGLV THLVTKLRAN
VNARTFAGNT PLHLAAGLGY PTLTRLLLKA GADIHAENEE PLCPLPSPPT SDSDSDSEGP
EKDTRSSFRG HTPLDLTCST KVKTLLLNAA QNTMEPPLTP PSPAGPGLSL GDTALQNLEQ
LLDGPEAQGS WAELAERLGL RSLVDTYRQT TSPSGSLLRS YELAGGDLAG LLEALSDMGL
EEGVRLLRGP ETRDKLPSTA EVKEDSAYGS QSVEQEAEKL GPPPEPPGGL CHGHPQPQVH


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Catalog number Product name Quantity
EIAAB27079 DNA-binding factor KBF2,H2TF1,Homo sapiens,Human,Lymphocyte translocation chromosome 10 protein,Lyt10,LYT10,NFKB2,Nuclear factor NF-kappa-B p100 subunit,Nuclear factor of kappa light polypeptide gene
18-003-42144 Nuclear factor NF-kappa-B p100 subunit - DNA-binding factor KBF2; H2TF1; Lymphocyte translocation chromosome 10; Oncogene Lyt-10; Lyt10 Polyclonal 0.05 mg Aff Pur
18-003-42271 Nuclear factor NF-kappa-B p100 subunit - DNA-binding factor KBF2; H2TF1; Lymphocyte translocation chromosome 10; Oncogene Lyt-10; Lyt10 Polyclonal 0.05 mg Aff Pur
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
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
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
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
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
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
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 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
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
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
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
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
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
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
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
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
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 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
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
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


 

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