ID   RELB_MOUSE              Reviewed;         558 AA.
AC   Q04863; Q8VE46;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Transcription factor RelB;
GN   Name=Relb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1732739; DOI=10.1128/mcb.12.2.674-684.1992;
RA   Ryseck R.P., Bull P., Takamiya M., Bours V., Siebenlist U., Dobrzanski P.,
RA   Bravo R.;
RT   "RelB, a new Rel family transcription activator that can interact with p50-
RT   NF-kappa B.";
RL   Mol. Cell. Biol. 12:674-684(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-116.
RX   PubMed=8441398; DOI=10.1128/mcb.13.3.1572-1582.1993;
RA   Dobrzanski P., Ryseck R.P., Bravo R.;
RT   "Both N- and C-terminal domains of RelB are required for full
RT   transactivation: role of the N-terminal leucine zipper-like motif.";
RL   Mol. Cell. Biol. 13:1572-1582(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 309-429.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=7845467; DOI=10.1038/373531a0;
RA   Burkly L., Hession C., Ogata L., Reilly C., Marconi L.A., Olson D.,
RA   Tizard R., Cate R., Lo D.;
RT   "Expression of relB is required for the development of thymic medulla and
RT   dendritic cells.";
RL   Nature 373:531-536(1995).
RN   [6]
RP   PHOSPHORYLATION AT THR-84 AND SER-552.
RX   PubMed=11781828; DOI=10.1038/sj.onc.1204884;
RA   Marienfeld R., Berberich-Siebelt F., Berberich I., Denk A., Serfling E.,
RA   Neumann M.;
RT   "Signal-specific and phosphorylation-dependent RelB degradation: a
RT   potential mechanism of NF-kappaB control.";
RL   Oncogene 20:8142-8147(2001).
RN   [7]
RP   INTERACTION WITH NFKBID.
RX   PubMed=11931770; DOI=10.1016/s1097-2765(02)00469-0;
RA   Fiorini E., Schmitz I., Marissen W.E., Osborn S.L., Touma M., Sasada T.,
RA   Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M., Reinherz E.L.,
RA   Clayton L.K.;
RT   "Peptide-induced negative selection of thymocytes activates transcription
RT   of an NF-kappa B inhibitor.";
RL   Mol. Cell 9:637-648(2002).
RN   [8]
RP   SELF-ASSOCIATION, INTERACTION WITH NFKB1 AND NFKB2, AND MUTAGENESIS OF
RP   SER-368.
RX   PubMed=12874295; DOI=10.1074/jbc.m301521200;
RA   Maier H.J., Marienfeld R., Wirth T., Baumann B.;
RT   "Critical role of RelB serine 368 for dimerization and p100
RT   stabilization.";
RL   J. Biol. Chem. 278:39242-39250(2003).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH BMAL1.
RX   PubMed=22894897; DOI=10.4161/cc.21669;
RA   Bellet M.M., Zocchi L., Sassone-Corsi P.;
RT   "The RelB subunit of NFkappaB acts as a negative regulator of circadian
RT   gene expression.";
RL   Cell Cycle 11:3304-3311(2012).
RN   [10]
RP   FUNCTION.
RX   PubMed=22565310; DOI=10.1172/jci60144;
RA   Hamidi T., Algul H., Cano C.E., Sandi M.J., Molejon M.I., Riemann M.,
RA   Calvo E.L., Lomberk G., Dagorn J.C., Weih F., Urrutia R., Schmid R.M.,
RA   Iovanna J.L.;
RT   "Nuclear protein 1 promotes pancreatic cancer development and protects
RT   cells from stress by inhibiting apoptosis.";
RL   J. Clin. Invest. 122:2092-2103(2012).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 277-378.
RX   PubMed=16154093; DOI=10.1016/j.str.2005.06.018;
RA   Huang D.B., Vu D., Ghosh G.;
RT   "NF-kappaB RelB forms an intertwined homodimer.";
RL   Structure 13:1365-1373(2005).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 91-378 IN COMPLEX WITH NFKB1.
RX   PubMed=17869269; DOI=10.1016/j.jmb.2007.08.039;
RA   Moorthy A.K., Huang D.B., Wang V.Y., Vu D., Ghosh G.;
RT   "X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of
RT   multiple dimers on tandem kappaB sites.";
RL   J. Mol. Biol. 373:723-734(2007).
CC   -!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor which is
CC       present in almost all cell types and is involved in many biological
CC       processed such as inflammation, immunity, differentiation, cell growth,
CC       tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric
CC       complex formed by the Rel-like domain-containing proteins RELA/p65,
CC       RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at
CC       kappa-B sites in the DNA of their target genes and the individual
CC       dimers have distinct preferences for different kappa-B sites that they
CC       can bind with distinguishable affinity and specificity. Different dimer
CC       combinations act as transcriptional activators or repressors,
CC       respectively. NF-kappa-B is controlled by various mechanisms of post-
CC       translational modification and subcellular compartmentalization as well
CC       as by interactions with other cofactors or corepressors. NF-kappa-B
CC       complexes are held in the cytoplasm in an inactive state complexed with
CC       members of the NF-kappa-B inhibitor (I-kappa-B) family. In a
CC       conventional activation pathway, I-kappa-B is phosphorylated by I-
CC       kappa-B kinases (IKKs) in response to different activators,
CC       subsequently degraded thus liberating the active NF-kappa-B complex
CC       which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50
CC       and RelB-p52 complexes are transcriptional activators. RELB neither
CC       associates with DNA nor with RELA/p65 or REL. Stimulates promoter
CC       activity in the presence of NFKB2/p49 (By similarity). As a member of
CC       the NUPR1/RELB/IER3 survival pathway, may allow the development of
CC       pancreatic intraepithelial neoplasias. Regulates the circadian clock by
CC       repressing the transcriptional activator activity of the CLOCK-BMAL1
CC       heterodimer in a CRY1/CRY2 independent manner. Increased repression of
CC       the heterodimer is seen in the presence of NFKB2/p52. Is required for
CC       both T and B lymphocyte maturation and function (By similarity).
CC       {ECO:0000250|UniProtKB:Q01201, ECO:0000269|PubMed:22565310,
CC       ECO:0000269|PubMed:22894897}.
CC   -!- SUBUNIT: Component of the NF-kappa-B RelB-p50 complex. Component of the
CC       NF-kappa-B RelB-p52 complex (By similarity). Self-associates; the
CC       interaction seems to be transient and may prevent degradation allowing
CC       for heterodimer formation p50 or p52. Interacts with NFKB1/p50,
CC       NFKB2/p52 and NFKB2/p100. Interacts with NFKBID. Interacts with BMAL1
CC       and the interaction is enhanced in the presence of CLOCK. {ECO:0000250,
CC       ECO:0000269|PubMed:11931770, ECO:0000269|PubMed:12874295,
CC       ECO:0000269|PubMed:17869269, ECO:0000269|PubMed:22894897}.
CC   -!- INTERACTION:
CC       Q04863; PRO_0000030313 [P25799]: Nfkb1; NbExp=2; IntAct=EBI-1209145, EBI-1209141;
CC       Q04863; Q9WTK5: Nfkb2; NbExp=3; IntAct=EBI-1209145, EBI-1209166;
CC       Q04863; Q9Z1E3: Nfkbia; NbExp=4; IntAct=EBI-1209145, EBI-644427;
CC       Q04863; O54910: Nfkbie; NbExp=2; IntAct=EBI-1209145, EBI-6688774;
CC       Q04863; Q04863: Relb; NbExp=3; IntAct=EBI-1209145, EBI-1209145;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250}. Note=Colocalizes with NEK6
CC       in the centrosome. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in intestine, thymus and spleen.
CC       Undetectable in liver, bome marrow, kidney and testis.
CC   -!- DOMAIN: Both N- and C-terminal domains are required for transcriptional
CC       activation.
CC   -!- PTM: Phosphorylation at 'Thr-103' and 'Ser-573' is followed by
CC       proteasomal degradation. {ECO:0000269|PubMed:11781828}.
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DR   EMBL; M83380; AAA40041.1; -; mRNA.
DR   EMBL; AK146932; BAE27543.1; -; mRNA.
DR   EMBL; BC019765; AAH19765.1; -; mRNA.
DR   EMBL; BC117793; AAI17794.1; -; mRNA.
DR   EMBL; S56076; AAB25493.2; -; mRNA.
DR   EMBL; S76754; AAB33259.1; -; Genomic_DNA.
DR   CCDS; CCDS39799.1; -.
DR   PIR; A42023; A42023.
DR   PIR; I58091; I58091.
DR   RefSeq; NP_001277386.1; NM_001290457.1.
DR   RefSeq; NP_033072.2; NM_009046.2.
DR   PDB; 1ZK9; X-ray; 2.18 A; A=277-378.
DR   PDB; 1ZKA; X-ray; 2.20 A; A=277-378.
DR   PDB; 2V2T; X-ray; 3.05 A; A=91-378.
DR   PDB; 3DO7; X-ray; 3.05 A; A=88-383.
DR   PDB; 3JSS; X-ray; 2.60 A; A=278-378.
DR   PDB; 3JUZ; X-ray; 2.51 A; A=278-378.
DR   PDB; 3JV0; X-ray; 2.65 A; A=278-378.
DR   PDB; 3JV4; X-ray; 3.15 A; A/C/E=278-378.
DR   PDB; 3JV6; X-ray; 2.78 A; A/C/E=278-378.
DR   PDB; 4JGM; X-ray; 3.00 A; A=277-378.
DR   PDB; 4JHB; X-ray; 2.44 A; A=277-378.
DR   PDBsum; 1ZK9; -.
DR   PDBsum; 1ZKA; -.
DR   PDBsum; 2V2T; -.
DR   PDBsum; 3DO7; -.
DR   PDBsum; 3JSS; -.
DR   PDBsum; 3JUZ; -.
DR   PDBsum; 3JV0; -.
DR   PDBsum; 3JV4; -.
DR   PDBsum; 3JV6; -.
DR   PDBsum; 4JGM; -.
DR   PDBsum; 4JHB; -.
DR   AlphaFoldDB; Q04863; -.
DR   SMR; Q04863; -.
DR   BioGRID; 202854; 5.
DR   DIP; DIP-39585N; -.
DR   IntAct; Q04863; 10.
DR   MINT; Q04863; -.
DR   STRING; 10090.ENSMUSP00000092355; -.
DR   iPTMnet; Q04863; -.
DR   PhosphoSitePlus; Q04863; -.
DR   jPOST; Q04863; -.
DR   MaxQB; Q04863; -.
DR   PaxDb; 10090-ENSMUSP00000092355; -.
DR   PeptideAtlas; Q04863; -.
DR   ProteomicsDB; 253203; -.
DR   Pumba; Q04863; -.
DR   Antibodypedia; 3573; 768 antibodies from 43 providers.
DR   DNASU; 19698; -.
DR   Ensembl; ENSMUST00000094762.10; ENSMUSP00000092355.4; ENSMUSG00000002983.18.
DR   Ensembl; ENSMUST00000098754.5; ENSMUSP00000096350.5; ENSMUSG00000002983.18.
DR   GeneID; 19698; -.
DR   KEGG; mmu:19698; -.
DR   UCSC; uc012fbg.1; mouse.
DR   AGR; MGI:103289; -.
DR   CTD; 5971; -.
DR   MGI; MGI:103289; Relb.
DR   VEuPathDB; HostDB:ENSMUSG00000002983; -.
DR   eggNOG; ENOG502QV8A; Eukaryota.
DR   GeneTree; ENSGT00940000160230; -.
DR   InParanoid; Q04863; -.
DR   OMA; NQYREGA; -.
DR   OrthoDB; 1059550at2759; -.
DR   PhylomeDB; Q04863; -.
DR   TreeFam; TF325632; -.
DR   Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR   Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR   BioGRID-ORCS; 19698; 3 hits in 81 CRISPR screens.
DR   ChiTaRS; Relb; mouse.
DR   EvolutionaryTrace; Q04863; -.
DR   PRO; PR:Q04863; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q04863; Protein.
DR   Bgee; ENSMUSG00000002983; Expressed in peripheral lymph node and 139 other cell types or tissues.
DR   ExpressionAtlas; Q04863; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0000785; C:chromatin; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0019882; P:antigen processing and presentation; IMP:MGI.
DR   GO; GO:0007249; P:canonical NF-kappaB signal transduction; IBA:GO_Central.
DR   GO; GO:0071470; P:cellular response to osmotic stress; ISO:MGI.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0030098; P:lymphocyte differentiation; ISO:MGI.
DR   GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:MGI.
DR   GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR   GO; GO:0045063; P:T-helper 1 cell differentiation; IMP:MGI.
DR   GO; GO:0042088; P:T-helper 1 type immune response; IMP:MGI.
DR   CDD; cd01177; IPT_NFkappaB; 1.
DR   CDD; cd07886; RHD-n_RelB; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.40.340; Rel homology domain (RHD), DNA-binding domain; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_dom.
DR   InterPro; IPR033926; IPT_NFkappaB.
DR   InterPro; IPR000451; NFkB/Dor.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR032399; RelB_leu_zip.
DR   InterPro; IPR030496; RelB_RHD_N.
DR   InterPro; IPR032400; RelB_transact.
DR   InterPro; IPR030492; RHD_CS.
DR   InterPro; IPR032397; RHD_dimer.
DR   InterPro; IPR011539; RHD_DNA_bind_dom.
DR   InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR   PANTHER; PTHR24169; NUCLEAR FACTOR NF-KAPPA-B PROTEIN; 1.
DR   PANTHER; PTHR24169:SF18; TRANSCRIPTION FACTOR RELB; 1.
DR   Pfam; PF16180; RelB_leu_zip; 1.
DR   Pfam; PF16181; RelB_transactiv; 1.
DR   Pfam; PF16179; RHD_dimer; 1.
DR   Pfam; PF00554; RHD_DNA_bind; 1.
DR   PRINTS; PR00057; NFKBTNSCPFCT.
DR   SMART; SM00429; IPT; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 1.
DR   PROSITE; PS01204; REL_1; 1.
DR   PROSITE; PS50254; REL_2; 1.
DR   Genevisible; Q04863; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Biological rhythms; Cytoplasm; Cytoskeleton;
KW   Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..558
FT                   /note="Transcription factor RelB"
FT                   /id="PRO_0000205174"
FT   DOMAIN          103..418
FT                   /note="RHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          22..50
FT                   /note="Leucine-zipper"
FT   MOTIF           387..391
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           411..416
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01201"
FT   MOD_RES         84
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:11781828"
FT   MOD_RES         552
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:11781828"
FT   MUTAGEN         368
FT                   /note="S->A,E: Strongly reduces transcriptional activity
FT                   and interaction with NFKB1/p50 and NFKB2/p52."
FT                   /evidence="ECO:0000269|PubMed:12874295"
FT   CONFLICT        51
FT                   /note="D -> V (in Ref. 1; AAA40041)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        142
FT                   /note="L -> Q (in Ref. 1; AAA40041)"
FT                   /evidence="ECO:0000305"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:3DO7"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:3DO7"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:3DO7"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          156..160
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          165..168
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          173..178
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          186..190
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   TURN            192..194
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          197..199
FT                   /evidence="ECO:0007829|PDB:3DO7"
FT   STRAND          204..207
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   TURN            210..212
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   HELIX           213..222
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          234..236
FT                   /evidence="ECO:0007829|PDB:3DO7"
FT   STRAND          241..245
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          255..257
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          270..274
FT                   /evidence="ECO:0007829|PDB:3DO7"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:2V2T"
FT   STRAND          279..281
FT                   /evidence="ECO:0007829|PDB:1ZKA"
FT   STRAND          283..287
FT                   /evidence="ECO:0007829|PDB:1ZK9"
FT   STRAND          289..292
FT                   /evidence="ECO:0007829|PDB:4JHB"
FT   STRAND          297..299
FT                   /evidence="ECO:0007829|PDB:3DO7"
FT   STRAND          301..304
FT                   /evidence="ECO:0007829|PDB:1ZK9"
FT   HELIX           308..310
FT                   /evidence="ECO:0007829|PDB:1ZKA"
FT   STRAND          314..317
FT                   /evidence="ECO:0007829|PDB:1ZK9"
FT   STRAND          320..323
FT                   /evidence="ECO:0007829|PDB:1ZK9"
FT   HELIX           328..330
FT                   /evidence="ECO:0007829|PDB:1ZK9"
FT   TURN            333..335
FT                   /evidence="ECO:0007829|PDB:4JHB"
FT   STRAND          336..340
FT                   /evidence="ECO:0007829|PDB:4JHB"
FT   STRAND          353..357
FT                   /evidence="ECO:0007829|PDB:1ZK9"
FT   TURN            362..364
FT                   /evidence="ECO:0007829|PDB:1ZK9"
FT   STRAND          371..375
FT                   /evidence="ECO:0007829|PDB:1ZK9"
SQ   SEQUENCE   558 AA;  60305 MW;  AA49781A891ED7B8 CRC64;
     MPSRRAARES APELGALGSS DLSSLSLTVS RTTDELEIID EYIKENGFGL DGTQLSEMPR
     LVPRGPASLS SVTLGPAAPP PPATPSWSCT LGRLVSPGPC PRPYLVITEQ PKQRGMRFRY
     ECEGRSAGSI LGESSTEASK TLPAIELRDC GGLREVEVTA CLVWKDWPHR VHPHSLVGKD
     CTDGVCRVRL RPHVSPRHSF NNLGIQCVRK KEIEAAIERK IQLGIDPYNA GSLKNHQEVD
     MNVVRICFQA SYRDQQGHLH RMDPILSEPV YDKKSTNTSE LRICRINKES GPCTGGEELY
     LLCDKVQKED ISVVFSTASW EGRADFSQAD VHRQIAIVFK TPPYEDLEIS EPVTVNVFLQ
     RLTDGVCSEP LPFTYLPRDH DSYGVDKKRK RGLPDVLGEL SSSDPHGIES KRRKKKPVFL
     DHFLPGHSSG LFLPPSALQP ADSDFFPASI SLPGLEPPGG PDLLDDGFAY DPSAPTLFTM
     LDLLPPAPPL ASAVVGSGGA GATVVESSGP EPLSLDSFAA PGPGDVGTAS LVGSNMFPNQ
     YREAAFGGGL LSPGPEAT
//