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Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]

 NFKB2_MOUSE             Reviewed;         899 AA.
Q9WTK5;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
05-DEC-2018, entry version 161.
RecName: Full=Nuclear factor NF-kappa-B p100 subunit;
AltName: Full=DNA-binding factor KBF2;
AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2;
Contains:
RecName: Full=Nuclear factor NF-kappa-B p52 subunit;
Name=Nfkb2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=129/Sv;
PubMed=10398801; DOI=10.1007/s002510050548;
Paxian S., Liptay S., Adler G., Hameister H., Schmid R.M.;
"Genomic organization and chromosomal mapping of mouse nuclear factor
kappa B 2 (NFKB2).";
Immunogenetics 49:743-750(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-425, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-425, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-425, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION.
PubMed=22894897; DOI=10.4161/cc.21669;
Bellet M.M., Zocchi L., Sassone-Corsi P.;
"The RelB subunit of NFkappaB acts as a negative regulator of
circadian gene expression.";
Cell Cycle 11:3304-3311(2012).
-!- 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 (By similarity). In concert with RELB, regulates the circadian
clock by repressing the transcriptional activator activity of the
CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000250,
ECO:0000269|PubMed:22894897}.
-!- 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 (By
similarity). Directly interacts with MEN1 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q04863:Relb; NbExp=2; IntAct=EBI-1209166, EBI-1209145;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Note=Nuclear, but also found in the cytoplasm in an
inactive form complexed to an inhibitor (I-kappa-B).
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in lymph nodes and thymus.
{ECO:0000269|PubMed:10398801}.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Subsequent to MAP3K14-dependent serine phosphorylation, p100
polyubiquitination occurs then triggering its proteasome-dependent
processing. {ECO:0000250}.
-!- PTM: Constitutive processing is tightly suppressed by its C-
terminal processing inhibitory domain, named PID, which contains
the death domain. {ECO:0000250}.
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EMBL; AF155373; AAD39547.1; -; mRNA.
EMBL; AF135125; AAD39462.1; -; Genomic_DNA.
EMBL; AF155372; AAD39546.1; -; mRNA.
EMBL; BC027423; AAH27423.1; -; mRNA.
CCDS; CCDS29874.1; -.
RefSeq; NP_001170840.1; NM_001177369.1.
RefSeq; NP_062281.1; NM_019408.3.
UniGene; Mm.102365; -.
PDB; 3JV5; X-ray; 2.65 A; A/B/C/D=225-328.
PDB; 3JV6; X-ray; 2.78 A; B/D/F=225-331.
PDBsum; 3JV5; -.
PDBsum; 3JV6; -.
ProteinModelPortal; Q9WTK5; -.
SMR; Q9WTK5; -.
BioGrid; 201752; 7.
IntAct; Q9WTK5; 3.
MINT; Q9WTK5; -.
STRING; 10090.ENSMUSP00000072859; -.
ChEMBL; CHEMBL3879845; -.
iPTMnet; Q9WTK5; -.
PhosphoSitePlus; Q9WTK5; -.
SwissPalm; Q9WTK5; -.
EPD; Q9WTK5; -.
MaxQB; Q9WTK5; -.
PaxDb; Q9WTK5; -.
PRIDE; Q9WTK5; -.
Ensembl; ENSMUST00000073116; ENSMUSP00000072859; ENSMUSG00000025225.
Ensembl; ENSMUST00000111881; ENSMUSP00000107512; ENSMUSG00000025225.
GeneID; 18034; -.
KEGG; mmu:18034; -.
UCSC; uc008hst.2; mouse.
CTD; 4791; -.
MGI; MGI:1099800; Nfkb2.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00940000160968; -.
HOVERGEN; HBG052613; -.
InParanoid; Q9WTK5; -.
KO; K04469; -.
OMA; QKPLPHY; -.
OrthoDB; EOG091G03PF; -.
PhylomeDB; Q9WTK5; -.
TreeFam; TF325632; -.
Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-MMU-448706; Interleukin-1 processing.
Reactome; R-MMU-4755510; SUMOylation of immune response proteins.
Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
ChiTaRS; Nfkb2; mouse.
PRO; PR:Q9WTK5; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000025225; Expressed in 259 organ(s), highest expression level in spleen.
ExpressionAtlas; Q9WTK5; baseline and differential.
Genevisible; Q9WTK5; MM.
GO; GO:0033257; C:Bcl3/NF-kappaB2 complex; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0001077; F:proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
GO; GO:0002268; P:follicular dendritic cell differentiation; IMP:MGI.
GO; GO:0002467; P:germinal center formation; IMP:MGI.
GO; GO:0048535; P:lymph node development; TAS:MGI.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0048536; P:spleen development; IMP:MGI.
CDD; cd00204; ANK; 3.
CDD; cd01177; IPT_NFkappaB; 1.
Gene3D; 1.25.40.20; -; 1.
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_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT_dom.
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; 7.
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; ANK repeat; Biological rhythms;
Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 899 Nuclear factor NF-kappa-B p100 subunit.
/FTId=PRO_0000030323.
CHAIN 1 454 Nuclear factor NF-kappa-B p52 subunit.
/FTId=PRO_0000030324.
DOMAIN 35 224 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
REPEAT 487 516 ANK 1.
REPEAT 526 555 ANK 2.
REPEAT 559 590 ANK 3.
REPEAT 599 628 ANK 4.
REPEAT 633 663 ANK 5.
REPEAT 667 696 ANK 6.
REPEAT 729 755 ANK 7.
DOMAIN 764 851 Death.
REGION 346 377 GRR.
MOTIF 337 341 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 351 404 Gly-rich.
SITE 454 455 Cleavage (when cotranslationally
processed).
MOD_RES 23 23 Phosphoserine.
{ECO:0000250|UniProtKB:Q00653}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000250|UniProtKB:Q00653}.
MOD_RES 425 425 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 713 713 Phosphoserine.
{ECO:0000250|UniProtKB:Q00653}.
MOD_RES 715 715 Phosphoserine.
{ECO:0000250|UniProtKB:Q00653}.
MOD_RES 717 717 Phosphoserine.
{ECO:0000250|UniProtKB:Q00653}.
MOD_RES 812 812 Phosphoserine.
{ECO:0000250|UniProtKB:Q00653}.
MOD_RES 865 865 Phosphoserine; by MAP3K14.
{ECO:0000250|UniProtKB:Q00653}.
MOD_RES 869 869 Phosphoserine; by MAP3K14.
{ECO:0000250|UniProtKB:Q00653}.
CROSSLNK 855 855 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q00653}.
STRAND 230 234 {ECO:0000244|PDB:3JV5}.
STRAND 236 239 {ECO:0000244|PDB:3JV5}.
STRAND 245 252 {ECO:0000244|PDB:3JV5}.
HELIX 255 257 {ECO:0000244|PDB:3JV5}.
STRAND 258 263 {ECO:0000244|PDB:3JV5}.
TURN 265 268 {ECO:0000244|PDB:3JV6}.
STRAND 271 273 {ECO:0000244|PDB:3JV5}.
HELIX 278 280 {ECO:0000244|PDB:3JV5}.
HELIX 282 284 {ECO:0000244|PDB:3JV5}.
STRAND 286 290 {ECO:0000244|PDB:3JV5}.
STRAND 303 314 {ECO:0000244|PDB:3JV5}.
STRAND 321 326 {ECO:0000244|PDB:3JV5}.
SEQUENCE 899 AA; 96832 MW; 3E98619F7D1C8AC7 CRC64;
MDNCYDPGLD GIPEYDDFEF SPSIVEPKDP APETADGPYL VIVEQPKQRG FRFRYGCEGP
SHGGLPGASS EKGRKTYPTV KICNYEGPAK IEVDLVTHSD PPRAHAHSLV GKQCSELGVC
AVSVGPKDMT AQFNNLGVLH VTKKNMMEIM IQKLQRQRLR SKPQGLTEAE RRELEQEAKE
LKKVMDLSIV RLRFSAFLRA SDGSFSLPLK PVISQPIHDS KSPGASNLKI SRMDKTAGSV
RGGDEVYLLC DKVQKDDIEV RFYEDDENGW QAFGDFSPTD VHKQYAIVFR TPPYHKMKIE
RPVTVFLQLK RKRGGDVSDS KQFTYYPLVE DKEEVQRKRR KALPTFSQPF GGGSHMGGGS
GGSAGGYGGA GGGGSLGFFS SSLAYNPYQS GAAPMGCYPG GGGGAQMAGS RRDTDAGEGA
EEPRTPPEAP QGEPQALDTL QRAREYNARL FGLAQRSARA LLDYGVTADA RALLAGQRHL
LMAQDENGDT PLHLAIIHGQ TGVIEQIAHV IYHAQYLGVI NLTNHLHQTP LHLAVITGQT
RVVSFLLQVG ADPTLLDRHG DSALHLALRA GAAAPELLQA LLRSGAHAVP QILHMPDFEG
LYPVHLAVHA RSPECLDLLV DCGAEVEAPE RQGGRTALHL ATEMEELGLV THLVTKLHAN
VNARTFAGNT PLHLAAGLGS PTLTRLLLKA GADIHAENEE PLCPLPSPST SGSDSDSEGP
ERDTQRNFRG HTPLDLTCST KVKTLLLNAA QNTTEPPLAP PSPAGPGLSL GDAALQNLEQ
LLDGPEAQGS WAELAERLGL RSLVDTYRKT PSPSGSLLRS YKLAGGDLVG LLEALSDMGL
HEGVRLLKGP ETRDKLPSTE VKEDSAYGSQ SVEQEAEKLC PPPEPPGGLC HGHPQPQVH


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