NFKB2
entrez
4791
canonical
uniprot
Q00653
canonical
ensembl
ENSG00000077150
resolver
ensp
ENSP00000189444
resolver
ensp
ENSP00000358983
resolver
ensp
ENSP00000410256
resolver
ensp
ENSP00000498308
resolver
ensp
ENSP00000499294
resolver
ensp
ENSP00000571631
resolver
genesymbol
NFKB2
resolver
genesymbol_syn
LYT10
resolver
hgnc
HGNC:7795
resolver
uniprot
A8K9D9
resolver
uniprot
D3DR83
resolver
uniprot
Q04860
resolver
uniprot
Q9BU75
resolver
uniprot
Q9H471
resolver
uniprot
Q9H472
resolver
uniprot_entry
NFKB2_HUMAN
resolver
uniprot_sec
A8K9D9
resolver
uniprot_sec
D3DR83
resolver
uniprot_sec
Q04860
resolver
uniprot_sec
Q9BU75
resolver
uniprot_sec
Q9H471
resolver
uniprot_sec
Q9H472
resolver
amino_acid_sequence
MESCYNPGLDGIIEYDDFKLNSSIVEPKEPAPETADGPYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSELGICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRPQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSKSPGASNLKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDENGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVFLQLKRKRGGDVSDSKQFTYYPLVEDKEEVQRKRRKALPTFSQPFGGGSHMGGGSGGAAGGYGGAGGGGSLGFFPSSLAYSPYQSGAGPMGCYPGGGGGAQMAATVPSRDSGEEAAEPSAPSRTPQCEPQAPEMLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIVYVIHHAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPAVPQLLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPLPSPPTSDSDSDSEGPEKDTRSSFRGHTPLDLTCSTKVKTLLLNAAQNTMEPPLTPPSPAGPGLSLGDTALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRGPETRDKLPSTAEVKEDSAYGSQSVEQEAEKLGPPPEPPGGLCHGHPQPQVH
uniprot
proteins
disease_involvement
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 variants affecting the gene represented in this entry.
uniprot
proteins
function
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-BMAL1 heterodimer. {ECO:0000269|PubMed:7925301}.
uniprot
proteins
mass_dalton
96749
uniprot
proteins
mutagenesis
MUTAGEN 247..249; /note="YLL->AAA: Two-fold reduction in heterodimerization with RelA."; /evidence="ECO:0000269|PubMed:8887665"; MUTAGEN 399; /note="P->A: No change in cleavage rate or products."; /evidence="ECO:0000269|PubMed:8887665"; MUTAGEN 404; /note="G->A: No change in cleavage rate or products."; /evidence="ECO:0000269|PubMed:8887665"; MUTAGEN 405; /note="A->P: No change in cleavage rate or products."; /evidence="ECO:0000269|PubMed:8887665"; MUTAGEN 406; /note="Q->N: No change in cleavage rate or products."; /evidence="ECO:0000269|PubMed:8887665"; MUTAGEN 713; /note="S->G: Loss of phosphorylation; when associated with A-715 and A-717."; /evidence="ECO:0000269|PubMed:8887665"; MUTAGEN 715; /note="S->A: Loss of phosphorylation; when associated with G-713 and A-717."; /evidence="ECO:0000269|PubMed:8887665"; MUTAGEN 717; /note="S->A: Loss of phosphorylation; when associated with G-713 and A-715."; /evidence="ECO:0000269|PubMed:8887665"; MUTAGEN 866; /note="S->A: Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-869."; /evidence="ECO:0000269|PubMed:11239468"; MUTAGEN 870; /note="S->A: Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-865."; /evidence="ECO:0000269|PubMed:11239468
uniprot
proteins
post_translational_modification
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.; PTM: Ubiquitinated by TRIM55; leading to processing by VCP and subsequent ubiquitin-dependent protein degradation by the proteasome. {ECO:0000269|PubMed:37816088}.
uniprot
proteins
pubmed
10597218
uniprot
proteins
pubmed
11239468
uniprot
proteins
pubmed
11526476
uniprot
proteins
pubmed
14676825
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
1531086
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16477006
uniprot
proteins
pubmed
1760839
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
1876189
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24140114
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25524009
uniprot
proteins
pubmed
37816088
uniprot
proteins
pubmed
7541912
uniprot
proteins
pubmed
7925301
uniprot
proteins
pubmed
7949142
uniprot
proteins
pubmed
7969113
uniprot
proteins
pubmed
8036016
uniprot
proteins
pubmed
8152812
uniprot
proteins
pubmed
8360178
uniprot
proteins
pubmed
8453667
uniprot
proteins
pubmed
8887665
uniprot
proteins
pubmed
9315679
uniprot
proteins
pubmed
9384586
uniprot
proteins
sequence_length
900
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).
uniprot
proteins