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Q00653

- NFKB2_HUMAN

UniProt

Q00653 - NFKB2_HUMAN

Protein

Nuclear factor NF-kappa-B p100 subunit

Gene

NFKB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 183 (01 Oct 2014)
      Sequence version 4 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei454 – 4552Cleavage (when cotranslationally processed)
    Sitei490 – 4912Breakpoint for translocation to form NFKB2-IGHA1 oncogene

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: BHF-UCL
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc
    4. transcription coactivator activity Source: ProtInc

    GO - Biological processi

    1. extracellular matrix organization Source: Ensembl
    2. follicular dendritic cell differentiation Source: Ensembl
    3. germinal center formation Source: Ensembl
    4. innate immune response Source: Reactome
    5. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    6. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    7. positive regulation of NF-kappaB transcription factor activity Source: Reactome
    8. positive regulation of type I interferon production Source: Reactome
    9. regulation of transcription, DNA-templated Source: UniProtKB
    10. spleen development Source: Ensembl
    11. toll-like receptor 10 signaling pathway Source: Reactome
    12. toll-like receptor 2 signaling pathway Source: Reactome
    13. toll-like receptor 3 signaling pathway Source: Reactome
    14. toll-like receptor 4 signaling pathway Source: Reactome
    15. toll-like receptor 5 signaling pathway Source: Reactome
    16. toll-like receptor 9 signaling pathway Source: Reactome
    17. toll-like receptor signaling pathway Source: Reactome
    18. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    19. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    20. transcription, DNA-templated Source: UniProtKB-KW
    21. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_23950. Interleukin-1 processing.
    REACT_24969. TRAF6 mediated NF-kB activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear factor NF-kappa-B p100 subunit
    Alternative name(s):
    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
    Short name:
    Lyt10
    Cleaved into the following chain:
    Gene namesi
    Name:NFKB2
    Synonyms:LYT10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:7795. NFKB2.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).

    GO - Cellular componenti

    1. Bcl3/NF-kappaB2 complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.
    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).
    In B-cell leukemia (B-CLL) cell line, LB40 and EB308, can be found after heterogeneous chromosomal aberrations, such as internal deletions.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi247 – 2493YLL → AAA: Two-fold reduction in heterodimerization with RelA. 1 Publication
    Mutagenesisi399 – 3991P → A: No change in cleavage rate or products. 1 Publication
    Mutagenesisi404 – 4041G → A: No change in cleavage rate or products. 1 Publication
    Mutagenesisi405 – 4051A → P: No change in cleavage rate or products. 1 Publication
    Mutagenesisi406 – 4061Q → N: No change in cleavage rate or products. 1 Publication
    Mutagenesisi713 – 7131S → G: Loss of phosphorylation; when associated with A-715 and A-717. 1 Publication
    Mutagenesisi715 – 7151S → A: Loss of phosphorylation; when associated with G-713 and A-717. 1 Publication
    Mutagenesisi717 – 7171S → A: Loss of phosphorylation; when associated with G-713 and A-715. 1 Publication
    Mutagenesisi866 – 8661S → A: Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-869. 2 Publications
    Mutagenesisi870 – 8701S → A: Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-865. 2 Publications

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi615577. phenotype.
    Orphaneti1572. Common variable immunodeficiency.
    PharmGKBiPA31600.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 900900Nuclear factor NF-kappa-B p100 subunitPRO_0000030321Add
    BLAST
    Chaini1 – 454454Nuclear factor NF-kappa-B p52 subunitPRO_0000030322Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei429 – 4291Phosphothreonine1 Publication
    Modified residuei713 – 7131Phosphoserine1 Publication
    Modified residuei715 – 7151Phosphoserine1 Publication
    Modified residuei717 – 7171Phosphoserine1 Publication
    Cross-linki855 – 855Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei866 – 8661Phosphoserine; by MAP3K141 Publication
    Modified residuei870 – 8701Phosphoserine; by MAP3K141 Publication

    Post-translational modificationi

    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.
    Subsequent to MAP3K14-dependent serine phosphorylation, p100 polyubiquitination occurs then triggering its proteasome-dependent processing.4 Publications
    Constitutive processing is tightly suppressed by its C-terminal processing inhibitory domain, named PID, which contains the death domain.

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ00653.
    PaxDbiQ00653.
    PRIDEiQ00653.

    PTM databases

    PhosphoSiteiQ00653.

    Miscellaneous databases

    PMAP-CutDBQ00653.

    Expressioni

    Gene expression databases

    ArrayExpressiQ00653.
    BgeeiQ00653.
    CleanExiHS_NFKB2.
    GenevestigatoriQ00653.

    Organism-specific databases

    HPAiCAB022098.
    HPA008422.
    HPA023900.

    Interactioni

    Subunit structurei

    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 MEN1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NFKB1P198384EBI-307326,EBI-300010
    RELQ048643EBI-307326,EBI-307352
    RELBQ012013EBI-307326,EBI-357837
    SUMO1P631652EBI-307326,EBI-80140

    Protein-protein interaction databases

    BioGridi110858. 48 interactions.
    DIPiDIP-24239N.
    DIP-27535N.
    IntActiQ00653. 30 interactions.
    MINTiMINT-7944680.
    STRINGi9606.ENSP00000189444.

    Structurei

    Secondary structure

    1
    900
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 446
    Beta strandi48 – 514
    Turni56 – 583
    Beta strandi79 – 835
    Beta strandi87 – 9610
    Beta strandi98 – 1014
    Beta strandi106 – 1116
    Beta strandi116 – 1183
    Beta strandi120 – 1245
    Beta strandi130 – 1323
    Beta strandi136 – 1405
    Turni143 – 1453
    Helixi146 – 15813
    Turni159 – 1613
    Helixi168 – 18215
    Beta strandi189 – 19810
    Beta strandi205 – 2073
    Beta strandi217 – 2193
    Beta strandi220 – 2223
    Turni223 – 2253
    Beta strandi230 – 2345
    Beta strandi236 – 2394
    Beta strandi240 – 2423
    Beta strandi245 – 2528
    Turni255 – 2573
    Beta strandi258 – 2647
    Beta strandi266 – 2683
    Beta strandi270 – 2734
    Helixi278 – 2803
    Turni283 – 2853
    Beta strandi286 – 2905
    Beta strandi303 – 3119
    Turni312 – 3143
    Beta strandi321 – 3266
    Helixi772 – 78211
    Beta strandi783 – 7864
    Helixi791 – 7988
    Helixi801 – 8088
    Helixi813 – 82311
    Helixi828 – 83811
    Helixi841 – 8488

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A3QX-ray2.10A/B37-327[»]
    2D96NMR-A766-859[»]
    3DO7X-ray3.05B37-329[»]
    ProteinModelPortaliQ00653.
    SMRiQ00653. Positions 37-329, 434-752, 772-859.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00653.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 343306RHDPROSITE-ProRule annotationAdd
    BLAST
    Repeati487 – 51933ANK 1Add
    BLAST
    Repeati526 – 55530ANK 2Add
    BLAST
    Repeati559 – 59133ANK 3Add
    BLAST
    Repeati599 – 62830ANK 4Add
    BLAST
    Repeati633 – 66331ANK 5Add
    BLAST
    Repeati667 – 69630ANK 6Add
    BLAST
    Repeati729 – 75830ANK 7Add
    BLAST
    Domaini764 – 85188DeathAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni346 – 37732GRRAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi337 – 3415Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi350 – 40051Gly-richAdd
    BLAST

    Domaini

    The C-terminus of p100 might be involved in cytoplasmic retention, inhibition of DNA-binding by p52 homodimers, and/or transcription activation.By similarity
    The glycine-rich region (GRR) appears to be a critical element in the generation of p52.

    Sequence similaritiesi

    Contains 7 ANK repeats.PROSITE-ProRule annotation
    Contains 1 death domain.Curated
    Contains 1 RHD (Rel-like) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000004822.
    HOVERGENiHBG052613.
    InParanoidiQ00653.
    KOiK04469.
    OMAiFRGHTPL.
    OrthoDBiEOG7W154S.
    PhylomeDBiQ00653.
    TreeFamiTF325632.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    1.25.40.20. 1 hit.
    2.60.40.10. 1 hit.
    2.60.40.340. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    IPR000451. NF_Rel_Dor.
    IPR008967. p53-like_TF_DNA-bd.
    IPR011539. RHD.
    [Graphical view]
    PfamiPF00023. Ank. 5 hits.
    PF00531. Death. 1 hit.
    PF00554. RHD. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    PR00057. NFKBTNSCPFCT.
    SMARTiSM00248. ANK. 6 hits.
    SM00005. DEATH. 1 hit.
    SM00429. IPT. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    SSF48403. SSF48403. 1 hit.
    SSF49417. SSF49417. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 5 hits.
    PS01204. REL_1. 1 hit.
    PS50254. REL_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q00653-1) [UniParc]FASTAAdd to Basket

    Also known as: p100

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MESCYNPGLD GIIEYDDFKL NSSIVEPKEP APETADGPYL VIVEQPKQRG    50
    FRFRYGCEGP SHGGLPGASS EKGRKTYPTV KICNYEGPAK IEVDLVTHSD 100
    PPRAHAHSLV GKQCSELGIC AVSVGPKDMT AQFNNLGVLH VTKKNMMGTM 150
    IQKLQRQRLR SRPQGLTEAE QRELEQEAKE LKKVMDLSIV RLRFSAFLRA 200
    SDGSFSLPLK PVISQPIHDS KSPGASNLKI SRMDKTAGSV RGGDEVYLLC 250
    DKVQKDDIEV RFYEDDENGW QAFGDFSPTD VHKQYAIVFR TPPYHKMKIE 300
    RPVTVFLQLK RKRGGDVSDS KQFTYYPLVE DKEEVQRKRR KALPTFSQPF 350
    GGGSHMGGGS GGAAGGYGGA GGGGSLGFFP SSLAYSPYQS GAGPMGCYPG 400
    GGGGAQMAAT VPSRDSGEEA AEPSAPSRTP QCEPQAPEML QRAREYNARL 450
    FGLAQRSARA LLDYGVTADA RALLAGQRHL LTAQDENGDT PLHLAIIHGQ 500
    TSVIEQIVYV IHHAQDLGVV NLTNHLHQTP LHLAVITGQT SVVSFLLRVG 550
    ADPALLDRHG DSAMHLALRA GAGAPELLRA LLQSGAPAVP QLLHMPDFEG 600
    LYPVHLAVRA RSPECLDLLV DSGAEVEATE RQGGRTALHL ATEMEELGLV 650
    THLVTKLRAN VNARTFAGNT PLHLAAGLGY PTLTRLLLKA GADIHAENEE 700
    PLCPLPSPPT SDSDSDSEGP EKDTRSSFRG HTPLDLTCST KVKTLLLNAA 750
    QNTMEPPLTP PSPAGPGLSL GDTALQNLEQ LLDGPEAQGS WAELAERLGL 800
    RSLVDTYRQT TSPSGSLLRS YELAGGDLAG LLEALSDMGL EEGVRLLRGP 850
    ETRDKLPSTA EVKEDSAYGS QSVEQEAEKL GPPPEPPGGL CHGHPQPQVH 900
    Length:900
    Mass (Da):96,749
    Last modified:October 17, 2006 - v4
    Checksum:i6BAD7038834783CA
    GO
    Isoform 3 (identifier: Q00653-3) [UniParc]FASTAAdd to Basket

    Also known as: p49

    The sequence of this isoform differs from the canonical sequence as follows:
         374-428: GSLGFFPSSL...EAAEPSAPSR → EGVLMEGGVK...RSSRPAWPTA
         429-900: Missing.

    Note: Ref.1 (CAA43716.1) sequence(s) differ(s) from that shown due to frameshifts in positions 407, 414.

    Show »
    Length:428
    Mass (Da):47,021
    Checksum:iE4D38A8635501807
    GO
    Isoform 4 (identifier: Q00653-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         860-860: Missing.

    Show »
    Length:899
    Mass (Da):96,678
    Checksum:iB3753FF15B7BDF57
    GO

    Sequence cautioni

    The sequence CAA43715.1 differs from that shown. Reason: Frameshift at positions 456, 458, 470 and 900.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441K → E in AAB21124. (PubMed:1531086)Curated
    Sequence conflicti213 – 2131I → T in CAA43715. (PubMed:1876189)Curated
    Sequence conflicti213 – 2131I → T in CAA43716. (PubMed:1876189)Curated
    Sequence conflicti213 – 2131I → T in AAA68171. (PubMed:7969113)Curated
    Sequence conflicti396 – 3961G → R in CAA43715. (PubMed:1876189)Curated
    Sequence conflicti433 – 4342EP → DA in AAB21124. (PubMed:1531086)Curated
    Sequence conflicti459 – 4591R → K AA sequence (PubMed:8360178)Curated
    Sequence conflicti465 – 4651G → C in CAA43715. (PubMed:1876189)Curated
    Sequence conflicti470 – 4701A → R in CAA43715. (PubMed:1876189)Curated
    Sequence conflicti470 – 4701A → R in AAB21124. (PubMed:1531086)Curated
    Sequence conflicti741 – 7411K → L in CAA43715. (PubMed:1876189)Curated
    Sequence conflicti860 – 8601A → T in AAB21124. (PubMed:1531086)Curated
    Sequence conflicti876 – 8761E → K in AAB21124. (PubMed:1531086)Curated
    Sequence conflicti891 – 8911C → S in CAA43715. (PubMed:1876189)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141E → K.1 Publication
    Corresponds to variant rs45581936 [ dbSNP | Ensembl ].
    VAR_022223
    Natural varianti351 – 3511G → R.1 Publication
    Corresponds to variant rs45580031 [ dbSNP | Ensembl ].
    VAR_022224
    Natural varianti392 – 3921A → G.
    Corresponds to variant rs11574848 [ dbSNP | Ensembl ].
    VAR_051781
    Natural varianti452 – 4521G → R.1 Publication
    Corresponds to variant rs45471103 [ dbSNP | Ensembl ].
    VAR_022225
    Natural varianti618 – 900283Missing in truncated form EB308.
    VAR_018452Add
    BLAST
    Natural varianti667 – 6693AGN → SAS in truncated form p80HT.
    VAR_006909
    Natural varianti670 – 900231Missing in truncated form p80HT.
    VAR_006910Add
    BLAST
    Natural varianti703 – 900198Missing in truncated form LB40.
    VAR_018453Add
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei374 – 42855GSLGF…SAPSR → EGVLMEGGVKVREAVEEKNL GEAGRGLHACNPALWEAKAG RLPEIRSSRPAWPTA in isoform 3. 1 PublicationVSP_040082Add
    BLAST
    Alternative sequencei429 – 900472Missing in isoform 3. 1 PublicationVSP_040083Add
    BLAST
    Alternative sequencei860 – 8601Missing in isoform 4. 4 PublicationsVSP_040084

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61498 mRNA. Translation: CAA43715.1. Frameshift.
    X61499 mRNA. Translation: CAA43716.1. Frameshift.
    S76638 mRNA. Translation: AAB21124.1.
    U09609 mRNA. Translation: AAA21462.2.
    BT009769 mRNA. Translation: AAP88771.1.
    AK292654 mRNA. Translation: BAF85343.1.
    AY865619 Genomic DNA. Translation: AAW56071.1.
    AL121928 Genomic DNA. Translation: CAC08399.1.
    CH471066 Genomic DNA. Translation: EAW49700.1.
    CH471066 Genomic DNA. Translation: EAW49701.1.
    CH471066 Genomic DNA. Translation: EAW49702.1.
    CH471066 Genomic DNA. Translation: EAW49704.1.
    CH471066 Genomic DNA. Translation: EAW49706.1.
    BC002844 mRNA. Translation: AAH02844.1.
    U20816 Genomic DNA. Translation: AAA68171.1.
    CCDSiCCDS41564.1. [Q00653-1]
    CCDS41565.1. [Q00653-4]
    PIRiA42024.
    A57034.
    I38609.
    S17233.
    RefSeqiNP_001070962.1. NM_001077494.3. [Q00653-1]
    NP_001248332.1. NM_001261403.2. [Q00653-4]
    NP_001275653.1. NM_001288724.1. [Q00653-4]
    NP_002493.3. NM_002502.5. [Q00653-4]
    XP_005269917.1. XM_005269860.1. [Q00653-1]
    XP_005269918.1. XM_005269861.2. [Q00653-1]
    UniGeneiHs.73090.

    Genome annotation databases

    EnsembliENST00000189444; ENSP00000189444; ENSG00000077150. [Q00653-4]
    ENST00000369966; ENSP00000358983; ENSG00000077150. [Q00653-1]
    ENST00000428099; ENSP00000410256; ENSG00000077150. [Q00653-4]
    GeneIDi4791.
    KEGGihsa:4791.
    UCSCiuc001kva.4. human. [Q00653-4]
    uc001kvb.4. human. [Q00653-1]

    Polymorphism databases

    DMDMi116242678.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61498 mRNA. Translation: CAA43715.1 . Frameshift.
    X61499 mRNA. Translation: CAA43716.1 . Frameshift.
    S76638 mRNA. Translation: AAB21124.1 .
    U09609 mRNA. Translation: AAA21462.2 .
    BT009769 mRNA. Translation: AAP88771.1 .
    AK292654 mRNA. Translation: BAF85343.1 .
    AY865619 Genomic DNA. Translation: AAW56071.1 .
    AL121928 Genomic DNA. Translation: CAC08399.1 .
    CH471066 Genomic DNA. Translation: EAW49700.1 .
    CH471066 Genomic DNA. Translation: EAW49701.1 .
    CH471066 Genomic DNA. Translation: EAW49702.1 .
    CH471066 Genomic DNA. Translation: EAW49704.1 .
    CH471066 Genomic DNA. Translation: EAW49706.1 .
    BC002844 mRNA. Translation: AAH02844.1 .
    U20816 Genomic DNA. Translation: AAA68171.1 .
    CCDSi CCDS41564.1. [Q00653-1 ]
    CCDS41565.1. [Q00653-4 ]
    PIRi A42024.
    A57034.
    I38609.
    S17233.
    RefSeqi NP_001070962.1. NM_001077494.3. [Q00653-1 ]
    NP_001248332.1. NM_001261403.2. [Q00653-4 ]
    NP_001275653.1. NM_001288724.1. [Q00653-4 ]
    NP_002493.3. NM_002502.5. [Q00653-4 ]
    XP_005269917.1. XM_005269860.1. [Q00653-1 ]
    XP_005269918.1. XM_005269861.2. [Q00653-1 ]
    UniGenei Hs.73090.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A3Q X-ray 2.10 A/B 37-327 [» ]
    2D96 NMR - A 766-859 [» ]
    3DO7 X-ray 3.05 B 37-329 [» ]
    ProteinModelPortali Q00653.
    SMRi Q00653. Positions 37-329, 434-752, 772-859.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110858. 48 interactions.
    DIPi DIP-24239N.
    DIP-27535N.
    IntActi Q00653. 30 interactions.
    MINTi MINT-7944680.
    STRINGi 9606.ENSP00000189444.

    Chemistry

    BindingDBi Q00653.
    ChEMBLi CHEMBL2094258.

    PTM databases

    PhosphoSitei Q00653.

    Polymorphism databases

    DMDMi 116242678.

    Proteomic databases

    MaxQBi Q00653.
    PaxDbi Q00653.
    PRIDEi Q00653.

    Protocols and materials databases

    DNASUi 4791.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000189444 ; ENSP00000189444 ; ENSG00000077150 . [Q00653-4 ]
    ENST00000369966 ; ENSP00000358983 ; ENSG00000077150 . [Q00653-1 ]
    ENST00000428099 ; ENSP00000410256 ; ENSG00000077150 . [Q00653-4 ]
    GeneIDi 4791.
    KEGGi hsa:4791.
    UCSCi uc001kva.4. human. [Q00653-4 ]
    uc001kvb.4. human. [Q00653-1 ]

    Organism-specific databases

    CTDi 4791.
    GeneCardsi GC10P104144.
    HGNCi HGNC:7795. NFKB2.
    HPAi CAB022098.
    HPA008422.
    HPA023900.
    MIMi 164012. gene.
    615577. phenotype.
    neXtProti NX_Q00653.
    Orphaneti 1572. Common variable immunodeficiency.
    PharmGKBi PA31600.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000004822.
    HOVERGENi HBG052613.
    InParanoidi Q00653.
    KOi K04469.
    OMAi FRGHTPL.
    OrthoDBi EOG7W154S.
    PhylomeDBi Q00653.
    TreeFami TF325632.

    Enzyme and pathway databases

    Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_23950. Interleukin-1 processing.
    REACT_24969. TRAF6 mediated NF-kB activation.

    Miscellaneous databases

    ChiTaRSi NFKB2. human.
    EvolutionaryTracei Q00653.
    GeneWikii NFKB2.
    GenomeRNAii 4791.
    NextBioi 18458.
    PMAP-CutDB Q00653.
    PROi Q00653.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00653.
    Bgeei Q00653.
    CleanExi HS_NFKB2.
    Genevestigatori Q00653.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    1.25.40.20. 1 hit.
    2.60.40.10. 1 hit.
    2.60.40.340. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    IPR000451. NF_Rel_Dor.
    IPR008967. p53-like_TF_DNA-bd.
    IPR011539. RHD.
    [Graphical view ]
    Pfami PF00023. Ank. 5 hits.
    PF00531. Death. 1 hit.
    PF00554. RHD. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    PR00057. NFKBTNSCPFCT.
    SMARTi SM00248. ANK. 6 hits.
    SM00005. DEATH. 1 hit.
    SM00429. IPT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    SSF48403. SSF48403. 1 hit.
    SSF49417. SSF49417. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 5 hits.
    PS01204. REL_1. 1 hit.
    PS50254. REL_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of an NF-kappa B subunit which stimulates HIV transcription in synergy with p65."
      Schmid R.M., Perkins N.D., Duckett C.S., Andrews P.C., Nabel G.J.
      Nature 352:733-736(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
      Tissue: Leukemia.
    2. "A novel mitogen-inducible gene product related to p50/p105-NF-kappa B participates in transactivation through a kappa B site."
      Bours V., Burd P.R., Brown K., Villalobos J., Park S., Ryseck R.P., Bravo R., Kelly K., Siebenlist U.
      Mol. Cell. Biol. 12:685-695(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Rearrangement and altered expression of the NFKB-2 gene in human cutaneous T-lymphoma cells."
      Thakur S., Lin H.C., Tseng W.T., Kumar S., Bravo R., Foss F., Gelinas C., Rabson A.B.
      Oncogene 9:2335-2344(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION, P80HT GENERATION.
    4. Rabson A.B.
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      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.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Thymus.
    7. NIEHS SNPs program
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-14; ARG-351 AND ARG-452.
    8. "The DNA sequence and comparative analysis of human chromosome 10."
      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.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Lymph.
    11. "Transcriptional regulation of NF-kappa B2: evidence for kappa B-mediated positive and negative autoregulation."
      Liptay S., Schmid R.M., Nabel E.G., Nabel G.J.
      Mol. Cell. Biol. 14:7695-7703(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-220.
    12. "Purification of the major histocompatibility complex class I transcription factor H2TF1. The full-length product of the nfkb2 gene."
      Potter D.A., Larson C.J., Eckes P., Schmid R.M., Nabel G.J., Verdine G.L., Sharp P.A.
      J. Biol. Chem. 268:18882-18890(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 459-470; 580-597 AND 636-647 (ISOFORM 1).
    13. "The oncoprotein Bcl-3 directly transactivates through kappa B motifs via association with DNA-binding p50B homodimers."
      Bours V., Franzoso G., Azarenko V., Park S., Kanno T., Brown K., Siebenlist U.
      Cell 72:729-739(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH BCL3.
    14. "Differential interactions of Rel-NF-kappa B complexes with I kappa B alpha determine pools of constitutive and inducible NF-kappa B activity."
      Dobrzanski P., Ryseck R.P., Bravo R.
      EMBO J. 13:4608-4616(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B RELB-P52 COMPLEX.
    15. "Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor necrosis factor."
      Beg A.A., Baldwin A.S. Jr.
      Oncogene 9:1487-1492(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NF-KAPPA-B P52-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
    16. "A new member of the IkappaB protein family, IkappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription."
      Li Z., Nabel G.J.
      Mol. Cell. Biol. 17:6184-6190(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBIE.
    17. "The generation of nfkb2 p52: mechanism and efficiency."
      Heusch M., Lin L., Geleziunas R., Greene W.C.
      Oncogene 18:6201-6208(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: COTRANSLATIONAL FOLDING/PROCESSING OF P100, GENERATION OF P52/P100.
    18. "Differential regulation of NF-kappaB2(p100) processing and control by amino-terminal sequences."
      Betts J.C., Nabel G.J.
      Mol. Cell. Biol. 16:6363-6371(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-713; SER-715 AND SER-717, MUTAGENESIS, DIMERIZATION, PROTEOLYTIC PROCESSING OF P100.
    19. "NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100."
      Xiao G., Harhaj E.W., Sun S.-C.
      Mol. Cell 7:401-409(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-866 AND SER-870, MUTAGENESIS OF SER-866 AND SER-870, PROTEOLYTIC PROCESSING OF P100.
    20. "B cell lymphoma-associated chromosomal translocation involves candidate oncogene lyt-10, homologous to NF-kappa B p50."
      Neri A., Chang C.C., Lombardi L., Salina M., Corradini P., Maiolo A.T., Chaganti R.S., Dalla-Favera R.
      Cell 67:1075-1087(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH IGHA1.
    21. "Heterogeneous chromosomal aberrations generate 3' truncations of the NFKB2/lyt-10 gene in lymphoid malignancies."
      Migliazza A., Lombardi L., Rocchi M., Trecca D., Chang C.-C., Antonacci R., Fracchiolla N.S., Ciana P., Maiolo A.T., Neri A.
      Blood 84:3850-3860(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL ABERRATIONS, GENERATION OF LB40 AND EB308.
    22. "Structural and functional characterization of the promoter regions of the NFKB2 gene."
      Lombardi L., Ciana P., Cappellini C., Trecca D., Guerrini L., Migliazza A., Maiolo A.T., Neri A.
      Nucleic Acids Res. 23:2328-2336(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE TWO PROMOTER REGIONS.
    23. "The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation."
      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.
      Oncogene 20:4917-4925(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEN1.
    24. "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."
      Amir R.E., Haecker H., Karin M., Ciechanover A.
      Oncogene 23:2540-2547(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-855.
    25. "IL-1 receptor-associated kinase 1 is critical for latent membrane protein 1-induced p65/RelA serine 536 phosphorylation and NF-kappaB activation."
      Song Y.J., Jen K.Y., Soni V., Kieff E., Cahir-McFarland E.
      Proc. Natl. Acad. Sci. U.S.A. 103:2689-2694(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
    26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Germline mutations in NFKB2 implicate the noncanonical NF-kappaB pathway in the pathogenesis of common variable immunodeficiency."
      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.
      Am. J. Hum. Genet. 93:812-824(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CVID10.
    30. "Structure of the human NF-kappaB p52 homodimer-DNA complex at 2.1-A resolution."
      Cramer P., Larson C.J., Verdine G.L., Mueller C.W.
      EMBO J. 16:7078-7090(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 37-327.
    31. "Solution structure of the death domain of nuclear factor NF-kappa-B p100."
      RIKEN structural genomics initiative (RSGI)
      Submitted (DEC-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 764-859.

    Entry informationi

    Entry nameiNFKB2_HUMAN
    AccessioniPrimary (citable) accession number: Q00653
    Secondary accession number(s): A8K9D9
    , D3DR83, Q04860, Q9BU75, Q9H471, Q9H472
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 183 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3