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P25799

- NFKB1_MOUSE

UniProt

P25799 - NFKB1_MOUSE

Protein

Nuclear factor NF-kappa-B p105 subunit

Gene

Nfkb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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 and the heterodimeric p65-p50 complex appears to be most abundant one. 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. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 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. Plays a role in the regulation of apoptosis. Isoform 5, isoform 6 and isoform 7 act as inhibitors of transactivation of p50 NF-kappa-B subunit, probably by sequestering it in the cytoplasm. Isoform 3 (p98) (but not p84 or p105) acts as a transactivator of NF-kappa-B-regulated gene expression. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei431 – 4322Cleavage (when cotranslationally processed)By similarity

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. double-stranded DNA binding Source: Ensembl
    3. nucleic acid binding transcription factor activity Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein homodimerization activity Source: MGI
    6. regulatory region DNA binding Source: UniProtKB
    7. sequence-specific DNA binding Source: MGI
    8. sequence-specific DNA binding transcription factor activity Source: InterPro
    9. transcription regulatory region sequence-specific DNA binding Source: Ensembl

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cellular response to interleukin-1 Source: Ensembl
    3. cellular response to lipopolysaccharide Source: MGI
    4. cellular response to mechanical stimulus Source: Ensembl
    5. lymph node development Source: MGI
    6. negative regulation of apoptotic process Source: Ensembl
    7. negative regulation of calcidiol 1-monooxygenase activity Source: Ensembl
    8. negative regulation of cytokine production Source: BHF-UCL
    9. negative regulation of inflammatory response Source: MGI
    10. negative regulation of interleukin-12 biosynthetic process Source: MGI
    11. negative regulation of transcription, DNA-templated Source: MGI
    12. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    13. positive regulation of canonical Wnt signaling pathway Source: Ensembl
    14. positive regulation of hyaluronan biosynthetic process Source: Ensembl
    15. positive regulation of transcription, DNA-templated Source: UniProtKB
    16. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    17. response to copper ion Source: Ensembl
    18. response to oxidative stress Source: Ensembl
    19. signal transduction Source: InterPro
    20. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Apoptosis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198700. Interleukin-1 processing.
    REACT_199121. Activation of NF-kappaB in B cells.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_218614. Regulated proteolysis of p75NTR.
    REACT_218887. NF-kB is activated and signals survival.
    REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    REACT_224208. Interleukin-1 signaling.
    REACT_225145. Downstream TCR signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear factor NF-kappa-B p105 subunit
    Alternative name(s):
    DNA-binding factor KBF1
    EBP-1
    NF-kappa-B1 p84/NF-kappa-B1 p98
    Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1
    Cleaved into the following chain:
    Gene namesi
    Name:Nfkb1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:97312. Nfkb1.

    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. cytosol Source: MGI
    2. mitochondrion Source: Ensembl
    3. nucleus Source: MGI
    4. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 971971Nuclear factor NF-kappa-B p105 subunitPRO_0000030312Add
    BLAST
    Chaini1 – 431431Nuclear factor NF-kappa-B p50 subunitBy similarityPRO_0000030313Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591S-nitrosocysteine; alternateBy similarity
    Lipidationi59 – 591S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternateBy similarity
    Modified residuei335 – 3351Phosphoserine; by PKASequence Analysis
    Modified residuei438 – 4381N6-acetyllysine; by EP300By similarity
    Modified residuei674 – 6741(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
    Modified residuei910 – 9101Phosphoserine; by GSK3-beta; in vitroBy similarity
    Modified residuei930 – 9301Phosphoserine; by IKKBBy similarity
    Modified residuei935 – 9351Phosphoserine; by IKKBBy similarity
    Modified residuei940 – 9401PhosphoserineBy similarity

    Post-translational modificationi

    While translation occurs, the particular unfolded structure after the GRR repeat promotes the generation of p50 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.
    Phosphorylation at 'Ser-930' and 'Ser-935' are required for BTRC/BTRCP-mediated proteolysis.By similarity
    Polyubiquitination seems to allow p105 processing.
    S-nitrosylation of Cys-59 affects DNA binding.By similarity
    The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Hydroxylation, Lipoprotein, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiP25799.
    PaxDbiP25799.
    PRIDEiP25799.

    PTM databases

    PhosphoSiteiP25799.

    Expressioni

    Inductioni

    By phorbol ester and TNF-alpha.

    Gene expression databases

    BgeeiP25799.
    GenevestigatoriP25799.

    Interactioni

    Subunit structurei

    Component of the NF-kappa-B p65-p50 complex. Component of the NF-kappa-B p65-p50 complex. Homodimer; component of the NF-kappa-B p50-p50 complex. Component of the NF-kappa-B p105-p50 complex. Component of the NF-kappa-B p50-c-Rel complex. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity. Interacts with DSIPI; this interaction prevents nuclear translocation and DNA-binding. Interacts with SPAG9 and UNC5CL. NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50. NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2. Interacts with GSK3B; the interaction prevents processing of p105 to p50. NFKB1/p50 interacts with NFKBIE By similarity. NFKB1/p50 interacts with NFKBIZ. Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID. Directly interacts with MEN1 By similarity. Interacts with HIF1AN By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hdac1O091062EBI-643958,EBI-301912
    NCOA1Q157882EBI-643958,EBI-455189From a different organism.
    RelaQ042075EBI-643958,EBI-644400
    RelbQ048632EBI-1209141,EBI-1209145

    Protein-protein interaction databases

    BioGridi201751. 13 interactions.
    DIPiDIP-85N.
    IntActiP25799. 9 interactions.
    MINTiMINT-236136.

    Structurei

    Secondary structure

    1
    971
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi41 – 466
    Beta strandi50 – 523
    Helixi58 – 603
    Beta strandi62 – 643
    Beta strandi74 – 763
    Beta strandi81 – 855
    Beta strandi92 – 987
    Beta strandi100 – 1034
    Beta strandi108 – 1136
    Beta strandi117 – 1193
    Beta strandi120 – 1245
    Beta strandi131 – 1333
    Beta strandi138 – 1403
    Helixi144 – 1463
    Helixi147 – 16014
    Beta strandi162 – 1643
    Helixi165 – 1695
    Helixi171 – 1733
    Beta strandi179 – 1824
    Helixi188 – 20316
    Beta strandi209 – 21911
    Beta strandi221 – 2233
    Beta strandi225 – 2284
    Beta strandi232 – 2398
    Beta strandi240 – 2423
    Turni243 – 2464
    Beta strandi250 – 2545
    Beta strandi256 – 2594
    Beta strandi265 – 2717
    Turni275 – 2773
    Beta strandi279 – 2846
    Helixi287 – 2893
    Beta strandi292 – 2954
    Helixi300 – 3023
    Turni305 – 3073
    Beta strandi308 – 3125
    Beta strandi325 – 3328
    Turni334 – 3363
    Beta strandi343 – 3486
    Beta strandi351 – 3544

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BFSX-ray2.20A245-350[»]
    1IKNX-ray2.30C245-363[»]
    1LE5X-ray2.75B/F39-350[»]
    1LE9X-ray3.00B/F39-350[»]
    1LEIX-ray2.70B39-350[»]
    1NFKX-ray2.30A/B39-363[»]
    1OOAX-ray2.45A/B39-363[»]
    1U36X-ray1.89A245-350[»]
    1U3JX-ray1.90A245-350[»]
    1U3YX-ray1.90A245-350[»]
    1U3ZX-ray1.90A245-350[»]
    1U41X-ray2.20A/B/C/D245-350[»]
    1U42X-ray2.70A245-350[»]
    1VKXX-ray2.90B39-350[»]
    2I9TX-ray2.80B39-350[»]
    2V2TX-ray3.05B38-363[»]
    3JV4X-ray3.15B/D/F245-359[»]
    ProteinModelPortaliP25799.
    SMRiP25799. Positions 39-350, 460-786, 802-885.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25799.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 365326RHDPROSITE-ProRule annotationAdd
    BLAST
    Repeati538 – 56730ANK 1Add
    BLAST
    Repeati577 – 60630ANK 2Add
    BLAST
    Repeati610 – 63930ANK 3Add
    BLAST
    Repeati646 – 67530ANK 4Add
    BLAST
    Repeati680 – 71031ANK 5Add
    BLAST
    Repeati714 – 74330ANK 6Add
    BLAST
    Repeati767 – 79731ANK 7Add
    BLAST
    Domaini801 – 88888DeathAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni370 – 39223GRRAdd
    BLAST
    Regioni433 – 971539Interaction with CFLARBy similarityAdd
    BLAST
    Regioni646 – 68035Essential for interaction with HIF1ANBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi358 – 3636Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi373 – 43159Gly-richAdd
    BLAST

    Domaini

    The C-terminus of p105 might be involved in cytoplasmic retention, inhibition of DNA-binding, and transcription activation.
    Glycine-rich region (GRR) appears to be a critical element in the generation of p50.

    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.
    GeneTreeiENSGT00500000044765.
    HOVERGENiHBG052613.
    InParanoidiB2RRQ6.
    KOiK02580.
    OMAiPGYGFPH.
    OrthoDBiEOG7W154S.
    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. 2 hits.
    PF12796. Ank_2. 1 hit.
    PF00531. Death. 1 hit.
    PF00554. RHD. 1 hit.
    [Graphical view]
    PRINTSiPR00057. 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 (7)i

    Sequence statusi: Complete.

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

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P25799-1) [UniParc]FASTAAdd to Basket

    Also known as: p105

    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

    MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ    50
    RGFRFRYVCE GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN 100
    GKNIHLHAHS LVGKHCEDGV CTVTAGPKDM VVGFANLGIL HVTKKKVFET 150
    LEARMTEACI RGYNPGLLVH SDLAYLQAEG GGDRQLTDRE KEIIRQAAVQ 200
    QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS KAPNASNLKI 250
    VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP 300
    TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE 350
    IKDKEEVQRK RQKLMPNFSD SFGGGSGAGA GGGGMFGSGG GGGSTGSPGP 400
    GYGYSNYGFP PYGGITFHPG VTKSNAGVTH GTINTKFKNG PKDCAKSDDE 450
    ESLTLPEKET EGEGPSLPMA CTKTEPIALA STMEDKEQDM GFQDNLFLEK 500
    ALQLARRHAN ALFDYAVTGD VKMLLAVQRH LTAVQDENGD SVLHLAIIHL 550
    HAQLVRDLLE VTSGLISDDI INMRNDLYQT PLHLAVITKQ EDVVEDLLRV 600
    GADLSLLDRW GNSVLHLAAK EGHDRILSIL LKSRKAAPLI DHPNGEGLNA 650
    IHIAVMSNSL PCLLLLVAAG AEVNAQEQKS GRTALHLAVE YDNISLAGCL 700
    LLEGDAHVDS TTYDGTTPLH IAAGRGSTRL AALLKAAGAD PLVENFEPLY 750
    DLDDSWEKAG EDEGVVPGTT PLDMAANWQV FDILNGKPYE PVFTSDDILP 800
    QGDMKQLTED TRLQLCKLLE IPDPDKNWAT LAQKLGLGIL NNAFRLSPAP 850
    SKTLMDNYEV SGGTIKELME ALQQMGYTEA IEVIQAAFRT PATTASSPVT 900
    TAQVHCLPLS SSSTRQHIDE LRDSDSVCDS GVETSFRKLS FTESLTGDSP 950
    LLSLNKMPHG YGQEGPIEGK I 971
    Length:971
    Mass (Da):105,615
    Last modified:July 27, 2011 - v2
    Checksum:i91EA9C595E375C30
    GO
    Isoform 2 (identifier: P25799-2) [UniParc]FASTAAdd to Basket

    Also known as: p84

    The sequence of this isoform differs from the canonical sequence as follows:
         780-971: VFDILNGKPY...GQEGPIEGKI → GT

    Show »
    Length:781
    Mass (Da):84,817
    Checksum:i51B98D66F21BF5EC
    GO
    Isoform 3 (identifier: P25799-3) [UniParc]FASTAAdd to Basket

    Also known as: p98

    The sequence of this isoform differs from the canonical sequence as follows:
         860-971: VSGGTIKELM...GQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL

    Show »
    Length:894
    Mass (Da):97,413
    Checksum:i8445F5C4CA02D7E4
    GO
    Isoform 4 (identifier: P25799-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         353-356: DKEE → GTWV
         357-971: Missing.

    Show »
    Length:356
    Mass (Da):39,756
    Checksum:i09E32E7A3B63F46A
    GO
    Isoform 5 (identifier: P25799-5) [UniParc]FASTAAdd to Basket

    Also known as: P70, I-kappa-B gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         1-364: Missing.

    Show »
    Length:607
    Mass (Da):64,782
    Checksum:i1B79975F022DF4E2
    GO
    Isoform 6 (identifier: P25799-6) [UniParc]FASTAAdd to Basket

    Also known as: p63, I-kappa-B gamma-1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-364: Missing.
         860-971: VSGGTIKELM...GQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL

    Show »
    Length:530
    Mass (Da):56,580
    Checksum:iC7384490B44048FC
    GO
    Isoform 7 (identifier: P25799-7) [UniParc]FASTAAdd to Basket

    Also known as: p55, I-kappa-B gamma-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-364: Missing.
         780-971: VFDILNGKPY...GQEGPIEGKI → GT

    Note: Inhibits the activity of the p50 NF-kappa-B subunit.

    Show »
    Length:417
    Mass (Da):43,983
    Checksum:iDEA2D2B56CDDC6D3
    GO

    Sequence cautioni

    The sequence BAC35117.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111L → P in AAR00341. 1 PublicationCurated
    Sequence conflicti265 – 2651E → G in BAC35117. (PubMed:16141072)Curated
    Sequence conflicti530 – 5301H → D in BAE34261. (PubMed:16141072)Curated
    Sequence conflicti546 – 5461A → G in BAE34261. (PubMed:16141072)Curated
    Sequence conflicti684 – 6841A → P in AAA40415. (PubMed:2203532)Curated
    Sequence conflicti684 – 6841A → P in AAB21851. (PubMed:1339305)Curated
    Sequence conflicti684 – 6841A → P in AAB28573. (PubMed:8398903)Curated
    Sequence conflicti732 – 7321A → T in BAE34261. (PubMed:16141072)Curated
    Sequence conflicti950 – 9501P → A in BAE43399. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 364364Missing in isoform 5, isoform 6 and isoform 7. 2 PublicationsVSP_017236Add
    BLAST
    Alternative sequencei353 – 3564DKEE → GTWV in isoform 4. 2 PublicationsVSP_017237
    Alternative sequencei357 – 971615Missing in isoform 4. 2 PublicationsVSP_017238Add
    BLAST
    Alternative sequencei780 – 971192VFDIL…IEGKI → GT in isoform 2 and isoform 7. 1 PublicationVSP_005583Add
    BLAST
    Alternative sequencei860 – 971112VSGGT…IEGKI → MNSGIVTASVTVVWRHPSAN SALQSLLLETAHCYL in isoform 3 and isoform 6. 1 PublicationVSP_005584Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57999 mRNA. Translation: AAA40415.1.
    S89033 mRNA. Translation: AAB21851.1.
    S66656 mRNA. Translation: AAB28573.1.
    AB119195 mRNA. Translation: BAC84979.1.
    AY521462 mRNA. Translation: AAS00547.1.
    AY521463 mRNA. Translation: AAS00548.1.
    CH466532 Genomic DNA. Translation: EDL12143.1.
    BC050841 mRNA. Translation: AAH50841.1.
    BC138535 mRNA. Translation: AAI38536.1.
    BC138536 mRNA. Translation: AAI38537.1.
    AY423849 mRNA. Translation: AAR00341.1.
    AK052726 mRNA. Translation: BAC35117.1. Different initiation.
    AK089660 mRNA. Translation: BAE43399.1.
    AK157915 mRNA. Translation: BAE34261.1.
    CCDSiCCDS17858.1. [P25799-1]
    PIRiA35697.
    RefSeqiNP_032715.2. NM_008689.2. [P25799-1]
    XP_006501169.1. XM_006501106.1. [P25799-3]
    UniGeneiMm.256765.

    Genome annotation databases

    EnsembliENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163. [P25799-1]
    ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163. [P25799-1]
    GeneIDi18033.
    KEGGimmu:18033.
    UCSCiuc008rlw.1. mouse. [P25799-1]
    uc008rly.1. mouse. [P25799-4]
    uc012cyf.1. mouse. [P25799-6]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57999 mRNA. Translation: AAA40415.1 .
    S89033 mRNA. Translation: AAB21851.1 .
    S66656 mRNA. Translation: AAB28573.1 .
    AB119195 mRNA. Translation: BAC84979.1 .
    AY521462 mRNA. Translation: AAS00547.1 .
    AY521463 mRNA. Translation: AAS00548.1 .
    CH466532 Genomic DNA. Translation: EDL12143.1 .
    BC050841 mRNA. Translation: AAH50841.1 .
    BC138535 mRNA. Translation: AAI38536.1 .
    BC138536 mRNA. Translation: AAI38537.1 .
    AY423849 mRNA. Translation: AAR00341.1 .
    AK052726 mRNA. Translation: BAC35117.1 . Different initiation.
    AK089660 mRNA. Translation: BAE43399.1 .
    AK157915 mRNA. Translation: BAE34261.1 .
    CCDSi CCDS17858.1. [P25799-1 ]
    PIRi A35697.
    RefSeqi NP_032715.2. NM_008689.2. [P25799-1 ]
    XP_006501169.1. XM_006501106.1. [P25799-3 ]
    UniGenei Mm.256765.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BFS X-ray 2.20 A 245-350 [» ]
    1IKN X-ray 2.30 C 245-363 [» ]
    1LE5 X-ray 2.75 B/F 39-350 [» ]
    1LE9 X-ray 3.00 B/F 39-350 [» ]
    1LEI X-ray 2.70 B 39-350 [» ]
    1NFK X-ray 2.30 A/B 39-363 [» ]
    1OOA X-ray 2.45 A/B 39-363 [» ]
    1U36 X-ray 1.89 A 245-350 [» ]
    1U3J X-ray 1.90 A 245-350 [» ]
    1U3Y X-ray 1.90 A 245-350 [» ]
    1U3Z X-ray 1.90 A 245-350 [» ]
    1U41 X-ray 2.20 A/B/C/D 245-350 [» ]
    1U42 X-ray 2.70 A 245-350 [» ]
    1VKX X-ray 2.90 B 39-350 [» ]
    2I9T X-ray 2.80 B 39-350 [» ]
    2V2T X-ray 3.05 B 38-363 [» ]
    3JV4 X-ray 3.15 B/D/F 245-359 [» ]
    ProteinModelPortali P25799.
    SMRi P25799. Positions 39-350, 460-786, 802-885.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201751. 13 interactions.
    DIPi DIP-85N.
    IntActi P25799. 9 interactions.
    MINTi MINT-236136.

    Chemistry

    ChEMBLi CHEMBL1949489.

    PTM databases

    PhosphoSitei P25799.

    Proteomic databases

    MaxQBi P25799.
    PaxDbi P25799.
    PRIDEi P25799.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029812 ; ENSMUSP00000029812 ; ENSMUSG00000028163 . [P25799-1 ]
    ENSMUST00000164430 ; ENSMUSP00000128345 ; ENSMUSG00000028163 . [P25799-1 ]
    GeneIDi 18033.
    KEGGi mmu:18033.
    UCSCi uc008rlw.1. mouse. [P25799-1 ]
    uc008rly.1. mouse. [P25799-4 ]
    uc012cyf.1. mouse. [P25799-6 ]

    Organism-specific databases

    CTDi 4790.
    MGIi MGI:97312. Nfkb1.

    Phylogenomic databases

    eggNOGi COG0666.
    GeneTreei ENSGT00500000044765.
    HOVERGENi HBG052613.
    InParanoidi B2RRQ6.
    KOi K02580.
    OMAi PGYGFPH.
    OrthoDBi EOG7W154S.
    TreeFami TF325632.

    Enzyme and pathway databases

    Reactomei REACT_198700. Interleukin-1 processing.
    REACT_199121. Activation of NF-kappaB in B cells.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_218614. Regulated proteolysis of p75NTR.
    REACT_218887. NF-kB is activated and signals survival.
    REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    REACT_224208. Interleukin-1 signaling.
    REACT_225145. Downstream TCR signaling.

    Miscellaneous databases

    ChiTaRSi NFKB1. mouse.
    EvolutionaryTracei P25799.
    NextBioi 293121.
    PROi P25799.
    SOURCEi Search...

    Gene expression databases

    Bgeei P25799.
    Genevestigatori P25799.

    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. 2 hits.
    PF12796. Ank_2. 1 hit.
    PF00531. Death. 1 hit.
    PF00554. RHD. 1 hit.
    [Graphical view ]
    PRINTSi 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 the p50 DNA binding subunit of NF-kappa B: homology to rel and dorsal."
      Ghosh S., Gifford A.M., Riviere L.R., Tempst P., Nolan G.P., Baltimore D.
      Cell 62:1019-1029(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung and Spleen.
    2. "I kappa B gamma, a 70 kd protein identical to the C-terminal half of p110 NF-kappa B: a new member of the I kappa B family."
      Inoue J., Kerr L.D., Kakizuka A., Verma I.M.
      Cell 68:1109-1120(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION.
    3. "The activity of a 70 kilodalton I kappa B molecule identical to the carboxyl terminus of the p105 NF-kappa B precursor is modulated by protein kinase A."
      Gerondakis S., Morrice N., Richardson I.B., Wettenhall R., Fecondo J., Grumont R.J.
      Cell Growth Differ. 4:617-627(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PARTIAL PROTEIN SEQUENCE.
    4. "Alternate RNA splicing of murine nfkb1 generates a nuclear isoform of the p50 precursor NF-kappa B1 that can function as a transactivator of NF-kappa B-regulated transcription."
      Grumont R.J., Fecondo J., Gerondakis S.
      Mol. Cell. Biol. 14:8460-8470(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
    5. "Mus musculus transcription factor NF-kappa-B DNA binding subunit(p105) mRNA, complete cds."
      Ohara O., Kitamura H., Nakagawa T.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: C57BL/6CrSlc.
      Tissue: Spleen.
    6. Bleich A., Hedrich H.J., Schlegelberger B., Maehler M.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: C3H/HeJBir and C57BL/6J.
    7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1 AND 4).
      Tissue: Brain and Embryo.
    9. Gerhauser I., Ulrich R., Baumgartner W.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-129.
      Strain: C57BL/6.
      Tissue: Lung carcinoma.
    10. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-971 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-971 (ISOFORM 1).
      Strain: C57BL/6J and NOD.
      Tissue: Inner ear, Kidney and Spleen.
    11. "Alternative splicing of RNA transcripts encoded by the murine p105 NF-kappa B gene generates I kappa B gamma isoforms with different inhibitory activities."
      Grumont R.J., Gerondakis S.
      Proc. Natl. Acad. Sci. U.S.A. 91:4367-4371(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 6 AND 7), SUBCELLULAR LOCATION.
    12. "Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome."
      Lin L., DeMartino G.N., Greene W.C.
      Cell 92:819-828(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: COTRANSLATIONAL FOLDING OF P105.
    13. "A novel IkappaB protein, IkappaB-zeta, induced by proinflammatory stimuli, negatively regulates nuclear factor-kappaB in the nuclei."
      Yamazaki S., Muta T., Takeshige K.
      J. Biol. Chem. 276:27657-27662(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBIZ.
    14. "Peptide-induced negative selection of thymocytes activates transcription of an NF-kappa B inhibitor."
      Fiorini E., Schmitz I., Marissen W.E., Osborn S.L., Touma M., Sasada T., Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M., Reinherz E.L., Clayton L.K.
      Mol. Cell 9:637-648(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBID.
    15. "A defect in nucleosome remodeling prevents IL-12(p35) gene transcription in neonatal dendritic cells."
      Goriely S., Van Lint C., Dadkhah R., Libin M., De Wit D., Demonte D., Willems F., Goldman M.
      J. Exp. Med. 199:1011-1016(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX.
    16. "Regulation of Toll/IL-1-receptor-mediated gene expression by the inducible nuclear protein IkappaBzeta."
      Yamamoto M., Yamazaki S., Uematsu S., Sato S., Hemmi H., Hoshino K., Kaisho T., Kuwata H., Takeuchi O., Takeshige K., Saitoh T., Yamaoka S., Yamamoto N., Yamamoto S., Muta T., Takeda K., Akira S.
      Nature 430:218-222(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBIZ.
    17. "Structure of NF-kappa B p50 homodimer bound to a kappa B site."
      Ghosh G., van Duyne G., Ghosh S., Sigler P.B.
      Nature 373:303-310(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 39-364.
    18. "The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits."
      Huang D.B., Huxford T., Chen Y.Q., Ghosh G.
      Structure 5:1427-1436(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 245-350.
    19. "The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation."
      Huxford T., Huang D.B., Malek S., Ghosh G.
      Cell 95:759-770(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 245-363.
    20. "Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA."
      Chen F.E., Huang D.B., Chen Y.Q., Ghosh G.
      Nature 391:410-413(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 39-350.
    21. "The X-ray crystal structure of the NF-kappa B p50.p65 heterodimer bound to the interferon beta -kappa B site."
      Berkowitz B., Huang D.B., Chen-Park F.E., Sigler P.B., Ghosh G.
      J. Biol. Chem. 277:24694-24700(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 39-350.
    22. "The kappa B DNA sequence from the HIV long terminal repeat functions as an allosteric regulator of HIV transcription."
      Chen-Park F.E., Huang D.B., Noro B., Thanos D., Ghosh G.
      J. Biol. Chem. 277:24701-24708(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-350.
    23. "Crystal structure of NF-kappaB (p50)2 complexed to a high-affinity RNA aptamer."
      Huang D.B., Vu D., Cassiday L.A., Zimmerman J.M., Maher L.J. III, Ghosh G.
      Proc. Natl. Acad. Sci. U.S.A. 100:9268-9273(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 38-351 HOMODIMER COMPLEXED WITH RNA APTAMER.
    24. "X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of multiple dimers on tandem kappaB sites."
      Moorthy A.K., Huang D.B., Wang V.Y., Vu D., Ghosh G.
      J. Mol. Biol. 373:723-734(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 91-378 IN COMPLEX WITH RELB.

    Entry informationi

    Entry nameiNFKB1_MOUSE
    AccessioniPrimary (citable) accession number: P25799
    Secondary accession number(s): B2RRQ6
    , Q3TZE8, Q3V2V6, Q6TDG8, Q75ZL1, Q80Y21, Q8C712
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 167 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3