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P25963

- IKBA_HUMAN

UniProt

P25963 - IKBA_HUMAN

Protein

NF-kappa-B inhibitor alpha

Gene

NFKBIA

Organism
Homo sapiens (Human)
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 1 (01 May 1992)
      Previous versions | rss
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    Functioni

    Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription.1 Publication

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. NF-kappaB binding Source: UniProtKB
    4. nuclear localization sequence binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. transcription factor binding Source: ProtInc
    7. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. cellular response to cold Source: BHF-UCL
    3. cytoplasmic sequestering of NF-kappaB Source: BHF-UCL
    4. cytoplasmic sequestering of transcription factor Source: UniProtKB
    5. Fc-epsilon receptor signaling pathway Source: Reactome
    6. innate immune response Source: Reactome
    7. lipopolysaccharide-mediated signaling pathway Source: Ensembl
    8. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    9. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    10. negative regulation of apoptotic process Source: Reactome
    11. negative regulation of DNA binding Source: UniProtKB
    12. negative regulation of lipid storage Source: BHF-UCL
    13. negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
    14. negative regulation of myeloid cell differentiation Source: Ensembl
    15. negative regulation of NF-kappaB transcription factor activity Source: MGI
    16. negative regulation of Notch signaling pathway Source: Ensembl
    17. neurotrophin TRK receptor signaling pathway Source: Reactome
    18. nucleotide-binding oligomerization domain containing 1 signaling pathway Source: Ensembl
    19. nucleotide-binding oligomerization domain containing 2 signaling pathway Source: Ensembl
    20. positive regulation of cellular protein metabolic process Source: BHF-UCL
    21. positive regulation of cholesterol efflux Source: BHF-UCL
    22. positive regulation of NF-kappaB transcription factor activity Source: Reactome
    23. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    24. positive regulation of type I interferon production Source: Reactome
    25. protein import into nucleus, translocation Source: Ensembl
    26. regulation of cell proliferation Source: Ensembl
    27. regulation of NF-kappaB import into nucleus Source: UniProtKB
    28. response to exogenous dsRNA Source: Ensembl
    29. response to muramyl dipeptide Source: Ensembl
    30. T cell receptor signaling pathway Source: Reactome
    31. toll-like receptor 10 signaling pathway Source: Reactome
    32. toll-like receptor 2 signaling pathway Source: Reactome
    33. toll-like receptor 3 signaling pathway Source: Reactome
    34. toll-like receptor 4 signaling pathway Source: Reactome
    35. toll-like receptor 5 signaling pathway Source: Reactome
    36. toll-like receptor 9 signaling pathway Source: Reactome
    37. toll-like receptor signaling pathway Source: Reactome
    38. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    39. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    40. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    41. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_12555. Downstream TCR signaling.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_24969. TRAF6 mediated NF-kB activation.
    SABIO-RKP25963.
    SignaLinkiP25963.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NF-kappa-B inhibitor alpha
    Alternative name(s):
    I-kappa-B-alpha
    Short name:
    IkB-alpha
    Short name:
    IkappaBalpha
    Major histocompatibility complex enhancer-binding protein MAD3
    Gene namesi
    Name:NFKBIA
    Synonyms:IKBA, MAD3, NFKBI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:7797. NFKBIA.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. I-kappaB/NF-kappaB complex Source: BHF-UCL
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Ectodermal dysplasia, anhidrotic, with T-cell immunodeficiency autosomal dominant (ADEDAID) [MIM:612132]: A form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. This form of ectodermal dysplasia is associated with decreased production of pro-inflammatory cytokines and certain interferons, rendering patients susceptible to infection.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321S → I in ADEDAID. 1 Publication
    Corresponds to variant rs28933100 [ dbSNP | Ensembl ].
    VAR_034871

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi21 – 211K → R: Little change in Tax-stimulated transactivation. No sumoylation. Greatly reduced Tax- or cytokine-stimulated transactivation and decrease in ubiquitination and degradation; when associated with R-22. 4 Publications
    Mutagenesisi22 – 221K → R: Little change in Tax-stimulated transactivation. No sumoylation. Greatly reduced Tax- or cytokine-stimulated transactivation and decrease in ubiquitination and degradation; when associated with R-21. 4 Publications
    Mutagenesisi31 – 311D → A: Loss of phosphorylation; when associated with A-35. 1 Publication
    Mutagenesisi32 – 321S → A: Loss of phosphorylation, ubiquitination and degradation; when associated with A-36. 2 Publications
    Mutagenesisi32 – 321S → T: Decrease in phosphorylation and degradation; when associated with T-36. 2 Publications
    Mutagenesisi35 – 351D → A: Loss in phosphorylation; when associated with A-31. 1 Publication
    Mutagenesisi35 – 351D → G: No change neither in phosphorylation, nor on degradation. 1 Publication
    Mutagenesisi36 – 361S → A: Loss of phosphorylation, ubiquitination, and degradation; when associated with A-32. 2 Publications
    Mutagenesisi36 – 361S → T: Decrease in phosphorylation and degradation; when associated with T-32. 2 Publications
    Mutagenesisi38 – 381K → R: No change in Tax-stimulated transactivation. No change in Tax-stimulated transactivation; when associated with R-47. 1 Publication
    Mutagenesisi42 – 421Y → F: No phosphorylation. 1 Publication
    Mutagenesisi45 – 528MVKELQEI → AAKEAQEA: No nuclear export.
    Mutagenesisi47 – 471K → R: Little change in Tax-stimulated transactivation. No change in Tax-stimulated transactivation; when associated with R-38. 1 Publication
    Mutagenesisi115 – 1206LHLAVI → AHAAVA: Greatly reduced nuclear localization. Great reduction in its ability to inhibit DNA binding of RELA.
    Mutagenesisi210 – 2101N → A: Almost abolished ability to inhibit NF-kappa-B DNA-binding activity; when associated with A-244. 1 Publication
    Mutagenesisi234 – 2341S → A: No inducible ubiquitination nor protein degradation. 1 Publication
    Mutagenesisi244 – 2441N → A: Almost abolished ability to inhibit NF-kappa-B DNA-binding activity; when associated with A-210. 1 Publication
    Mutagenesisi262 – 2621S → A: No inducible ubiquitination nor protein degradation. 1 Publication
    Mutagenesisi263 – 2631T → A: No inducible ubiquitination nor protein degradation. 1 Publication

    Keywords - Diseasei

    Disease mutation, Ectodermal dysplasia

    Organism-specific databases

    MIMi612132. phenotype.
    Orphaneti251579. Giant cell glioblastoma.
    251576. Gliosarcoma.
    98813. Hypohidrotic ectodermal dysplasia with immunodeficiency.
    PharmGKBiPA31601.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317NF-kappa-B inhibitor alphaPRO_0000066999Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki21 – 21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO or ubiquitin)2 Publications
    Cross-linki22 – 22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Modified residuei32 – 321Phosphoserine; by IKKA and IKKE3 Publications
    Modified residuei36 – 361Phosphoserine; by IKKA, IKKB, IKKE and TBK13 Publications
    Modified residuei42 – 421Phosphotyrosine; by Tyr-kinases2 Publications
    Modified residuei210 – 2101(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei244 – 2441(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei283 – 2831Phosphoserine; by CK23 Publications
    Modified residuei288 – 2881Phosphoserine; by CK22 Publications
    Modified residuei291 – 2911Phosphothreonine; by CK23 Publications
    Modified residuei293 – 2931Phosphoserine; by CK22 Publications
    Modified residuei299 – 2991Phosphothreonine; by CK22 Publications

    Post-translational modificationi

    Phosphorylated; disables inhibition of NF-kappa-B DNA-binding activity. Phosphorylation at positions 32 and 36 is prerequisite to recognition by UBE2D3 leading to polyubiquitination and subsequent degradation.3 Publications
    Sumoylated; sumoylation requires the presence of the nuclear import signal. Sumoylation blocks ubiquitination and proteasome-mediated degradation of the protein thereby increasing the protein stability.3 Publications
    Monoubiquitinated at Lys-21 and/or Lys-22 by UBE2D3. Ubiquitin chain elongation is then performed by CDC34 in cooperation with the SCF(FBXW11) E3 ligase complex, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. The resulting polyubiquitination leads to protein degradation. Also ubiquitinated by SCF(BTRC) following stimulus-dependent phosphorylation at Ser-32 and Ser-36.5 Publications
    Deubiquitinated by porcine reproductive and respiratory syndrome virus Nsp2 protein, which thereby interferes with NFKBIA degradation and impairs subsequent NF-kappa-B activation.

    Keywords - PTMi

    Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP25963.
    PaxDbiP25963.
    PeptideAtlasiP25963.
    PRIDEiP25963.

    PTM databases

    PhosphoSiteiP25963.

    Miscellaneous databases

    PMAP-CutDBP25963.

    Expressioni

    Inductioni

    Induced in adherent monocytes.

    Gene expression databases

    ArrayExpressiP25963.
    BgeeiP25963.
    CleanExiHS_NFKBIA.
    GenevestigatoriP25963.

    Organism-specific databases

    HPAiCAB003815.
    HPA029207.

    Interactioni

    Subunit structurei

    Interacts with RELA; the interaction requires the nuclear import signal. Interacts with NKIRAS1 and NKIRAS2. Part of a 70-90 kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14. Interacts with HBV protein X. Interacts with isoform 1 and isoform 2 of RWDD3; the interaction enhances sumoylation. Interacts (when phosphorylated at the 2 serine residues in the destruction motif D-S-G-X(2,3,4)-S) with BTRC. Associates with the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC; the association is mediated via interaction with BTRC. Part of a SCF(BTRC)-like complex lacking CUL1, which is associated with RELA; RELA interacts directly with NFKBIA. Interacts with PRMT2. Interacts with PRKACA in platelets; this interaction is disrupted by thrombin and collagen. Interacts with HIF1AN. Interacts with MEFV.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-307386,EBI-307386
    CHUKO1511114EBI-307386,EBI-81249
    ChukQ60680-22EBI-307386,EBI-646264From a different organism.
    COMMD1Q8N6683EBI-307386,EBI-1550112
    IKBKBO1492012EBI-307386,EBI-81266
    IKBKGQ9Y6K95EBI-307386,EBI-81279
    NFKB1P198382EBI-307386,EBI-300010
    RELAQ0420614EBI-307386,EBI-73886
    RPS3P233966EBI-307386,EBI-351193
    UBCP0CG483EBI-307386,EBI-3390054
    UL54Q9J0X93EBI-307386,EBI-7967856From a different organism.

    Protein-protein interaction databases

    BioGridi110859. 102 interactions.
    DIPiDIP-139N.
    IntActiP25963. 45 interactions.
    MINTiMINT-120458.
    STRINGi9606.ENSP00000216797.

    Structurei

    Secondary structure

    1
    317
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni72 – 743
    Helixi79 – 835
    Beta strandi87 – 915
    Helixi101 – 1044
    Helixi114 – 1207
    Helixi124 – 1285
    Helixi147 – 1548
    Helixi157 – 1659
    Turni167 – 1704
    Beta strandi171 – 1733
    Helixi175 – 1773
    Helixi186 – 1927
    Helixi196 – 20510
    Turni214 – 2163
    Helixi220 – 2267
    Helixi230 – 2378
    Turni238 – 2403
    Helixi253 – 2564
    Helixi263 – 2708
    Helixi275 – 2773
    Turni285 – 2873

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IKNX-ray2.30D67-302[»]
    1NFIX-ray2.70E/F70-282[»]
    DisProtiDP00468.
    ProteinModelPortaliP25963.
    SMRiP25963. Positions 3-294.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25963.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati73 – 10331ANK 1Add
    BLAST
    Repeati110 – 13930ANK 2Add
    BLAST
    Repeati143 – 17230ANK 3Add
    BLAST
    Repeati182 – 21130ANK 4Add
    BLAST
    Repeati216 – 24530ANK 5Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi30 – 367Destruction motif
    Motifi45 – 5410Nuclear export signal
    Motifi110 – 12011Nuclear import signalAdd
    BLAST

    Sequence similaritiesi

    Belongs to the NF-kappa-B inhibitor family.Curated
    Contains 5 ANK repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000059576.
    HOVERGENiHBG018875.
    InParanoidiP25963.
    KOiK04734.
    OMAiSIHGYLA.
    OrthoDBiEOG7W154S.
    PhylomeDBiP25963.
    TreeFamiTF320166.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    [Graphical view]
    PfamiPF00023. Ank. 4 hits.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 5 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25963-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFQAAERPQE WAMEGPRDGL KKERLLDDRH DSGLDSMKDE EYEQMVKELQ    50
    EIRLEPQEVP RGSEPWKQQL TEDGDSFLHL AIIHEEKALT MEVIRQVKGD 100
    LAFLNFQNNL QQTPLHLAVI TNQPEIAEAL LGAGCDPELR DFRGNTPLHL 150
    ACEQGCLASV GVLTQSCTTP HLHSILKATN YNGHTCLHLA SIHGYLGIVE 200
    LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG ADVNRVTYQG 250
    YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEFTE 300
    DELPYDDCVF GGQRLTL 317
    Length:317
    Mass (Da):35,609
    Last modified:May 1, 1992 - v1
    Checksum:i088B313226786395
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321S → I in ADEDAID. 1 Publication
    Corresponds to variant rs28933100 [ dbSNP | Ensembl ].
    VAR_034871

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69043 mRNA. Translation: AAA16489.1.
    AJ249294
    , AJ249295, AJ249283, AJ249284, AJ249285, AJ249286 Genomic DNA. Translation: CAB65556.2.
    AY033600 mRNA. Translation: AAK51149.1.
    BT007091 mRNA. Translation: AAP35754.1.
    AY496422 Genomic DNA. Translation: AAR29599.1.
    AK313421 mRNA. Translation: BAG36213.1.
    AL133163 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW65875.1.
    BC002601 mRNA. Translation: AAH02601.1.
    BC004983 mRNA. Translation: AAH04983.1.
    CCDSiCCDS9656.1.
    PIRiA39935.
    RefSeqiNP_065390.1. NM_020529.2.
    UniGeneiHs.81328.

    Genome annotation databases

    EnsembliENST00000216797; ENSP00000216797; ENSG00000100906.
    GeneIDi4792.
    KEGGihsa:4792.
    UCSCiuc001wtf.4. human.

    Polymorphism databases

    DMDMi126682.

    Cross-referencesi

    Web resourcesi

    NFKBIAbase

    NFKBIA mutation db

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69043 mRNA. Translation: AAA16489.1 .
    AJ249294
    , AJ249295 , AJ249283 , AJ249284 , AJ249285 , AJ249286 Genomic DNA. Translation: CAB65556.2 .
    AY033600 mRNA. Translation: AAK51149.1 .
    BT007091 mRNA. Translation: AAP35754.1 .
    AY496422 Genomic DNA. Translation: AAR29599.1 .
    AK313421 mRNA. Translation: BAG36213.1 .
    AL133163 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW65875.1 .
    BC002601 mRNA. Translation: AAH02601.1 .
    BC004983 mRNA. Translation: AAH04983.1 .
    CCDSi CCDS9656.1.
    PIRi A39935.
    RefSeqi NP_065390.1. NM_020529.2.
    UniGenei Hs.81328.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IKN X-ray 2.30 D 67-302 [» ]
    1NFI X-ray 2.70 E/F 70-282 [» ]
    DisProti DP00468.
    ProteinModelPortali P25963.
    SMRi P25963. Positions 3-294.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110859. 102 interactions.
    DIPi DIP-139N.
    IntActi P25963. 45 interactions.
    MINTi MINT-120458.
    STRINGi 9606.ENSP00000216797.

    Chemistry

    BindingDBi P25963.
    ChEMBLi CHEMBL2898.
    DrugBanki DB00945. Acetylsalicylic acid.

    PTM databases

    PhosphoSitei P25963.

    Polymorphism databases

    DMDMi 126682.

    Proteomic databases

    MaxQBi P25963.
    PaxDbi P25963.
    PeptideAtlasi P25963.
    PRIDEi P25963.

    Protocols and materials databases

    DNASUi 4792.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216797 ; ENSP00000216797 ; ENSG00000100906 .
    GeneIDi 4792.
    KEGGi hsa:4792.
    UCSCi uc001wtf.4. human.

    Organism-specific databases

    CTDi 4792.
    GeneCardsi GC14M035870.
    HGNCi HGNC:7797. NFKBIA.
    HPAi CAB003815.
    HPA029207.
    MIMi 164008. gene.
    612132. phenotype.
    neXtProti NX_P25963.
    Orphaneti 251579. Giant cell glioblastoma.
    251576. Gliosarcoma.
    98813. Hypohidrotic ectodermal dysplasia with immunodeficiency.
    PharmGKBi PA31601.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000059576.
    HOVERGENi HBG018875.
    InParanoidi P25963.
    KOi K04734.
    OMAi SIHGYLA.
    OrthoDBi EOG7W154S.
    PhylomeDBi P25963.
    TreeFami TF320166.

    Enzyme and pathway databases

    Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_12555. Downstream TCR signaling.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_24969. TRAF6 mediated NF-kB activation.
    SABIO-RK P25963.
    SignaLinki P25963.

    Miscellaneous databases

    ChiTaRSi NFKBIA. human.
    EvolutionaryTracei P25963.
    GeneWikii I%CE%BAB%CE%B1.
    GenomeRNAii 4792.
    NextBioi 18466.
    PMAP-CutDB P25963.
    PROi P25963.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25963.
    Bgeei P25963.
    CleanExi HS_NFKBIA.
    Genevestigatori P25963.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    [Graphical view ]
    Pfami PF00023. Ank. 4 hits.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 5 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of an immediate-early gene induced in adherent monocytes that encodes I kappa B-like activity."
      Haskill S., Beg A.A., Tompkins S.M., Morris J.S., Yurochko A.D., Sampson-Johannes A., Mondal K., Ralph P., Baldwin A.S. Jr.
      Cell 65:1281-1289(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Monocyte.
    2. "Clonal deleterious mutations in the IkappaB alpha gene in the malignant cells in Hodgkin's lymphoma."
      Jungnickel B., Staratschek-Jox A., Braeuninger A., Spieker T., Wolf J., Diehl V., Hansmann M.-L., Rajewsky K., Kueppers R.
      J. Exp. Med. 191:395-402(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Lymph node.
    3. "Homo sapiens IkBa mRNA."
      Liu B., Huang A.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. SeattleSNPs variation discovery resource
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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].
      Tissue: Cerebellum.
    7. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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].
      Tissue: Brain and Kidney.
    10. "I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B p65 DNA binding."
      Ganchi P.A., Sun S.C., Greene W.C., Ballard D.W.
      Mol. Biol. Cell 3:1339-1352(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RELA.
    11. "Signal-induced degradation of IkappaB alpha requires site-specific ubiquitination."
      Scherer D.C., Brockman J.A., Chen Z., Maniatis T., Ballard D.W.
      Proc. Natl. Acad. Sci. U.S.A. 92:11259-11263(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-21 AND LYS-22, FUNCTION, MUTAGENESIS OF LYS-21; LYS-22; LYS-38 AND LYS-47.
    12. "Tyrosine phosphorylation of IkappaB-alpha activates NF-kappaB without proteolytic degradation of IkappaB-alpha."
      Imbert V., Rupec R.A., Livolsi A., Pahl H.L., Traenckner E.B.-M., Mueller-Dieckmann C., Farahifar D., Rossi B., Auberger P., Baeuerle P.A., Peyron J.-F.
      Cell 86:787-798(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-42, MUTAGENESIS OF TYR-42.
    13. "Casein kinase II phosphorylates I kappa B alpha at S-283, S-289, S-293, and T-291 and is required for its degradation."
      McElhinny J.A., Trushin S.A., Bren G.D., Chester N., Paya C.V.
      Mol. Cell. Biol. 16:899-906(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-283; SER-288; SER-293 AND THR-291.
    14. "Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation."
      DiDonato J.A., Mercurio F., Rosette C., Wu-Li J., Suyang H., Ghosh S., Karin M.
      Mol. Cell. Biol. 16:1295-1304(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-21; LYS-22; ASP-31; SER-32; ASP-35; SER-36; SER-234; SER-262 AND THR-263.
    15. "Phosphorylation of IkappaBalpha in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability."
      Lin R., Beauparlant P., Makris C., Meloche S., Hiscott J.
      Mol. Cell. Biol. 16:1401-1409(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-291; SER-283 AND THR-299.
    16. "Nuclear localization of IkappaB alpha is mediated by the second ankyrin repeat: the IkappaB alpha ankyrin repeats define a novel class of cis-acting nuclear import sequences."
      Sachdev S., Hoffmann A., Hannink M.
      Mol. Cell. Biol. 18:2524-2534(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 115-LEU--ILE-120.
    17. "A complex containing betaTrCP recruits Cdc34 to catalyse ubiquitination of IkappaBalpha."
      Vuillard L., Nicholson J., Hay R.T.
      FEBS Lett. 455:311-314(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY THE SCF(FBXW11) COMPLEX.
    18. "Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha."
      Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C., Yamanaka K., Pagano M., Iwai K., Ciechanover A.
      J. Biol. Chem. 274:14823-14830(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-32 AND SER-36, MUTAGENESIS OF SER-32 AND SER-36, UBIQUITINATION BY UBE2D2 AND UBE2D3.
    19. "Direct association and nuclear import of the hepatitis B virus X protein with the NF-kappaB inhibitor IkappaBalpha."
      Weil R., Sirma H., Giannini C., Kremsdorf D., Bessia C., Dargemont C., Brechot C., Israel A.
      Mol. Cell. Biol. 19:6345-6354(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HBV PROTEIN X.
    20. "IKK epsilon is part of a novel PMA-inducible IkappaB kinase complex."
      Peters R.T., Liao S.-M., Maniatis T.
      Mol. Cell 5:513-522(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-32 AND SER-36.
    21. Cited for: PHOSPHORYLATION BY TBK1.
    22. "A subclass of Ras proteins that regulate the degradation of IkappaB."
      Fenwick C., Na S.-Y., Voll R.E., Zhong H., Im S.-Y., Lee J.W., Ghosh S.
      Science 287:869-873(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NKIRAS1 AND NKIRAS2.
    23. "A nuclear export signal in the N-terminal regulatory domain of IkappaBalpha controls cytoplasmic localization of inactive NF-kappaB/IkappaBalpha complexes."
      Huang T.T., Kudo N., Yoshida M., Miyamoto S.
      Proc. Natl. Acad. Sci. U.S.A. 97:1014-1019(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, MUTAGENESIS OF 45-MET--ILE-52.
    24. "SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting."
      Rodriguez M.S., Dargemont C., Hay R.T.
      J. Biol. Chem. 276:12654-12659(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-21, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-21 AND LYS-22.
    25. "Thrombin and collagen induce a feedback inhibitory signaling pathway in platelets involving dissociation of the catalytic subunit of protein kinase A from an NFkappaB-IkappaB complex."
      Gambaryan S., Kobsar A., Rukoyatkina N., Herterich S., Geiger J., Smolenski A., Lohmann S.M., Walter U.
      J. Biol. Chem. 285:18352-18363(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKACA.
    26. "Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis."
      Ganesh L., Yoshimoto T., Moorthy N.C., Akahata W., Boehm M., Nabel E.G., Nabel G.J.
      Mol. Cell. Biol. 26:3864-3874(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT2, SUBCELLULAR LOCATION.
    27. "Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)."
      Cockman M.E., Lancaster D.E., Stolze I.P., Hewitson K.S., McDonough M.A., Coleman M.L., Coles C.H., Yu X., Hay R.T., Ley S.C., Pugh C.W., Oldham N.J., Masson N., Schofield C.J., Ratcliffe P.J.
      Proc. Natl. Acad. Sci. U.S.A. 103:14767-14772(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-210 AND ASN-244, MUTAGENESIS OF ASN-210 AND ASN-244.
    28. "RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia."
      Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M., Silberstein S., Stalla G.K., Holsboer F., Arzt E.
      Cell 131:309-323(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RWDD3, SUMOYLATION, MUTAGENESIS OF LYS-21 AND LSY-22.
    29. "The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-kappaB through its N-terminal fragment."
      Chae J.J., Wood G., Richard K., Jaffe H., Colburn N.T., Masters S.L., Gumucio D.L., Shoham N.G., Kastner D.L.
      Blood 112:1794-1803(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEFV.
    30. "Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate."
      Wu K., Kovacev J., Pan Z.Q.
      Mol. Cell 37:784-796(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-21 AND LYS-22.
    31. "The cysteine protease domain of porcine reproductive and respiratory syndrome virus nonstructural protein 2 possesses deubiquitinating and interferon antagonism functions."
      Sun Z., Chen Z., Lawson S.R., Fang Y.
      J. Virol. 84:7832-7846(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEUBIQUITINATION BY PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME VIRUS NSP2 PROTEIN.
    32. "In silico structural and functional characterization of the RSUME splice variants."
      Gerez J., Fuertes M., Tedesco L., Silberstein S., Sevlever G., Paez-Pereda M., Holsboer F., Turjanski A.G., Arzt E.
      PLoS ONE 8:E57795-E57795(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RWDD3.
    33. "Structure of an IkappaBalpha/NF-kappaB complex."
      Jacobs M.D., Harrison S.C.
      Cell 95:749-758(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 70-282.
    34. "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 73-302.
    35. Cited for: VARIANT ADEDAID ILE-32.
    36. "A novel mutation in NFKBIA/IKBA results in a degradation-resistant N-truncated protein and is associated with ectodermal dysplasia with immunodeficiency."
      Lopez-Granados E., Keenan J.E., Kinney M.C., Leo H., Jain N., Ma C.A., Quinones R., Gelfand E.W., Jain A.
      Hum. Mutat. 29:861-868(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN ADEDAID.

    Entry informationi

    Entry nameiIKBA_HUMAN
    AccessioniPrimary (citable) accession number: P25963
    Secondary accession number(s): B2R8L6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 167 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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