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O14920

- IKKB_HUMAN

UniProt

O14920 - IKKB_HUMAN

Protein

Inhibitor of nuclear factor kappa-B kinase subunit beta

Gene

IKBKB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.7 Publications

    Catalytic activityi

    ATP + [I-kappa-B protein] = ADP + [I-kappa-B phosphoprotein].

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei44 – 441ATPPROSITE-ProRule annotation
    Active sitei145 – 1451Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi21 – 299ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. IkappaB kinase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein heterodimerization activity Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. protein kinase activity Source: UniProtKB
    7. protein kinase binding Source: UniProtKB
    8. protein serine/threonine kinase activity Source: Reactome
    9. scaffold protein binding Source: MGI

    GO - Biological processi

    1. B cell homeostasis Source: Ensembl
    2. cellular response to tumor necrosis factor Source: UniProtKB
    3. Fc-epsilon receptor signaling pathway Source: Reactome
    4. I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    5. I-kappaB phosphorylation Source: GOC
    6. inflammatory response Source: UniProtKB
    7. innate immune response Source: UniProtKB
    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. neurotrophin TRK receptor signaling pathway Source: Reactome
    12. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    13. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
    14. positive regulation of cation channel activity Source: Ensembl
    15. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Reactome
    16. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    17. positive regulation of sodium ion transport Source: Ensembl
    18. positive regulation of transcription, DNA-templated Source: UniProtKB
    19. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    20. positive regulation of type I interferon production Source: Reactome
    21. protein phosphorylation Source: UniProtKB
    22. response to virus Source: UniProtKB
    23. serine phosphorylation of STAT protein Source: UniProtKB
    24. T cell receptor signaling pathway Source: Reactome
    25. toll-like receptor 10 signaling pathway Source: Reactome
    26. toll-like receptor 2 signaling pathway Source: Reactome
    27. toll-like receptor 3 signaling pathway Source: Reactome
    28. toll-like receptor 4 signaling pathway Source: Reactome
    29. toll-like receptor 5 signaling pathway Source: Reactome
    30. toll-like receptor 9 signaling pathway Source: Reactome
    31. toll-like receptor signaling pathway Source: Reactome
    32. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    33. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    34. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.10. 2681.
    ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_12555. Downstream TCR signaling.
    REACT_13415. p75NTR recruits signalling complexes.
    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_22442. Interleukin-1 signaling.
    REACT_24918. IRAK1 recruits IKK complex.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_75776. NOD1/2 Signaling Pathway.
    SABIO-RKO14920.
    SignaLinkiO14920.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inhibitor of nuclear factor kappa-B kinase subunit beta (EC:2.7.11.10)
    Short name:
    I-kappa-B-kinase beta
    Short name:
    IKK-B
    Short name:
    IKK-beta
    Short name:
    IkBKB
    Alternative name(s):
    I-kappa-B kinase 2
    Short name:
    IKK2
    Nuclear factor NF-kappa-B inhibitor kinase beta
    Short name:
    NFKBIKB
    Gene namesi
    Name:IKBKB
    Synonyms:IKKB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:5960. IKBKB.

    Subcellular locationi

    Cytoplasm. Nucleus. Membrane raft
    Note: Colocalized with DPP4 in membrane rafts.

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. cytoplasm Source: HPA
    3. cytoplasmic side of plasma membrane Source: BHF-UCL
    4. cytosol Source: Reactome
    5. IkappaB kinase complex Source: UniProtKB
    6. membrane raft Source: UniProtKB-SubCell
    7. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Immunodeficiency 15 (IMD15) [MIM:615592]: An autosomal recessive primary immunodeficiency disorder characterized by onset in infancy of life-threatening bacterial, fungal, and viral infections and failure to thrive. Laboratory studies show hypo- or agammaglobulinemia with relatively normal numbers of B and T-cells, and impaired differentiation and activation of immune cells.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441K → A: Loss of kinase activity and no effect on binding to NIK. 3 Publications
    Mutagenesisi163 – 1631K → R: Monoubiquitinated; when associated with E-177 and E-181. 2 Publications
    Mutagenesisi177 – 1815SLCTS → ALCTA: COmplete loss of TBK1-mediated phosphorylation. 3 Publications
    Mutagenesisi177 – 1771S → A: Decrease of activity. 3 Publications
    Mutagenesisi177 – 1771S → E: Full activation. Interaction with TRIM21 is enhanced; when associated with E-181. Monoubiquitinated; when associated with R-163 and E-181. Strongly promoted NF-kappa-B gene expression; when associated with E-181. 3 Publications
    Mutagenesisi181 – 1811S → A: Decrease of activity. 3 Publications
    Mutagenesisi181 – 1811S → E: Full activation. Interaction with TRIM21 is enhanced; when associated with E-177. Monoubiquitinated; when associated with R-163 and E-177. Strongly promoted NF-kappa-B gene expression; when associated with E-177. 3 Publications
    Mutagenesisi191 – 1911P → A: Loss of hypoxic inducibility. 2 Publications

    Keywords - Diseasei

    SCID

    Organism-specific databases

    MIMi615592. phenotype.
    PharmGKBiPA29776.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 756756Inhibitor of nuclear factor kappa-B kinase subunit betaPRO_0000086013Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki163 – 163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Modified residuei177 – 1771Phosphoserine; by TBK1 and PKC/PRKCZ4 Publications
    Modified residuei179 – 1791S-nitrosocysteine1 Publication
    Modified residuei180 – 1801O-acetylthreonine; by Yersinia yopJ2 Publications
    Modified residuei181 – 1811Phosphoserine; by TBK1, PKC/PRKCZ and PDPK15 Publications
    Modified residuei191 – 1911Hydroxyproline1 Publication
    Modified residuei670 – 6701Phosphoserine; by autocatalysis2 Publications
    Modified residuei672 – 6721Phosphoserine4 Publications
    Modified residuei675 – 6751Phosphoserine; by autocatalysis2 Publications
    Modified residuei682 – 6821Phosphoserine; by autocatalysis2 Publications
    Modified residuei689 – 6891Phosphoserine; by autocatalysis2 Publications
    Modified residuei692 – 6921Phosphoserine; by autocatalysis2 Publications
    Modified residuei695 – 6951Phosphoserine; by autocatalysis2 Publications
    Modified residuei697 – 6971Phosphoserine; by autocatalysis2 Publications
    Modified residuei705 – 7051Phosphoserine; by autocatalysis2 Publications
    Modified residuei733 – 7331Phosphoserine; by autocatalysis2 Publications
    Modified residuei740 – 7401Phosphoserine; by autocatalysis2 Publications
    Modified residuei750 – 7501Phosphoserine; by autocatalysis2 Publications

    Post-translational modificationi

    Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which enhances activity. Once activated, autophosphorylates on the C-terminal serine cluster; which decreases activity and prevents prolonged activation of the inflammatory response. Phosphorylated by the IKK-related kinases TBK1 and IKBKE, which is associated with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent gene transcription. Dephosphorylated at Ser-177 and Ser-181 by PPM1A and PPM1B.4 Publications
    Acetylation of Thr-180 by Yersinia yopJ prevents phosphorylation and activation, thus blocking the I-kappa-B pathway.2 Publications
    Ubiquitinated. Monoubiquitination involves TRIM21 that leads to inhibition of Tax-induced NF-kappa-B signaling. According to PubMed:19675099, 'Ser-163' does not serve as a monoubiquitination site. According to PubMed:16267042, ubiquitination on 'Ser-163' modulates phosphorylation on C-terminal serine residues. Monoubiquitination by TRIM21 is disrupted by Yersinia yopJ.2 Publications
    Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic conditions results in activation of NF-kappaB.1 Publication

    Keywords - PTMi

    Acetylation, Hydroxylation, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiO14920.
    PaxDbiO14920.
    PRIDEiO14920.

    PTM databases

    PhosphoSiteiO14920.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, placenta, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis and peripheral blood.

    Gene expression databases

    ArrayExpressiO14920.
    BgeeiO14920.
    CleanExiHS_IKBKB.
    GenevestigatoriO14920.

    Organism-specific databases

    HPAiCAB004447.
    HPA001249.

    Interactioni

    Subunit structurei

    Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex. The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65. Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. Interacts with SQSTM1 through PRKCZ or PRKCI. Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6. May interact with MAVS/IPS1. Interacts with NALP2. Interacts with TICAM1. Interacts with Yersinia yopJ. Interacts with FAF1; the interaction disrupts the IKK complex formation. Interacts with ATM. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with NIBP; the interaction is direct. Interacts with ARRB1 and ARRB2. Interacts with TRIM21. Interacts with NLRC5; prevents IKBKB phosphorylation and kinase activity. Interacts with PDPK1. Interacts with EIF2AK2/PKR. The phosphorylated form interacts with PPM1A and PPM1B. Interacts with ZNF268 isoform 2; the interaction is further increased in a TNF-alpha-dependent manner. Interacts with IKBKE. Interacts with NAA10, leading to NAA10 degradation By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC37Q165433EBI-81266,EBI-295634
    CHUKO1511113EBI-81266,EBI-81249
    CREBBPQ927932EBI-81266,EBI-81215
    HSP90AB1P082382EBI-81266,EBI-352572
    IKBKGQ9Y6K924EBI-81266,EBI-81279
    KEAP1Q141456EBI-81266,EBI-751001
    MAP3K14Q995583EBI-81266,EBI-358011
    NCOA3Q9Y6Q93EBI-81266,EBI-81196
    NFKBIAP2596312EBI-81266,EBI-307386
    PPP2CAP677753EBI-81266,EBI-712311
    RPS3P233964EBI-81266,EBI-351193
    STAP2Q9UGK37EBI-81266,EBI-1553984
    taxP034093EBI-81266,EBI-5236464From a different organism.
    TSC1Q925743EBI-81266,EBI-1047085
    VACWR196P247723EBI-81266,EBI-4291651From a different organism.
    Zc3h12aQ5D1E74EBI-81266,EBI-5326026From a different organism.

    Protein-protein interaction databases

    BioGridi109767. 113 interactions.
    DIPiDIP-27527N.
    IntActiO14920. 59 interactions.
    MINTiMINT-107608.
    STRINGi9606.ENSP00000339151.

    Structurei

    Secondary structure

    1
    756
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 228
    Beta strandi29 – 346
    Turni35 – 373
    Beta strandi40 – 445
    Helixi52 – 6716
    Turni81 – 833
    Helixi84 – 863
    Beta strandi87 – 915
    Beta strandi94 – 974
    Helixi104 – 1096
    Helixi111 – 1133
    Helixi119 – 13820
    Helixi148 – 1503
    Beta strandi151 – 1555
    Beta strandi157 – 1648
    Helixi182 – 1854
    Turni186 – 1883
    Helixi191 – 1955
    Helixi202 – 21716
    Helixi228 – 2358
    Beta strandi244 – 2474
    Beta strandi253 – 2586
    Helixi267 – 28014
    Turni285 – 2895
    Turni292 – 2943
    Turni296 – 2983
    Helixi299 – 3079
    Beta strandi310 – 3167
    Turni317 – 3204
    Beta strandi321 – 3277
    Helixi333 – 34412
    Helixi348 – 3503
    Beta strandi353 – 3553
    Helixi367 – 3704
    Turni382 – 3854
    Beta strandi386 – 3894
    Helixi408 – 4158
    Helixi423 – 49977
    Turni500 – 5045
    Helixi509 – 52012
    Helixi527 – 54822
    Helixi559 – 57517
    Helixi579 – 5813
    Helixi588 – 66174
    Helixi706 – 72924
    Helixi734 – 7363
    Helixi740 – 7423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BRTX-ray2.25A/C701-730[»]
    3BRVX-ray2.20A/C701-745[»]
    4E3CX-ray3.98A/B/C/D/E/F11-669[»]
    4KIKX-ray2.83A/B2-664[»]
    ProteinModelPortaliO14920.
    SMRiO14920. Positions 2-663, 702-743.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14920.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 300286Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni458 – 47922Leucine-zipperAdd
    BLAST
    Regioni737 – 7426NEMO-binding

    Domaini

    The kinase domain is located in the N-terminal region. The leucine zipper is important to allow homo- and hetero-dimerization. At the C-terminal region is located the region responsible for the interaction with NEMO/IKBKG.1 Publication

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000038048.
    HOVERGENiHBG018241.
    InParanoidiO14920.
    KOiK07209.
    OMAiWEAFEKV.
    OrthoDBiEOG7FBRH3.
    PhylomeDBiO14920.
    TreeFamiTF324269.

    Family and domain databases

    InterProiIPR022007. IKKbetaNEMObind.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF12179. IKKbetaNEMObind. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14920-1) [UniParc]FASTAAdd to Basket

    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

    MSWSPSLTTQ TCGAWEMKER LGTGGFGNVI RWHNQETGEQ IAIKQCRQEL    50
    SPRNRERWCL EIQIMRRLTH PNVVAARDVP EGMQNLAPND LPLLAMEYCQ 100
    GGDLRKYLNQ FENCCGLREG AILTLLSDIA SALRYLHENR IIHRDLKPEN 150
    IVLQQGEQRL IHKIIDLGYA KELDQGSLCT SFVGTLQYLA PELLEQQKYT 200
    VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE VDIVVSEDLN 250
    GTVKFSSSLP YPNNLNSVLA ERLEKWLQLM LMWHPRQRGT DPTYGPNGCF 300
    KALDDILNLK LVHILNMVTG TIHTYPVTED ESLQSLKARI QQDTGIPEED 350
    QELLQEAGLA LIPDKPATQC ISDGKLNEGH TLDMDLVFLF DNSKITYETQ 400
    ISPRPQPESV SCILQEPKRN LAFFQLRKVW GQVWHSIQTL KEDCNRLQQG 450
    QRAAMMNLLR NNSCLSKMKN SMASMSQQLK AKLDFFKTSI QIDLEKYSEQ 500
    TEFGITSDKL LLAWREMEQA VELCGRENEV KLLVERMMAL QTDIVDLQRS 550
    PMGRKQGGTL DDLEEQAREL YRRLREKPRD QRTEGDSQEM VRLLLQAIQS 600
    FEKKVRVIYT QLSKTVVCKQ KALELLPKVE EVVSLMNEDE KTVVRLQEKR 650
    QKELWNLLKI ACSKVRGPVS GSPDSMNASR LSQPGQLMSQ PSTASNSLPE 700
    PAKKSEELVA EAHNLCTLLE NAIQDTVREQ DQSFTALDWS WLQTEEEEHS 750
    CLEQAS 756
    Length:756
    Mass (Da):86,564
    Last modified:January 1, 1998 - v1
    Checksum:iF9CADF671AE9E14E
    GO
    Isoform 2 (identifier: O14920-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHN → MFSGGCHSPGFGRPSPAFPAPGSPPPAPRPCR

    Show »
    Length:754
    Mass (Da):85,945
    Checksum:i9C31F5C1DC92661E
    GO
    Isoform 3 (identifier: O14920-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         231-256: WHSKVRQKSEVDIVVSEDLNGTVKFS → CVRMWPGTVAHSCNPSTLGGRGRWIS
         257-756: Missing.

    Show »
    Length:256
    Mass (Da):29,236
    Checksum:i8B4762DD49F4065A
    GO
    Isoform 4 (identifier: O14920-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-66: MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMR → MSSDGTI

    Note: No experimental confirmation available.

    Show »
    Length:697
    Mass (Da):79,509
    Checksum:i21B61110941FE1D9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti259 – 2591L → S in BAG63942. (PubMed:14702039)Curated
    Sequence conflicti259 – 2591L → S in BAH14789. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti360 – 3601A → S in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. 2 Publications
    VAR_035626
    Natural varianti369 – 3691Q → R.1 Publication
    Corresponds to variant rs56411242 [ dbSNP | Ensembl ].
    VAR_040567
    Natural varianti526 – 5261R → Q.1 Publication
    Corresponds to variant rs2272736 [ dbSNP | Ensembl ].
    VAR_040568
    Natural varianti554 – 5541R → W.1 Publication
    Corresponds to variant rs17875749 [ dbSNP | Ensembl ].
    VAR_021124
    Natural varianti710 – 7101A → T.1 Publication
    Corresponds to variant rs34309584 [ dbSNP | Ensembl ].
    VAR_040569
    Natural varianti734 – 7341F → L.1 Publication
    Corresponds to variant rs56301637 [ dbSNP | Ensembl ].
    VAR_040570
    Natural varianti736 – 7361A → T.
    Corresponds to variant rs17611716 [ dbSNP | Ensembl ].
    VAR_051628

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6666MSWSP…IQIMR → MSSDGTI in isoform 4. 1 PublicationVSP_043408Add
    BLAST
    Alternative sequencei1 – 3434MSWSP…IRWHN → MFSGGCHSPGFGRPSPAFPA PGSPPPAPRPCR in isoform 2. 1 PublicationVSP_041825Add
    BLAST
    Alternative sequencei231 – 25626WHSKV…TVKFS → CVRMWPGTVAHSCNPSTLGG RGRWIS in isoform 3. 1 PublicationVSP_041826Add
    BLAST
    Alternative sequencei257 – 756500Missing in isoform 3. 1 PublicationVSP_041827Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF029684 mRNA. Translation: AAC51860.1.
    AF080158 mRNA. Translation: AAD08997.1.
    AF031416 mRNA. Translation: AAC64675.1.
    AK302723 mRNA. Translation: BAG63942.1.
    AK303528 mRNA. Translation: BAG64556.1.
    AK316418 mRNA. Translation: BAH14789.1.
    AY663108 Genomic DNA. Translation: AAT65965.1.
    AC083973 Genomic DNA. No translation available.
    BC006231 mRNA. Translation: AAH06231.1.
    CCDSiCCDS55228.1. [O14920-2]
    CCDS56535.1. [O14920-4]
    CCDS6128.1. [O14920-1]
    RefSeqiNP_001177649.1. NM_001190720.2. [O14920-2]
    NP_001229707.1. NM_001242778.1. [O14920-4]
    NP_001547.1. NM_001556.2. [O14920-1]
    UniGeneiHs.597664.

    Genome annotation databases

    EnsembliENST00000416505; ENSP00000404920; ENSG00000104365. [O14920-4]
    ENST00000519735; ENSP00000430483; ENSG00000104365. [O14920-3]
    ENST00000520810; ENSP00000430684; ENSG00000104365. [O14920-1]
    ENST00000520835; ENSP00000430868; ENSG00000104365. [O14920-2]
    GeneIDi3551.
    KEGGihsa:3551.
    UCSCiuc003xow.2. human. [O14920-1]
    uc011lcq.2. human. [O14920-2]
    uc011lcr.2. human. [O14920-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF029684 mRNA. Translation: AAC51860.1 .
    AF080158 mRNA. Translation: AAD08997.1 .
    AF031416 mRNA. Translation: AAC64675.1 .
    AK302723 mRNA. Translation: BAG63942.1 .
    AK303528 mRNA. Translation: BAG64556.1 .
    AK316418 mRNA. Translation: BAH14789.1 .
    AY663108 Genomic DNA. Translation: AAT65965.1 .
    AC083973 Genomic DNA. No translation available.
    BC006231 mRNA. Translation: AAH06231.1 .
    CCDSi CCDS55228.1. [O14920-2 ]
    CCDS56535.1. [O14920-4 ]
    CCDS6128.1. [O14920-1 ]
    RefSeqi NP_001177649.1. NM_001190720.2. [O14920-2 ]
    NP_001229707.1. NM_001242778.1. [O14920-4 ]
    NP_001547.1. NM_001556.2. [O14920-1 ]
    UniGenei Hs.597664.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BRT X-ray 2.25 A/C 701-730 [» ]
    3BRV X-ray 2.20 A/C 701-745 [» ]
    4E3C X-ray 3.98 A/B/C/D/E/F 11-669 [» ]
    4KIK X-ray 2.83 A/B 2-664 [» ]
    ProteinModelPortali O14920.
    SMRi O14920. Positions 2-663, 702-743.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109767. 113 interactions.
    DIPi DIP-27527N.
    IntActi O14920. 59 interactions.
    MINTi MINT-107608.
    STRINGi 9606.ENSP00000339151.

    Chemistry

    BindingDBi O14920.
    ChEMBLi CHEMBL2111328.
    DrugBanki DB01169. Arsenic trioxide.
    DB00995. Auranofin.
    GuidetoPHARMACOLOGYi 2039.

    PTM databases

    PhosphoSitei O14920.

    Proteomic databases

    MaxQBi O14920.
    PaxDbi O14920.
    PRIDEi O14920.

    Protocols and materials databases

    DNASUi 3551.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000416505 ; ENSP00000404920 ; ENSG00000104365 . [O14920-4 ]
    ENST00000519735 ; ENSP00000430483 ; ENSG00000104365 . [O14920-3 ]
    ENST00000520810 ; ENSP00000430684 ; ENSG00000104365 . [O14920-1 ]
    ENST00000520835 ; ENSP00000430868 ; ENSG00000104365 . [O14920-2 ]
    GeneIDi 3551.
    KEGGi hsa:3551.
    UCSCi uc003xow.2. human. [O14920-1 ]
    uc011lcq.2. human. [O14920-2 ]
    uc011lcr.2. human. [O14920-4 ]

    Organism-specific databases

    CTDi 3551.
    GeneCardsi GC08P042146.
    HGNCi HGNC:5960. IKBKB.
    HPAi CAB004447.
    HPA001249.
    MIMi 603258. gene.
    615592. phenotype.
    neXtProti NX_O14920.
    PharmGKBi PA29776.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000038048.
    HOVERGENi HBG018241.
    InParanoidi O14920.
    KOi K07209.
    OMAi WEAFEKV.
    OrthoDBi EOG7FBRH3.
    PhylomeDBi O14920.
    TreeFami TF324269.

    Enzyme and pathway databases

    BRENDAi 2.7.11.10. 2681.
    Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_12555. Downstream TCR signaling.
    REACT_13415. p75NTR recruits signalling complexes.
    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_22442. Interleukin-1 signaling.
    REACT_24918. IRAK1 recruits IKK complex.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_75776. NOD1/2 Signaling Pathway.
    SABIO-RK O14920.
    SignaLinki O14920.

    Miscellaneous databases

    EvolutionaryTracei O14920.
    GeneWikii IKK2.
    GenomeRNAii 3551.
    NextBioi 13864.
    PROi O14920.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14920.
    Bgeei O14920.
    CleanExi HS_IKBKB.
    Genevestigatori O14920.

    Family and domain databases

    InterProi IPR022007. IKKbetaNEMObind.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF12179. IKKbetaNEMObind. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation."
      Mercurio F., Zhu H., Murray B.W., Shevchenko A., Bennett B.L., Li J.W., Young D.B., Barbosa M., Mann M., Manning A., Rao A.
      Science 278:860-866(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-44; SER-177 AND SER-181.
      Tissue: Cervix carcinoma.
    2. "IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK."
      Woronicz J.D., Gao X., Cao Z., Rothe M., Goeddel D.V.
      Science 278:866-869(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-44.
    3. "IkappaB kinase-alpha and -beta genes are coexpressed in adult and embryonic tissues but localized to different human chromosomes."
      Hu M.C.-T., Wang Y.-P.
      Gene 222:31-40(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart.
    4. "Assignment of IkappaB kinase beta (IKBKB) to human chromosome band 8p12-->p11 by in situ hybridization."
      Shindo M., Nakano H., Sakon S., Yagita H., Mihara M., Okumura K.
      Cytogenet. Cell Genet. 82:32-33(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GENE MAPPING.
    5. "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] (ISOFORMS 2 AND 4).
      Tissue: Testis and Thymus.
    6. SeattleSNPs variation discovery resource
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TRP-554.
    7. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 3).
      Tissue: Lung.
    9. "Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling."
      Mittal R., Peak-Chew S.Y., McMahon H.T.
      Proc. Natl. Acad. Sci. U.S.A. 103:18574-18579(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 170-182 (ISOFORM 1), INACTIVATION BY YERSINIA YOPJ, ACETYLATION AT THR-180, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Coordinate regulation of IkappaB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-kappaB-inducing kinase."
      Nemoto S., DiDonato J.A., Lin A.
      Mol. Cell. Biol. 18:7336-7343(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IKK PHOSPHORYLATION.
    11. "IKAP is a scaffold protein of the IkappaB kinase complex."
      Cohen L., Henzel W.J., Baeuerle P.A.
      Nature 395:292-296(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CHUK; NFKBIA; RELA; IKBKAP AND MAP3K14.
    12. "The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."
      Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.
      EMBO J. 18:3044-3053(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SQSTM1; PRKCZ AND PRKCI.
    13. "Activation of IkappaB kinase beta by protein kinase C isoforms."
      Lallena M.J., Diaz-Meco M.T., Bren G., Paya C.V., Moscat J.
      Mol. Cell. Biol. 19:2180-2188(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-177 AND SER-181.
    14. "Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation."
      Delhase M., Hayakawa M., Chen Y., Karin M.
      Science 284:309-313(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-177; SER-181; SER-670; SER-672; SER-675; SER-682; SER-689; SER-692; SER-695; SER-697; SER-705; SER-733; SER-740 AND SER-750.
    15. "PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex."
      Bonnet M.C., Weil R., Dam E., Hovanessian A.G., Meurs E.F.
      Mol. Cell. Biol. 20:4532-4542(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF2AK2.
    16. Cited for: PHOSPHORYLATION AT SER-177 AND SER-181 BY TBK1, MUTAGENESIS OF 177-SER--SER-181.
    17. "Direct phosphorylation of NF-kappa B1 p105 by the Ikappa B kinase complex on serine 927 is essential for signal-induced p105 proteolysis."
      Salmeron A., Janzen J., Soneji Y., Bump N., Kamens J., Allen H., Ley S.C.
      J. Biol. Chem. 276:22215-22222(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF NFKB1.
    18. "Association of the adaptor TANK with the I kappa B kinase (IKK) regulator NEMO connects IKK complexes with IKK epsilon and TBK1 kinases."
      Chariot A., Leonardi A., Muller J., Bonif M., Brown K., Siebenlist U.
      J. Biol. Chem. 277:37029-37036(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IKBKG AND TANK.
    19. "Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase."
      Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J., O'Malley B.W.
      Mol. Cell. Biol. 22:3549-3561(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CREBBP; NCOA2; NCOA3; IKKA AND IKBKG.
    20. "Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation."
      Tegethoff S., Behlke J., Scheidereit C.
      Mol. Cell. Biol. 23:2029-2041(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPOSITION OF THE IKK COMPLEX.
    21. "Mechanisms of the TRIF-induced interferon-stimulated response element and NF-kappaB activation and apoptosis pathways."
      Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.
      J. Biol. Chem. 279:15652-15661(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM1.
    22. "PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-kappaB and caspase-1 activation in macrophages."
      Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C., Reed J.C.
      J. Biol. Chem. 279:51897-51907(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NALP2.
    23. "beta-Arrestin inhibits NF-kappaB activity by means of its interaction with the NF-kappaB inhibitor IkappaBalpha."
      Witherow D.S., Garrison T.R., Miller W.E., Lefkowitz R.J.
      Proc. Natl. Acad. Sci. U.S.A. 101:8603-8607(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB1 AND ARRB2.
    24. Cited for: S-NITROSYLATION AT CYS-179.
    25. "NIBP, a novel NIK and IKK(beta)-binding protein that enhances NF-(kappa)B activation."
      Hu W.-H., Pendergast J.S., Mo X.-M., Brambilla R., Bracchi-Ricard V., Li F., Walters W.M., Blits B., He L., Schaal S.M., Bethea J.R.
      J. Biol. Chem. 280:29233-29241(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NIBP.
    26. "3-Phosphoinositide-dependent protein kinase-1-mediated IkappaB kinase beta (IkkB) phosphorylation activates NF-kappaB signaling."
      Tanaka H., Fujita N., Tsuruo T.
      J. Biol. Chem. 280:40965-40973(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-181 BY PDPK1, INTERACTION WITH PDPK1.
    27. "Site-specific monoubiquitination of IkappaB kinase IKKbeta regulates its phosphorylation and persistent activation."
      Carter R.S., Pennington K.N., Arrate P., Oltz E.M., Ballard D.W.
      J. Biol. Chem. 280:43272-43279(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-163.
    28. "Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus."
      Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., Tschopp J.
      Nature 437:1167-1172(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAVS.
    29. "Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving insight into hypoxia-induced NFkappaB activity."
      Cummins E.P., Berra E., Comerford K.M., Ginouves A., Fitzgerald K.T., Seeballuck F., Godson C., Nielsen J.E., Moynagh P., Pouyssegur J., Taylor C.T.
      Proc. Natl. Acad. Sci. U.S.A. 103:18154-18159(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: HYDROXYLATION AT PRO-191, MUTAGENESIS OF PRO-191.
    30. "Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation."
      Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J., Orth K.
      Science 312:1211-1214(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YOPJ, ACETYLATION.
    31. "Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli."
      Wu Z.H., Shi Y., Tibbetts R.S., Miyamoto S.
      Science 311:1141-1146(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATM.
    32. Cited for: IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, SUBCELLULAR LOCATION.
    33. "FAF1 suppresses IkappaB kinase (IKK) activation by disrupting the IKK complex assembly."
      Park M.Y., Moon J.H., Lee K.S., Choi H.I., Chung J., Hong H.J., Kim E.
      J. Biol. Chem. 282:27572-27577(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FAF1.
    34. "Negative feedback loop in T cell activation through IkappaB kinase-induced phosphorylation and degradation of Bcl10."
      Lobry C., Lopez T., Israel A., Weil R.
      Proc. Natl. Acad. Sci. U.S.A. 104:908-913(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BCL10.
    35. "The I kappa B/NF-kappa B system: a key determinant of mucosal inflammation and protection."
      Jobin C., Sartor R.B.
      Am. J. Physiol. 278:C451-C462(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    36. "The IkappaB kinase complex: master regulator of NF-kappaB signaling."
      Solt L.A., May M.J.
      Immunol. Res. 42:3-18(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, DOMAIN.
    37. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    38. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    39. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "Phosphorylation of ARD1 by IKKbeta contributes to its destabilization and degradation."
      Kuo H.P., Lee D.F., Xia W., Lai C.C., Li L.Y., Hung M.C.
      Biochem. Biophys. Res. Commun. 389:156-161(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NAA10, FUNCTION IN PHOSPHORYLATION OF NAA10.
    41. "PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation."
      Sun W., Yu Y., Dotti G., Shen T., Tan X., Savoldo B., Pass A.K., Chu M., Zhang D., Lu X., Fu S., Lin X., Yang J.
      Cell. Signal. 21:95-102(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEPHOSPHORYLATION AT SER-177 AND SER-181, INTERACTION WITH PPM1A AND PPM1B.
    42. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    43. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    44. "NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways."
      Cui J., Zhu L., Xia X., Wang H.Y., Legras X., Hong J., Ji J., Shen P., Zheng S., Chen Z.J., Wang R.F.
      Cell 141:483-496(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NLRC5.
    45. "Ro52-mediated monoubiquitination of IKK{beta} down-regulates NF-{kappa}B signalling."
      Wada K., Niida M., Tanaka M., Kamitani T.
      J. Biochem. 146:821-832(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM21, MONOUBIQUITINATION, UBIQUITINATION INACTIVATION BY YERSINIA YOPJ, MUTAGENESIS OF LYS-163; SER-177 AND SER-181.
    46. "Respiratory syncytial virus-mediated NF-kappa B p65 phosphorylation at serine 536 is dependent on RIG-I, TRAF6, and IKK beta."
      Yoboua F., Martel A., Duval A., Mukawera E., Grandvaux N.
      J. Virol. 84:7267-7277(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RELA.
    47. "Nuclear IKKbeta is an adaptor protein for IkappaBalpha ubiquitination and degradation in UV-induced NF-kappaB activation."
      Tsuchiya Y., Asano T., Nakayama K., Kato T. Jr., Karin M., Kamata H.
      Mol. Cell 39:570-582(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.
    48. "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.
    49. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    50. Cited for: FUNCTION, PHOSPHORYLATION BY TBK1 AND IKBKE.
    51. "The zinc finger protein ZNF268 is overexpressed in human cervical cancer and contributes to tumorigenesis via enhancing NF-kappaB signaling."
      Wang W., Guo M., Hu L., Cai J., Zeng Y., Luo J., Shu Z., Li W., Huang Z.
      J. Biol. Chem. 287:42856-42866(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF268, SUBUNIT.
    52. "IKKepsilon-mediated tumorigenesis requires K63-linked polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase complex."
      Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.
      Cell Rep. 3:724-733(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IKBKE.
    53. Cited for: INVOLVEMENT IN IMD15.
    54. "Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site."
      Rushe M., Silvian L., Bixler S., Chen L.L., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A.
      Structure 16:798-808(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 701-742.
    55. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-360.
    56. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-360; ARG-369; GLN-526; THR-710 AND LEU-734.

    Entry informationi

    Entry nameiIKKB_HUMAN
    AccessioniPrimary (citable) accession number: O14920
    Secondary accession number(s): B4DZ30, B4E0U4, O75327
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 166 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3