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O88522

- NEMO_MOUSE

UniProt

O88522 - NEMO_MOUSE

Protein

NF-kappa-B essential modulator

Gene

Ikbkg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri389 – 41022C2HC-typeAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein heterodimerization activity Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. activation of NF-kappaB-inducing kinase activity Source: MGI
    2. B cell homeostasis Source: MGI
    3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198543. IRAK1 recruits IKK complex.
    REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_199121. Activation of NF-kappaB in B cells.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_204812. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_211125. NOD1/2 Signaling Pathway.
    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:
    NF-kappa-B essential modulator
    Short name:
    NEMO
    Alternative name(s):
    IkB kinase-associated protein 1
    Short name:
    IKKAP1
    Short name:
    mFIP-3
    Inhibitor of nuclear factor kappa-B kinase subunit gamma
    Short name:
    I-kappa-B kinase subunit gamma
    Short name:
    IKK-gamma
    Short name:
    IKKG
    Short name:
    IkB kinase subunit gamma
    NF-kappa-B essential modifier
    Gene namesi
    Name:Ikbkg
    Synonyms:Nemo
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1338074. Ikbkg.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. IkappaB kinase complex Source: MGI
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi278 – 2781K → R: Slight decrease in TRAF6-induced polyubiquitination. 1 Publication
    Mutagenesisi293 – 2931V → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-301 and A-302. 1 Publication
    Mutagenesisi301 – 3011Y → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-293 and A-302. 1 Publication
    Mutagenesisi302 – 3021K → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-293 and A-301. 1 Publication
    Mutagenesisi305 – 3051F → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs of NF-kappa-B activation. 1 Publication
    Mutagenesisi309 – 3091R → A: Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-312 and A-313. 1 Publication
    Mutagenesisi312 – 3121R → A: Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-309 and A-313. 1 Publication
    Mutagenesisi313 – 3131E → A: Impairs linear polyubiquitin-binding. Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-309 and A-312. Abolishes linear polyubiquitin-binding; when associated with A-317 and A-320. 1 Publication
    Mutagenesisi314 – 3141K → R: Slight decrease in TRAF6-induced polyubiquitination. Important decrease in TRAF6-induced polyubiquitination; when associated with R-318 and R-319. 1 Publication
    Mutagenesisi316 – 3161V → P: Loss of interaction with TRAF6 and TRAF6-induced polyubiquitination. 1 Publication
    Mutagenesisi317 – 3171E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-320. 1 Publication
    Mutagenesisi318 – 3181K → R: Slight decrease in TRAF6-induced polyubiquitination. Decrease in TRAF6-induced polyubiquitination; when associated with R-319. Important decrease in TRAF6-induced polyubiquitination; when associated with R-314 and R-319. 1 Publication
    Mutagenesisi319 – 3191K → R: Slight decrease in TRAF6-induced polyubiquitination. Decrease in TRAF6-induced polyubiquitination; when associated with R-318. Important decrease in TRAF6-induced polyubiquitination; when associated with R-314 and R-318. 1 Publication
    Mutagenesisi320 – 3201E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-317. 1 Publication
    Mutagenesisi369 – 3691S → A: Decreases phosphorylation and increases NF-kappa-B activity. 1 Publication
    Mutagenesisi375 – 3751S → A: Decreases phosphorylation and increases NF-kappa-B activity. 1 Publication
    Mutagenesisi392 – 3921K → R: 40% decrease in IL1-induced NF-kappa-B activation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 412412NF-kappa-B essential modulatorPRO_0000096783Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311Phosphoserine; by IKKBBy similarity
    Modified residuei43 – 431Phosphoserine; by IKKBBy similarity
    Disulfide bondi54 – 54InterchainBy similarity
    Modified residuei68 – 681PhosphoserineBy similarity
    Modified residuei85 – 851Phosphoserine; by ATMBy similarity
    Cross-linki111 – 111Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki139 – 139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki143 – 143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki226 – 226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki246 – 246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki270 – 270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Cross-linki270 – 270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Cross-linki276 – 276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki278 – 278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki285 – 285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki295 – 295Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki302 – 302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Cross-linki302 – 302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Cross-linki314 – 314Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki318 – 318Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki319 – 319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Disulfide bondi340 – 340InterchainBy similarity
    Modified residuei369 – 3691Phosphoserine; by IKKB1 Publication
    Modified residuei380 – 3801PhosphoserineBy similarity
    Cross-linki392 – 392Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-68 attenuates aminoterminal homodimerization.By similarity
    Polyubiquitinated on Lys-278 through 'Lys-63'; the ubiquitination is mediated by NOD2 and RIPK2 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway. Polyubiquitinated on Lys-392 through 'Lys-63'; the ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway. Monoubiquitinated on Lys-270 and Lys-302; promotes nuclear export. Polyubiquitinated through 'Lys-27' by TRIM23; involved in antiviral innate and inflammatory responses. Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-270, Lys-278, Lys-285, Lys-295, Lys-302 and Lys-319; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation By similarity.By similarity
    Sumoylated on Lys-270 and Lys-302 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.By similarity
    Neddylated by TRIM40, resulting in stabilization of NFKBIA and down-regulation of NF-kappa-B activity.By similarity

    Keywords - PTMi

    Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO88522.
    PaxDbiO88522.
    PRIDEiO88522.

    PTM databases

    PhosphoSiteiO88522.

    Expressioni

    Gene expression databases

    ArrayExpressiO88522.
    BgeeiO88522.
    CleanExiMM_IKBKG.
    GenevestigatoriO88522.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. 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. Interacts with COPS3, CYLD, NALP2, TRPC4AP and LRDD. Interacts with ATM; the complex is exported from the nucleus. Interacts with TRAF6. Interacts with IKBKE. Interacts with TANK; the interaction is enhanced by TBK1 and IKBKE. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with ZFAND5. Interacts with RIPK2. Interacts with TNIP1 and TNFAIP3; TNIP1 facilitates the TNFAIP3-mediated de-ubiquitination of IKBKG. Interacts with TNFAIP3; the interaction is induced by TNF stimulation and by polyubiquitin. Interacts with NLRP10.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ChukQ606804EBI-998011,EBI-646245
    IkbkbO883513EBI-998011,EBI-447960
    Rnf31Q924T72EBI-998011,EBI-647680
    UBCP0CG483EBI-998011,EBI-3390054From a different organism.
    UbcP629912EBI-998011,EBI-413074
    VACWR196P247722EBI-998011,EBI-4291651From a different organism.

    Protein-protein interaction databases

    BioGridi200602. 41 interactions.
    DIPiDIP-29811N.
    IntActiO88522. 14 interactions.
    MINTiMINT-143245.
    STRINGi10090.ENSMUSP00000004330.

    Structurei

    Secondary structure

    1
    412
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi253 – 28937
    Helixi291 – 33343

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V4HX-ray2.90A/B251-337[»]
    2ZVNX-ray3.00B/D/F/H253-337[»]
    2ZVOX-ray2.90B/D250-339[»]
    3F89X-ray2.80A/B250-339[»]
    3JSVX-ray2.70C/D250-343[»]
    4OWFX-ray2.00A/B250-339[»]
    ProteinModelPortaliO88522.
    SMRiO88522. Positions 49-109, 193-248, 256-341, 387-412.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO88522.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni44 – 11168Interaction with CHUK/IKBKBBy similarityAdd
    BLAST
    Regioni150 – 250101Interaction with TANKAdd
    BLAST
    Regioni242 – 343102Ubiquitin-binding (UBD)Add
    BLAST
    Regioni246 – 358113Self-associationBy similarityAdd
    BLAST
    Regioni249 – 412164Required for interaction with TNFAIP3By similarityAdd
    BLAST
    Regioni250 – 33990Linear polyubiquitin-binding, does not bind to 'Lys-63'-linked polyubiquitinAdd
    BLAST
    Regioni315 – 33622Leucine-zipperSequence AnalysisAdd
    BLAST
    Regioni375 – 41238Interaction with CYLDBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili49 – 345297Sequence AnalysisAdd
    BLAST

    Domaini

    The leucine-zipper domain and the C2HC-type zinc-finger are essential for polyubiquitin binding and for the activation of IRF3.By similarity

    Sequence similaritiesi

    Contains 1 C2HC-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri389 – 41022C2HC-typeAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG138369.
    GeneTreeiENSGT00530000063808.
    HOGENOMiHOG000293233.
    HOVERGENiHBG000417.
    InParanoidiQ924H4.
    KOiK07210.
    TreeFamiTF326608.

    Family and domain databases

    InterProiIPR021063. NEMO_N.
    [Graphical view]
    PfamiPF11577. NEMO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O88522-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKHPWKNQL SEMVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET    50
    LQRCLEENQE LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA 100
    RKLVERLSLE KLDLRSQREQ ALKELEQLKK CQQQMAEDKA SVKAQVTSLL 150
    GELQESQSRL EAATKDRQAL EGRIRAVSEQ VRQLESEREV LQQQHSVQVD 200
    QLRMQNQSVE AALRMERQAA SEEKRKLAQL QAAYHQLFQD YDSHIKSSKG 250
    MQLEDLRQQL QQAEEALVAK QELIDKLKEE AEQHKIVMET VPVLKAQADI 300
    YKADFQAERH AREKLVEKKE YLQEQLEQLQ REFNKLKVGC HESARIEDMR 350
    KRHVETPQPP LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM 400
    DTLQIHVMEC IE 412
    Length:412
    Mass (Da):47,972
    Last modified:July 27, 2011 - v2
    Checksum:i66C693C857A2D5E6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131M → T in AAC40153. (PubMed:9657155)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF069542 mRNA. Translation: AAC40153.1.
    AF326207 Genomic DNA. Translation: AAK69186.1.
    AF513109 mRNA. Translation: AAP47160.1.
    AK154095 mRNA. Translation: BAE32372.1.
    AL669976 Genomic DNA. Translation: CAM45971.1.
    CH466650 Genomic DNA. Translation: EDL29810.1.
    CCDSiCCDS41023.1.
    RefSeqiNP_001154895.1. NM_001161423.1.
    NP_034677.2. NM_010547.2.
    XP_006527913.1. XM_006527850.1.
    XP_006527914.1. XM_006527851.1.
    XP_006527915.1. XM_006527852.1.
    UniGeneiMm.12967.

    Genome annotation databases

    EnsembliENSMUST00000114127; ENSMUSP00000109762; ENSMUSG00000004221.
    ENSMUST00000114128; ENSMUSP00000109763; ENSMUSG00000004221.
    ENSMUST00000114133; ENSMUSP00000109768; ENSMUSG00000004221.
    ENSMUST00000164101; ENSMUSP00000126770; ENSMUSG00000004221.
    GeneIDi16151.
    KEGGimmu:16151.
    UCSCiuc009toz.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF069542 mRNA. Translation: AAC40153.1 .
    AF326207 Genomic DNA. Translation: AAK69186.1 .
    AF513109 mRNA. Translation: AAP47160.1 .
    AK154095 mRNA. Translation: BAE32372.1 .
    AL669976 Genomic DNA. Translation: CAM45971.1 .
    CH466650 Genomic DNA. Translation: EDL29810.1 .
    CCDSi CCDS41023.1.
    RefSeqi NP_001154895.1. NM_001161423.1.
    NP_034677.2. NM_010547.2.
    XP_006527913.1. XM_006527850.1.
    XP_006527914.1. XM_006527851.1.
    XP_006527915.1. XM_006527852.1.
    UniGenei Mm.12967.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V4H X-ray 2.90 A/B 251-337 [» ]
    2ZVN X-ray 3.00 B/D/F/H 253-337 [» ]
    2ZVO X-ray 2.90 B/D 250-339 [» ]
    3F89 X-ray 2.80 A/B 250-339 [» ]
    3JSV X-ray 2.70 C/D 250-343 [» ]
    4OWF X-ray 2.00 A/B 250-339 [» ]
    ProteinModelPortali O88522.
    SMRi O88522. Positions 49-109, 193-248, 256-341, 387-412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200602. 41 interactions.
    DIPi DIP-29811N.
    IntActi O88522. 14 interactions.
    MINTi MINT-143245.
    STRINGi 10090.ENSMUSP00000004330.

    PTM databases

    PhosphoSitei O88522.

    Proteomic databases

    MaxQBi O88522.
    PaxDbi O88522.
    PRIDEi O88522.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000114127 ; ENSMUSP00000109762 ; ENSMUSG00000004221 .
    ENSMUST00000114128 ; ENSMUSP00000109763 ; ENSMUSG00000004221 .
    ENSMUST00000114133 ; ENSMUSP00000109768 ; ENSMUSG00000004221 .
    ENSMUST00000164101 ; ENSMUSP00000126770 ; ENSMUSG00000004221 .
    GeneIDi 16151.
    KEGGi mmu:16151.
    UCSCi uc009toz.2. mouse.

    Organism-specific databases

    CTDi 8517.
    MGIi MGI:1338074. Ikbkg.

    Phylogenomic databases

    eggNOGi NOG138369.
    GeneTreei ENSGT00530000063808.
    HOGENOMi HOG000293233.
    HOVERGENi HBG000417.
    InParanoidi Q924H4.
    KOi K07210.
    TreeFami TF326608.

    Enzyme and pathway databases

    Reactomei REACT_198543. IRAK1 recruits IKK complex.
    REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_199121. Activation of NF-kappaB in B cells.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_204812. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_211125. NOD1/2 Signaling Pathway.
    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

    EvolutionaryTracei O88522.
    NextBioi 288945.
    PROi O88522.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88522.
    Bgeei O88522.
    CleanExi MM_IKBKG.
    Genevestigatori O88522.

    Family and domain databases

    InterProi IPR021063. NEMO_N.
    [Graphical view ]
    Pfami PF11577. NEMO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complementation cloning of NEMO, a component of the I-kappaB kinase complex essential for NF-kappaB activation."
      Yamaoka S., Courtois G., Bessia C., Whiteside S.T., Weil R., Agou F., Kirk H.E., Kay R.J., Israel A.
      Cell 93:1231-1240(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: T-cell.
    2. "Human-mouse comparative sequence analysis of the NEMO gene reveals an alternative promoter within the neighboring G6PD gene."
      Galgoczy P., Rosenthal A., Platzer M.
      Gene 271:93-98(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Ikbkg gene modulates the herpes virus susceptibility in mice."
      Perelygin A.A., Perelygina L.M.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    4. "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].
      Strain: NOD.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex."
      Mercurio F., Murray B.W., Shevchenko A., Bennett B.L., Young D.B., Li J.W., Pascual G., Motiwala A., Zhu H., Mann M., Manning A.M.
      Mol. Cell. Biol. 19:1526-1538(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-412, PROTEIN SEQUENCE OF 144-159.
      Tissue: Cervix carcinoma.
    8. "Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis."
      Li Y., Kang J., Friedman J., Tarassishin L., Ye J., Kovalenko A., Wallach D., Horwitz M.S.
      Proc. Natl. Acad. Sci. U.S.A. 96:1042-1047(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Role of ikkgamma/nemo in assembly of the IkappaB kinase complex."
      Li X.-H., Fang X., Gaynor R.B.
      J. Biol. Chem. 276:4494-4500(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IKK COMPLEX.
    10. "Regulation of Ikappa B kinase (IKK)gamma /NEMO function by IKKbeta -mediated phosphorylation."
      Prajapati S., Gaynor R.B.
      J. Biol. Chem. 277:24331-24339(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-369, MUTAGENESIS OF SER-369 AND SER-375.
    11. "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 TANK AND IKBKB.
    12. "ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting NF-kappaB."
      Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A., Acquaviva R., Formisano S., Vito P., Leonardi A.
      J. Biol. Chem. 281:18482-18488(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNIP1 AND TNFAIP3.
    13. "Identification of TRAF6-dependent NEMO polyubiquitination sites through analysis of a new NEMO mutation causing incontinentia pigmenti."
      Sebban-Benin H., Pescatore A., Fusco F., Pascuale V., Gautheron J., Yamaoka S., Moncla A., Ursini M.V., Courtois G.
      Hum. Mol. Genet. 16:2805-2815(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-278; LYS-314; LYS-318; LYS-319 AND LYS-392, MUTAGENESIS OF LYS-278; LYS-314; VAL-316; LYS-318; LYS-319 AND LYS-392.
    14. Cited for: INTERACTION WITH TERF2IP.
    15. "Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation."
      Rahighi S., Ikeda F., Kawasaki M., Akutsu M., Suzuki N., Kato R., Kensche T., Uejima T., Bloor S., Komander D., Randow F., Wakatsuki S., Dikic I.
      Cell 136:1098-1109(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 250-343 IN COMPLEX WITH UBIQUITIN, UBIQUITIN-BINDING, MUTAGENESIS OF VAL-293; TYR-301; LYS-302; PHE-305; ARG-309; ARG-312; GLU-313; GLU-313; GLU-317 AND GLU-320.
    16. "DARPin-assisted crystallography of the CC2-LZ domain of NEMO reveals a coupling between dimerization and ubiquitin binding."
      Grubisha O., Kaminska M., Duquerroy S., Fontan E., Cordier F., Haouz A., Raynal B., Chiaravalli J., Delepierre M., Israel A., Veron M., Agou F.
      J. Mol. Biol. 395:89-104(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 251-337, UBIQUITIN-BINDING, OLIGOMETRIZATION.

    Entry informationi

    Entry nameiNEMO_MOUSE
    AccessioniPrimary (citable) accession number: O88522
    Secondary accession number(s): Q924H4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 126 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