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Q6TMG5

- NEMO_RAT

UniProt

Q6TMG5 - NEMO_RAT

Protein

NF-kappa-B essential modulator

Gene

Ikbkg

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination By similarity.By similarity

    Regions

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

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. peroxisome proliferator activated receptor binding Source: RGD
    3. protein heterodimerization activity Source: RGD
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. activation of NF-kappaB-inducing kinase activity Source: Ensembl
    2. B cell homeostasis Source: Ensembl
    3. cellular response to DNA damage stimulus Source: Ensembl
    4. NF-kappaB import into nucleus Source: RGD
    5. positive regulation of NF-kappaB transcription factor activity Source: RGD
    6. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_194364. RIP-mediated NFkB activation via ZBP1.
    REACT_197513. FCERI mediated NF-kB activation.
    REACT_198989. IRAK1 recruits IKK complex.
    REACT_199026. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_199247. Activation of NF-kappaB in B cells.

    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
    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi735223. Ikbkg.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. IkappaB kinase complex Source: RGD
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 412412NF-kappa-B essential modulatorPRO_0000269197Add
    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)By similarity
    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)By similarity
    Cross-linki319 – 319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Disulfide bondi340 – 340InterchainBy similarity
    Modified residuei369 – 3691Phosphoserine; by IKKBBy similarity
    Modified residuei380 – 3801PhosphoserineBy similarity
    Cross-linki392 – 392Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    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

    Expressioni

    Gene expression databases

    GenevestigatoriQ6TMG5.

    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 IKBKE and TBK1. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with ZFAND5. 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 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi259339. 1 interaction.
    STRINGi10116.ENSRNOP00000053114.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6TMG5.
    SMRiQ6TMG5. Positions 49-109, 193-248, 387-412.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni44 – 11168Interaction with CHUK/IKBKBBy similarityAdd
    BLAST
    Regioni150 – 250101Interaction with TANKBy similarityAdd
    BLAST
    Regioni242 – 343102Ubiquitin-binding (UBD)Add
    BLAST
    Regioni246 – 358113Self-associationBy similarityAdd
    BLAST
    Regioni249 – 412164Required for interaction with TNFAIP3By similarityAdd
    BLAST
    Regioni315 – 33622Leucine-zipperSequence AnalysisAdd
    BLAST
    Regioni375 – 41238Interaction with CYLDBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili49 – 343295Sequence 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.
    InParanoidiQ6TMG5.
    KOiK07210.
    OMAiPETFQRC.
    OrthoDBiEOG7D2FD7.
    PhylomeDBiQ6TMG5.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q6TMG5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRHLWKNQL SEMVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET    50
    LQRCLEENQE LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA 100
    RKLVERLSLE KLDLRRQREQ ALEDLEHLKK CQQQMAEDKA SVKAQVTSLL 150
    GELQESQSRL EAATKERQTL EGRIRAVSEQ VRQLESEREV LQQQHSVQVD 200
    QLRMQNQSVE AALRMERQAA SEEKRKLAQL QAAYHQLFQD YDSHIKSSKG 250
    MQLEDLRQQL QQAEEALVAK QELIDKLKEE AEQHKIVMET VPVLKAQADI 300
    YKADFQAERH AREKLVERKE LLQEQLEQLQ REFNKLKVGC HESARIEDMR 350
    KRHVETSQPP LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM 400
    DTLQIHVMEC IE 412
    Length:412
    Mass (Da):48,066
    Last modified:July 5, 2004 - v1
    Checksum:i6D5D96B08A4CCEC2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY392762 mRNA. Translation: AAQ94056.1.
    RefSeqiNP_954534.1. NM_199103.1.
    XP_006229646.1. XM_006229584.1.
    XP_006229647.1. XM_006229585.1.
    XP_006229648.1. XM_006229586.1.
    UniGeneiRn.214715.

    Genome annotation databases

    EnsembliENSRNOT00000056275; ENSRNOP00000053114; ENSRNOG00000037237.
    GeneIDi309295.
    KEGGirno:309295.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY392762 mRNA. Translation: AAQ94056.1 .
    RefSeqi NP_954534.1. NM_199103.1.
    XP_006229646.1. XM_006229584.1.
    XP_006229647.1. XM_006229585.1.
    XP_006229648.1. XM_006229586.1.
    UniGenei Rn.214715.

    3D structure databases

    ProteinModelPortali Q6TMG5.
    SMRi Q6TMG5. Positions 49-109, 193-248, 387-412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 259339. 1 interaction.
    STRINGi 10116.ENSRNOP00000053114.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000056275 ; ENSRNOP00000053114 ; ENSRNOG00000037237 .
    GeneIDi 309295.
    KEGGi rno:309295.

    Organism-specific databases

    CTDi 8517.
    RGDi 735223. Ikbkg.

    Phylogenomic databases

    eggNOGi NOG138369.
    GeneTreei ENSGT00530000063808.
    HOGENOMi HOG000293233.
    HOVERGENi HBG000417.
    InParanoidi Q6TMG5.
    KOi K07210.
    OMAi PETFQRC.
    OrthoDBi EOG7D2FD7.
    PhylomeDBi Q6TMG5.

    Enzyme and pathway databases

    Reactomei REACT_194364. RIP-mediated NFkB activation via ZBP1.
    REACT_197513. FCERI mediated NF-kB activation.
    REACT_198989. IRAK1 recruits IKK complex.
    REACT_199026. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_199247. Activation of NF-kappaB in B cells.

    Miscellaneous databases

    NextBioi 660548.

    Gene expression databases

    Genevestigatori Q6TMG5.

    Family and domain databases

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

    Publicationsi

    1. "Two carboxyl-terminal activation regions of Epstein-Barr virus latent membrane protein 1 activate NF-kappaB through distinct signaling pathways in fibroblast cell lines."
      Saito N., Courtois G., Chiba A., Yamamoto N., Nitta T., Hironaka N., Rowe M., Yamamoto N., Yamaoka S.
      J. Biol. Chem. 278:46565-46575(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Fischer 344.

    Entry informationi

    Entry nameiNEMO_RAT
    AccessioniPrimary (citable) accession number: Q6TMG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3