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Q9R0T8

- IKKE_MOUSE

UniProt

Q9R0T8 - IKKE_MOUSE

Protein

Inhibitor of nuclear factor kappa-B kinase subunit epsilon

Gene

Ikbke

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase that plays an essential role in regulating inflammatory responses to viral infection, through the activation of the type I IFN, NF-kappa-B and STAT signaling. Also involved in TNFA and inflammatory cytokines, like Interleukin-1, signaling. Following activation of viral RNA sensors, such as RIG-I-like receptors, associates with DDX3X and phosphorylates interferon regulatory factors (IRFs), IRF3 and IRF7, as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB. In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD can be recruited to the IKBKE-containing-complexes. Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway through, at least, the phosphorylation of CYLD. 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. In addition, is also required for the induction of a subset of ISGs which displays antiviral activity, may be through the phosphorylation of STAT1 at 'Ser-708'. Phosphorylation of STAT1 at 'Ser-708' seems also to promote the assembly and DNA binding of ISGF3 (STAT1:STAT2:IRF9) complexes compared to GAF (STAT1:STAT1) complexes, in this way regulating the balance between type I and type II IFN responses. Protects cells against DNA damage-induced cell death. Also plays an important role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Phosphorylates AKT1.6 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Kinase activity is inhibited competitively by amlexanox.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei38 – 381ATPPROSITE-ProRule annotation
    Active sitei135 – 1351Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 239ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. IkappaB kinase activity Source: MGI
    3. NF-kappaB-inducing kinase activity Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. I-kappaB phosphorylation Source: GOC
    2. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
    3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    4. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    DNA damage

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.10. 3474.
    ReactomeiREACT_198521. TRAF6 mediated IRF7 activation.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inhibitor of nuclear factor kappa-B kinase subunit epsilon (EC:2.7.11.10)
    Short name:
    I-kappa-B kinase epsilon
    Short name:
    IKK-E
    Short name:
    IKK-epsilon
    Short name:
    IkBKE
    Alternative name(s):
    Inducible I kappa-B kinase
    Short name:
    IKK-i
    Gene namesi
    Name:Ikbke
    Synonyms:Ikke, Ikki
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1929612. Ikbke.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. NucleusPML body By similarity
    Note: Targeting to PML nuclear bodies upon DNA damage is TOPORS-dependent.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Animals are hypersusceptible to influenza virus infection because of a defect in the activation of a subset of type 1 IFN-stimulated genes, however the amounts of IFNB produced are normals. Lungs of mice infected 7 days with influenza virus exhibit an inflammatory infiltrate consisting of lymphocytes, macrophages and neutrophils. After West Nile virus infection, animals display earlier neurological symptoms, a higher degree of neurovirulence and a failure to recover, compared to wild type. Animals are protected from high-fat diet-induced obesity, liver and adipose inflammation, hepatic steatosis and insulin resistance. They show an increased energy expenditure and thermogenesis and maintain insulin sensitivity in liver and adipose tissue.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381K → A: Dominant negative. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 717717Inhibitor of nuclear factor kappa-B kinase subunit epsilonPRO_0000086018Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki30 – 30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei172 – 1721Phosphoserine; by autocatalysis and IKKB
    Cross-linki231 – 231Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
    Cross-linki403 – 403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei503 – 5031Phosphothreonine1 Publication
    Modified residuei665 – 6651PhosphoserineBy similarity

    Post-translational modificationi

    Sumoylation by TOPORS upon DNA damage is required for protection of cells against DNA damage-induced cell death. Desumoylated by SENP1 By similarity.By similarity
    Autophosphorylated and phosphorylated by IKBKB/IKKB. Phosphorylation at Ser-172 is enhanced by the interaction with DDX3X. Phosphorylated at Thr-503 upon IFN activation.1 Publication
    'Lys-63'-linked polyubiquitinated at Lys-30 and Lys-403 by TRAF2:BIRC2 and TRAF2:BIRC3 complexes. Ubiquitination is induced by LPS, TNFA and interleukin-1 and required for full kinase activity and KF-kappa-B pathway activation By similarity.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ9R0T8.

    PTM databases

    PhosphoSiteiQ9R0T8.

    Expressioni

    Tissue specificityi

    Expressed in bone marrow-derived macrophages and at low levels in liver and white adipose tissue (at protein level). Detected in muscle and lung.3 Publications

    Inductioni

    Induced by lipopolysaccharide (LPS) and TNFA. Under high-fat diet, highly induced (via NF-kappa-B) in adipocytes and M1-polarized adipose tissue macrophages.2 Publications

    Gene expression databases

    ArrayExpressiQ9R0T8.
    BgeeiQ9R0T8.
    CleanExiMM_IKBKE.
    GenevestigatoriQ9R0T8.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with MAVS/IPS1. Interacts with the adapter proteins AZI2/NAP1, TANK and TBKBP1/SINTBAD. Interacts with SIKE1. Interacts with TICAM1/TRIF, IRF3 and DDX58/RIG-I; interactions are disrupted by the interaction between IKBKE and SIKE1. Interacts with TOPORS; induced by DNA damage. Interacts with CYLD, IKBKB, IKBKG and MYD88. Interacts with DDX3X; the interaction is found to be induced upon virus infection.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Traf3ip2Q8N7N63EBI-6664658,EBI-646165

    Protein-protein interaction databases

    BioGridi208014. 1 interaction.
    IntActiQ9R0T8. 2 interactions.
    STRINGi10090.ENSMUSP00000054126.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R0T8.
    SMRiQ9R0T8. Positions 2-648.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 315307Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni385 – 650266Interaction with DDX3XBy similarityAdd
    BLAST
    Regioni452 – 47322Leucine-zipperAdd
    BLAST

    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.
    GeneTreeiENSGT00530000063051.
    HOGENOMiHOG000220867.
    HOVERGENiHBG008494.
    InParanoidiQ8C2I3.
    KOiK07211.
    OMAiHIYIHAH.
    OrthoDBiEOG7Z95KH.
    TreeFamiTF324269.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9R0T8-1 [UniParc]FASTAAdd to Basket

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    MQSTTNYLWH TDDLLGQGAT ASVYKARNKK SGEVVAVKVF NSASYRRPPE    50
    VQVREFEVLR RLNHQNIVKL FAVEETGGSR QKVLIMEYCS SGSLLSVLED 100
    PENTFGLSEE EFLVVLRCVV AGMNHLRENG IVHRDIKPGN IMRLVGEEGQ 150
    SIYKLSDFGA ARKLDDDEKF VSVYGTEEYL HPDMYERAVL RKPQQKAFGV 200
    TVDLWSIGVT LYHAATGSLP FIPFGGPRRN KEIMYRITTE KPAGAISGTQ 250
    KQENGPLEWS YSLPITCRLS MGLQNQLVPI LANILEVEED KCWGFDQFFA 300
    ETSDILQRTV IHVFSLPQAV LHHVYIHAHN TIAIFLEAVY EQTNVTPKHQ 350
    EYLFEGHPCV LEPSLSAQHI AHTAASSPLT LFSMSSDTPK GLAFRDPALD 400
    VPKFVPKVDL QADYSTAKGV LGAGYQALWL ARVLLDGQAL MLRGLHWVLE 450
    VLQDTCQQTL EVTRTALLYL SSSLGTERFS SGAGMPDVQE RKEATELRTR 500
    LQTLSEILSK CSHNVTETQR SLSCLGEELL KNRDQIHEDN KSIQKIQCCL 550
    DKMHFIYKQF KKSRMRPGLS YNEEQIHKLD KVNFSHLAKR LLQVFQEECV 600
    QTYQVSLVTH GKRMRQVQRA QNHLHLIGHS VATCNSEARG AQESLNKIFD 650
    QLLLDRASEQ GAEVSPQPMA PHPGPDPKDL VFHMQELCND MKLLAFDLQD 700
    NNRLIERLHR VPSAPDV 717
    Length:717
    Mass (Da):80,953
    Last modified:July 27, 2011 - v2
    Checksum:i0863ECC180AE385A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti471 – 4711S → G in BAA85154. (PubMed:10421793)Curated
    Sequence conflicti483 – 4831A → S in BAA85154. (PubMed:10421793)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB016589 mRNA. Translation: BAA85154.1.
    AK088580 mRNA. Translation: BAC40434.1.
    AK149911 mRNA. Translation: BAE29161.1.
    CT010206 mRNA. Translation: CAJ18414.1.
    CH466520 Genomic DNA. Translation: EDL39710.1.
    CCDSiCCDS15269.1.
    RefSeqiNP_062751.2. NM_019777.3.
    XP_006529824.1. XM_006529761.1.
    UniGeneiMm.386783.

    Genome annotation databases

    EnsembliENSMUST00000062108; ENSMUSP00000054126; ENSMUSG00000042349.
    GeneIDi56489.
    KEGGimmu:56489.
    UCSCiuc007cnf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB016589 mRNA. Translation: BAA85154.1 .
    AK088580 mRNA. Translation: BAC40434.1 .
    AK149911 mRNA. Translation: BAE29161.1 .
    CT010206 mRNA. Translation: CAJ18414.1 .
    CH466520 Genomic DNA. Translation: EDL39710.1 .
    CCDSi CCDS15269.1.
    RefSeqi NP_062751.2. NM_019777.3.
    XP_006529824.1. XM_006529761.1.
    UniGenei Mm.386783.

    3D structure databases

    ProteinModelPortali Q9R0T8.
    SMRi Q9R0T8. Positions 2-648.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208014. 1 interaction.
    IntActi Q9R0T8. 2 interactions.
    STRINGi 10090.ENSMUSP00000054126.

    PTM databases

    PhosphoSitei Q9R0T8.

    Proteomic databases

    PRIDEi Q9R0T8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000062108 ; ENSMUSP00000054126 ; ENSMUSG00000042349 .
    GeneIDi 56489.
    KEGGi mmu:56489.
    UCSCi uc007cnf.1. mouse.

    Organism-specific databases

    CTDi 9641.
    MGIi MGI:1929612. Ikbke.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00530000063051.
    HOGENOMi HOG000220867.
    HOVERGENi HBG008494.
    InParanoidi Q8C2I3.
    KOi K07211.
    OMAi HIYIHAH.
    OrthoDBi EOG7Z95KH.
    TreeFami TF324269.

    Enzyme and pathway databases

    BRENDAi 2.7.11.10. 3474.
    Reactomei REACT_198521. TRAF6 mediated IRF7 activation.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.

    Miscellaneous databases

    NextBioi 312766.
    PROi Q9R0T8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9R0T8.
    Bgeei Q9R0T8.
    CleanExi MM_IKBKE.
    Genevestigatori Q9R0T8.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "IKK-i, a novel lipopolysaccharide-inducible kinase that is related to IkappaB kinases."
      Shimada T., Kawai T., Takeda K., Matsumoto M., Inoue J., Tatsumi Y., Kanamaru A., Akira S.
      Int. Immunol. 11:1357-1362(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Macrophage.
    2. "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: C57BL/6J and NOD.
      Tissue: Bone marrow and Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. 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].
    5. "The roles of two IkappaB kinase-related kinases in lipopolysaccharide and double stranded RNA signaling and viral infection."
      Hemmi H., Takeuchi O., Sato S., Yamamoto M., Kaisho T., Sanjo H., Kawai T., Hoshino K., Takeda K., Akira S.
      J. Exp. Med. 199:1641-1650(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    6. "SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK."
      Ryzhakov G., Randow F.
      EMBO J. 26:3180-3190(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AZI2; TANK AND TBKBP1.
    7. "Multiple functions of the IKK-related kinase IKKepsilon in interferon-mediated antiviral immunity."
      Tenoever B.R., Ng S.L., Chua M.A., McWhirter S.M., Garcia-Sastre A., Maniatis T.
      Science 315:1274-1278(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN STAT1 ACTIVATION, PHOSPHORYLATION AT THR-503, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-38.
    8. Cited for: FUNCTION IN ENERGY BALANCE, DISRUPTION PHENOTYPE, INDUCTION BY HIGH-FAT DIET, TISSUE SPECIFICITY.
    9. "Inhibitor of kappaB kinase epsilon (IKK(epsilon)), STAT1, and IFIT2 proteins define novel innate immune effector pathway against West Nile virus infection."
      Perwitasari O., Cho H., Diamond M.S., Gale M. Jr.
      J. Biol. Chem. 286:44412-44423(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN STAT1 ACTIVATION, DISRUPTION PHENOTYPE.
    10. "IkappaB kinase epsilon (IKK(epsilon)) regulates the balance between type I and type II interferon responses."
      Ng S.L., Friedman B.A., Schmid S., Gertz J., Myers R.M., Tenoever B.R., Maniatis T.
      Proc. Natl. Acad. Sci. U.S.A. 108:21170-21175(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION REGULATION IN IFN RESPONSE.
    11. "An inhibitor of the protein kinases TBK1 and IKK-[?] improves obesity-related metabolic dysfunctions in mice."
      Reilly S.M., Chiang S.H., Decker S.J., Chang L., Uhm M., Larsen M.J., Rubin J.R., Mowers J., White N.M., Hochberg I., Downes M., Yu R.T., Liddle C., Evans R.M., Oh D., Li P., Olefsky J.M., Saltiel A.R.
      Nat. Med. 19:313-321(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ENERGY BALANCE, DISRUPTION PHENOTYPE, INDUCTION BY HIGH-FAT DIET, TISSUE SPECIFICITY, ENZYME REGULATION.

    Entry informationi

    Entry nameiIKKE_MOUSE
    AccessioniPrimary (citable) accession number: Q9R0T8
    Secondary accession number(s): Q8C2I3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 120 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

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3