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Q9UHD2

- TBK1_HUMAN

UniProt

Q9UHD2 - TBK1_HUMAN

Protein

Serine/threonine-protein kinase TBK1

Gene

TBK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents. Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB. In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes. Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus. Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy. Phosphorylates and activates AKT1. Seems to play a 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. Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C. Phosphorylates Borna disease virus (BDV) P protein.18 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei38 – 381ATPCurated
    Active sitei135 – 1351Proton acceptor2 Publications

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. nucleic acid binding Source: Ensembl
    3. phosphoprotein binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: ProtInc
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. defense response to Gram-positive bacterium Source: Ensembl
    2. defense response to virus Source: UniProtKB-KW
    3. I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    4. inflammatory response Source: UniProtKB
    5. innate immune response Source: UniProtKB
    6. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    7. negative regulation of gene expression Source: Ensembl
    8. negative regulation of type I interferon production Source: Reactome
    9. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    10. positive regulation of interferon-alpha production Source: BHF-UCL
    11. positive regulation of interferon-beta biosynthetic process Source: Ensembl
    12. positive regulation of interferon-beta production Source: BHF-UCL
    13. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    14. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    15. positive regulation of type I interferon production Source: Reactome
    16. response to virus Source: UniProtKB
    17. toll-like receptor 3 signaling pathway Source: Reactome
    18. toll-like receptor 4 signaling pathway Source: Reactome
    19. toll-like receptor signaling pathway Source: Reactome
    20. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    21. type I interferon production Source: UniProtKB
    22. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Antiviral defense, Host-virus interaction, Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_118811. IRF3 mediated activation of type 1 IFN.
    REACT_163734. STAT6-mediated induction of chemokines.
    REACT_163977. Regulation of innate immune responses to cytosolic DNA.
    REACT_163993. IRF3-mediated induction of type I IFN.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    SABIO-RKQ9UHD2.
    SignaLinkiQ9UHD2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase TBK1 (EC:2.7.11.1)
    Alternative name(s):
    NF-kappa-B-activating kinase
    T2K
    TANK-binding kinase 1
    Gene namesi
    Name:TBK1
    Synonyms:NAK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:11584. TBK1.

    Subcellular locationi

    Cytoplasm 2 Publications
    Note: Upon mitogen stimulation or triggering of the immune system, TBK1 is recruited to the exocyst by EXOC2.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. endosome membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Glaucoma 1, open angle, P (GLC1P) [MIM:177700]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. GLC1P is characterized by early onset, thin central corneas and low intraocular pressure.2 Publications
    Note: The disease may be caused by mutations affecting the gene represented in this entry. A copy number variation on chromosome 12q14 consisting of a 300 kb duplication that includes TBK1, XPOT, RASSF3 and GNS has been found in individuals affected by glaucoma. TBK1 is the most likely candidate for the disorder (PubMed:21447600).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 301K → R: Decreases ubiquitination. Abolishes ubiquitination, phosphorylation and kinase activity; when associated with R-401. 1 Publication
    Mutagenesisi33 – 331D → A: Decreases phosphorylation and kinase activity. 1 Publication
    Mutagenesisi38 – 381K → A: Loss of kinase activity. 3 Publications
    Mutagenesisi135 – 1351D → N: Loss of kinase activity. 3 Publications
    Mutagenesisi172 – 1721S → A: Loss of kinase activity. No effect on dimerization. 2 Publications
    Mutagenesisi172 – 1721S → E: Decreased kinase activity. 2 Publications
    Mutagenesisi316 – 3161L → E: Decreases kinase activity. No effect on phosphorylation. 1 Publication
    Mutagenesisi325 – 3251Y → E: Abolishes phosphorylation and kinase activity. 1 Publication
    Mutagenesisi355 – 3551E → R: Decreases phosphorylation and kinase activity. Abolishes dimerization; when associated with A-357 or R-448. 2 Publications
    Mutagenesisi357 – 3571R → A: Decreases phosphorylation and kinase activity. Abolishes dimerization; when associated with R-355. 1 Publication
    Mutagenesisi401 – 4011K → R: Decreases ubiquitination. Abolishes ubiquitination, phosphorylation and kinase activity; when associated with R-30. 1 Publication
    Mutagenesisi448 – 4481E → R: Decreases phosphorylation and kinase activity. Abolishes dimerization; when associated with R-355. 1 Publication
    Mutagenesisi459 – 4591H → E: Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-466 and E-470. 1 Publication
    Mutagenesisi466 – 4661I → E: Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-459 and E-470. 1 Publication
    Mutagenesisi470 – 4701F → E: Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-459 and E-466. 1 Publication
    Mutagenesisi547 – 5471R → D: Decreases phosphorylation and kinase activity. Abolishes dimerization. 1 Publication
    Mutagenesisi577 – 5771Y → A: Decreases kinase activity. 1 Publication
    Mutagenesisi580 – 5801E → A: Decreases kinase activity. 1 Publication
    Mutagenesisi582 – 5821I → A: Decreases kinase activity. 1 Publication
    Mutagenesisi589 – 5891K → D: Decreases phosphorylation and kinase activity. 1 Publication
    Mutagenesisi690 – 6901M → A: Decreases interaction with TANK. 1 Publication
    Mutagenesisi693 – 6931L → A: Almost abolishes interaction with TANK. 1 Publication
    Mutagenesisi694 – 6941K → E: Strongly decreases interaction with TANK and TBKBP1. No effect on phosphorylation. 1 Publication
    Mutagenesisi704 – 7041L → A: Strongly decreases interaction with AZI2, TANK and TBKBP1. No effect on phosphorylation. 1 Publication
    Mutagenesisi708 – 7081N → A: Decreases interaction with TANK. 1 Publication
    Mutagenesisi711 – 7111L → A: Almost abolishes interaction with TANK. 1 Publication

    Keywords - Diseasei

    Glaucoma

    Organism-specific databases

    MIMi177700. phenotype.
    Orphaneti1930. Herpetic encephalitis.
    PharmGKBiPA36348.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 729729Serine/threonine-protein kinase TBK1PRO_0000086743Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki30 – 30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei172 – 1721Phosphoserine; by autocatalysis and IKKB3 Publications
    Cross-linki401 – 401Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki670 – 670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Autophosphorylation at Ser-172 activates the kinase, and is an essential step for virus-triggered signaling. Phosphorylated by IKBKB/IKKB at Ser-172. Phosphorylation requires homodimerization and ubiquitination at Lys-30 and Lys-401. Dephosphorylated at Ser-172 by PPM1B and this negatively regulates its role in mediating antiviral response.4 Publications
    'Lys-63'-linked polyubiquitination by MIB1 after RNA virus infection, or by NRDP1 after LPS stimulation at Lys-30 and Lys-401, participates in kinase activation. 'Lys-48'-linked polyubiquitination at Lys-670 by DTX4 leads to proteasomal degradation. 'Lys-48'-linked polyubiquitination by TRAIP also leads to proteasomal degradation.2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UHD2.
    PaxDbiQ9UHD2.
    PeptideAtlasiQ9UHD2.
    PRIDEiQ9UHD2.

    PTM databases

    PhosphoSiteiQ9UHD2.

    Expressioni

    Tissue specificityi

    Ubiquitous with higher expression in testis. Expressed in the ganglion cells, nerve fiber layer and microvasculature of the retina.2 Publications

    Gene expression databases

    ArrayExpressiQ9UHD2.
    BgeeiQ9UHD2.
    CleanExiHS_TBK1.
    GenevestigatoriQ9UHD2.

    Organism-specific databases

    HPAiHPA045797.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with DDX3X, TIRAP and TRAF2. Part of a ternary complex consisting of TANK, TRAF2 and TBK1. Interacts with AZI2, TANK and TBKBP1; these interactions are mutually exclusive and mediate TBK1 activation. Interacts with GSK3B; this interaction promotes TBK1 self-association and autophosphorylation. Interacts with SIKE1; SIKE1 is associated with TBK1 under physiological condition and dissociated from TBK1 upon viral infection or TLR3 stimulation. Interacts with TICAM1/TRIF, IRF3 and DDX58/RIG-I. Interacts with CYLD. Interacts with OPTN and TRAF3. Interacts with SRC. Interacts with the exocyst complex subunit SEC5/EXOC2; this interaction is sufficient to trigger TBK1 activity. Interacts with TMEM173/MITA. Interacts with IFIT3 (via N-terminus). Interacts with MAVS only in the presence of IFIT3. Interacts with HCV NS3, Ebola virus VP35 and Borna disease virus protein P; these interactions lead to inhibition of cellular antiviral response by blocking necessary interactions between the TBK1 and its substrates IRF3 and IRF7.19 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    I0DF373EBI-356402,EBI-9543922From a different organism.
    I6W9F26EBI-356402,EBI-9518472From a different organism.
    K7Y1A22EBI-356402,EBI-8788634From a different organism.
    P279582EBI-356402,EBI-6919131From a different organism.
    AGO2Q9UKV82EBI-356402,EBI-528269
    ATG9AQ7Z3C62EBI-356402,EBI-727146
    AZI2Q9H6S12EBI-356402,EBI-359973
    CALCOCO2Q131375EBI-356402,EBI-739580
    CDC42BPGQ6DT372EBI-356402,EBI-689124
    CYorf15BQ9BZA42EBI-356402,EBI-6115828
    Ddx3xQ621678EBI-356402,EBI-773173From a different organism.
    HSP90AB1P082382EBI-356402,EBI-352572
    IKBKEQ141642EBI-356402,EBI-307369
    IKBKGQ9Y6K92EBI-356402,EBI-81279
    IRF3Q146537EBI-356402,EBI-2650369
    IRF7Q929852EBI-356402,EBI-968267
    MIB1Q86YT62EBI-356402,EBI-2129148
    MIB2Q96AX92EBI-356402,EBI-2130249
    MTPAPQ9NVV42EBI-356402,EBI-2556166
    OPTNQ96CV911EBI-356402,EBI-748974
    STAT6P422267EBI-356402,EBI-1186478
    TANKQ928446EBI-356402,EBI-356349
    TBKBP1A7MCY67EBI-356402,EBI-359969
    TMEM173Q86WV63EBI-356402,EBI-2800345
    TRAF2Q129333EBI-356402,EBI-355744
    TXLNAP402224EBI-356402,EBI-359793
    TxlngQ8BHN12EBI-356402,EBI-6116854From a different organism.

    Protein-protein interaction databases

    BioGridi118878. 79 interactions.
    DIPiDIP-27529N.
    IntActiQ9UHD2. 58 interactions.
    MINTiMINT-1131333.
    STRINGi9606.ENSP00000329967.

    Structurei

    Secondary structure

    729
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 33
    Beta strandi5 – 1713
    Beta strandi19 – 2810
    Turni29 – 313
    Beta strandi34 – 407
    Helixi42 – 465
    Helixi49 – 6113
    Beta strandi65 – 673
    Beta strandi70 – 756
    Turni77 – 793
    Beta strandi82 – 876
    Helixi94 – 996
    Helixi101 – 1033
    Helixi109 – 12820
    Helixi138 – 1403
    Beta strandi141 – 1455
    Beta strandi151 – 1555
    Turni161 – 1633
    Helixi167 – 1693
    Beta strandi173 – 1753
    Helixi177 – 1793
    Helixi182 – 1887
    Helixi202 – 21615
    Beta strandi220 – 2223
    Helixi227 – 2293
    Helixi231 – 24010
    Beta strandi247 – 2504
    Beta strandi257 – 2626
    Helixi271 – 28414
    Beta strandi285 – 2873
    Turni289 – 2913
    Helixi305 – 3073
    Beta strandi308 – 3158
    Turni316 – 3194
    Beta strandi320 – 3278
    Helixi332 – 34312
    Helixi347 – 3493
    Beta strandi350 – 3545
    Beta strandi357 – 3593
    Helixi367 – 3693
    Beta strandi375 – 3773
    Beta strandi379 – 3835
    Helixi408 – 48073
    Helixi498 – 52629
    Beta strandi530 – 5323
    Helixi535 – 5395
    Helixi544 – 5463
    Helixi548 – 57124
    Helixi577 – 60327
    Helixi605 – 64743
    Turni648 – 6514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4EFOX-ray1.77A/B302-383[»]
    4EUTX-ray2.60A/B2-385[»]
    4EUUX-ray1.80A/B2-308[»]
    4IM0X-ray2.40A1-657[»]
    4IM2X-ray2.50A1-657[»]
    4IM3X-ray3.34A1-657[»]
    4IW0X-ray4.00A2-657[»]
    4IWOX-ray2.61A2-657[»]
    4IWPX-ray3.06A2-657[»]
    4IWQX-ray3.00A2-657[»]
    ProteinModelPortaliQ9UHD2.
    SMRiQ9UHD2. Positions 2-657.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 310302Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini309 – 38577Ubiquitin-likeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni621 – 6299Interaction with AZI2, TANK and TBKBP1

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili407 – 657251Add
    BLAST
    Coiled coili658 – 71356Sequence AnalysisAdd
    BLAST

    Domaini

    Comprises A N-terminal kinase domain, a ubiquitin-like domain and a C-terminal coiled-coil region mediating homodimerization.2 Publications

    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
    Contains 1 ubiquitin-like domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000220867.
    HOVERGENiHBG008494.
    InParanoidiQ9UHD2.
    KOiK05410.
    OMAiLLYQELM.
    OrthoDBiEOG7Z95KH.
    PhylomeDBiQ9UHD2.
    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.

    Q9UHD2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQSTSNHLWL LSDILGQGAT ANVFRGRHKK TGDLFAIKVF NNISFLRPVD    50
    VQMREFEVLK KLNHKNIVKL FAIEEETTTR HKVLIMEFCP CGSLYTVLEE 100
    PSNAYGLPES EFLIVLRDVV GGMNHLRENG IVHRDIKPGN IMRVIGEDGQ 150
    SVYKLTDFGA ARELEDDEQF VSLYGTEEYL HPDMYERAVL RKDHQKKYGA 200
    TVDLWSIGVT FYHAATGSLP FRPFEGPRRN KEVMYKIITG KPSGAISGVQ 250
    KAENGPIDWS GDMPVSCSLS RGLQVLLTPV LANILEADQE KCWGFDQFFA 300
    ETSDILHRMV IHVFSLQQMT AHKIYIHSYN TATIFHELVY KQTKIISSNQ 350
    ELIYEGRRLV LEPGRLAQHF PKTTEENPIF VVSREPLNTI GLIYEKISLP 400
    KVHPRYDLDG DASMAKAITG VVCYACRIAS TLLLYQELMR KGIRWLIELI 450
    KDDYNETVHK KTEVVITLDF CIRNIEKTVK VYEKLMKINL EAAELGEISD 500
    IHTKLLRLSS SQGTIETSLQ DIDSRLSPGG SLADAWAHQE GTHPKDRNVE 550
    KLQVLLNCMT EIYYQFKKDK AERRLAYNEE QIHKFDKQKL YYHATKAMTH 600
    FTDECVKKYE AFLNKSEEWI RKMLHLRKQL LSLTNQCFDI EEEVSKYQEY 650
    TNELQETLPQ KMFTASSGIK HTMTPIYPSS NTLVEMTLGM KKLKEEMEGV 700
    VKELAENNHI LERFGSLTMD GGLRNVDCL 729
    Length:729
    Mass (Da):83,642
    Last modified:May 1, 2000 - v1
    Checksum:iB58E4FE1B502276D
    GO

    Sequence cautioni

    The sequence BAA92129.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti151 – 1511S → F.1 Publication
    Corresponds to variant rs55824172 [ dbSNP | Ensembl ].
    VAR_069754
    Natural varianti271 – 2711R → Q.1 Publication
    Corresponds to variant rs56196591 [ dbSNP | Ensembl ].
    VAR_041208
    Natural varianti291 – 2911K → E.1 Publication
    Corresponds to variant rs34774243 [ dbSNP | Ensembl ].
    VAR_041209
    Natural varianti296 – 2961D → H in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
    VAR_041210
    Natural varianti306 – 3061L → I.1 Publication
    Corresponds to variant rs201970436 [ dbSNP | Ensembl ].
    VAR_069755
    Natural varianti388 – 3881N → D.1 Publication
    Corresponds to variant rs17857028 [ dbSNP | Ensembl ].
    VAR_024746
    Natural varianti410 – 4101G → R in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041211
    Natural varianti464 – 4641V → A.2 Publications
    Corresponds to variant rs35635889 [ dbSNP | Ensembl ].
    VAR_041212
    Natural varianti570 – 5701K → Q.1 Publication
    Corresponds to variant rs17853341 [ dbSNP | Ensembl ].
    VAR_024747

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191838 mRNA. Translation: AAF05989.1.
    AF174536 mRNA. Translation: AAF69106.1.
    AK002192 mRNA. Translation: BAA92129.1. Different initiation.
    AK291039 mRNA. Translation: BAF83728.1.
    CH471054 Genomic DNA. Translation: EAW97133.1.
    BC034950 mRNA. Translation: AAH34950.1.
    CCDSiCCDS8968.1.
    RefSeqiNP_037386.1. NM_013254.3.
    XP_005268866.1. XM_005268809.1.
    XP_005268867.1. XM_005268810.1.
    UniGeneiHs.505874.

    Genome annotation databases

    EnsembliENST00000331710; ENSP00000329967; ENSG00000183735.
    GeneIDi29110.
    KEGGihsa:29110.
    UCSCiuc001ssc.2. human.

    Polymorphism databases

    DMDMi74761953.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191838 mRNA. Translation: AAF05989.1 .
    AF174536 mRNA. Translation: AAF69106.1 .
    AK002192 mRNA. Translation: BAA92129.1 . Different initiation.
    AK291039 mRNA. Translation: BAF83728.1 .
    CH471054 Genomic DNA. Translation: EAW97133.1 .
    BC034950 mRNA. Translation: AAH34950.1 .
    CCDSi CCDS8968.1.
    RefSeqi NP_037386.1. NM_013254.3.
    XP_005268866.1. XM_005268809.1.
    XP_005268867.1. XM_005268810.1.
    UniGenei Hs.505874.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4EFO X-ray 1.77 A/B 302-383 [» ]
    4EUT X-ray 2.60 A/B 2-385 [» ]
    4EUU X-ray 1.80 A/B 2-308 [» ]
    4IM0 X-ray 2.40 A 1-657 [» ]
    4IM2 X-ray 2.50 A 1-657 [» ]
    4IM3 X-ray 3.34 A 1-657 [» ]
    4IW0 X-ray 4.00 A 2-657 [» ]
    4IWO X-ray 2.61 A 2-657 [» ]
    4IWP X-ray 3.06 A 2-657 [» ]
    4IWQ X-ray 3.00 A 2-657 [» ]
    ProteinModelPortali Q9UHD2.
    SMRi Q9UHD2. Positions 2-657.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118878. 79 interactions.
    DIPi DIP-27529N.
    IntActi Q9UHD2. 58 interactions.
    MINTi MINT-1131333.
    STRINGi 9606.ENSP00000329967.

    Chemistry

    BindingDBi Q9UHD2.
    ChEMBLi CHEMBL5408.
    GuidetoPHARMACOLOGYi 2237.

    PTM databases

    PhosphoSitei Q9UHD2.

    Polymorphism databases

    DMDMi 74761953.

    Proteomic databases

    MaxQBi Q9UHD2.
    PaxDbi Q9UHD2.
    PeptideAtlasi Q9UHD2.
    PRIDEi Q9UHD2.

    Protocols and materials databases

    DNASUi 29110.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331710 ; ENSP00000329967 ; ENSG00000183735 .
    GeneIDi 29110.
    KEGGi hsa:29110.
    UCSCi uc001ssc.2. human.

    Organism-specific databases

    CTDi 29110.
    GeneCardsi GC12P064845.
    HGNCi HGNC:11584. TBK1.
    HPAi HPA045797.
    MIMi 177700. phenotype.
    604834. gene.
    neXtProti NX_Q9UHD2.
    Orphaneti 1930. Herpetic encephalitis.
    PharmGKBi PA36348.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000220867.
    HOVERGENi HBG008494.
    InParanoidi Q9UHD2.
    KOi K05410.
    OMAi LLYQELM.
    OrthoDBi EOG7Z95KH.
    PhylomeDBi Q9UHD2.
    TreeFami TF324269.

    Enzyme and pathway databases

    Reactomei REACT_118811. IRF3 mediated activation of type 1 IFN.
    REACT_163734. STAT6-mediated induction of chemokines.
    REACT_163977. Regulation of innate immune responses to cytosolic DNA.
    REACT_163993. IRF3-mediated induction of type I IFN.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    SABIO-RK Q9UHD2.
    SignaLinki Q9UHD2.

    Miscellaneous databases

    GeneWikii TANK-binding_kinase_1.
    GenomeRNAii 29110.
    NextBioi 52179.
    PROi Q9UHD2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHD2.
    Bgeei Q9UHD2.
    CleanExi HS_TBK1.
    Genevestigatori Q9UHD2.

    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. "NF-kB activation by a signaling complex containing TRAF2, TANK, and TBK1, a novel IKK-related kinase."
      Pomerantz J.L., Baltimore D.
      EMBO J. 18:6694-6704(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TANK AND TRAF2, MUTAGENESIS OF LYS-38.
      Tissue: Spleen.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PHOSPHORYLATION OF NFKBIA AND IKBKB, TISSUE SPECIFICITY.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANTS ASP-388 AND GLN-570.
      Tissue: Testis.
    6. "IKK-i and TBK-1 are enzymatically distinct from the homologous enzyme IKK-2: comparative analysis of recombinant human IKK-i, TBK-1, and IKK-2."
      Kishore N., Huynh Q.K., Mathialagan S., Hall T., Rouw S., Creely D., Lange G., Caroll J., Reitz B., Donnelly A., Boddupalli H., Combs R.G., Kretzmer K., Tripp C.S.
      J. Biol. Chem. 277:13840-13847(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-172, PHOSPHORYLATION AT SER-172.
    7. "Toll/IL-1 receptor domain-containing adaptor inducing IFN-beta (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-kappa B and IFN-regulatory factor-3, in the Toll-like receptor signaling."
      Sato S., Sugiyama M., Yamamoto M., Watanabe Y., Kawai T., Takeda K., Akira S.
      J. Immunol. 171:4304-4310(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIRAP AND TICAM1.
    8. "IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway."
      Fitzgerald K.A., McWhirter S.M., Faia K.L., Rowe D.C., Latz E., Golenbock D.T., Coyle A.J., Liao S.-M., Maniatis T.
      Nat. Immunol. 4:491-496(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Triggering the interferon antiviral response through an IKK-related pathway."
      Sharma S., tenOever B.R., Grandvaux N., Zhou G.-P., Lin R., Hiscott J.
      Science 300:1148-1151(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Identification of NAP1, a regulatory subunit of IkappaB kinase-related kinases that potentiates NF-kappaB signaling."
      Fujita F., Taniguchi Y., Kato T., Narita Y., Furuya A., Ogawa T., Sakurai H., Joh T., Itoh M., Delhase M., Karin M., Nakanishi M.
      Mol. Cell. Biol. 23:7780-7793(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AZI2.
    11. "Identification of Ser-386 of interferon regulatory factor 3 as critical target for inducible phosphorylation that determines activation."
      Mori M., Yoneyama M., Ito T., Takahashi K., Inagaki F., Fujita T.
      J. Biol. Chem. 279:9698-9702(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF IRF3.
    12. "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.
    13. "NAK is recruited to the TNFR1 complex in a TNFalpha-dependent manner and mediates the production of RANTES: identification of endogenous TNFR-interacting proteins by a proteomic approach."
      Kuai J., Wooters J., Hall J.P., Rao V.R., Nickbarg E., Li B., Chatterjee-Kishore M., Qiu Y., Lin L.-L.
      J. Biol. Chem. 279:53266-53271(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "Constitutive and interleukin-1-inducible phosphorylation of p65 NF-{kappa}B at serine 536 is mediated by multiple protein kinases including I{kappa}B kinase (IKK)-{alpha}, IKK{beta}, IKK{epsilon}, TRAF family member-associated (TANK)-binding kinase 1 (TBK1), and an unknown kinase and couples p65 to TATA-binding protein-associated factor II31-mediated interleukin-8 transcription."
      Buss H., Dorrie A., Schmitz M.L., Hoffmann E., Resch K., Kracht M.
      J. Biol. Chem. 279:55633-55643(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RELA.
    15. "Activation of TBK1 and IKKvarepsilon kinases by vesicular stomatitis virus infection and the role of viral ribonucleoprotein in the development of interferon antiviral immunity."
      tenOever B.R., Sharma S., Zou W., Sun Q., Grandvaux N., Julkunen I., Hemmi H., Yamamoto M., Akira S., Yeh W.C., Lin R., Hiscott J.
      J. Virol. 78:10636-10649(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF IRF7.
    16. "SIKE is an IKK epsilon/TBK1-associated suppressor of TLR3- and virus-triggered IRF-3 activation pathways."
      Huang J., Liu T., Xu L.-G., Chen D., Zhai Z., Shu H.-B.
      EMBO J. 24:4018-4028(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIKE1; IRF3; TICAM1 AND DDX58.
    17. "Interaction between the HCV NS3 protein and the host TBK1 protein leads to inhibition of cellular antiviral responses."
      Otsuka M., Kato N., Moriyama M., Taniguchi H., Wang Y., Dharel N., Kawabe T., Omata M.
      Hepatology 41:1004-1012(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCV NS3.
    18. "Viral targeting of the interferon-beta-inducing Traf family member-associated NF-kappa-B activator (TANK)-binding kinase-1."
      Unterstab G., Ludwig S., Anton A., Planz O., Dauber B., Krappmann D., Heins G., Ehrhardt C., Wolff T.
      Proc. Natl. Acad. Sci. U.S.A. 102:13640-13645(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BORNA DISEASE VIRUS P PROTEIN.
    19. "RalB GTPase-mediated activation of the IkappaB family kinase TBK1 couples innate immune signaling to tumor cell survival."
      Chien Y., Kim S., Bumeister R., Loo Y.M., Kwon S.W., Johnson C.L., Balakireva M.G., Romeo Y., Kopelovich L., Gale M. Jr., Yeaman C., Camonis J.H., Zhao Y., White M.A.
      Cell 127:157-170(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EXOC2.
    20. "Involvement of the ubiquitin-like domain of TBK1/IKK-i kinases in regulation of IFN-inducible genes."
      Ikeda F., Hecker C.M., Rozenknop A., Nordmeier R.D., Rogov V., Hofmann K., Akira S., Dotsch V., Dikic I.
      EMBO J. 26:3451-3462(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    21. "The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response."
      Soulat D., Burckstummer T., Westermayer S., Goncalves A., Bauch A., Stefanovic A., Hantschel O., Bennett K.L., Decker T., Superti-Furga G.
      EMBO J. 27:2135-2146(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF DDX3X.
    22. Cited for: INTERACTION WITH CYLD.
    23. "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.
    24. "The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling."
      Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.
      J. Biol. Chem. 284:19122-19131(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRC.
    25. "Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKepsilon and TBK-1."
      Prins K.C., Cardenas W.B., Basler C.F.
      J. Virol. 83:3069-3077(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EBOLAVIRUS PROTEIN VP35, AUTOPHOSPHORYLATION.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon."
      Wang C., Chen T., Zhang J., Yang M., Li N., Xu X., Cao X.
      Nat. Immunol. 10:744-752(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY NRDP1.
    28. "ISG56 is a negative-feedback regulator of virus-triggered signaling and cellular antiviral response."
      Li Y., Li C., Xue P., Zhong B., Mao A.P., Ran Y., Chen H., Wang Y.Y., Yang F., Shu H.B.
      Proc. Natl. Acad. Sci. U.S.A. 106:7945-7950(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMEM173/MITA.
    29. "Glycogen synthase kinase 3beta regulates IRF3 transcription factor-mediated antiviral response via activation of the kinase TBK1."
      Lei C.Q., Zhong B., Zhang Y., Zhang J., Wang S., Shu H.B.
      Immunity 33:878-889(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPHOSPHORYLATION, SUBUNIT, INTERACTION WITH GSK3B.
    30. "Optineurin negatively regulates the induction of IFNbeta in response to RNA virus infection."
      Mankouri J., Fragkoudis R., Richards K.H., Wetherill L.F., Harris M., Kohl A., Elliott R.M., Macdonald A.
      PLoS Pathog. 6:E1000778-E1000778(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH OPTN AND TRAF3.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. Cited for: INVOLVEMENT IN GLC1P, TISSUE SPECIFICITY, VARIANTS PHE-151; ILE-306 AND ALA-464.
    33. "Mapping a dynamic innate immunity protein interaction network regulating type I interferon production."
      Li S., Wang L., Berman M., Kong Y.Y., Dorf M.E.
      Immunity 35:426-440(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY MIB1.
    34. "IFN-induced TPR protein IFIT3 potentiates antiviral signaling by bridging MAVS and TBK1."
      Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.
      J. Immunol. 187:2559-2568(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH IFIT3 AND MAVS.
    35. "TANK-binding kinase 1 attenuates PTAP-dependent retroviral budding through targeting endosomal sorting complex required for transport-I."
      Da Q., Yang X., Xu Y., Gao G., Cheng G., Tang H.
      J. Immunol. 186:3023-3030(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF VPS37C.
    36. Cited for: FUNCTION, INTERACTION WITH AZI2; TANK AND TBKBP1, MUTAGENESIS OF ASP-135; MET-690; LEU-693; LYS-694; LEU-704; ASN-708 AND LEU-711.
    37. "IkappaB kinase epsilon and TANK-binding kinase 1 activate AKT by direct phosphorylation."
      Xie X., Zhang D., Zhao B., Lu M.K., You M., Condorelli G., Wang C.Y., Guan K.L.
      Proc. Natl. Acad. Sci. U.S.A. 108:6474-6479(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF AKT1.
    38. "Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth."
      Wild P., Farhan H., McEwan D.G., Wagner S., Rogov V.V., Brady N.R., Richter B., Korac J., Waidmann O., Choudhary C., Dotsch V., Bumann D., Dikic I.
      Science 333:228-233(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF OPTN.
    39. "Emerging roles for the non-canonical IKKs in cancer."
      Shen R.R., Hahn W.C.
      Oncogene 30:631-641(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION, DOMAIN.
    40. Cited for: FUNCTION, PHOSPHORYLATION BY IKBKB/IKKB.
    41. "PPM1B negatively regulates antiviral response via dephosphorylating TBK1."
      Zhao Y., Liang L., Fan Y., Sun S., An L., Shi Z., Cheng J., Jia W., Sun W., Mori-Akiyama Y., Zhang H., Fu S., Yang J.
      Cell. Signal. 24:2197-2204(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEPHOSPHORYLATION AT SER-172.
    42. Cited for: INVOLVEMENT IN GLC1P.
    43. "TRAF-interacting protein (TRIP) negatively regulates IFN-beta production and antiviral response by promoting proteasomal degradation of TANK-binding kinase 1."
      Zhang M., Wang L., Zhao X., Zhao K., Meng H., Zhao W., Gao C.
      J. Exp. Med. 209:1703-1711(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY TRAIP.
    44. "NLRP4 negatively regulates type I interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase DTX4."
      Cui J., Li Y., Zhu L., Liu D., Songyang Z., Wang H.Y., Wang R.F.
      Nat. Immunol. 13:387-395(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-670 BY DTX4.
    45. "Crystal structure and mechanism of activation of TANK-binding kinase 1."
      Larabi A., Devos J.M., Ng S.L., Nanao M.H., Round A., Maniatis T., Panne D.
      Cell Rep. 3:734-746(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-657 IN COMPLEX WITH INHIBITORS, FUNCTION, ACTIVE SITE, HOMODIMER, UBIQUITINATION AT LYS-30 AND LYS-401, MUTAGENESIS OF LYS-30; ASP-33; LYS-38; ASP-135; GLU-355; ARG-357; LYS-401; ARG-547; TYR-577; GLU-580; ILE-582 AND LYS-589.
    46. Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-657 IN COMPLEX WITH INHIBITORS, FUNCTION, ACTIVE SITE, AUTOPHOSPHORYLATION, HOMODIMER, INTERACTION WITH AZI2, MUTAGENESIS OF LYS-38; ASP-135; SER-172; LEU-316; TYR-325; GLU-355; GLU-448; HIS-459; ILE-466 AND PHE-470.
    47. "Structural insights into the functions of TBK1 in innate antimicrobial immunity."
      Shu C., Sankaran B., Chaton C.T., Herr A.B., Mishra A., Peng J., Li P.
      Structure 21:1137-1148(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-657 IN COMPLEX WITH INHIBITORS, FUNCTION, PHOSPHORYLATION AT SER-172.
    48. "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] GLN-271; GLU-291; HIS-296; ARG-410 AND ALA-464.

    Entry informationi

    Entry nameiTBK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHD2
    Secondary accession number(s): A8K4S4, Q8IYV3, Q9NUJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 129 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

    Miscellaneous

    In cancer cells, pathological TBK1 activation promotes oncogenic transformation by suppressing programmed cell death. Mechanistically, the RALB-SEC5/EXOC2-TBK1 signaling cascade seems to participate in both innate immune signaling and cell transformation. Additionally, TBK1 supports oncogenesis by directly phosphorylating and activating AKT1 at the exocyst (PubMed:21042276).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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