Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase TBK1

Gene

Tbk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a 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

  • ATP binding Source: UniProtKB-KW
  • nucleic acid binding Source: MGI
  • phosphoprotein binding Source: MGI
  • protein serine/threonine kinase activity Source: ParkinsonsUK-UCL

GO - Biological processi

  • activation of innate immune response Source: MGI
  • defense response to Gram-positive bacterium Source: MGI
  • defense response to virus Source: UniProtKB-KW
  • dendritic cell proliferation Source: MGI
  • innate immune response Source: UniProtKB-KW
  • negative regulation of gene expression Source: UniProtKB
  • peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • positive regulation of interferon-alpha production Source: MGI
  • positive regulation of interferon-beta biosynthetic process Source: MGI
  • positive regulation of interferon-beta production Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of xenophagy Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-3134975. Regulation of innate immune responses to cytosolic DNA.
R-MMU-3249367. STAT6-mediated induction of chemokines.
R-MMU-3270619. IRF3-mediated induction of type I IFN.
R-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase TBK1 (EC:2.7.11.1)
Alternative name(s):
T2K
TANK-binding kinase 1
Gene namesi
Name:Tbk1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1929658. Tbk1.

Subcellular locationi

  • Cytoplasm

  • Note: Upon mitogen stimulation or triggering of the immune system, TBK1 is recruited to the exocyst by EXOC2.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice display embryonic lethality at E14.5 due to massive liver degeneration and apoptosis. Embryonic fibroblasts from mice lacking Tbk1 exhibit dramatically reduced transcription of NF-kappa-B, as well as marked defects in interferon alpha and beta, and RANTES gene expression after infection with Sendai or Newcastle disease virus.3 Publications

Chemistry

ChEMBLiCHEMBL2189160.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 729729Serine/threonine-protein kinase TBK1PRO_0000086744Add
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 IKKB1 Publication
Cross-linki401 – 401Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki670 – 670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

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.1 Publication
'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 (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9WUN2.
MaxQBiQ9WUN2.
PaxDbiQ9WUN2.
PRIDEiQ9WUN2.

PTM databases

iPTMnetiQ9WUN2.
PhosphoSiteiQ9WUN2.

Expressioni

Gene expression databases

BgeeiQ9WUN2.
CleanExiMM_TBK1.
ExpressionAtlasiQ9WUN2. baseline and differential.
GenevisibleiQ9WUN2. MM.

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 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 TICAM1 and this interaction is enhanced in the presence of WDFY1 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TankP703476EBI-764193,EBI-646116
Tbkbp1A2A9T02EBI-764193,EBI-7987134
Tmem173Q3TBT33EBI-764193,EBI-3862093

GO - Molecular functioni

Protein-protein interaction databases

BioGridi208009. 15 interactions.
DIPiDIP-29880N.
IntActiQ9WUN2. 11 interactions.
MINTiMINT-111979.
STRINGi10090.ENSMUSP00000020316.

Chemistry

BindingDBiQ9WUN2.

Structurei

Secondary structure

1
729
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Beta strandi22 – 287Combined sources
Turni29 – 313Combined sources
Beta strandi34 – 396Combined sources
Helixi49 – 6012Combined sources
Beta strandi70 – 756Combined sources
Turni77 – 793Combined sources
Beta strandi82 – 876Combined sources
Helixi94 – 985Combined sources
Helixi101 – 1033Combined sources
Helixi109 – 12719Combined sources
Beta strandi128 – 1303Combined sources
Helixi138 – 1403Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi149 – 1557Combined sources
Helixi176 – 1794Combined sources
Helixi182 – 19211Combined sources
Beta strandi194 – 1974Combined sources
Beta strandi200 – 2023Combined sources
Helixi203 – 21614Combined sources
Beta strandi220 – 2223Combined sources
Helixi231 – 2399Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi258 – 2625Combined sources
Helixi271 – 28414Combined sources
Helixi289 – 2924Combined sources
Helixi295 – 30713Combined sources
Beta strandi309 – 3157Combined sources
Turni316 – 3194Combined sources
Beta strandi320 – 3267Combined sources
Beta strandi328 – 3303Combined sources
Helixi332 – 34312Combined sources
Helixi347 – 3493Combined sources
Beta strandi351 – 3544Combined sources
Beta strandi357 – 3593Combined sources
Helixi367 – 3693Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi379 – 3824Combined sources
Helixi408 – 48376Combined sources
Beta strandi484 – 4863Combined sources
Helixi495 – 52430Combined sources
Beta strandi530 – 5323Combined sources
Helixi536 – 5394Combined sources
Helixi544 – 5463Combined sources
Helixi548 – 57124Combined sources
Helixi577 – 64468Combined sources
Helixi645 – 6473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JL9X-ray3.10A2-656[»]
4JLCX-ray3.00A2-656[»]
ProteinModelPortaliQ9WUN2.
SMRiQ9WUN2. Positions 2-656.
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 TBKBP1By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili407 – 6572511 PublicationAdd
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.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4250. Eukaryota.
ENOG410XRMU. LUCA.
GeneTreeiENSGT00820000127009.
HOGENOMiHOG000220867.
HOVERGENiHBG008494.
InParanoidiQ9WUN2.
KOiK05410.
OMAiFRGRHKK.
OrthoDBiEOG7Z95KH.
PhylomeDBiQ9WUN2.
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]
SMARTiSM00220. S_TKc. 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.

Q9WUN2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSTSNHLWL LSDILGQGAT ANVFRGRHKK TGDLYAVKVF NNISFLRPVD
60 70 80 90 100
VQMREFEVLK KLNHKNIVKL FAIEEETTTR HKVLIMEFCP CGSLYTVLEE
110 120 130 140 150
PSNAYGLPES EFLIVLRDVV GGMNHLRENG IVHRDIKPGN IMRVIGEDGQ
160 170 180 190 200
SVYKLTDFGA ARELEDDEQF VSLYGTEEYL HPDMYERAVL RKDHQKKYGA
210 220 230 240 250
TVDLWSVGVT FYHAATGSLP FRPFEGPRRN KEVMYKIITG KPSGAISGVQ
260 270 280 290 300
KAENGPIDWS GDMPLSCSLS QGLQALLTPV LANILEADQE KCWGFDQFFA
310 320 330 340 350
ETSDVLHRMV IHVFSLQHMT AHKIYIHSYN TAAVFHELVY KQTKIVSSNQ
360 370 380 390 400
ELIYEGRRLV LELGRLAQHF PKTTEENPIF VTSREQLNTV GLRYEKISLP
410 420 430 440 450
KIHPRYDLDG DASMAKAVTG VVCYACRTAS TLLLYQELMR KGVRWLVELV
460 470 480 490 500
KDDYNETVHK KTEVVITLDF CIRNIEKTVK VYEKLMKVNL EAAELGEISD
510 520 530 540 550
IHTKLLRLSS SQGTIESSLQ DISSRLSPGG LLADTWAHQE GTHPRDRNVE
560 570 580 590 600
KLQVLLNCIT EIYYQFKKDK AERRLAYNEE QIHKFDKQKL YYHATKAMSH
610 620 630 640 650
FSEECVRKYE AFKDKSEEWM RKMLHLRKQL LSLTNQCFDI EEEVSKYQDY
660 670 680 690 700
TNELQETLPQ KMLAASGGVK HAMAPIYPSS NTLVEMTLGM KKLKEEMEGV
710 720
VKELAENNHI LERFGSLTMD GGLRNVDCL
Length:729
Mass (Da):83,425
Last modified:November 1, 1999 - v1
Checksum:i978ADDE3061DACD1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti468 – 4681L → V in BAB23440 (PubMed:16141072).Curated
Sequence conflicti594 – 5941A → S in BAB23244 (PubMed:16141072).Curated
Sequence conflicti631 – 6311L → S in BAB23440 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191839 mRNA. Translation: AAF05990.1.
AF145705 mRNA. Translation: AAD34590.1.
AK004269 mRNA. Translation: BAB23244.1.
AK004649 mRNA. Translation: BAB23440.1.
CCDSiCCDS24212.1.
RefSeqiNP_062760.3. NM_019786.4.
UniGeneiMm.34580.

Genome annotation databases

EnsembliENSMUST00000020316; ENSMUSP00000020316; ENSMUSG00000020115.
GeneIDi56480.
KEGGimmu:56480.
UCSCiuc007hft.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191839 mRNA. Translation: AAF05990.1.
AF145705 mRNA. Translation: AAD34590.1.
AK004269 mRNA. Translation: BAB23244.1.
AK004649 mRNA. Translation: BAB23440.1.
CCDSiCCDS24212.1.
RefSeqiNP_062760.3. NM_019786.4.
UniGeneiMm.34580.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JL9X-ray3.10A2-656[»]
4JLCX-ray3.00A2-656[»]
ProteinModelPortaliQ9WUN2.
SMRiQ9WUN2. Positions 2-656.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208009. 15 interactions.
DIPiDIP-29880N.
IntActiQ9WUN2. 11 interactions.
MINTiMINT-111979.
STRINGi10090.ENSMUSP00000020316.

Chemistry

BindingDBiQ9WUN2.
ChEMBLiCHEMBL2189160.

PTM databases

iPTMnetiQ9WUN2.
PhosphoSiteiQ9WUN2.

Proteomic databases

EPDiQ9WUN2.
MaxQBiQ9WUN2.
PaxDbiQ9WUN2.
PRIDEiQ9WUN2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020316; ENSMUSP00000020316; ENSMUSG00000020115.
GeneIDi56480.
KEGGimmu:56480.
UCSCiuc007hft.3. mouse.

Organism-specific databases

CTDi29110.
MGIiMGI:1929658. Tbk1.

Phylogenomic databases

eggNOGiKOG4250. Eukaryota.
ENOG410XRMU. LUCA.
GeneTreeiENSGT00820000127009.
HOGENOMiHOG000220867.
HOVERGENiHBG008494.
InParanoidiQ9WUN2.
KOiK05410.
OMAiFRGRHKK.
OrthoDBiEOG7Z95KH.
PhylomeDBiQ9WUN2.
TreeFamiTF324269.

Enzyme and pathway databases

ReactomeiR-MMU-3134975. Regulation of innate immune responses to cytosolic DNA.
R-MMU-3249367. STAT6-mediated induction of chemokines.
R-MMU-3270619. IRF3-mediated induction of type I IFN.
R-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

NextBioi312746.
PROiQ9WUN2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WUN2.
CleanExiMM_TBK1.
ExpressionAtlasiQ9WUN2. baseline and differential.
GenevisibleiQ9WUN2. MM.

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]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    Tissue: Spleen.
  2. "Mus musculus homolog to human T2K cDNA."
    Wisniewski D., Marcy A.I.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss Webster / NIH.
  3. "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.
    Tissue: Lung.
  4. "Deficiency of T2K leads to apoptotic liver degeneration and impaired NF-kappaB-dependent gene transcription."
    Bonnard M., Mirtsos C., Suzuki S., Graham K., Huang J., Ng M., Itie A., Wakeham A., Shahinian A., Henzel W.J., Elia A.J., Shillinglaw W., Mak T.W., Cao Z., Yeh W.-C.
    EMBO J. 19:4976-4985(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  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. "IFN-regulatory factor 3-dependent gene expression is defective in Tbk1-deficient mouse embryonic fibroblasts."
    McWhirter S.M., Fitzgerald K.A., Rosains J., Rowe D.C., Golenbock D.T., Maniatis T.
    Proc. Natl. Acad. Sci. U.S.A. 101:233-238(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "Immune activation of type I IFNs by Listeria monocytogenes occurs independently of TLR4, TLR2, and receptor interacting protein 2 but involves TNFR-associated NF kappa B kinase-binding kinase 1."
    O'Connell R.M., Vaidya S.A., Perry A.K., Saha S.K., Dempsey P.W., Cheng G.
    J. Immunol. 174:1602-1607(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Lung, Spleen and Testis.
  9. "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, ENZYME REGULATION, PHOSPHORYLATION AT SER-172.
  10. "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 (3.0 ANGSTROMS) OF 2-656 IN COMPLEX WITH INHIBITORS, SUBUNIT, COILED-COIL.

Entry informationi

Entry nameiTBK1_MOUSE
AccessioniPrimary (citable) accession number: Q9WUN2
Secondary accession number(s): Q9CT90, Q9DC03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 130 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

3D-structure, Complete proteome, 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.