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Q9UHD2

- TBK1_HUMAN

UniProt

Q9UHD2 - TBK1_HUMAN

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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

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

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
Complete GO annotation...

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 IKKB2 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

BgeeiQ9UHD2.
CleanExiHS_TBK1.
ExpressionAtlasiQ9UHD2. baseline and differential.
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. 86 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 – 33Combined sources
Beta strandi5 – 1713Combined sources
Beta strandi19 – 2810Combined sources
Turni29 – 313Combined sources
Beta strandi34 – 407Combined sources
Helixi42 – 465Combined sources
Helixi49 – 6113Combined sources
Beta strandi65 – 673Combined sources
Beta strandi70 – 756Combined sources
Turni77 – 793Combined sources
Beta strandi82 – 876Combined sources
Helixi94 – 996Combined sources
Helixi101 – 1033Combined sources
Helixi109 – 12820Combined sources
Helixi138 – 1403Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi151 – 1555Combined sources
Turni161 – 1633Combined sources
Helixi167 – 1693Combined sources
Beta strandi173 – 1753Combined sources
Helixi177 – 1793Combined sources
Helixi182 – 1887Combined sources
Helixi202 – 21615Combined sources
Beta strandi220 – 2223Combined sources
Helixi227 – 2293Combined sources
Helixi231 – 24010Combined sources
Beta strandi247 – 2504Combined sources
Beta strandi257 – 2626Combined sources
Helixi271 – 28414Combined sources
Beta strandi285 – 2873Combined sources
Turni289 – 2913Combined sources
Helixi305 – 3073Combined sources
Beta strandi308 – 3158Combined sources
Turni316 – 3194Combined sources
Beta strandi320 – 3278Combined sources
Helixi332 – 34312Combined sources
Helixi347 – 3493Combined sources
Beta strandi350 – 3545Combined sources
Beta strandi357 – 3593Combined sources
Helixi367 – 3693Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi379 – 3835Combined sources
Helixi408 – 48073Combined sources
Helixi498 – 52629Combined sources
Beta strandi530 – 5323Combined sources
Helixi535 – 5395Combined sources
Helixi544 – 5463Combined sources
Helixi548 – 57124Combined sources
Helixi577 – 60327Combined sources
Helixi605 – 64743Combined sources
Turni648 – 6514Combined sources

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.
GeneTreeiENSGT00760000119118.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQSTSNHLWL LSDILGQGAT ANVFRGRHKK TGDLFAIKVF 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
TVDLWSIGVT FYHAATGSLP FRPFEGPRRN KEVMYKIITG KPSGAISGVQ
260 270 280 290 300
KAENGPIDWS GDMPVSCSLS RGLQVLLTPV LANILEADQE KCWGFDQFFA
310 320 330 340 350
ETSDILHRMV IHVFSLQQMT AHKIYIHSYN TATIFHELVY KQTKIISSNQ
360 370 380 390 400
ELIYEGRRLV LEPGRLAQHF PKTTEENPIF VVSREPLNTI GLIYEKISLP
410 420 430 440 450
KVHPRYDLDG DASMAKAITG VVCYACRIAS TLLLYQELMR KGIRWLIELI
460 470 480 490 500
KDDYNETVHK KTEVVITLDF CIRNIEKTVK VYEKLMKINL EAAELGEISD
510 520 530 540 550
IHTKLLRLSS SQGTIETSLQ DIDSRLSPGG SLADAWAHQE GTHPKDRNVE
560 570 580 590 600
KLQVLLNCMT EIYYQFKKDK AERRLAYNEE QIHKFDKQKL YYHATKAMTH
610 620 630 640 650
FTDECVKKYE AFLNKSEEWI RKMLHLRKQL LSLTNQCFDI EEEVSKYQEY
660 670 680 690 700
TNELQETLPQ KMFTASSGIK HTMTPIYPSS NTLVEMTLGM KKLKEEMEGV
710 720
VKELAENNHI LERFGSLTMD GGLRNVDCL
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. 86 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.
GeneTreei ENSGT00760000119118.
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

Bgeei Q9UHD2.
CleanExi HS_TBK1.
ExpressionAtlasi Q9UHD2. baseline and differential.
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

« 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, 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 29, 2014
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
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