Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Serine/threonine-protein kinase TBK1 (EC 2 7 11 1) (NF-kappa-B-activating kinase) (T2K) (TANK-binding kinase 1)

 TBK1_HUMAN              Reviewed;         729 AA.
Q9UHD2; A8K4S4; Q8IYV3; Q9NUJ5;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 162.
RecName: Full=Serine/threonine-protein kinase TBK1;
EC=2.7.11.1;
AltName: Full=NF-kappa-B-activating kinase;
AltName: Full=T2K;
AltName: Full=TANK-binding kinase 1;
Name=TBK1; Synonyms=NAK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TANK AND TRAF2,
AND MUTAGENESIS OF LYS-38.
TISSUE=Spleen;
PubMed=10581243; DOI=10.1093/emboj/18.23.6694;
Pomerantz J.L., Baltimore D.;
"NF-kB activation by a signaling complex containing TRAF2, TANK, and
TBK1, a novel IKK-related kinase.";
EMBO J. 18:6694-6704(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PHOSPHORYLATION OF NFKBIA AND
IKBKB, AND TISSUE SPECIFICITY.
PubMed=10783893; DOI=10.1038/35008109;
Tojima Y., Fujimoto A., Delhase M., Chen Y., Hatakeyama S.,
Nakayama K., Kaneko Y., Nimura Y., Motoyama N., Ikeda K., Karin M.,
Nakanishi M.;
"NAK is an IkappaB kinase-activating kinase.";
Nature 404:778-782(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-388 AND
GLN-570.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, MUTAGENESIS OF SER-172, AND PHOSPHORYLATION AT SER-172.
PubMed=11839743; DOI=10.1074/jbc.M110474200;
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.;
"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.";
J. Biol. Chem. 277:13840-13847(2002).
[7]
INTERACTION WITH TIRAP AND TICAM1.
PubMed=14530355; DOI=10.4049/jimmunol.171.8.4304;
Sato S., Sugiyama M., Yamamoto M., Watanabe Y., Kawai T., Takeda K.,
Akira S.;
"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.";
J. Immunol. 171:4304-4310(2003).
[8]
FUNCTION.
PubMed=12692549; DOI=10.1038/ni921;
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.;
"IKKepsilon and TBK1 are essential components of the IRF3 signaling
pathway.";
Nat. Immunol. 4:491-496(2003).
[9]
FUNCTION.
PubMed=12702806; DOI=10.1126/science.1081315;
Sharma S., tenOever B.R., Grandvaux N., Zhou G.-P., Lin R.,
Hiscott J.;
"Triggering the interferon antiviral response through an IKK-related
pathway.";
Science 300:1148-1151(2003).
[10]
INTERACTION WITH AZI2.
PubMed=14560022; DOI=10.1128/MCB.23.21.7780-7793.2003;
Fujita F., Taniguchi Y., Kato T., Narita Y., Furuya A., Ogawa T.,
Sakurai H., Joh T., Itoh M., Delhase M., Karin M., Nakanishi M.;
"Identification of NAP1, a regulatory subunit of IkappaB kinase-
related kinases that potentiates NF-kappaB signaling.";
Mol. Cell. Biol. 23:7780-7793(2003).
[11]
FUNCTION IN PHOSPHORYLATION OF IRF3.
PubMed=14703513; DOI=10.1074/jbc.M310616200;
Mori M., Yoneyama M., Ito T., Takahashi K., Inagaki F., Fujita T.;
"Identification of Ser-386 of interferon regulatory factor 3 as
critical target for inducible phosphorylation that determines
activation.";
J. Biol. Chem. 279:9698-9702(2004).
[12]
INTERACTION WITH TICAM1.
PubMed=14739303; DOI=10.1074/jbc.M311629200;
Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.;
"Mechanisms of the TRIF-induced interferon-stimulated response element
and NF-kappaB activation and apoptosis pathways.";
J. Biol. Chem. 279:15652-15661(2004).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15485837; DOI=10.1074/jbc.M411037200;
Kuai J., Wooters J., Hall J.P., Rao V.R., Nickbarg E., Li B.,
Chatterjee-Kishore M., Qiu Y., Lin L.-L.;
"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.";
J. Biol. Chem. 279:53266-53271(2004).
[14]
FUNCTION IN PHOSPHORYLATION OF RELA.
PubMed=15489227; DOI=10.1074/jbc.M409825200;
Buss H., Dorrie A., Schmitz M.L., Hoffmann E., Resch K., Kracht M.;
"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.";
J. Biol. Chem. 279:55633-55643(2004).
[15]
FUNCTION IN PHOSPHORYLATION OF IRF7.
PubMed=15367631; DOI=10.1128/JVI.78.19.10636-10649.2004;
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.;
"Activation of TBK1 and IKKvarepsilon kinases by vesicular stomatitis
virus infection and the role of viral ribonucleoprotein in the
development of interferon antiviral immunity.";
J. Virol. 78:10636-10649(2004).
[16]
INTERACTION WITH SIKE1; IRF3; TICAM1 AND DDX58.
PubMed=16281057; DOI=10.1038/sj.emboj.7600863;
Huang J., Liu T., Xu L.-G., Chen D., Zhai Z., Shu H.-B.;
"SIKE is an IKK epsilon/TBK1-associated suppressor of TLR3- and virus-
triggered IRF-3 activation pathways.";
EMBO J. 24:4018-4028(2005).
[17]
INTERACTION WITH HCV NS3 (MICROBIAL INFECTION).
PubMed=15841462; DOI=10.1002/hep.20666;
Otsuka M., Kato N., Moriyama M., Taniguchi H., Wang Y., Dharel N.,
Kawabe T., Omata M.;
"Interaction between the HCV NS3 protein and the host TBK1 protein
leads to inhibition of cellular antiviral responses.";
Hepatology 41:1004-1012(2005).
[18]
FUNCTION, AND INTERACTION WITH BORNA DISEASE VIRUS P PROTEIN.
PubMed=16155125; DOI=10.1073/pnas.0502883102;
Unterstab G., Ludwig S., Anton A., Planz O., Dauber B., Krappmann D.,
Heins G., Ehrhardt C., Wolff T.;
"Viral targeting of the interferon-beta-inducing Traf family member-
associated NF-kappa-B activator (TANK)-binding kinase-1.";
Proc. Natl. Acad. Sci. U.S.A. 102:13640-13645(2005).
[19]
INTERACTION WITH EXOC2.
PubMed=17018283; DOI=10.1016/j.cell.2006.08.034;
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.;
"RalB GTPase-mediated activation of the IkappaB family kinase TBK1
couples innate immune signaling to tumor cell survival.";
Cell 127:157-170(2006).
[20]
DOMAIN.
PubMed=17599067; DOI=10.1038/sj.emboj.7601773;
Ikeda F., Hecker C.M., Rozenknop A., Nordmeier R.D., Rogov V.,
Hofmann K., Akira S., Dotsch V., Dikic I.;
"Involvement of the ubiquitin-like domain of TBK1/IKK-i kinases in
regulation of IFN-inducible genes.";
EMBO J. 26:3451-3462(2007).
[21]
FUNCTION IN PHOSPHORYLATION OF DDX3X.
PubMed=18583960; DOI=10.1038/emboj.2008.126;
Soulat D., Burckstummer T., Westermayer S., Goncalves A., Bauch A.,
Stefanovic A., Hantschel O., Bennett K.L., Decker T.,
Superti-Furga G.;
"The DEAD-box helicase DDX3X is a critical component of the TANK-
binding kinase 1-dependent innate immune response.";
EMBO J. 27:2135-2146(2008).
[22]
INTERACTION WITH CYLD.
PubMed=18636086; DOI=10.1038/embor.2008.136;
Friedman C.S., O'Donnell M.A., Legarda-Addison D., Ng A.,
Cardenas W.B., Yount J.S., Moran T.M., Basler C.F., Komuro A.,
Horvath C.M., Xavier R., Ting A.T.;
"The tumour suppressor CYLD is a negative regulator of RIG-I-mediated
antiviral response.";
EMBO Rep. 9:930-936(2008).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[24]
INTERACTION WITH SRC.
PubMed=19419966; DOI=10.1074/jbc.M808233200;
Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A.,
Anthonsen M.W.;
"The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible
gene I)-elicited antiviral signaling.";
J. Biol. Chem. 284:19122-19131(2009).
[25]
INTERACTION WITH EBOLAVIRUS PROTEIN VP35, AND AUTOPHOSPHORYLATION.
PubMed=19153231; DOI=10.1128/JVI.01875-08;
Prins K.C., Cardenas W.B., Basler C.F.;
"Ebola virus protein VP35 impairs the function of interferon
regulatory factor-activating kinases IKKepsilon and TBK-1.";
J. Virol. 83:3069-3077(2009).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[27]
UBIQUITINATION BY NRDP1.
PubMed=19483718; DOI=10.1038/ni.1742;
Wang C., Chen T., Zhang J., Yang M., Li N., Xu X., Cao X.;
"The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated
production of type I interferon.";
Nat. Immunol. 10:744-752(2009).
[28]
INTERACTION WITH TMEM173/MITA.
PubMed=19416887; DOI=10.1073/pnas.0900818106;
Li Y., Li C., Xue P., Zhong B., Mao A.P., Ran Y., Chen H., Wang Y.Y.,
Yang F., Shu H.B.;
"ISG56 is a negative-feedback regulator of virus-triggered signaling
and cellular antiviral response.";
Proc. Natl. Acad. Sci. U.S.A. 106:7945-7950(2009).
[29]
AUTOPHOSPHORYLATION, SUBUNIT, AND INTERACTION WITH GSK3B.
PubMed=21145761; DOI=10.1016/j.immuni.2010.11.021;
Lei C.Q., Zhong B., Zhang Y., Zhang J., Wang S., Shu H.B.;
"Glycogen synthase kinase 3beta regulates IRF3 transcription factor-
mediated antiviral response via activation of the kinase TBK1.";
Immunity 33:878-889(2010).
[30]
INTERACTION WITH OPTN AND TRAF3.
PubMed=20174559; DOI=10.1371/journal.ppat.1000778;
Mankouri J., Fragkoudis R., Richards K.H., Wetherill L.F., Harris M.,
Kohl A., Elliott R.M., Macdonald A.;
"Optineurin negatively regulates the induction of IFNbeta in response
to RNA virus infection.";
PLoS Pathog. 6:E1000778-E1000778(2010).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[32]
INVOLVEMENT IN GLC1P, TISSUE SPECIFICITY, AND VARIANTS PHE-151;
ILE-306 AND ALA-464.
PubMed=21447600; DOI=10.1093/hmg/ddr123;
Fingert J.H., Robin A.L., Stone J.L., Roos B.R., Davis L.K.,
Scheetz T.E., Bennett S.R., Wassink T.H., Kwon Y.H., Alward W.L.,
Mullins R.F., Sheffield V.C., Stone E.M.;
"Copy number variations on chromosome 12q14 in patients with normal
tension glaucoma.";
Hum. Mol. Genet. 20:2482-2494(2011).
[33]
UBIQUITINATION BY MIB1.
PubMed=21903422; DOI=10.1016/j.immuni.2011.06.014;
Li S., Wang L., Berman M., Kong Y.Y., Dorf M.E.;
"Mapping a dynamic innate immunity protein interaction network
regulating type I interferon production.";
Immunity 35:426-440(2011).
[34]
SUBCELLULAR LOCATION, AND INTERACTION WITH IFIT3 AND MAVS.
PubMed=21813773; DOI=10.4049/jimmunol.1100963;
Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.;
"IFN-induced TPR protein IFIT3 potentiates antiviral signaling by
bridging MAVS and TBK1.";
J. Immunol. 187:2559-2568(2011).
[35]
FUNCTION IN PHOSPHORYLATION OF VPS37C.
PubMed=21270402; DOI=10.4049/jimmunol.1000262;
Da Q., Yang X., Xu Y., Gao G., Cheng G., Tang H.;
"TANK-binding kinase 1 attenuates PTAP-dependent retroviral budding
through targeting endosomal sorting complex required for transport-
I.";
J. Immunol. 186:3023-3030(2011).
[36]
FUNCTION, INTERACTION WITH AZI2; TANK AND TBKBP1, AND MUTAGENESIS OF
ASP-135; MET-690; LEU-693; LYS-694; LEU-704; ASN-708 AND LEU-711.
PubMed=21931631; DOI=10.1371/journal.pone.0023971;
Goncalves A., Burckstummer T., Dixit E., Scheicher R., Gorna M.W.,
Karayel E., Sugar C., Stukalov A., Berg T., Kralovics R.,
Planyavsky M., Bennett K.L., Colinge J., Superti-Furga G.;
"Functional dissection of the TBK1 molecular network.";
PLoS ONE 6:E23971-E23971(2011).
[37]
FUNCTION IN PHOSPHORYLATION OF AKT1.
PubMed=21464307; DOI=10.1073/pnas.1016132108;
Xie X., Zhang D., Zhao B., Lu M.K., You M., Condorelli G., Wang C.Y.,
Guan K.L.;
"IkappaB kinase epsilon and TANK-binding kinase 1 activate AKT by
direct phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 108:6474-6479(2011).
[38]
FUNCTION IN PHOSPHORYLATION OF OPTN.
PubMed=21617041; DOI=10.1126/science.1205405;
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.;
"Phosphorylation of the autophagy receptor optineurin restricts
Salmonella growth.";
Science 333:228-233(2011).
[39]
REVIEW ON FUNCTION, AND DOMAIN.
PubMed=21042276; DOI=10.1038/onc.2010.493;
Shen R.R., Hahn W.C.;
"Emerging roles for the non-canonical IKKs in cancer.";
Oncogene 30:631-641(2011).
[40]
FUNCTION, AND PHOSPHORYLATION BY IKBKB/IKKB.
PubMed=21138416; DOI=10.1042/BJ20101701;
Clark K., Peggie M., Plater L., Sorcek R.J., Young E.R., Madwed J.B.,
Hough J., McIver E.G., Cohen P.;
"Novel cross-talk within the IKK family controls innate immunity.";
Biochem. J. 434:93-104(2011).
[41]
DEPHOSPHORYLATION AT SER-172.
PubMed=22750291; DOI=10.1016/j.cellsig.2012.06.017;
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.;
"PPM1B negatively regulates antiviral response via dephosphorylating
TBK1.";
Cell. Signal. 24:2197-2204(2012).
[42]
INVOLVEMENT IN GLC1P.
PubMed=22306015; DOI=10.1016/j.exer.2011.12.021;
Kawase K., Allingham R.R., Meguro A., Mizuki N., Roos B.,
Solivan-Timpe F.M., Robin A.L., Ritch R., Fingert J.H.;
"Confirmation of TBK1 duplication in normal tension glaucoma.";
Exp. Eye Res. 96:178-180(2012).
[43]
UBIQUITINATION BY TRAIP.
PubMed=22945920; DOI=10.1084/jem.20120024;
Zhang M., Wang L., Zhao X., Zhao K., Meng H., Zhao W., Gao C.;
"TRAF-interacting protein (TRIP) negatively regulates IFN-beta
production and antiviral response by promoting proteasomal degradation
of TANK-binding kinase 1.";
J. Exp. Med. 209:1703-1711(2012).
[44]
UBIQUITINATION AT LYS-670 BY DTX4.
PubMed=22388039; DOI=10.1038/ni.2239;
Cui J., Li Y., Zhu L., Liu D., Songyang Z., Wang H.Y., Wang R.F.;
"NLRP4 negatively regulates type I interferon signaling by targeting
the kinase TBK1 for degradation via the ubiquitin ligase DTX4.";
Nat. Immunol. 13:387-395(2012).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[46]
INVOLVEMENT IN FTDALS4, AND VARIANTS FTDALS4 ILE-306; GLU-401 AND
LYS-696.
PubMed=25943890; DOI=10.1007/s00401-015-1436-x;
Pottier C., Bieniek K.F., Finch N., van de Vorst M., Baker M.,
Perkersen R., Brown P., Ravenscroft T., van Blitterswijk M.,
Nicholson A.M., DeTure M., Knopman D.S., Josephs K.A., Parisi J.E.,
Petersen R.C., Boylan K.B., Boeve B.F., Graff-Radford N.R.,
Veltman J.A., Gilissen C., Murray M.E., Dickson D.W., Rademakers R.;
"Whole-genome sequencing reveals important role for TBK1 and OPTN
mutations in frontotemporal lobar degeneration without motor neuron
disease.";
Acta Neuropathol. 130:77-92(2015).
[47]
INTERACTION WITH TICAM1.
PubMed=25736436; DOI=10.15252/embr.201439637;
Hu Y.H., Zhang Y., Jiang L.Q., Wang S., Lei C.Q., Sun M.S., Shu H.B.,
Liu Y.;
"WDFY1 mediates TLR3/4 signaling by recruiting TRIF.";
EMBO Rep. 16:447-455(2015).
[48]
INVOLVEMENT IN FTDALS4, VARIANTS FTDALS4 HIS-47; CYS-105; THR-305;
GLN-308; GLN-357; ARG-559; VAL-571; VAL-598; GLU-643 DEL AND LYS-696,
AND CHARACTERIZATION OF VARIANTS FTDALS4 HIS-47; GLN-308; GLN-357;
ARG-559 AND LYS-696.
PubMed=25803835; DOI=10.1038/nn.4000;
Freischmidt A., Wieland T., Richter B., Ruf W., Schaeffer V.,
Mueller K., Marroquin N., Nordin F., Huebers A., Weydt P., Pinto S.,
Press R., Millecamps S., Molko N., Bernard E., Desnuelle C.,
Soriani M.H., Dorst J., Graf E., Nordstroem U., Feiler M.S., Putz S.,
Boeckers T.M., Meyer T., Winkler A.S., Winkelman J., de Carvalho M.,
Thal D.R., Otto M., Braennstroem T., Volk A.E., Kursula P.,
Danzer K.M., Lichtner P., Dikic I., Meitinger T., Ludolph A.C.,
Strom T.M., Andersen P.M., Weishaupt J.H.;
"Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal
dementia.";
Nat. Neurosci. 18:631-636(2015).
[49]
FUNCTION.
PubMed=27103069; DOI=10.15252/embj.201593350;
Sellier C., Campanari M.L., Julie Corbier C., Gaucherot A.,
Kolb-Cheynel I., Oulad-Abdelghani M., Ruffenach F., Page A., Ciura S.,
Kabashi E., Charlet-Berguerand N.;
"Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2
to induce motor neuron dysfunction and cell death.";
EMBO J. 35:1276-1297(2016).
[50]
INTERACTION WITH TRIM26, AND FUNCTION.
PubMed=26611359; DOI=10.1093/jmcb/mjv068;
Ran Y., Zhang J., Liu L.L., Pan Z.Y., Nie Y., Zhang H.Y., Wang Y.Y.;
"Autoubiquitination of TRIM26 links TBK1 to NEMO in RLR-mediated
innate antiviral immune response.";
J. Mol. Cell Biol. 8:31-43(2016).
[51]
UBIQUITINATION BY RNF128.
PubMed=27776110; DOI=10.1038/ni.3588;
Song G., Liu B., Li Z., Wu H., Wang P., Zhao K., Jiang G., Zhang L.,
Gao C.;
"E3 ubiquitin ligase RNF128 promotes innate antiviral immunity through
K63-linked ubiquitination of TBK1.";
Nat. Immunol. 17:1342-1351(2016).
[52]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-657 IN COMPLEX WITH
INHIBITORS, FUNCTION, ACTIVE SITE, HOMODIMER, UBIQUITINATION AT LYS-30
AND LYS-401, AND 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.
PubMed=23453971; DOI=10.1016/j.celrep.2013.01.034;
Larabi A., Devos J.M., Ng S.L., Nanao M.H., Round A., Maniatis T.,
Panne D.;
"Crystal structure and mechanism of activation of TANK-binding kinase
1.";
Cell Rep. 3:734-746(2013).
[53]
X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-657 IN COMPLEX WITH
INHIBITORS, FUNCTION, ACTIVE SITE, AUTOPHOSPHORYLATION, HOMODIMER,
INTERACTION WITH AZI2, AND MUTAGENESIS OF LYS-38; ASP-135; SER-172;
LEU-316; TYR-325; GLU-355; GLU-448; HIS-459; ILE-466 AND PHE-470.
PubMed=23453972; DOI=10.1016/j.celrep.2013.01.033;
Tu D., Zhu Z., Zhou A.Y., Yun C.H., Lee K.E., Toms A.V., Li Y.,
Dunn G.P., Chan E., Thai T., Yang S., Ficarro S.B., Marto J.A.,
Jeon H., Hahn W.C., Barbie D.A., Eck M.J.;
"Structure and ubiquitination-dependent activation of TANK-binding
kinase 1.";
Cell Rep. 3:747-758(2013).
[54]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-657 IN COMPLEX WITH
INHIBITORS, FUNCTION, AND PHOSPHORYLATION AT SER-172.
PubMed=23746807; DOI=10.1016/j.str.2013.04.025;
Shu C., Sankaran B., Chaton C.T., Herr A.B., Mishra A., Peng J.,
Li P.;
"Structural insights into the functions of TBK1 in innate
antimicrobial immunity.";
Structure 21:1137-1148(2013).
[55]
VARIANTS [LARGE SCALE ANALYSIS] GLN-271; GLU-291; HIS-296; ARG-410 AND
ALA-464.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: 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 (PubMed:21617041). Phosphorylates SMCR8 component of the
C9orf72-SMCR8 complex, promoting autophagosome maturation
(PubMed:27103069). Phosphorylates and activates AKT1
(PubMed:21464307). 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 (PubMed:21270402).
Phosphorylates Borna disease virus (BDV) P protein
(PubMed:16155125). {ECO:0000269|PubMed:10581243,
ECO:0000269|PubMed:10783893, ECO:0000269|PubMed:11839743,
ECO:0000269|PubMed:12692549, ECO:0000269|PubMed:12702806,
ECO:0000269|PubMed:14703513, ECO:0000269|PubMed:15367631,
ECO:0000269|PubMed:15485837, ECO:0000269|PubMed:15489227,
ECO:0000269|PubMed:16155125, ECO:0000269|PubMed:18583960,
ECO:0000269|PubMed:21138416, ECO:0000269|PubMed:21270402,
ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:21617041,
ECO:0000269|PubMed:21931631, ECO:0000269|PubMed:23453971,
ECO:0000269|PubMed:23453972, ECO:0000269|PubMed:23746807,
ECO:0000269|PubMed:26611359, ECO:0000269|PubMed:27103069}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: 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 (PubMed:25736436). Interacts with TRIM26
(PubMed:26611359). {ECO:0000269|PubMed:10581243,
ECO:0000269|PubMed:14530355, ECO:0000269|PubMed:14560022,
ECO:0000269|PubMed:14739303, ECO:0000269|PubMed:16155125,
ECO:0000269|PubMed:16281057, ECO:0000269|PubMed:17018283,
ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19153231,
ECO:0000269|PubMed:19416887, ECO:0000269|PubMed:19419966,
ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:21145761,
ECO:0000269|PubMed:21813773, ECO:0000269|PubMed:21931631,
ECO:0000269|PubMed:23453971, ECO:0000269|PubMed:23453972,
ECO:0000269|PubMed:23746807, ECO:0000269|PubMed:25736436,
ECO:0000269|PubMed:26611359}.
-!- SUBUNIT: (Microbial infection) Interacts with HCV NS3; this
interaction leads to inhibition of cellular antiviral response by
blocking necessary interactions between the TBK1 and its
substrates IRF3 and IRF7. {ECO:0000269|PubMed:15841462}.
-!- INTERACTION:
I0DF37:- (xeno); NbExp=3; IntAct=EBI-356402, EBI-9543922;
I6W9F2:- (xeno); NbExp=6; IntAct=EBI-356402, EBI-9518472;
K7Y1A2:- (xeno); NbExp=2; IntAct=EBI-356402, EBI-8788634;
P27958:- (xeno); NbExp=2; IntAct=EBI-356402, EBI-6919131;
Q9UKV8:AGO2; NbExp=2; IntAct=EBI-356402, EBI-528269;
Q7Z3C6:ATG9A; NbExp=2; IntAct=EBI-356402, EBI-727146;
Q9H6S1:AZI2; NbExp=3; IntAct=EBI-356402, EBI-359973;
Q13137:CALCOCO2; NbExp=5; IntAct=EBI-356402, EBI-739580;
Q6DT37:CDC42BPG; NbExp=2; IntAct=EBI-356402, EBI-689124;
Q62167:Ddx3x (xeno); NbExp=8; IntAct=EBI-356402, EBI-773173;
O41932:GAMMAHV.ORF11 (xeno); NbExp=4; IntAct=EBI-356402, EBI-9544132;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-356402, EBI-352572;
Q14164:IKBKE; NbExp=2; IntAct=EBI-356402, EBI-307369;
Q9Y6K9:IKBKG; NbExp=2; IntAct=EBI-356402, EBI-81279;
Q14653:IRF3; NbExp=9; IntAct=EBI-356402, EBI-2650369;
Q92985:IRF7; NbExp=2; IntAct=EBI-356402, EBI-968267;
Q7Z434:MAVS; NbExp=2; IntAct=EBI-356402, EBI-995373;
Q86YT6:MIB1; NbExp=2; IntAct=EBI-356402, EBI-2129148;
Q96AX9:MIB2; NbExp=2; IntAct=EBI-356402, EBI-2130249;
Q9NVV4:MTPAP; NbExp=2; IntAct=EBI-356402, EBI-2556166;
Q96CV9:OPTN; NbExp=12; IntAct=EBI-356402, EBI-748974;
O14730:RIOK3; NbExp=3; IntAct=EBI-356402, EBI-1047061;
P42226:STAT6; NbExp=7; IntAct=EBI-356402, EBI-1186478;
Q92844:TANK; NbExp=7; IntAct=EBI-356402, EBI-356349;
A7MCY6:TBKBP1; NbExp=8; IntAct=EBI-356402, EBI-359969;
Q8IUC6:TICAM1; NbExp=3; IntAct=EBI-356402, EBI-525995;
Q86WV6:TMEM173; NbExp=8; IntAct=EBI-356402, EBI-2800345;
Q12933:TRAF2; NbExp=3; IntAct=EBI-356402, EBI-355744;
P40222:TXLNA; NbExp=4; IntAct=EBI-356402, EBI-359793;
Q8BHN1:Txlng (xeno); NbExp=2; IntAct=EBI-356402, EBI-6116854;
Q05127:VP35 (xeno); NbExp=2; IntAct=EBI-356402, EBI-6148294;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15485837,
ECO:0000269|PubMed:21813773}. Note=Upon mitogen stimulation or
triggering of the immune system, TBK1 is recruited to the exocyst
by EXOC2.
-!- TISSUE SPECIFICITY: Ubiquitous with higher expression in testis.
Expressed in the ganglion cells, nerve fiber layer and
microvasculature of the retina. {ECO:0000269|PubMed:10783893,
ECO:0000269|PubMed:21447600}.
-!- DOMAIN: Comprises A N-terminal kinase domain, a ubiquitin-like
domain and a C-terminal coiled-coil region mediating
homodimerization. {ECO:0000269|PubMed:17599067,
ECO:0000269|PubMed:21042276}.
-!- PTM: 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. {ECO:0000269|PubMed:11839743,
ECO:0000269|PubMed:21138416, ECO:0000269|PubMed:23453971,
ECO:0000269|PubMed:23746807}.
-!- PTM: '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. 'Lys-63'-linked
polyubiquitination by RNF128 at Lys-30 and Lys-401 leads to the
activation of antiviral responses. {ECO:0000269|PubMed:22388039,
ECO:0000269|PubMed:23453971, ECO:0000269|PubMed:27776110}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:21447600, ECO:0000269|PubMed:22306015}.
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). {ECO:0000269|PubMed:21447600}.
-!- DISEASE: Frontotemporal dementia and/or amyotrophic lateral
sclerosis 4 (FTDALS4) [MIM:616439]: A neurodegenerative disorder
characterized by frontotemporal dementia and/or amyotrophic
lateral sclerosis in affected individuals. There is high
intrafamilial variation. Frontotemporal dementia is characterized
by frontal and temporal lobe atrophy associated with neuronal
loss, gliosis, and dementia. Patients exhibit progressive changes
in social, behavioral, and/or language function. Amyotrophic
lateral sclerosis is characterized by the death of motor neurons
in the brain, brainstem, and spinal cord, resulting in fatal
paralysis. {ECO:0000269|PubMed:25803835,
ECO:0000269|PubMed:25943890}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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). {ECO:0000305|PubMed:21042276}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. I-kappa-B kinase subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=BAA92129.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF191838; AAF05989.1; -; mRNA.
EMBL; AF174536; AAF69106.1; -; mRNA.
EMBL; AK002192; BAA92129.1; ALT_INIT; mRNA.
EMBL; AK291039; BAF83728.1; -; mRNA.
EMBL; CH471054; EAW97133.1; -; Genomic_DNA.
EMBL; BC034950; AAH34950.1; -; mRNA.
CCDS; CCDS8968.1; -.
RefSeq; NP_037386.1; NM_013254.3.
RefSeq; XP_005268866.1; XM_005268809.1.
RefSeq; XP_005268867.1; XM_005268810.1.
UniGene; Hs.505874; -.
PDB; 4EFO; X-ray; 1.77 A; A/B=302-383.
PDB; 4EUT; X-ray; 2.60 A; A/B=2-385.
PDB; 4EUU; X-ray; 1.80 A; A/B=2-308.
PDB; 4IM0; X-ray; 2.40 A; A=1-657.
PDB; 4IM2; X-ray; 2.50 A; A=1-657.
PDB; 4IM3; X-ray; 3.34 A; A=1-657.
PDB; 4IW0; X-ray; 4.00 A; A=2-657.
PDB; 4IWO; X-ray; 2.61 A; A=2-657.
PDB; 4IWP; X-ray; 3.06 A; A=2-657.
PDB; 4IWQ; X-ray; 3.00 A; A=2-657.
PDB; 5EOA; X-ray; 2.50 A; C/D=677-729.
PDB; 5EOF; X-ray; 2.05 A; C/D=677-729.
PDB; 5EP6; X-ray; 1.45 A; B/D=677-729.
PDBsum; 4EFO; -.
PDBsum; 4EUT; -.
PDBsum; 4EUU; -.
PDBsum; 4IM0; -.
PDBsum; 4IM2; -.
PDBsum; 4IM3; -.
PDBsum; 4IW0; -.
PDBsum; 4IWO; -.
PDBsum; 4IWP; -.
PDBsum; 4IWQ; -.
PDBsum; 5EOA; -.
PDBsum; 5EOF; -.
PDBsum; 5EP6; -.
ProteinModelPortal; Q9UHD2; -.
SMR; Q9UHD2; -.
BioGrid; 118878; 126.
CORUM; Q9UHD2; -.
DIP; DIP-27529N; -.
IntAct; Q9UHD2; 79.
MINT; MINT-1131333; -.
STRING; 9606.ENSP00000329967; -.
BindingDB; Q9UHD2; -.
ChEMBL; CHEMBL5408; -.
GuidetoPHARMACOLOGY; 2237; -.
iPTMnet; Q9UHD2; -.
PhosphoSitePlus; Q9UHD2; -.
BioMuta; TBK1; -.
DMDM; 74761953; -.
EPD; Q9UHD2; -.
MaxQB; Q9UHD2; -.
PaxDb; Q9UHD2; -.
PeptideAtlas; Q9UHD2; -.
PRIDE; Q9UHD2; -.
DNASU; 29110; -.
Ensembl; ENST00000331710; ENSP00000329967; ENSG00000183735.
GeneID; 29110; -.
KEGG; hsa:29110; -.
UCSC; uc001ssc.3; human.
CTD; 29110; -.
DisGeNET; 29110; -.
EuPathDB; HostDB:ENSG00000183735.9; -.
GeneCards; TBK1; -.
HGNC; HGNC:11584; TBK1.
HPA; HPA045797; -.
HPA; HPA060211; -.
MalaCards; TBK1; -.
MIM; 177700; phenotype.
MIM; 604834; gene.
MIM; 616439; phenotype.
neXtProt; NX_Q9UHD2; -.
OpenTargets; ENSG00000183735; -.
Orphanet; 1930; Herpetic encephalitis.
PharmGKB; PA36348; -.
eggNOG; KOG4250; Eukaryota.
eggNOG; ENOG410XRMU; LUCA.
GeneTree; ENSGT00900000140902; -.
HOGENOM; HOG000220867; -.
HOVERGEN; HBG008494; -.
InParanoid; Q9UHD2; -.
KO; K05410; -.
OMA; FRGRHKK; -.
OrthoDB; EOG091G0354; -.
PhylomeDB; Q9UHD2; -.
TreeFam; TF324269; -.
Reactome; R-HSA-1606341; IRF3 mediated activation of type 1 IFN.
Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
Reactome; R-HSA-3249367; STAT6-mediated induction of chemokines.
Reactome; R-HSA-3270619; IRF3-mediated induction of type I IFN.
Reactome; R-HSA-9013973; TICAM1-dependent activation of IRF3/IRF7.
Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
SABIO-RK; Q9UHD2; -.
SignaLink; Q9UHD2; -.
SIGNOR; Q9UHD2; -.
GeneWiki; TANK-binding_kinase_1; -.
GenomeRNAi; 29110; -.
PRO; PR:Q9UHD2; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000183735; -.
CleanEx; HS_TBK1; -.
ExpressionAtlas; Q9UHD2; baseline and differential.
Genevisible; Q9UHD2; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0003676; F:nucleic acid binding; IEA:Ensembl.
GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
GO; GO:0004672; F:protein kinase activity; TAS:Reactome.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0044565; P:dendritic cell proliferation; IEA:Ensembl.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:HGNC.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:BHF-UCL.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; IEA:Ensembl.
GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:BHF-UCL.
GO; GO:0016239; P:positive regulation of macroautophagy; IDA:HGNC.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; NAS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:1904417; P:positive regulation of xenophagy; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:1901214; P:regulation of neuron death; NAS:ParkinsonsUK-UCL.
GO; GO:0032479; P:regulation of type I interferon production; TAS:Reactome.
GO; GO:0009615; P:response to virus; TAS:UniProtKB.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0032606; P:type I interferon production; TAS:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
3D-structure; Amyotrophic lateral sclerosis; Antiviral defense;
ATP-binding; Coiled coil; Complete proteome; Cytoplasm;
Disease mutation; Glaucoma; Host-virus interaction; Immunity;
Innate immunity; Isopeptide bond; Kinase; Neurodegeneration;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 729 Serine/threonine-protein kinase TBK1.
/FTId=PRO_0000086743.
DOMAIN 9 310 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 309 385 Ubiquitin-like.
NP_BIND 15 23 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 621 629 Interaction with AZI2, TANK and TBKBP1.
{ECO:0000269|PubMed:21931631}.
COILED 407 657
COILED 658 713 {ECO:0000255}.
ACT_SITE 135 135 Proton acceptor.
{ECO:0000305|PubMed:23453971,
ECO:0000305|PubMed:23453972}.
BINDING 38 38 ATP. {ECO:0000305}.
MOD_RES 172 172 Phosphoserine; by autocatalysis and IKKB.
{ECO:0000269|PubMed:11839743,
ECO:0000269|PubMed:23746807}.
MOD_RES 716 716 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 30 30 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:23453971}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:23453971}.
CROSSLNK 670 670 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22388039}.
VARIANT 47 47 R -> H (in FTDALS4; loss of kinase
activity). {ECO:0000269|PubMed:25803835}.
/FTId=VAR_073938.
VARIANT 105 105 Y -> C (in FTDALS4).
{ECO:0000269|PubMed:25803835}.
/FTId=VAR_073939.
VARIANT 151 151 S -> F (in dbSNP:rs55824172).
{ECO:0000269|PubMed:21447600}.
/FTId=VAR_069754.
VARIANT 271 271 R -> Q (in dbSNP:rs56196591).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041208.
VARIANT 291 291 K -> E (in dbSNP:rs34774243).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041209.
VARIANT 296 296 D -> H (in a breast pleomorphic lobular
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041210.
VARIANT 305 305 I -> T (in FTDALS4; dbSNP:rs770942184).
{ECO:0000269|PubMed:25803835}.
/FTId=VAR_073940.
VARIANT 306 306 L -> I (in FTDALS4; unknown pathological
significance; dbSNP:rs201970436).
{ECO:0000269|PubMed:21447600,
ECO:0000269|PubMed:25943890}.
/FTId=VAR_069755.
VARIANT 308 308 R -> Q (in FTDALS4; reduced kinase
activity). {ECO:0000269|PubMed:25803835}.
/FTId=VAR_073941.
VARIANT 357 357 R -> Q (in FTDALS4; reduced kinase
activity; dbSNP:rs758357594).
{ECO:0000269|PubMed:25803835}.
/FTId=VAR_073942.
VARIANT 388 388 N -> D (in dbSNP:rs17857028).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_024746.
VARIANT 401 401 K -> E (in FTDALS4; dbSNP:rs756751089).
{ECO:0000269|PubMed:25943890}.
/FTId=VAR_073943.
VARIANT 410 410 G -> R (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041211.
VARIANT 464 464 V -> A (in dbSNP:rs35635889).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:21447600}.
/FTId=VAR_041212.
VARIANT 559 559 M -> R (in FTDALS4; loss of kinase
activity). {ECO:0000269|PubMed:25803835}.
/FTId=VAR_073944.
VARIANT 570 570 K -> Q (in dbSNP:rs17853341).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_024747.
VARIANT 571 571 A -> V (in FTDALS4; dbSNP:rs765035140).
{ECO:0000269|PubMed:25803835}.
/FTId=VAR_073945.
VARIANT 598 598 M -> V (in FTDALS4).
{ECO:0000269|PubMed:25803835}.
/FTId=VAR_073946.
VARIANT 643 643 Missing (in FTDALS4).
{ECO:0000269|PubMed:25803835}.
/FTId=VAR_073947.
VARIANT 696 696 E -> K (in FTDALS4; loss of kinase
activity; impairs binding to OPTN;
dbSNP:rs748112833).
{ECO:0000269|PubMed:25803835,
ECO:0000269|PubMed:25943890}.
/FTId=VAR_073948.
MUTAGEN 30 30 K->R: Decreases ubiquitination. Abolishes
ubiquitination, phosphorylation and
kinase activity; when associated with R-
401. {ECO:0000269|PubMed:23453971}.
MUTAGEN 33 33 D->A: Decreases phosphorylation and
kinase activity.
{ECO:0000269|PubMed:23453971}.
MUTAGEN 38 38 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:10581243,
ECO:0000269|PubMed:23453971,
ECO:0000269|PubMed:23453972}.
MUTAGEN 135 135 D->N: Loss of kinase activity.
{ECO:0000269|PubMed:21931631,
ECO:0000269|PubMed:23453971,
ECO:0000269|PubMed:23453972}.
MUTAGEN 172 172 S->A: Loss of kinase activity. No effect
on dimerization.
{ECO:0000269|PubMed:11839743,
ECO:0000269|PubMed:23453972}.
MUTAGEN 172 172 S->E: Decreased kinase activity.
{ECO:0000269|PubMed:11839743,
ECO:0000269|PubMed:23453972}.
MUTAGEN 316 316 L->E: Decreases kinase activity. No
effect on phosphorylation.
{ECO:0000269|PubMed:23453972}.
MUTAGEN 325 325 Y->E: Abolishes phosphorylation and
kinase activity.
{ECO:0000269|PubMed:23453972}.
MUTAGEN 355 355 E->R: Decreases phosphorylation and
kinase activity. Abolishes dimerization;
when associated with A-357 or R-448.
{ECO:0000269|PubMed:23453971,
ECO:0000269|PubMed:23453972}.
MUTAGEN 357 357 R->A: Decreases phosphorylation and
kinase activity. Abolishes dimerization;
when associated with R-355.
{ECO:0000269|PubMed:23453971}.
MUTAGEN 401 401 K->R: Decreases ubiquitination. Abolishes
ubiquitination, phosphorylation and
kinase activity; when associated with R-
30. {ECO:0000269|PubMed:23453971}.
MUTAGEN 448 448 E->R: Decreases phosphorylation and
kinase activity. Abolishes dimerization;
when associated with R-355.
{ECO:0000269|PubMed:23453972}.
MUTAGEN 459 459 H->E: Abolishes dimerization and
decreases kinase activity but no effect
on phosphorylation; when associated with
E-466 and E-470.
{ECO:0000269|PubMed:23453972}.
MUTAGEN 466 466 I->E: Abolishes dimerization and
decreases kinase activity but no effect
on phosphorylation; when associated with
E-459 and E-470.
{ECO:0000269|PubMed:23453972}.
MUTAGEN 470 470 F->E: Abolishes dimerization and
decreases kinase activity but no effect
on phosphorylation; when associated with
E-459 and E-466.
{ECO:0000269|PubMed:23453972}.
MUTAGEN 547 547 R->D: Decreases phosphorylation and
kinase activity. Abolishes dimerization.
{ECO:0000269|PubMed:23453971}.
MUTAGEN 577 577 Y->A: Decreases kinase activity.
{ECO:0000269|PubMed:23453971}.
MUTAGEN 580 580 E->A: Decreases kinase activity.
{ECO:0000269|PubMed:23453971}.
MUTAGEN 582 582 I->A: Decreases kinase activity.
{ECO:0000269|PubMed:23453971}.
MUTAGEN 589 589 K->D: Decreases phosphorylation and
kinase activity.
{ECO:0000269|PubMed:23453971}.
MUTAGEN 690 690 M->A: Decreases interaction with TANK.
{ECO:0000269|PubMed:21931631}.
MUTAGEN 693 693 L->A: Almost abolishes interaction with
TANK. {ECO:0000269|PubMed:21931631}.
MUTAGEN 694 694 K->E: Strongly decreases interaction with
TANK and TBKBP1. No effect on
phosphorylation.
{ECO:0000269|PubMed:21931631}.
MUTAGEN 704 704 L->A: Strongly decreases interaction with
AZI2, TANK and TBKBP1. No effect on
phosphorylation.
{ECO:0000269|PubMed:21931631}.
MUTAGEN 708 708 N->A: Decreases interaction with TANK.
{ECO:0000269|PubMed:21931631}.
MUTAGEN 711 711 L->A: Almost abolishes interaction with
TANK. {ECO:0000269|PubMed:21931631}.
STRAND 1 3 {ECO:0000244|PDB:4IM3}.
STRAND 5 17 {ECO:0000244|PDB:4EUU}.
STRAND 19 28 {ECO:0000244|PDB:4EUU}.
TURN 29 31 {ECO:0000244|PDB:4EUU}.
STRAND 34 40 {ECO:0000244|PDB:4EUU}.
HELIX 42 46 {ECO:0000244|PDB:4EUU}.
HELIX 49 61 {ECO:0000244|PDB:4EUU}.
STRAND 65 67 {ECO:0000244|PDB:4IWO}.
STRAND 70 75 {ECO:0000244|PDB:4EUU}.
TURN 77 79 {ECO:0000244|PDB:4EUU}.
STRAND 82 87 {ECO:0000244|PDB:4EUU}.
HELIX 94 99 {ECO:0000244|PDB:4EUU}.
HELIX 101 103 {ECO:0000244|PDB:4EUU}.
HELIX 109 128 {ECO:0000244|PDB:4EUU}.
HELIX 138 140 {ECO:0000244|PDB:4EUU}.
STRAND 141 145 {ECO:0000244|PDB:4EUU}.
STRAND 151 155 {ECO:0000244|PDB:4EUU}.
TURN 161 163 {ECO:0000244|PDB:4IWQ}.
HELIX 167 169 {ECO:0000244|PDB:4EUT}.
STRAND 173 175 {ECO:0000244|PDB:4EUT}.
HELIX 177 179 {ECO:0000244|PDB:4EUU}.
HELIX 182 188 {ECO:0000244|PDB:4EUU}.
HELIX 202 216 {ECO:0000244|PDB:4EUU}.
STRAND 220 222 {ECO:0000244|PDB:4EUU}.
HELIX 227 229 {ECO:0000244|PDB:4EUU}.
HELIX 231 240 {ECO:0000244|PDB:4EUU}.
STRAND 247 250 {ECO:0000244|PDB:4EUU}.
STRAND 257 262 {ECO:0000244|PDB:4EUU}.
HELIX 271 284 {ECO:0000244|PDB:4EUU}.
STRAND 285 287 {ECO:0000244|PDB:4IWP}.
TURN 289 291 {ECO:0000244|PDB:4EUU}.
HELIX 305 307 {ECO:0000244|PDB:4EFO}.
STRAND 308 315 {ECO:0000244|PDB:4EFO}.
TURN 316 319 {ECO:0000244|PDB:4EFO}.
STRAND 320 327 {ECO:0000244|PDB:4EFO}.
HELIX 332 343 {ECO:0000244|PDB:4EFO}.
HELIX 347 349 {ECO:0000244|PDB:4EFO}.
STRAND 350 354 {ECO:0000244|PDB:4EFO}.
STRAND 357 359 {ECO:0000244|PDB:4EFO}.
HELIX 367 369 {ECO:0000244|PDB:4EFO}.
STRAND 375 377 {ECO:0000244|PDB:4IM0}.
STRAND 379 383 {ECO:0000244|PDB:4EFO}.
HELIX 408 480 {ECO:0000244|PDB:4IM0}.
HELIX 498 526 {ECO:0000244|PDB:4IM0}.
STRAND 530 532 {ECO:0000244|PDB:4IWO}.
HELIX 535 539 {ECO:0000244|PDB:4IM0}.
HELIX 544 546 {ECO:0000244|PDB:4IM0}.
HELIX 548 571 {ECO:0000244|PDB:4IM0}.
HELIX 577 603 {ECO:0000244|PDB:4IM0}.
HELIX 605 647 {ECO:0000244|PDB:4IM0}.
TURN 648 651 {ECO:0000244|PDB:4IM0}.
HELIX 680 714 {ECO:0000244|PDB:5EP6}.
STRAND 715 717 {ECO:0000244|PDB:5EP6}.
SEQUENCE 729 AA; 83642 MW; B58E4FE1B502276D CRC64;
MQSTSNHLWL LSDILGQGAT ANVFRGRHKK TGDLFAIKVF NNISFLRPVD VQMREFEVLK
KLNHKNIVKL FAIEEETTTR HKVLIMEFCP CGSLYTVLEE PSNAYGLPES EFLIVLRDVV
GGMNHLRENG IVHRDIKPGN IMRVIGEDGQ SVYKLTDFGA ARELEDDEQF VSLYGTEEYL
HPDMYERAVL RKDHQKKYGA TVDLWSIGVT FYHAATGSLP FRPFEGPRRN KEVMYKIITG
KPSGAISGVQ KAENGPIDWS GDMPVSCSLS RGLQVLLTPV LANILEADQE KCWGFDQFFA
ETSDILHRMV IHVFSLQQMT AHKIYIHSYN TATIFHELVY KQTKIISSNQ ELIYEGRRLV
LEPGRLAQHF PKTTEENPIF VVSREPLNTI GLIYEKISLP KVHPRYDLDG DASMAKAITG
VVCYACRIAS TLLLYQELMR KGIRWLIELI KDDYNETVHK KTEVVITLDF CIRNIEKTVK
VYEKLMKINL EAAELGEISD IHTKLLRLSS SQGTIETSLQ DIDSRLSPGG SLADAWAHQE
GTHPKDRNVE KLQVLLNCMT EIYYQFKKDK AERRLAYNEE QIHKFDKQKL YYHATKAMTH
FTDECVKKYE AFLNKSEEWI RKMLHLRKQL LSLTNQCFDI EEEVSKYQEY TNELQETLPQ
KMFTASSGIK HTMTPIYPSS NTLVEMTLGM KKLKEEMEGV VKELAENNHI LERFGSLTMD
GGLRNVDCL


Related products :

Catalog number Product name Quantity
EIAAB41578 Homo sapiens,Human,NAK,NF-kappa-B-activating kinase,Serine_threonine-protein kinase TBK1,T2K,TANK-binding kinase 1,TBK1
EIAAB41577 Mouse,Mus musculus,Serine_threonine-protein kinase TBK1,T2K,TANK-binding kinase 1,Tbk1
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
H0370 Serine threonine-protein kinase TBK1 (TBK1), Mouse, ELISA Kit 96T
H0369 Serine threonine-protein kinase TBK1 (TBK1), Human, ELISA Kit 96T
TBK1_MOUSE ELISA Kit FOR Serine per threonine-protein kinase TBK1; organism: Mouse; gene name: Tbk1 96T
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB41234 Homo sapiens,Human,MAP3K7IP3,Mitogen-activated protein kinase kinase kinase 7-interacting protein 3,NF-kappa-B-activating protein 1,TAB3,TAB-3,TAK1-binding protein 3,TGF-beta-activated kinase 1 and MA
20-272-190722 NAK - Mouse monoclonal [108A429] to NAK; EC 2.7.11.1; TANK-binding kinase 1; T2K; NF-kappa-B-activating kinase Monoclonal 0.05 mg
31-031 Cdk7 is the catalytic subunit of the CDK-activating kinase (CAK) complex, a serine-threonine kinase. CAK activates the cyclin-associated kinases CDC2_CDK1, CDK2, CDK4 and CDK6 by threonine phosphoryla 0.1 mg
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
EIAAB41580 Mouse,Mus musculus,Similar to NAP1 TBK1 adapter,Sintbad,TANK-binding kinase 1-binding protein 1,TBK1-binding protein 1,Tbkbp1
EM580 Serine per threonine-protein kinase TBK1 Elisa Kit 96T
abx110203 Polyclonal Rabbit Serine per threonine-protein kinase TBK1 Antibody 100 μg
abx109211 Polyclonal Rabbit Serine per threonine-protein kinase TBK1 Antibody (HRP) 100 μg
TBK1-101AP TANK binding Kinase 1 WB control: PC-TBK1 Host: Rabbit Affinity purifed 100-150ul
TBK1-101AP PC-TBK1 (WB control) TANK binding Kinase 1 Immunogen: peptide Host: Rabbit 100-150ul
DL-TBK1-Hu Human TANK Binding Kinase 1 (TBK1) ELISA Kit 96T
abx105912 Polyclonal Rabbit Serine per threonine-protein kinase TBK1 Antibody (Biotin) 100 μg
abx107327 Polyclonal Rabbit Serine per threonine-protein kinase TBK1 Antibody (FITC) 100 μg
TBK1-101AP TANK binding Kinase 1 Antigenic peptide: P-TBK1 Host: Rabbit Affinity purifed 100ul


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur