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Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Putative NF-kappa-B-activating protein 031N) (Virus-induced-signaling adapter) (VISA)

 MAVS_HUMAN              Reviewed;         540 AA.
Q7Z434; A8K6X0; B2BD33; B2BD34; F5H6C8; M1P2Z0; Q2HWT5; Q3I0Y2;
Q5T7I6; Q86VY7; Q9H1H3; Q9H4Y1; Q9H8D3; Q9ULE9;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
13-NOV-2019, entry version 171.
RecName: Full=Mitochondrial antiviral-signaling protein {ECO:0000305};
Short=MAVS {ECO:0000305};
AltName: Full=CARD adapter inducing interferon beta;
Short=Cardif;
AltName: Full=Interferon beta promoter stimulator protein 1;
Short=IPS-1;
AltName: Full=Putative NF-kappa-B-activating protein 031N;
AltName: Full=Virus-induced-signaling adapter;
Short=VISA;
Name=MAVS {ECO:0000312|HGNC:HGNC:29233};
Synonyms=IPS1, KIAA1271, VISA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
MUTAGENESIS OF THR-54 AND 67-GLY--VAL-69, INTERACTION WITH DDX58/RIG-I
AND TRAF6, SUBCELLULAR LOCATION, AND VARIANTS LYS-198 AND PHE-409.
PubMed=16125763; DOI=10.1016/j.cell.2005.08.012;
Seth R.B., Sun L., Ea C.-K., Chen Z.J.;
"Identification and characterization of MAVS, a mitochondrial
antiviral signaling protein that activates NF-kappaB and IRF 3.";
Cell 122:669-682(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH
DDX58/RIG-I; IRF3; TRAF2 AND TRAF6, MUTAGENESIS OF GLN-145; GLU-155
AND GLU-457, FUNCTION, AND VARIANT GLU-93.
PubMed=16153868; DOI=10.1016/j.molcel.2005.08.014;
Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.;
"VISA is an adapter protein required for virus-triggered IFN-beta
Signaling.";
Mol. Cell 19:727-740(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDX58/RIG-I;
IKBKE; CHUK AND IKBKB, FUNCTION, CLEAVAGE SITE, MUTAGENESIS OF
CYS-508, AND VARIANTS LYS-198 AND PHE-409.
PubMed=16177806; DOI=10.1038/nature04193;
Meylan E., Curran J., Hofmann K., Moradpour D., Binder M.,
Bartenschlager R., Tschopp J.;
"Cardif is an adaptor protein in the RIG-I antiviral pathway and is
targeted by hepatitis C virus.";
Nature 437:1167-1172(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
INTERACTION WITH DDX58/RIG-I; IFIH1/MDA5; FADD AND RIPK1, FUNCTION,
AND VARIANT GLU-93.
PubMed=16127453; DOI=10.1038/ni1243;
Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H.,
Ishii K.J., Takeuchi O., Akira S.;
"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I
interferon induction.";
Nat. Immunol. 6:981-988(2005).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
PubMed=18207245; DOI=10.1016/j.molimm.2007.11.018;
Lad S.P., Yang G., Scott D.A., Chao T.H., Correia Jda S.,
de la Torre J.C., Li E.;
"Identification of MAVS splicing variants that interfere with
RIGI/MAVS pathway signaling.";
Mol. Immunol. 45:2277-2287(2008).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=22427742; DOI=10.1371/journal.pbio.1001282;
Patel M.R., Loo Y.M., Horner S.M., Gale M. Jr., Malik H.S.;
"Convergent evolution of escape from hepaciviral antagonism in
primates.";
PLoS Biol. 10:E1001282-E1001282(2012).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:337-345(1999).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung fibroblast;
PubMed=12761501; DOI=10.1038/sj.onc.1206406;
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
Sugano S.;
"Large-scale identification and characterization of human genes that
activate NF-kappaB and MAPK signaling pathways.";
Oncogene 22:3307-3318(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5),
AND VARIANT GLU-93.
TISSUE=Pericardium, Placenta, and Tongue;
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).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[11]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-93; LYS-198
AND PHE-409.
TISSUE=Brain;
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).
[13]
INTERACTION WITH HCV NS3/4A PROTEASE (MICROBIAL INFECTION), CLEAVAGE
SITE, AND MUTAGENESIS OF CYS-435; CYS-452 AND CYS-508.
PubMed=16301520; DOI=10.1073/pnas.0508531102;
Li X.D., Sun L., Seth R.B., Pineda G., Chen Z.J.;
"Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral
signaling protein off the mitochondria to evade innate immunity.";
Proc. Natl. Acad. Sci. U.S.A. 102:17717-17722(2005).
[14]
INTERACTION WITH DHX58/LGP2 AND IKBKE.
PubMed=17020950; DOI=10.1128/jvi.01325-06;
Komuro A., Horvath C.M.;
"RNA- and virus-independent inhibition of antiviral signaling by RNA
helicase LGP2.";
J. Virol. 80:12332-12342(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
INTERACTION WITH HEPATITIS GB VIRUS B NS3/4A PROTEASE (MICROBIAL
INFECTION), CLEAVAGE SITE, AND MUTAGENESIS OF CYS-508.
PubMed=17093192; DOI=10.1128/jvi.02076-06;
Chen Z., Benureau Y., Rijnbrand R., Yi J., Wang T., Warter L.,
Lanford R.E., Weinman S.A., Lemon S.M., Martin A., Li K.;
"GB virus B disrupts RIG-I signaling by NS3/4A-mediated cleavage of
the adaptor protein MAVS.";
J. Virol. 81:964-976(2007).
[17]
CLEAVAGE BY HAV PROTEIN 3CD (MICROBIAL INFECTION), CLEAVAGE SITE, AND
MUTAGENESIS OF GLN-427 AND GLU-463.
PubMed=17438296; DOI=10.1073/pnas.0611506104;
Yang Y., Liang Y., Qu L., Chen Z., Yi M., Li K., Lemon S.M.;
"Disruption of innate immunity due to mitochondrial targeting of a
picornaviral protease precursor.";
Proc. Natl. Acad. Sci. U.S.A. 104:7253-7258(2007).
[18]
UBIQUITINATION.
PubMed=17460044; DOI=10.1073/pnas.0611551104;
Arimoto K., Takahashi H., Hishiki T., Konishi H., Fujita T.,
Shimotohno K.;
"Negative regulation of the RIG-I signaling by the ubiquitin ligase
RNF125.";
Proc. Natl. Acad. Sci. U.S.A. 104:7500-7505(2007).
[19]
INTERACTION WITH IFIH1.
PubMed=17600090; DOI=10.1073/pnas.0700544104;
Diao F., Li S., Tian Y., Zhang M., Xu L.G., Zhang Y., Wang R.P.,
Chen D., Zhai Z., Zhong B., Tien P., Shu H.B.;
"Negative regulation of MDA5- but not RIG-I-mediated innate antiviral
signaling by the dihydroxyacetone kinase.";
Proc. Natl. Acad. Sci. U.S.A. 104:11706-11711(2007).
[20]
INTERACTION WITH ATG5 AND ATG12, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF THR-54.
PubMed=17709747; DOI=10.1073/pnas.0704014104;
Jounai N., Takeshita F., Kobiyama K., Sawano A., Miyawaki A.,
Xin K.Q., Ishii K.J., Kawai T., Akira S., Suzuki K., Okuda K.;
"The Atg5-Atg12 conjugate associates with innate antiviral immune
responses.";
Proc. Natl. Acad. Sci. U.S.A. 104:14050-14055(2007).
[21]
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).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(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 NLRX1.
PubMed=18200010; DOI=10.1038/nature06501;
Moore C.B., Bergstralh D.T., Duncan J.A., Lei Y., Morrison T.E.,
Zimmermann A.G., Accavitti-Loper M.A., Madden V.J., Sun L., Ye Z.,
Lich J.D., Heise M.T., Chen Z., Ting J.P.-Y.;
"NLRX1 is a regulator of mitochondrial antiviral immunity.";
Nature 451:573-577(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-157; SER-165;
SER-222; SER-233; THR-234 AND SER-258, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[27]
FUNCTION.
PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
Chiu Y.-H., Macmillan J.B., Chen Z.J.;
"RNA polymerase III detects cytosolic DNA and induces type I
interferons through the RIG-I pathway.";
Cell 138:576-591(2009).
[28]
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).
[29]
INTERACTION WITH PSMA7.
PubMed=19734229; DOI=10.4049/jimmunol.0901646;
Jia Y., Song T., Wei C., Ni C., Zheng Z., Xu Q., Ma H., Li L.,
Zhang Y., He X., Xu Y., Shi W., Zhong H.;
"Negative regulation of MAVS-mediated innate immune response by
PSMA7.";
J. Immunol. 183:4241-4248(2009).
[30]
INTERACTION WITH PCBP2, AND UBIQUITINATION BY ITCH.
PubMed=19881509; DOI=10.1038/ni.1815;
You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z.;
"PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin
ligase AIP4.";
Nat. Immunol. 10:1300-1308(2009).
[31]
INTERACTION WITH C1QBP.
PubMed=19164550; DOI=10.1073/pnas.0811029106;
Xu L., Xiao N., Liu F., Ren H., Gu J.;
"Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at
mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 106:1530-1535(2009).
[32]
INTERACTION WITH TMEM173/STING.
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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-165, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[34]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20451243; DOI=10.1016/j.cell.2010.04.018;
Dixit E., Boulant S., Zhang Y., Lee A.S., Odendall C., Shum B.,
Hacohen N., Chen Z.J., Whelan S.P., Fransen M., Nibert M.L.,
Superti-Furga G., Kagan J.C.;
"Peroxisomes are signaling platforms for antiviral innate immunity.";
Cell 141:668-681(2010).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-258, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[36]
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).
[37]
PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND MUTAGENESIS OF
GLN-148.
PubMed=21436888; DOI=10.1371/journal.ppat.1001311;
Mukherjee A., Morosky S.A., Delorme-Axford E., Dybdahl-Sissoko N.,
Oberste M.S., Wang T., Coyne C.B.;
"The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate
host type I interferon and apoptotic signaling.";
PLoS Pathog. 7:E1001311-E1001311(2011).
[38]
INTERACTION WITH IFIT3 AND TBK1.
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).
[39]
FUNCTION, INTERACTION WITH NDFIP1 AND SMURF1, AND UBIQUITINATION BY
SMURF1.
PubMed=23087404; DOI=10.4049/jimmunol.1201445;
Wang Y., Tong X., Ye X.;
"Ndfip1 negatively regulates RIG-I-dependent immune signaling by
enhancing E3 ligase Smurf1-mediated MAVS degradation.";
J. Immunol. 189:5304-5313(2012).
[40]
INTERACTION WITH HRSV NS1 (MICROBIAL INFECTION).
PubMed=22383950; DOI=10.1371/journal.pone.0029386;
Boyapalle S., Wong T., Garay J., Teng M., San Juan-Vergara H.,
Mohapatra S., Mohapatra S.;
"Respiratory syncytial virus NS1 protein colocalizes with
mitochondrial antiviral signaling protein MAVS following infection.";
PLoS ONE 7:E29386-E29386(2012).
[41]
INTERACTION WITH ANKRD17.
PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
Menning M., Kufer T.A.;
"A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
Nod2-mediated inflammatory responses.";
FEBS Lett. 587:2137-2142(2013).
[42]
INTERACTION WITH MUL1.
PubMed=23399697; DOI=10.1038/icb.2013.7;
Jenkins K., Khoo J.J., Sadler A., Piganis R., Wang D., Borg N.A.,
Hjerrild K., Gould J., Thomas B.J., Nagley P., Hertzog P.J.,
Mansell A.;
"Mitochondrially localised MUL1 is a novel modulator of antiviral
signaling.";
Immunol. Cell Biol. 91:321-330(2013).
[43]
INTERACTION WITH UBXN1.
PubMed=23545497; DOI=10.1016/j.celrep.2013.02.027;
Wang P., Yang L., Cheng G., Yang G., Xu Z., You F., Sun Q., Lin R.,
Fikrig E., Sutton R.E.;
"UBXN1 interferes with Rig-I-like receptor-mediated antiviral immune
response by targeting MAVS.";
Cell Rep. 3:1057-1070(2013).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-165; SER-180;
SER-188; THR-215 AND SER-222, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[46]
PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION).
PubMed=24390337; DOI=10.1128/jvi.02712-13;
Feng Q., Langereis M.A., Lork M., Nguyen M., Hato S.V., Lanke K.,
Emdad L., Bhoopathi P., Fisher P.B., Lloyd R.E., van Kuppeveld F.J.;
"Enterovirus 2Apro targets MDA5 and MAVS in infected cells.";
J. Virol. 88:3369-3378(2014).
[47]
FUNCTION, DOMAIN, INTERACTION WITH IRF3, PHOSPHORYLATION AT SER-442,
UBIQUITINATION, AND MUTAGENESIS OF SER-442.
PubMed=25636800; DOI=10.1126/science.aaa2630;
Liu S., Cai X., Wu J., Cong Q., Chen X., Li T., Du F., Ren J.,
Wu Y.T., Grishin N.V., Chen Z.J.;
"Phosphorylation of innate immune adaptor proteins MAVS, STING, and
TRIF induces IRF3 activation.";
Science 347:AAA2630-AAA2630(2015).
[48]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[49]
INTERACTION WITH TTLL12; TBK1 AND IKBKE.
PubMed=28011935; DOI=10.4049/jimmunol.1601194;
Ju L.G., Zhu Y., Lei P.J., Yan D., Zhu K., Wang X., Li Q.L., Li X.J.,
Chen J.W., Li L.Y., Wu M.;
"TTLL12 Inhibits the Activation of Cellular Antiviral Signaling
through Interaction with VISA/MAVS.";
J. Immunol. 198:1274-1284(2017).
[50]
INTERACTION WITH SENECA VALLEY VIRUS PROTEASE 3C (MICROBIAL
INFECTION), PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND
MUTAGENESIS OF GLN-148; GLN-159; GLN-162; GLN-196 AND GLN-198.
PubMed=28566380; DOI=10.1128/jvi.00823-17;
Qian S., Fan W., Liu T., Wu M., Zhang H., Cui X., Zhou Y., Hu J.,
Wei S., Chen H., Li X., Qian P.;
"Seneca Valley virus suppresses host type I interferon production by
targeting adaptor proteins MAVS, TRIF, and TANK for cleavage.";
J. Virol. 91:0-0(2017).
[51]
PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION).
PubMed=28253362; DOI=10.1371/journal.ppat.1006243;
Wang B., Xi X., Lei X., Zhang X., Cui S., Wang J., Jin Q., Zhao Z.;
"Correction: Enterovirus 71 Protease 2Apro Targets MAVS to Inhibit
Anti-Viral Type I Interferon Responses.";
PLoS Pathog. 13:E1006243-E1006243(2017).
[52]
INTERACTION WITH GPATCH3.
PubMed=28414768; DOI=10.1371/journal.ppat.1006328;
Nie Y., Ran Y., Zhang H.Y., Huang Z.F., Pan Z.Y., Wang S.Y.,
Wang Y.Y.;
"GPATCH3 negatively regulates RLR-mediated innate antiviral responses
by disrupting the assembly of VISA signalosome.";
PLoS Pathog. 13:E1006328-E1006328(2017).
[53]
STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS) OF 3-93, SUBUNIT, AND
MUTAGENESIS OF GLU-26 AND TRP-56.
PubMed=24569476; DOI=10.7554/elife.01489;
Xu H., He X., Zheng H., Huang L.J., Hou F., Yu Z., de la Cruz M.J.,
Borkowski B., Zhang X., Chen Z.J., Jiang Q.X.;
"Structural basis for the prion-like MAVS filaments in antiviral
innate immunity.";
Elife 3:E01489-E01489(2014).
[54]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-99 IN COMPLEX WITH
DDX58/RIG-I, STRUCTURE BY ELECTRON MICROSCOPY (3.64 ANGSTROMS) OF
1-97, AND SUBUNIT.
PubMed=25018021; DOI=10.1016/j.molcel.2014.06.010;
Wu B., Peisley A., Tetrault D., Li Z., Egelman E.H., Magor K.E.,
Walz T., Penczek P.A., Hur S.;
"Molecular imprinting as a signal-activation mechanism of the viral
RNA sensor RIG-I.";
Mol. Cell 55:511-523(2014).
[55] {ECO:0000244|PDB:5JEK}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 433-450 IN COMPLEX WITH
IRF3, INTERACTION WITH IRF3, PHOSPHORYLATION AT SER-442, AND
MUTAGENESIS OF SER-442.
PubMed=27302953; DOI=10.1073/pnas.1603269113;
Zhao B., Shu C., Gao X., Sankaran B., Du F., Shelton C.L., Herr A.B.,
Ji J.Y., Li P.;
"Structural basis for concerted recruitment and activation of IRF-3 by
innate immune adaptor proteins.";
Proc. Natl. Acad. Sci. U.S.A. 113:E3403-E3412(2016).
-!- FUNCTION: Required for innate immune defense against viruses
(PubMed:16125763, PubMed:16127453, PubMed:16153868,
PubMed:16177806, PubMed:19631370, PubMed:20451243,
PubMed:23087404). Acts downstream of DHX33, DDX58/RIG-I and
IFIH1/MDA5, which detect intracellular dsRNA produced during viral
replication, to coordinate pathways leading to the activation of
NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of
antiviral cytokines such as IFN-beta and RANTES (CCL5)
(PubMed:16125763, PubMed:16127453, PubMed:16153868,
PubMed:16177806, PubMed:19631370, PubMed:20451243,
PubMed:23087404, PubMed:25636800). Peroxisomal and mitochondrial
MAVS act sequentially to create an antiviral cellular state
(PubMed:20451243). Upon viral infection, peroxisomal MAVS induces
the rapid interferon-independent expression of defense factors
that provide short-term protection, whereas mitochondrial MAVS
activates an interferon-dependent signaling pathway with delayed
kinetics, which amplifies and stabilizes the antiviral response
(PubMed:20451243). May activate the same pathways following
detection of extracellular dsRNA by TLR3 (PubMed:16153868). May
protect cells from apoptosis (PubMed:16125763).
{ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453,
ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:16177806,
ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20451243,
ECO:0000269|PubMed:23087404, ECO:0000269|PubMed:25636800}.
-!- SUBUNIT: Self-associates and polymerizes (via CARD domains) to
form 400 nM long three-stranded helical filaments on mitochondria,
filament nucleation requires interaction with DDX58/RIG-I whose
CARD domains act as a template for filament assembly
(PubMed:24569476, PubMed:25018021). Interacts with DDX58/RIG-I,
IFIH1/MDA5, TRAF2, TRAF6 and C1QBP (PubMed:16125763,
PubMed:16127453, PubMed:17600090). May interact with FADD, RIPK1,
CHUK and IKBKB (PubMed:16153868, PubMed:16177806,
PubMed:16127453). Interacts (when phosphorylated) with IRF3;
following activation and phosphorylation on the pLxIS motif by
TBK1, recruits IRF3 (PubMed:25636800, PubMed:27302953). Interacts
with NLRX1 (PubMed:18200010). Interaction with NLRX1 requires the
CARD domain (PubMed:18200010). Interacts with PSMA7
(PubMed:19734229). Interacts with TRAFD1 (By similarity).
Interacts (via C-terminus) with PCBP2 in a complex containing
MAVS/IPS1, PCBP2 and ITCH (PubMed:19881509). Interacts with CYLD
(PubMed:18636086). Interacts with SRC (PubMed:19419966). Interacts
with DHX58/LGP2 and IKBKE (PubMed:16177806, PubMed:17020950,
PubMed:28011935). Interacts with TMEM173/STING (PubMed:19416887).
Interacts with IFIT3 (via N-terminus) (PubMed:21813773). Interacts
with TBK1 only in the presence of IFIT3 (PubMed:21813773,
PubMed:28011935). Interacts with TTLL12; the interaction prevents
MAVS binding to TBK1 and IKBKE (PubMed:28011935). Interacts with
MUL1 (PubMed:23399697). Interacts with ANKRD17 (PubMed:23711367).
Interacts with NDFIP1 (PubMed:23087404). Interacts with SMURF1;
the interaction is mediated by NDFIP1 and leads to MAVS
ubiquitination and degradation (PubMed:23087404). Interacts with
UBXN1; this interaction inhibits MAVS-mediated antiviral pathway
(PubMed:23545497). Interacts (via C-terminus) with GPATCH3; the
interaction is markedly increased upon viral infection
(PubMed:28414768). Directly interacts (via CARD domain) with ATG5
and ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5
conjugates (PubMed:17709747). Interacts with DHX33 (via the
helicase C-terminal domain) (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q8VCF0, ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868,
ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:17020950,
ECO:0000269|PubMed:17600090, ECO:0000269|PubMed:17709747,
ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18636086,
ECO:0000269|PubMed:19164550, ECO:0000269|PubMed:19416887,
ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:19734229,
ECO:0000269|PubMed:19881509, ECO:0000269|PubMed:21813773,
ECO:0000269|PubMed:23087404, ECO:0000269|PubMed:23399697,
ECO:0000269|PubMed:23545497, ECO:0000269|PubMed:23711367,
ECO:0000269|PubMed:24569476, ECO:0000269|PubMed:25018021,
ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27302953,
ECO:0000269|PubMed:28011935, ECO:0000269|PubMed:28414768}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis C/HCV
NS3/4A protease; this interaction leads to MAVS cleavage.
{ECO:0000269|PubMed:16301520}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis GB virus B
NS3/4A protease; this interaction leads to MAVS cleavage.
{ECO:0000269|PubMed:17093192}.
-!- SUBUNIT: (Microbial infection) Interacts with human respiratory
syncytial virus/HRSV protein NS1; this interaction disrupts MAVS
binding to DDX58/RIG-I. {ECO:0000269|PubMed:22383950}.
-!- SUBUNIT: (Microbial infection) Interacts with Seneca Valley virus
protease 3C; this interaction allows the cleavage of MAVS and
subsequent suppression of host innate immunity.
{ECO:0000269|PubMed:28566380}.
-!- INTERACTION:
A2T3M4:- (xeno); NbExp=4; IntAct=EBI-995373, EBI-9522123;
P00519:ABL1; NbExp=6; IntAct=EBI-995373, EBI-375543;
Q9H1Y0:ATG5; NbExp=4; IntAct=EBI-15577799, EBI-1047414;
P46379:BAG6; NbExp=2; IntAct=EBI-995373, EBI-347552;
Q07021:C1QBP; NbExp=5; IntAct=EBI-995373, EBI-347528;
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-995373, EBI-739580;
O00571:DDX3X; NbExp=4; IntAct=EBI-995373, EBI-353779;
O95786:DDX58; NbExp=13; IntAct=EBI-995373, EBI-995350;
O95786-1:DDX58; NbExp=8; IntAct=EBI-15577799, EBI-15577823;
Q9BYX4:IFIH1; NbExp=5; IntAct=EBI-995373, EBI-6115771;
Q14164:IKBKE; NbExp=4; IntAct=EBI-995373, EBI-307369;
Q13568:IRF5; NbExp=2; IntAct=EBI-995373, EBI-3931258;
Q9Y2W7:KCNIP3; NbExp=3; IntAct=EBI-995373, EBI-751501;
Q6WB96:M2 (xeno); NbExp=4; IntAct=EBI-995373, EBI-6863628;
Q8IWA4:MFN1; NbExp=2; IntAct=EBI-995373, EBI-1048197;
Q96P20:NLRP3; NbExp=4; IntAct=EBI-995373, EBI-6253230;
Q91WS2-1:Nlrp6 (xeno); NbExp=2; IntAct=EBI-15577799, EBI-16182226;
Q86UT6-1:NLRX1; NbExp=3; IntAct=EBI-15577799, EBI-15680006;
Q9Y6K5:OAS3; NbExp=2; IntAct=EBI-995373, EBI-6115729;
O43353:RIPK2; NbExp=3; IntAct=EBI-995373, EBI-358522;
Q96EQ8:RNF125; NbExp=2; IntAct=EBI-15577799, EBI-2339208;
P42224:STAT1; NbExp=3; IntAct=EBI-995373, EBI-1057697;
Q9UHD2:TBK1; NbExp=2; IntAct=EBI-995373, EBI-356402;
Q86WV6:TMEM173; NbExp=7; IntAct=EBI-995373, EBI-2800345;
Q12933:TRAF2; NbExp=4; IntAct=EBI-995373, EBI-355744;
Q9Y4K3:TRAF6; NbExp=4; IntAct=EBI-995373, EBI-359276;
Q14139:UBE4A; NbExp=2; IntAct=EBI-995373, EBI-1048119;
P61964:WDR5; NbExp=3; IntAct=EBI-15577799, EBI-540834;
Q69027:X (xeno); NbExp=2; IntAct=EBI-995373, EBI-3650820;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:16125763}. Mitochondrion
{ECO:0000269|PubMed:11780052, ECO:0000269|PubMed:17709747}.
Peroxisome {ECO:0000269|PubMed:20451243}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q7Z434-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z434-2; Sequence=VSP_010262, VSP_010263;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q7Z434-3; Sequence=VSP_010261, VSP_010264;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q7Z434-4; Sequence=VSP_045872;
Note=No experimental confirmation available.;
Name=5; Synonyms=MAVS1b, exon 3 deletion;
IsoId=Q7Z434-5; Sequence=VSP_047817, VSP_047818;
Note=Selectively activates an IFNbeta but not an IL8 promoter.
Interacts with RIP1 and FADD and exhibits anti-viral activity
against VSV infection.;
Name=6; Synonyms=MAVS1a, exon 2 deletion;
IsoId=Q7Z434-6; Sequence=VSP_047816, VSP_010263;
-!- TISSUE SPECIFICITY: Present in T-cells, monocytes, epithelial
cells and hepatocytes (at protein level). Ubiquitously expressed,
with highest levels in heart, skeletal muscle, liver, placenta and
peripheral blood leukocytes. {ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868}.
-!- DOMAIN: The pLxIS motif constitutes an IRF3-binding motif:
following phosphorylation by TBK1, the phosphorylated pLxIS motif
of MAVS recruits IRF3 (PubMed:25636800). IRF3 is then
phosphorylated and activated by TBK1 to induce type-I interferons
and other cytokines (PubMed:25636800).
{ECO:0000269|PubMed:25636800}.
-!- DOMAIN: Both CARD and transmembrane domains are essential for
antiviral function. The CARD domain is responsible for interaction
with DDX58/RIG-I and IFIH1/MDA5. {ECO:0000269|PubMed:16125763}.
-!- DOMAIN: The transmembrane domain and residues 300-444 are
essential for its interaction with DHX58/LGP2.
{ECO:0000269|PubMed:17020950}.
-!- PTM: Following activation, phosphorylated by TBK1 at Ser-442 in
the pLxIS motif (PubMed:25636800, PubMed:27302953). The
phosphorylated pLxIS motif constitutes an IRF3-binding motif,
leading to recruitment of the transcription factor IRF3 to induce
type-I interferons and other cytokines (PubMed:25636800).
{ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27302953}.
-!- PTM: (Microbial infection) Cleaved and degraded by hepatitis A
virus (HAV) protein 3ABC allowing the virus to disrupt the
activation of host IRF3 through the MDA5 pathway.
{ECO:0000269|PubMed:17438296}.
-!- PTM: (Microbial infection) Cleaved by the protease 2A of
coxsackievirus B3, poliovirus and enterovirus 71 allowing the
virus to disrupt the host type I interferon production.
{ECO:0000269|PubMed:24390337, ECO:0000269|PubMed:28253362}.
-!- PTM: Ubiquitinated (PubMed:19881509, PubMed:23087404,
PubMed:25636800). Undergoes 'Lys-48'-linked polyubiquitination
catalyzed by ITCH; ITCH-dependent polyubiquitination is mediated
by the interaction with PCBP2 and leads to MAVS/IPS1 proteasomal
degradation (PubMed:19881509). Ubiquitinated by RNF125, leading to
its degradation by the proteasome (PubMed:17460044). Undergoes
'Lys-48'-linked ubiquitination catalyzed by SMURF1
(PubMed:23087404). {ECO:0000269|PubMed:17460044,
ECO:0000269|PubMed:19881509, ECO:0000269|PubMed:23087404,
ECO:0000269|PubMed:25636800}.
-!- PTM: (Microbial infection) Cleaved by Seneca Valley virus protease
3C allowing the virus to suppress interferon type-I production.
{ECO:0000269|PubMed:28566380}.
-!- MISCELLANEOUS: Cleavage by HCV protease complex leads to
inactivation.
-!- SEQUENCE CAUTION:
Sequence=BAA86585.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
Sequence=BAB14684.1; Type=Frameshift; Evidence={ECO:0000305};
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EMBL; DQ174270; AAZ80417.1; -; mRNA.
EMBL; DQ167126; ABA54890.1; -; mRNA.
EMBL; DQ181928; ABA19229.1; -; mRNA.
EMBL; AB232371; BAE79738.1; -; mRNA.
EMBL; EF467323; ABR24161.1; -; mRNA.
EMBL; EF467324; ABR24162.1; -; mRNA.
EMBL; KC415005; AGF94754.1; -; mRNA.
EMBL; AB033097; BAA86585.1; ALT_INIT; mRNA.
EMBL; AB097003; BAC77356.1; -; mRNA.
EMBL; AK023799; BAB14684.1; ALT_FRAME; mRNA.
EMBL; AK123956; BAC85734.1; -; mRNA.
EMBL; AK130992; BAC85473.1; -; mRNA.
EMBL; AK291785; BAF84474.1; -; mRNA.
EMBL; AK296897; BAG59455.1; -; mRNA.
EMBL; AL109804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL353194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471133; EAX10481.1; -; Genomic_DNA.
EMBL; BC044952; AAH44952.1; -; mRNA.
CCDS; CCDS33437.1; -. [Q7Z434-1]
CCDS; CCDS56176.1; -. [Q7Z434-4]
RefSeq; NP_001193420.1; NM_001206491.1. [Q7Z434-4]
RefSeq; NP_065797.2; NM_020746.4. [Q7Z434-1]
PDB; 2MS7; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U=1-100.
PDB; 2MS8; NMR; -; A=1-100.
PDB; 2VGQ; X-ray; 2.10 A; A=1-93.
PDB; 3J6C; EM; 9.60 A; A=3-93.
PDB; 3J6J; EM; 3.64 A; A/B/C/D/E/G/I/L=1-97.
PDB; 3RC5; X-ray; 1.60 A; B=502-508.
PDB; 4P4H; X-ray; 3.40 A; I/J/K/L/M/N/O/P=1-99.
PDB; 4Z8M; X-ray; 2.95 A; C/D=450-468.
PDB; 5JEK; X-ray; 2.40 A; C/D=433-448.
PDBsum; 2MS7; -.
PDBsum; 2MS8; -.
PDBsum; 2VGQ; -.
PDBsum; 3J6C; -.
PDBsum; 3J6J; -.
PDBsum; 3RC5; -.
PDBsum; 4P4H; -.
PDBsum; 4Z8M; -.
PDBsum; 5JEK; -.
SMR; Q7Z434; -.
BioGrid; 121570; 121.
DIP; DIP-35445N; -.
IntAct; Q7Z434; 76.
MINT; Q7Z434; -.
STRING; 9606.ENSP00000401980; -.
iPTMnet; Q7Z434; -.
PhosphoSitePlus; Q7Z434; -.
SwissPalm; Q7Z434; -.
BioMuta; MAVS; -.
DMDM; 47115748; -.
CPTAC; CPTAC-977; -.
EPD; Q7Z434; -.
jPOST; Q7Z434; -.
MassIVE; Q7Z434; -.
MaxQB; Q7Z434; -.
PaxDb; Q7Z434; -.
PeptideAtlas; Q7Z434; -.
PRIDE; Q7Z434; -.
ProteomicsDB; 27148; -.
ProteomicsDB; 3402; -.
ProteomicsDB; 69137; -. [Q7Z434-1]
ProteomicsDB; 69138; -. [Q7Z434-2]
ProteomicsDB; 69139; -. [Q7Z434-3]
DNASU; 57506; -.
Ensembl; ENST00000416600; ENSP00000413749; ENSG00000088888. [Q7Z434-4]
Ensembl; ENST00000428216; ENSP00000401980; ENSG00000088888. [Q7Z434-1]
GeneID; 57506; -.
KEGG; hsa:57506; -.
UCSC; uc002wjw.5; human. [Q7Z434-1]
CTD; 57506; -.
DisGeNET; 57506; -.
GeneCards; MAVS; -.
HGNC; HGNC:29233; MAVS.
HPA; CAB009187; -.
HPA; HPA049850; -.
HPA; HPA053524; -.
MIM; 609676; gene.
neXtProt; NX_Q7Z434; -.
OpenTargets; ENSG00000088888; -.
PharmGKB; PA164722208; -.
eggNOG; ENOG410IS5U; Eukaryota.
eggNOG; ENOG410Y2HK; LUCA.
GeneTree; ENSGT00510000049120; -.
HOGENOM; HOG000056441; -.
InParanoid; Q7Z434; -.
KO; K12648; -.
OMA; HNGYREE; -.
OrthoDB; 887440at2759; -.
PhylomeDB; Q7Z434; -.
TreeFam; TF333444; -.
Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
SignaLink; Q7Z434; -.
SIGNOR; Q7Z434; -.
ChiTaRS; MAVS; human.
EvolutionaryTrace; Q7Z434; -.
GeneWiki; VISA_(gene); -.
GenomeRNAi; 57506; -.
Pharos; Q7Z434; -.
PMAP-CutDB; Q7Z434; -.
PRO; PR:Q7Z434; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000088888; Expressed in 229 organ(s), highest expression level in caecum.
Genevisible; Q7Z434; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
GO; GO:0050700; F:CARD domain binding; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0035591; F:signaling adaptor activity; IMP:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; IMP:BHF-UCL.
GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; IDA:BHF-UCL.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:BHF-UCL.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:BHF-UCL.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; IMP:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:BHF-UCL.
GO; GO:0035549; P:positive regulation of interferon-beta secretion; IMP:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:0071660; P:positive regulation of IP-10 production; IDA:BHF-UCL.
GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IMP:UniProtKB.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:UniProtKB.
GO; GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd08811; CARD_IPS1; 1.
InterPro; IPR031964; CARD_dom.
InterPro; IPR042144; CARD_IPS1.
InterPro; IPR026148; Mt_antiviral_sig_pro_met.
PANTHER; PTHR21446:SF6; PTHR21446:SF6; 1.
Pfam; PF16739; CARD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiviral defense;
Complete proteome; Host-virus interaction; Immunity; Innate immunity;
Membrane; Methylation; Mitochondrion; Mitochondrion outer membrane;
Peroxisome; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 540 Mitochondrial antiviral-signaling
protein.
/FTId=PRO_0000144096.
TOPO_DOM 1 513 Cytoplasmic. {ECO:0000305}.
TRANSMEM 514 534 Helical. {ECO:0000255}.
TOPO_DOM 535 540 Mitochondrial intermembrane.
{ECO:0000305}.
DOMAIN 10 77 CARD.
REGION 10 77 Required for interaction with NLRX1.
{ECO:0000269|PubMed:18200010}.
REGION 143 147 Interaction with TRAF2.
{ECO:0000269|PubMed:16153868}.
REGION 153 158 Interaction with TRAF6.
REGION 455 460 Interaction with TRAF6.
MOTIF 439 442 pLxIS motif.
{ECO:0000269|PubMed:25636800}.
COMPBIAS 103 153 Pro-rich.
SITE 148 149 (Microbial infection) Cleavage; by viral
Seneca Valley virus protease 3C.
{ECO:0000269|PubMed:28566380}.
SITE 148 148 (Microbial infection) Cleavage by CV3B.
{ECO:0000269|PubMed:21436888}.
SITE 208 209 (Microbial infection) Cleavage by
protease 2A of enterovirus 71.
{ECO:0000269|PubMed:28253362}.
SITE 250 251 (Microbial infection) Cleavage by
protease 2A of enterovirus 71.
{ECO:0000269|PubMed:28253362}.
SITE 264 265 (Microbial infection) Cleavage by
protease 2A of enterovirus 71.
{ECO:0000269|PubMed:28253362}.
SITE 427 428 Cleavage; by HAV protein 3ABC.
{ECO:0000269|PubMed:17438296}.
SITE 508 509 Cleavage; by HCV and hepatitis GB virus B
NS3/4A protease complex.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 180 180 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 215 215 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 233 233 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 234 234 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 236 236 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8VCF0}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VCF0}.
MOD_RES 442 442 Phosphoserine; by TBK1.
{ECO:0000269|PubMed:25636800,
ECO:0000269|PubMed:27302953}.
VAR_SEQ 1 141 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045872.
VAR_SEQ 40 131 DRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCE
LVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAERPGPPT
PAAAHSIPYN -> GPRTVPQTHWSHRHFLLRGQGPPHLLR
PTASPTTAAERRSQVTPCLSRRPRRQSPQERIQSKPCRRSA
PEPSQGIQMVAPWSPPLTWQPSAL (in isoform 6).
{ECO:0000303|PubMed:18207245}.
/FTId=VSP_047816.
VAR_SEQ 64 148 RRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPP
DPLEPPSLPAERPGPPTPAAAHSIPYNSCREKEPSYPMPVQ
ETQ -> LPTWAGEETPGGQSSGRGLDFSSLTSGAVWLWQM
SDFWSCFSTWTVSIWLILHWVLLRLNLQVFAKCLAQSKWPL
LLPSLSCPTW (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010261.
VAR_SEQ 98 124 RTSDRPPDPLEPPSLPAERPGPPTPAA -> QFRASPADAQ
PQSHPKESRWWPPGVLL (in isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18207245}.
/FTId=VSP_047817.
VAR_SEQ 99 131 TSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYN -> ERPA
LALLDPQPAPWPPLSFSLSLYFLPFSVILFLVTVKR (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010262.
VAR_SEQ 125 540 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18207245}.
/FTId=VSP_047818.
VAR_SEQ 132 540 Missing (in isoform 2 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18207245}.
/FTId=VSP_010263.
VAR_SEQ 149 540 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010264.
VARIANT 79 79 C -> F (in dbSNP:rs11905552).
/FTId=VAR_048609.
VARIANT 79 79 C -> S (in dbSNP:rs11908032).
/FTId=VAR_059197.
VARIANT 93 93 Q -> E (in dbSNP:rs17857295).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16127453,
ECO:0000269|PubMed:16153868}.
/FTId=VAR_048610.
VARIANT 198 198 Q -> K (in dbSNP:rs7262903).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:16177806}.
/FTId=VAR_048611.
VARIANT 409 409 S -> F (in dbSNP:rs7269320).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:16177806}.
/FTId=VAR_018448.
MUTAGEN 26 26 E->A,R: Impairs filament formation and
abolishes antiviral signaling activity.
{ECO:0000269|PubMed:24569476}.
MUTAGEN 54 54 T->A: Impairs ability to induce IFN-beta.
Loss of interaction with the ATG5-ATG12
conjugate. {ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:17709747}.
MUTAGEN 56 56 W->A,E,R: Impairs filament formation and
abolishes antiviral signaling activity.
{ECO:0000269|PubMed:24569476}.
MUTAGEN 67 69 GWV->AAA: Impairs ability to induce IFN-
beta. {ECO:0000269|PubMed:16125763}.
MUTAGEN 145 145 Q->N: No interaction with TRAF2.
{ECO:0000269|PubMed:16153868}.
MUTAGEN 148 148 Q->A: Complete loss of cleavage by Seneca
Valley virus protease 3C.
{ECO:0000269|PubMed:28566380}.
MUTAGEN 155 155 E->D: No interaction with TRAF6; when
associated with D-457.
{ECO:0000269|PubMed:16153868}.
MUTAGEN 159 159 Q->A: No effect on cleavage by Seneca
Valley virus protease 3C.
{ECO:0000269|PubMed:28566380}.
MUTAGEN 162 162 Q->A: No effect on cleavage by Seneca
Valley virus protease 3C.
{ECO:0000269|PubMed:28566380}.
MUTAGEN 196 196 Q->A: No effect on cleavage by Seneca
Valley virus protease 3C.
{ECO:0000269|PubMed:28566380}.
MUTAGEN 198 198 Q->A: No effect on cleavage by Seneca
Valley virus protease 3C.
{ECO:0000269|PubMed:28566380}.
MUTAGEN 209 209 G->A: Complete loss of cleavage by
protease 2A of enterovirus 71.
{ECO:0000269|PubMed:28253362}.
MUTAGEN 251 251 G->A: Complete loss of cleavage by
protease 2A of enterovirus 71.
{ECO:0000269|PubMed:28253362}.
MUTAGEN 265 265 G->A: Complete loss of cleavage by
enterovirus 71.
{ECO:0000269|PubMed:28253362}.
MUTAGEN 427 427 Q->A: No cleavage by HHAV 3ABC.
{ECO:0000269|PubMed:17438296}.
MUTAGEN 435 435 C->R: No effect on cleavage by NS3/4A
protease complex.
{ECO:0000269|PubMed:16301520}.
MUTAGEN 442 442 S->A: Abolished ability to bind and
activate IRF3.
{ECO:0000269|PubMed:25636800,
ECO:0000269|PubMed:27302953}.
MUTAGEN 452 452 C->R: No effect on cleavage by NS3/4A
protease complex.
{ECO:0000269|PubMed:16301520}.
MUTAGEN 457 457 E->D: No interaction with TRAF6; when
associated with D-155.
{ECO:0000269|PubMed:16153868}.
MUTAGEN 463 463 E->A: No effect on cleavage by HHAV 3ABC.
{ECO:0000269|PubMed:17438296}.
MUTAGEN 508 508 C->A,R: No cleavage by HCV and hepatitis
GB virus B NS3/4A protease complex.
{ECO:0000269|PubMed:16177806,
ECO:0000269|PubMed:16301520,
ECO:0000269|PubMed:17093192}.
CONFLICT 42 42 L -> P (in Ref. 8; BAC77356).
{ECO:0000305}.
CONFLICT 191 191 T -> N (in Ref. 9; BAF84474).
{ECO:0000305}.
CONFLICT 356 356 A -> V (in Ref. 8; BAC77356).
{ECO:0000305}.
CONFLICT 373 373 S -> P (in Ref. 8; BAC77356).
{ECO:0000305}.
HELIX 3 14 {ECO:0000244|PDB:2VGQ}.
HELIX 16 19 {ECO:0000244|PDB:2VGQ}.
HELIX 24 27 {ECO:0000244|PDB:2VGQ}.
HELIX 28 30 {ECO:0000244|PDB:2VGQ}.
HELIX 36 49 {ECO:0000244|PDB:2VGQ}.
HELIX 51 62 {ECO:0000244|PDB:2VGQ}.
HELIX 68 78 {ECO:0000244|PDB:2VGQ}.
HELIX 82 92 {ECO:0000244|PDB:2VGQ}.
STRAND 95 97 {ECO:0000244|PDB:2MS8}.
STRAND 456 459 {ECO:0000244|PDB:4Z8M}.
STRAND 504 507 {ECO:0000244|PDB:3RC5}.
SEQUENCE 540 AA; 56528 MW; 0E23E3E115941EE8 CRC64;
MPFAEDKTYK YICRNFSNFC NVDVVEILPY LPCLTARDQD RLRATCTLSG NRDTLWHLFN
TLQRRPGWVE YFIAALRGCE LVDLADEVAS VYQSYQPRTS DRPPDPLEPP SLPAERPGPP
TPAAAHSIPY NSCREKEPSY PMPVQETQAP ESPGENSEQA LQTLSPRAIP RNPDGGPLES
SSDLAALSPL TSSGHQEQDT ELGSTHTAGA TSSLTPSRGP VSPSVSFQPL ARSTPRASRL
PGPTGSVVST GTSFSSSSPG LASAGAAEGK QGAESDQAEP IICSSGAEAP ANSLPSKVPT
TLMPVNTVAL KVPANPASVS TVPSKLPTSS KPPGAVPSNA LTNPAPSKLP INSTRAGMVP
SKVPTSMVLT KVSASTVPTD GSSRNEETPA APTPAGATGG SSAWLDSSSE NRGLGSELSK
PGVLASQVDS PFSGCFEDLA ISASTSLGMG PCHGPEENEY KSEGTFGIHV AENPSIQLLE
GNPGPPADPD GGPRPQADRK FQEREVPCHR PSPGALWLQV AVTGVLVVTL LVVLYRRRLH


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[MAVS IPS1 KIAA1271 VISA] Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Putative NF-kappa-B-activating protein 031N) (Virus-induced-signaling adapter) (VISA)
[Mavs Ips1 Visa] Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Virus-induced-signaling adapter) (VISA)
[Mavs Ips1 Visa] Mitochondrial antiviral-signaling protein (MAVS) (Interferon beta promoter stimulator protein 1) (IPS-1) (Virus-induced-signaling adapter) (VISA)
[TICAM1 PRVTIRB TRIF] TIR domain-containing adapter molecule 1 (TICAM-1) (Proline-rich, vinculin and TIR domain-containing protein B) (Putative NF-kappa-B-activating protein 502H) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (MyD88-3) (TIR domain-containing adapter protein inducing IFN-beta)
[IFIH1 MDA5 RH116] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Clinically amyopathic dermatomyositis autoantigen 140 kDa) (CADM-140 autoantigen) (Helicase with 2 CARD domains) (Helicard) (Interferon-induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (Murabutide down-regulated protein) (RIG-I-like receptor 2) (RLR-2) (RNA helicase-DEAD box protein 116)
[Ticam1 Trif] TIR domain-containing adapter molecule 1 (TICAM-1) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (TIR domain-containing adapter protein inducing IFN-beta)
[IKBKB IKKB] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[TBK1 NAK] Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (NF-kappa-B-activating kinase) (T2K) (TANK-binding kinase 1)
[IKBKE IKKE IKKI KIAA0151] Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i)
[CHUK IKKA TCF16] Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA) (Transcription factor 16) (TCF-16)
[TMEM173 ERIS MITA STING] Stimulator of interferon genes protein (hSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (hMITA) (Transmembrane protein 173)
[TICAM2 TIRAP3 TIRP TRAM] TIR domain-containing adapter molecule 2 (TICAM-2) (Putative NF-kappa-B-activating protein 502) (TRIF-related adapter molecule) (Toll-like receptor adaptor protein 3) (Toll/interleukin-1 receptor domain-containing protein) (MyD88-4)
[BCL10 CIPER CLAP] B-cell lymphoma/leukemia 10 (B-cell CLL/lymphoma 10) (Bcl-10) (CARD-containing molecule enhancing NF-kappa-B) (CARD-like apoptotic protein) (hCLAP) (CED-3/ICH-1 prodomain homologous E10-like regulator) (CIPER) (Cellular homolog of vCARMEN) (cCARMEN) (Cellular-E10) (c-E10) (Mammalian CARD-containing adapter molecule E10) (mE10)
[Ifih1] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Helicase with 2 CARD domains) (Helicard) (Interferon induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (RIG-I-like receptor 2) (RLR-2)
[AZI2 NAP1 TBKBP2] 5-azacytidine-induced protein 2 (NF-kappa-B-activating kinase-associated protein 1) (Nak-associated protein 1) (TILP)
[Tmem173 Eris Mita Mpys Sting] Stimulator of interferon genes protein (mSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (MMITA) (Transmembrane protein 173)
[DDX58] Probable ATP-dependent RNA helicase DDX58 (EC 3.6.4.13) (DEAD box protein 58) (RIG-I-like receptor 1) (RLR-1) (Retinoic acid-inducible gene 1 protein) (RIG-1) (Retinoic acid-inducible gene I protein) (RIG-I)
[Azi2 Az2 Nap1 Tbkp2] 5-azacytidine-induced protein 2 (NF-kappa-B-activating kinase-associated protein 1) (Nak-associated protein 1)
[EIF2AK2 PKR PRKR] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[Ikbkb Ikkb] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[Ikbkb Ikkb] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[Chuk Ikka] Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[PYCARD ASC CARD5 TMS1] Apoptosis-associated speck-like protein containing a CARD (hASC) (Caspase recruitment domain-containing protein 5) (PYD and CARD domain-containing protein) (Target of methylation-induced silencing 1)
[TRAF6 RNF85] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6)
[IKBKG FIP3 NEMO] NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[Ikbke Ikke Ikki] Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i)
[IRF3] Interferon regulatory factor 3 (IRF-3)
[IFI27] Interferon alpha-inducible protein 27, mitochondrial (p27) (Interferon alpha-induced 11.5 kDa protein) (Interferon-stimulated gene 12a protein) (ISG12(a)) (ISG12A)

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