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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_MOUSE              Reviewed;         503 AA.
Q8VCF0;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
16-OCT-2019, entry version 153.
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 {ECO:0000303|PubMed:24037184};
AltName: Full=Virus-induced-signaling adapter;
Short=VISA {ECO:0000303|PubMed:24037184};
Name=Mavs {ECO:0000312|MGI:MGI:2444773};
Synonyms=Ips1 {ECO:0000303|PubMed:24037184},
Visa {ECO:0000303|PubMed:24037184};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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].
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].
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 [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Eye, Liver, and Salivary gland;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-384, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
INTERACTION WITH TRAFD1.
PubMed=18849341; DOI=10.1074/jbc.m806923200;
Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T.,
Yoshimura A.;
"FLN29 deficiency reveals its negative regulatory role in the Toll-
like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like
helicase signaling pathway.";
J. Biol. Chem. 283:33858-33864(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-172 AND
SER-384, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
INTERACTION WITH 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).
[10]
FUNCTION, AND INTERACTION WITH DHX33.
PubMed=24037184; DOI=10.1038/cmi.2013.40;
Liu Y., Lu N., Yuan B., Weng L., Wang F., Liu Y.J., Zhang Z.;
"The interaction between the helicase DHX33 and IPS-1 as a novel
pathway to sense double-stranded RNA and RNA viruses in myeloid
dendritic cells.";
Cell. Mol. Immunol. 11:49-57(2014).
[11]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-234, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Required for innate immune defense against viruses
(PubMed:24037184). 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:24037184). Peroxisomal and mitochondrial MAVS act
sequentially to create an antiviral cellular state (By
similarity). 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
(By similarity). May activate the same pathways following
detection of extracellular dsRNA by TLR3 (By similarity). May
protect cells from apoptosis (By similarity).
{ECO:0000250|UniProtKB:Q7Z434, ECO:0000269|PubMed:24037184}.
-!- 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 (By
similarity). Interacts with DDX58/RIG-I, IFIH1/MDA5, TRAF2, TRAF6
and C1QBP (By similarity). May interact with FADD, RIPK1, IKBKE,
CHUK and IKBKB (By similarity). Interacts (when phosphorylated)
with IRF3; following activation and phosphorylation on the pLxIS
motif by TBK1, recruits IRF3 (By similarity). Interacts with NLRX1
(By similarity). Interaction with NLRX1 requires the CARD domain
(By similarity). Interacts with PSMA7 (By similarity). Interacts
with TRAFD1 (PubMed:18849341). Interacts (via C-terminus) with
PCBP2 in a complex containing MAVS/IPS1, PCBP2 and ITCH (By
similarity). Interacts with CYLD (By similarity). Interacts with
SRC (By similarity). Interacts with DHX58/LGP2 and IKBKE (By
similarity). Interacts with TMEM173/STING (By similarity).
Interacts with IFIT3 (via N-terminus) (By similarity). Interacts
with TBK1 only in the presence of IFIT3 (By similarity). Interacts
with TTLL12; the interaction prevents MAVS binding to TBK1 and
IKBKE (By similarity). Interacts with MUL1 (By similarity).
Interacts with ANKRD17 (By similarity). Interacts with NDFIP1 (By
similarity). Interacts with SMURF1; the interaction is mediated by
NDFIP1 and leads to MAVS ubiquitination and degradation
(PubMed:23087404). Interacts (via C-terminus) with GPATCH3; the
interaction is markedly increased upon viral infection (By
similarity). Directly interacts (via CARD domain) with ATG5 and
ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5
conjugates (By similarity). Interacts with DHX33 (via the helicase
C-terminal domain) (PubMed:24037184).
{ECO:0000250|UniProtKB:Q7Z434, ECO:0000269|PubMed:18849341,
ECO:0000269|PubMed:23087404, ECO:0000269|PubMed:24037184}.
-!- INTERACTION:
Q60803:Traf3; NbExp=4; IntAct=EBI-3862816, EBI-520135;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000250|UniProtKB:Q7Z434}. Mitochondrion
{ECO:0000250|UniProtKB:Q7Z434}. Peroxisome
{ECO:0000250|UniProtKB:Q7Z434}.
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:Q7Z434}.
-!- DOMAIN: The transmembrane domain and residues 285-420 are
essential for its interaction with DHX58/LGP2.
{ECO:0000250|UniProtKB:Q7Z434}.
-!- DOMAIN: The pLxIS motif constitutes an IRF3-binding motif:
following phosphorylation by TBK1, the phosphorylated pLxIS motif
of MAVS recruits IRF3. IRF3 is then phosphorylated and activated
by TBK1 to induce type-I interferons and other cytokines.
{ECO:0000250|UniProtKB:Q7Z434}.
-!- 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:0000250|UniProtKB:Q7Z434}.
-!- DOMAIN: The transmembrane domain and residues 300-444 are
essential for its interaction with DHX58/LGP2.
{ECO:0000250|UniProtKB:Q7Z434}.
-!- PTM: Following activation, phosphorylated by TBK1 at Ser-418 in
the pLxIS motif. 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.
{ECO:0000250|UniProtKB:Q7Z434}.
-!- PTM: Ubiquitinated. 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. Ubiquitinated by RNF125, leading to its degradation
by the proteasome. Undergoes 'Lys-48'-linked ubiquitination
catalyzed by SMURF1. {ECO:0000250|UniProtKB:Q7Z434}.
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EMBL; DQ174271; AAZ80418.1; -; mRNA.
EMBL; DQ167127; ABA54891.1; -; mRNA.
EMBL; AK028421; BAC25940.1; -; mRNA.
EMBL; BC020006; AAH20006.1; -; mRNA.
EMBL; BC025825; AAH25825.1; -; mRNA.
EMBL; BC031352; AAH31352.1; -; mRNA.
EMBL; BC037391; AAH37391.1; -; mRNA.
CCDS; CCDS16760.1; -.
RefSeq; NP_001193314.1; NM_001206385.1.
RefSeq; NP_659137.1; NM_144888.2.
PDB; 4GHU; X-ray; 2.20 A; B=138-158.
PDBsum; 4GHU; -.
SMR; Q8VCF0; -.
BioGrid; 230748; 12.
DIP; DIP-43890N; -.
IntAct; Q8VCF0; 6.
MINT; Q8VCF0; -.
STRING; 10090.ENSMUSP00000105828; -.
iPTMnet; Q8VCF0; -.
PhosphoSitePlus; Q8VCF0; -.
SwissPalm; Q8VCF0; -.
EPD; Q8VCF0; -.
jPOST; Q8VCF0; -.
MaxQB; Q8VCF0; -.
PaxDb; Q8VCF0; -.
PeptideAtlas; Q8VCF0; -.
PRIDE; Q8VCF0; -.
Ensembl; ENSMUST00000041362; ENSMUSP00000038339; ENSMUSG00000037523.
Ensembl; ENSMUST00000110199; ENSMUSP00000105828; ENSMUSG00000037523.
GeneID; 228607; -.
KEGG; mmu:228607; -.
UCSC; uc008mld.2; mouse.
CTD; 57506; -.
MGI; MGI:2444773; Mavs.
eggNOG; ENOG410IS5U; Eukaryota.
eggNOG; ENOG410Y2HK; LUCA.
GeneTree; ENSGT00510000049120; -.
HOGENOM; HOG000231697; -.
InParanoid; Q8VCF0; -.
KO; K12648; -.
OMA; HNGYREE; -.
OrthoDB; 887440at2759; -.
PhylomeDB; Q8VCF0; -.
TreeFam; TF333444; -.
Reactome; R-MMU-936440; Negative regulators of DDX58/IFIH1 signaling.
ChiTaRS; Mavs; mouse.
PRO; PR:Q8VCF0; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000037523; Expressed in 261 organ(s), highest expression level in brown adipose tissue.
ExpressionAtlas; Q8VCF0; baseline and differential.
Genevisible; Q8VCF0; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0050700; F:CARD domain binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0035591; F:signaling adaptor activity; IMP:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; ISO:MGI.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:MGI.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; ISS:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
GO; GO:0035549; P:positive regulation of interferon-beta secretion; ISS:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
GO; GO:0071660; P:positive regulation of IP-10 production; ISO:MGI.
GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; IMP:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISS:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; IMP:MGI.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISO:MGI.
GO; GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB.
GO; GO:0039529; P:RIG-I signaling pathway; IGI:MGI.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
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; Antiviral defense; Complete proteome; Immunity;
Innate immunity; Membrane; Methylation; Mitochondrion;
Mitochondrion outer membrane; Peroxisome; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1 503 Mitochondrial antiviral-signaling
protein.
/FTId=PRO_0000144097.
TOPO_DOM 1 478 Cytoplasmic. {ECO:0000305}.
TRANSMEM 479 496 Helical. {ECO:0000255}.
TOPO_DOM 497 503 Mitochondrial intermembrane.
{ECO:0000305}.
DOMAIN 10 77 CARD.
REGION 10 77 Required for interaction with NLRX1.
{ECO:0000250|UniProtKB:Q7Z434}.
REGION 143 147 Interaction with TRAF2.
{ECO:0000250|UniProtKB:Q7Z434}.
REGION 153 158 Interaction with TRAF6 1.
{ECO:0000250|UniProtKB:Q7Z434}.
REGION 337 503 Interaction with DHX33.
{ECO:0000269|PubMed:24037184}.
REGION 431 436 Interaction with TRAF6 2.
{ECO:0000250|UniProtKB:Q7Z434}.
MOTIF 415 418 pLxIS motif.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 234 234 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 251 251 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 418 418 Phosphoserine; by TBK1.
{ECO:0000250|UniProtKB:Q7Z434}.
SEQUENCE 503 AA; 53399 MW; FE4CA1920772BF3E CRC64;
MTFAEDKTYK YIRDNHSKFC CVDVLEILPY LSCLTASDQD RLRASYRQIG NRDTLWGLFN
NLQRRPGWVE VFIRALQICE LPGLADQVTR VYQSYLPPGT SLRSLEPLQL PDFPAAVSGP
SAFAPGHNIP DHGLRETPSC PKPVQDTQPP ESPVENSEQL LQTNSGAVAR MSGGSLIPSP
NQQALSPQPS REHQEQEPEL GGAHAANVAS VPIATYGPVS PTVSFQPLPR TALRTNLLSG
VTVSALSADT SLSSSSTGSA FAKGAGDQAK AATCFSTTLT NSVTTSSVPS PRLVPVKTMS
SKLPLSSKST AAMTSTVLTN TAPSKLPSNS VYAGTVPSRV PASVAKAPAN TIPPERNSKQ
AKETPEGPAT KVTTGGNQTG PNSSIRSLHS GPEMSKPGVL VSQLDEPFSA CSVDLAISPS
SSLVSEPNHG PEENEYSSFR IQVDESPSAD LLGSPEPLAT QQPQEEEEHC ASSMPWAKWL
GATSALLAVF LAVMLYRSRR LAQ


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CSB-EL013526MO Mouse Mitochondrial antiviral-signaling protein(MAVS) ELISA kit 96T
CSB-EL013526RA Rat Mitochondrial antiviral-signaling protein(MAVS) ELISA kit SpeciesRat 96T
CSB-EL013526HU Human Mitochondrial antiviral-signaling protein(MAVS) ELISA kit 96T
CSB-EL013526MO Mouse Mitochondrial antiviral-signaling protein(MAVS) ELISA kit SpeciesMouse 96T
CSB-EL013526HU Human Mitochondrial antiviral-signaling protein(MAVS) ELISA kit SpeciesHuman 96T
EIAAB41675 Bos taurus,Bovine,TICAM1,TICAM-1,TIR domain-containing adapter molecule 1,TIR domain-containing adapter protein inducing IFN-beta,Toll-interleukin-1 receptor domain-containing adapter protein inducing
MAVS_MOUSE ELISA Kit FOR Mitochondrial antiviral-signaling protein; organism: Mouse; gene name: Mavs 96T
CSB-EL013526RA Rat mitochondrial antiviral signaling protein (MAVS) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB41674 Mouse,Mus musculus,Ticam1,TICAM-1,TIR domain-containing adapter molecule 1,TIR domain-containing adapter protein inducing IFN-beta,Toll-interleukin-1 receptor domain-containing adapter protein inducin
4053 (NT) Virus-induced signaling adapter 0.5 mg
Pathways :
WP1835: Interferon alpha/beta signaling
WP1136: Type II interferon signaling (IFNG)
WP2218: sGC
WP1371: G Protein Signaling Pathways
WP1836: Interferon gamma signaling
WP813: G Protein Signaling Pathways
WP1049: G Protein Signaling Pathways
WP35: G Protein Signaling Pathways
WP1566: Citrate cycle (TCA cycle)
WP2272: Pathogenic Escherichia coli infection
WP505: TGF Beta Signaling Pathway
WP786: Type II interferon signaling (IFNG)
WP230: TGF Beta Signaling Pathway
WP1434: Osteopontin Signaling
WP1224: EBV LMP1 signaling
WP1367: TGF-beta Receptor Signaling Pathway
WP232: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1289: Type II interferon signaling (IFNG)
WP809: TGF-beta Receptor Signaling Pathway
WP2203: TSLP Signaling Pathway
WP1370: TGF Beta Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP1048: TGF Beta Signaling Pathway
WP560: TGF Beta Signaling Pathway

Related Genes :
[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)
[TMEM173 ERIS MITA STING] Stimulator of interferon genes protein (hSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (hMITA) (Transmembrane protein 173)
[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)
[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)
[IFI27] Interferon alpha-inducible protein 27, mitochondrial (p27) (Interferon alpha-induced 11.5 kDa protein) (Interferon-stimulated gene 12a protein) (ISG12(a)) (ISG12A)
[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)
[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)
[MX1] Interferon-induced GTP-binding protein Mx1 (Interferon-induced protein p78) (IFI-78K) (Interferon-regulated resistance GTP-binding protein MxA) (Myxoma resistance protein 1) (Myxovirus resistance protein 1) [Cleaved into: Interferon-induced GTP-binding protein Mx1, N-terminally processed]
[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)
[TMEM173 STING] Stimulator of interferon genes protein (poSTING) (Transmembrane protein 173)
[Tmem173 Sting] Stimulator of interferon genes protein (rSTING) (Transmembrane protein 173)
[IFIT1 G10P1 IFI56 IFNAI1 ISG56] Interferon-induced protein with tetratricopeptide repeats 1 (IFIT-1) (Interferon-induced 56 kDa protein) (IFI-56K) (P56)
[TMEM173 STING] Stimulator of interferon genes protein (STING) (Transmembrane protein 173)
[IRF3] Interferon regulatory factor 3 (IRF-3)
[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)
[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)]
[RSAD2 CIG5] Radical S-adenosyl methionine domain-containing protein 2 (Cytomegalovirus-induced gene 5 protein) (Viperin) (Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible)
[ISG15 G1P2 UCRP] Ubiquitin-like protein ISG15 (Interferon-induced 15 kDa protein) (Interferon-induced 17 kDa protein) (IP17) (Ubiquitin cross-reactive protein) (hUCRP)
[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)
[Eif2ak2 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) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2)
[FADD MORT1 GIG3] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Growth-inhibiting gene 3 protein) (Mediator of receptor induced toxicity) (Protein FADD)
[Isg15 G1p2 Ucrp] Ubiquitin-like protein ISG15 (Interferon-induced 15 kDa protein) (Interferon-induced 17 kDa protein) (IP17) (Ubiquitin cross-reactive protein)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

Bibliography :