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Q7Z434 (MAVS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial antiviral-signaling protein

Short name=MAVS
Alternative name(s):
CARD adapter inducing interferon beta
Short name=Cardif
Interferon beta promoter stimulator protein 1
Short name=IPS-1
Putative NF-kappa-B-activating protein 031N
Virus-induced-signaling adapter
Short name=VISA
Gene names
Name:MAVS
Synonyms:IPS1, KIAA1271, VISA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for innate immune defense against viruses. Acts downstream of 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). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state. 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. May activate the same pathways following detection of extracellular dsRNA by TLR3. May protect cells from apoptosis. Ref.1 Ref.2 Ref.3 Ref.4 Ref.23 Ref.30

Subunit structure

Interacts with DDX58/RIG-I, IFIH1/MDA5, TRAF2, TRAF6 and C1QBP. May interact with IRF3, FADD, RIPK1, CHUK and IKBKB. Interacts with and is cleaved by HCV and hepatitis GB virus B NS3/4A proteases. Interacts with and is cleaved by HHAV protein 3ABC. Interacts with NLRX1. Interaction with NLRX1 requires the CARD domain. Interacts with PSMA7. Interacts with TRAFD1 By similarity. Interacts (via C-terminus) with PCBP2 in a complex containing MAVS/IPS1, PCBP2 and ITCH. Interacts with CYLD. Interacts with SRC. Interacts with DHX58/LGP2 and IKBKE. Interacts with TMEM173/MITA. Interacts with IFIT3 (via N-terminus). Interacts with TBK1 only in the presence of IFIT3. Interacts with MUL1. Interacts with human respiratory syncytial virus (HRSV) NS1 protein; this interaction disrupts MAVS binding to DDX58/RIG-I. Ref.1 Ref.2 Ref.3 Ref.4 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.20 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.33 Ref.34 Ref.35

Subcellular location

Mitochondrion outer membrane. Mitochondrion. Peroxisome Ref.1 Ref.30.

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. Ref.1 Ref.2 Ref.4

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.

The transmembrane domain and residues 300-444 are essential for its interaction with DHX58/LGP2.

Post-translational modification

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. Ref.26

Miscellaneous

Cleavage by HCV protease complex leads to inactivation.

Sequence similarities

Contains 1 CARD domain.

Sequence caution

The sequence BAA86585.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB14684.1 differs from that shown. Reason: Frameshift at position 333.

Ontologies

Keywords
   Biological processAntiviral defense
Host-virus interaction
Immunity
Innate immunity
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
Peroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRIG-I signaling pathway

Inferred from electronic annotation. Source: Ensembl

activation of innate immune response

Inferred from mutant phenotype PubMed 18818105. Source: BHF-UCL

cellular response to exogenous dsRNA

Inferred from mutant phenotype Ref.4. Source: BHF-UCL

defense response to bacterium

Inferred from mutant phenotype Ref.23. Source: UniProtKB

defense response to virus

Inferred from direct assay Ref.30. Source: UniProtKB

innate immune response

Inferred from mutant phenotype PubMed 19609254Ref.23. Source: UniProtKB

negative regulation of type I interferon production

Traceable author statement. Source: Reactome

negative regulation of viral genome replication

Inferred from direct assay Ref.30. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.7. Source: UniProtKB

positive regulation of IP-10 production

Inferred from direct assay Ref.4. Source: BHF-UCL

positive regulation of chemokine (C-C motif) ligand 5 production

Inferred from direct assay Ref.4. Source: BHF-UCL

positive regulation of defense response to virus by host

Inferred from mutant phenotype PubMed 19609254. Source: UniProtKB

positive regulation of interferon-alpha production

Inferred from mutant phenotype PubMed 19609254. Source: UniProtKB

positive regulation of interferon-beta production

Inferred from mutant phenotype PubMed 19609254Ref.23. Source: UniProtKB

positive regulation of interleukin-8 production

Inferred from direct assay Ref.4. Source: BHF-UCL

positive regulation of protein import into nucleus, translocation

Inferred from direct assay PubMed 18818105. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay Ref.4. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.4. Source: BHF-UCL

positive regulation of transcription factor import into nucleus

Inferred from direct assay PubMed 18818105. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.4PubMed 18818105. Source: BHF-UCL

positive regulation of tumor necrosis factor production

Inferred from direct assay Ref.4. Source: BHF-UCL

positive regulation of type I interferon-mediated signaling pathway

Inferred from direct assay Ref.30. Source: UniProtKB

regulation of peroxisome organization

Inferred from mutant phenotype Ref.30. Source: UniProtKB

signal transduction

Inferred from mutant phenotype Ref.30. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial membrane

Inferred from direct assay Ref.30. Source: UniProtKB

mitochondrial outer membrane

Inferred from direct assay PubMed 18818105. Source: BHF-UCL

mitochondrion

Inferred from direct assay. Source: HPA

peroxisomal membrane

Inferred from direct assay Ref.30. Source: UniProtKB

   Molecular_functionCARD domain binding

Inferred from physical interaction Ref.4. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.17Ref.28Ref.24Ref.26PubMed 19893624Ref.33Ref.35. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.4. Source: BHF-UCL

signal transducer activity

Inferred from mutant phenotype Ref.7Ref.30. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z434-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q7Z434-2)

The sequence of this isoform differs from the canonical sequence as follows:
     99-131: TSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYN → ERPALALLDPQPAPWPPLSFSLSLYFLPFSVILFLVTVKR
     132-540: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q7Z434-3)

The sequence of this isoform differs from the canonical sequence as follows:
     64-148: RRPGWVEYFI...SYPMPVQETQ → LPTWAGEETP...LLPSLSCPTW
     149-540: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q7Z434-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-141: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q7Z434-5)

Also known as: MAVS1b; exon 3 deletion;

The sequence of this isoform differs from the canonical sequence as follows:
     98-124: RTSDRPPDPLEPPSLPAERPGPPTPAA → QFRASPADAQPQSHPKESRWWPPGVLL
     125-540: Missing.
Note: Selectively activates an IFNbeta but not an IL8 promoter. Interacts with RIP1 and FADD and exhibits anti-viral activity against VSV infection.
Isoform 6 (identifier: Q7Z434-6)

Also known as: MAVS1a; exon 2 deletion;

The sequence of this isoform differs from the canonical sequence as follows:
     40-131: DRLRATCTLS...PAAAHSIPYN → GPRTVPQTHW...PPLTWQPSAL
     132-540: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 540540Mitochondrial antiviral-signaling protein
PRO_0000144096

Regions

Topological domain1 – 513513Cytoplasmic Probable
Transmembrane514 – 53421Helical; Potential
Topological domain535 – 5406Mitochondrial intermembrane Probable
Domain10 – 7768CARD
Region10 – 7768Required for interaction with NLRX1
Region143 – 1475Interaction with TRAF2
Region153 – 1586Interaction with TRAF6
Region455 – 4606Interaction with TRAF6
Compositional bias103 – 15351Pro-rich

Sites

Site427 – 4282Cleavage; by HHAV protein 3ABC
Site508 – 5092Cleavage; by HCV and hepatitis GB virus B NS3/4A protease complex

Amino acid modifications

Modified residue1521Phosphoserine Ref.21 Ref.29
Modified residue1571Phosphoserine Ref.21
Modified residue1651Phosphoserine Ref.21 Ref.29
Modified residue2221Phosphoserine Ref.14 Ref.21
Modified residue2331Phosphoserine Ref.21
Modified residue2341Phosphothreonine Ref.21
Modified residue2531Phosphoserine Ref.31
Modified residue2581Phosphoserine Ref.21 Ref.31
Modified residue4081Phosphoserine By similarity

Natural variations

Alternative sequence1 – 141141Missing in isoform 4.
VSP_045872
Alternative sequence40 – 13192DRLRA…SIPYN → GPRTVPQTHWSHRHFLLRGQ GPPHLLRPTASPTTAAERRS QVTPCLSRRPRRQSPQERIQ SKPCRRSAPEPSQGIQMVAP WSPPLTWQPSAL in isoform 6.
VSP_047816
Alternative sequence64 – 14885RRPGW…VQETQ → LPTWAGEETPGGQSSGRGLD FSSLTSGAVWLWQMSDFWSC FSTWTVSIWLILHWVLLRLN LQVFAKCLAQSKWPLLLPSL SCPTW in isoform 3.
VSP_010261
Alternative sequence98 – 12427RTSDR…PTPAA → QFRASPADAQPQSHPKESRW WPPGVLL in isoform 5.
VSP_047817
Alternative sequence99 – 13133TSDRP…SIPYN → ERPALALLDPQPAPWPPLSF SLSLYFLPFSVILFLVTVKR in isoform 2.
VSP_010262
Alternative sequence125 – 540416Missing in isoform 5.
VSP_047818
Alternative sequence132 – 540409Missing in isoform 2 and isoform 6.
VSP_010263
Alternative sequence149 – 540392Missing in isoform 3.
VSP_010264
Natural variant791C → F.
Corresponds to variant rs11905552 [ dbSNP | Ensembl ].
VAR_048609
Natural variant791C → S.
Corresponds to variant rs11908032 [ dbSNP | Ensembl ].
VAR_059197
Natural variant931Q → E. Ref.2 Ref.4 Ref.8 Ref.11
Corresponds to variant rs17857295 [ dbSNP | Ensembl ].
VAR_048610
Natural variant1981Q → K. Ref.1 Ref.3 Ref.11
Corresponds to variant rs7262903 [ dbSNP | Ensembl ].
VAR_048611
Natural variant4091S → F. Ref.1 Ref.3 Ref.11
Corresponds to variant rs7269320 [ dbSNP | Ensembl ].
VAR_018448

Experimental info

Mutagenesis541T → A: Impairs ability to induce IFN-beta. Ref.1
Mutagenesis67 – 693GWV → AAA: Impairs ability to induce IFN-beta. Ref.1
Mutagenesis1451Q → N: No interaction with TRAF2. Ref.2
Mutagenesis1551E → D: No interaction with TRAF6; when associated with D-457. Ref.2
Mutagenesis4271Q → A: No cleavage by HHAV 3ABC. Ref.16
Mutagenesis4351C → R: No effect on cleavage by NS3/4A protease complex. Ref.12
Mutagenesis4521C → R: No effect on cleavage by NS3/4A protease complex. Ref.12
Mutagenesis4571E → D: No interaction with TRAF6; when associated with D-155. Ref.2
Mutagenesis4631E → A: No effect on cleavage by HHAV 3ABC. Ref.16
Mutagenesis5081C → A or R: No cleavage by HCV and hepatitis GB virus B NS3/4A protease complex. Ref.3 Ref.12 Ref.15
Sequence conflict421L → P in BAC77356. Ref.7
Sequence conflict1911T → N in BAF84474. Ref.8
Sequence conflict3561A → V in BAC77356. Ref.7
Sequence conflict3731S → P in BAC77356. Ref.7

Secondary structure

............... 540
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 0E23E3E115941EE8

FASTA54056,528
        10         20         30         40         50         60 
MPFAEDKTYK YICRNFSNFC NVDVVEILPY LPCLTARDQD RLRATCTLSG NRDTLWHLFN 

        70         80         90        100        110        120 
TLQRRPGWVE YFIAALRGCE LVDLADEVAS VYQSYQPRTS DRPPDPLEPP SLPAERPGPP 

       130        140        150        160        170        180 
TPAAAHSIPY NSCREKEPSY PMPVQETQAP ESPGENSEQA LQTLSPRAIP RNPDGGPLES 

       190        200        210        220        230        240 
SSDLAALSPL TSSGHQEQDT ELGSTHTAGA TSSLTPSRGP VSPSVSFQPL ARSTPRASRL 

       250        260        270        280        290        300 
PGPTGSVVST GTSFSSSSPG LASAGAAEGK QGAESDQAEP IICSSGAEAP ANSLPSKVPT 

       310        320        330        340        350        360 
TLMPVNTVAL KVPANPASVS TVPSKLPTSS KPPGAVPSNA LTNPAPSKLP INSTRAGMVP 

       370        380        390        400        410        420 
SKVPTSMVLT KVSASTVPTD GSSRNEETPA APTPAGATGG SSAWLDSSSE NRGLGSELSK 

       430        440        450        460        470        480 
PGVLASQVDS PFSGCFEDLA ISASTSLGMG PCHGPEENEY KSEGTFGIHV AENPSIQLLE 

       490        500        510        520        530        540 
GNPGPPADPD GGPRPQADRK FQEREVPCHR PSPGALWLQV AVTGVLVVTL LVVLYRRRLH 

« Hide

Isoform 2 [UniParc].

Checksum: E05D88F9EA1218AA
Show »

FASTA13815,996
Isoform 3 [UniParc].

Checksum: C1593E51F98F2DCE
Show »

FASTA14817,043
Isoform 4 [UniParc].

Checksum: 4DB7ED11FEA04082
Show »

FASTA39940,468
Isoform 5 (MAVS1b) (exon 3 deletion) [UniParc].

Checksum: EAEB6D179AF1F6A4
Show »

FASTA12414,385
Isoform 6 (MAVS1a) (exon 2 deletion) [UniParc].

Checksum: D49F388351EB0ADB
Show »

FASTA13115,012

References

« Hide 'large scale' references
[1]"Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3."
Seth R.B., Sun L., Ea C.-K., Chen Z.J.
Cell 122:669-682(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, VARIANTS LYS-198 AND PHE-409.
[2]"VISA is an adapter protein required for virus-triggered IFN-beta Signaling."
Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.
Mol. Cell 19:727-740(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH DDX58/RIG-I; IRF3; TRAF2 AND TRAF6, MUTAGENESIS OF GLN-145; GLU-155 AND GLU-457, FUNCTION, VARIANT GLU-93.
[3]"Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus."
Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., Tschopp J.
Nature 437:1167-1172(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDX58/RIG-I; IKBKE; CHUK AND IKBKB, FUNCTION, CLEAVAGE SITE, MUTAGENESIS OF CYS-508, VARIANTS LYS-198 AND PHE-409.
[4]"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction."
Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., Ishii K.J., Takeuchi O., Akira S.
Nat. Immunol. 6:981-988(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH DDX58/RIG-I; IFIH1/MDA5; FADD AND RIPK1, FUNCTION, VARIANT GLU-93.
[5]"Identification of MAVS splicing variants that interfere with RIGI/MAVS pathway signaling."
Lad S.P., Yang G., Scott D.A., Chao T.H., Correia Jda S., de la Torre J.C., Li E.
Mol. Immunol. 45:2277-2287(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
[6]"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."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[7]"Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung fibroblast.
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), VARIANT GLU-93.
Tissue: Pericardium, Placenta and Tongue.
[9]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-93; LYS-198 AND PHE-409.
Tissue: Brain.
[12]"Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity."
Li X.D., Sun L., Seth R.B., Pineda G., Chen Z.J.
Proc. Natl. Acad. Sci. U.S.A. 102:17717-17722(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV NS3/4A PROTEASE, CLEAVAGE SITE, MUTAGENESIS OF CYS-435; CYS-452 AND CYS-508.
[13]"RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2."
Komuro A., Horvath C.M.
J. Virol. 80:12332-12342(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DHX58/LGP2 AND IKBKE.
[14]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"GB virus B disrupts RIG-I signaling by NS3/4A-mediated cleavage of the adaptor protein MAVS."
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.
J. Virol. 81:964-976(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HEPATITIS GB VIRUS B NS3/4A PROTEASE, CLEAVAGE SITE, MUTAGENESIS OF CYS-508.
[16]"Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor."
Yang Y., Liang Y., Qu L., Chen Z., Yi M., Li K., Lemon S.M.
Proc. Natl. Acad. Sci. U.S.A. 104:7253-7258(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN HEPATITIS A VIRUS PROTEIN 3ABC, CLEAVAGE SITE, MUTAGENESIS OF GLN-427 AND GLU-463.
[17]"The tumour suppressor CYLD is a negative regulator of RIG-I-mediated antiviral response."
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.
EMBO Rep. 9:930-936(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CYLD.
[18]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[19]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"NLRX1 is a regulator of mitochondrial antiviral immunity."
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.
Nature 451:573-577(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NLRX1.
[21]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-157; SER-165; SER-222; SER-233; THR-234 AND SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway."
Chiu Y.-H., Macmillan J.B., Chen Z.J.
Cell 138:576-591(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling."
Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.
J. Biol. Chem. 284:19122-19131(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRC.
[25]"Negative regulation of MAVS-mediated innate immune response by PSMA7."
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.
J. Immunol. 183:4241-4248(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSMA7.
[26]"PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4."
You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z.
Nat. Immunol. 10:1300-1308(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCBP2, UBIQUITINATION BY ITCH.
[27]"Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at mitochondria."
Xu L., Xiao N., Liu F., Ren H., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 106:1530-1535(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C1QBP.
[28]"ISG56 is a negative-feedback regulator of virus-triggered signaling and cellular antiviral response."
Li Y., Li C., Xue P., Zhong B., Mao A.P., Ran Y., Chen H., Wang Y.Y., Yang F., Shu H.B.
Proc. Natl. Acad. Sci. U.S.A. 106:7945-7950(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM173/MITA.
[29]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[30]"Peroxisomes are signaling platforms for antiviral innate immunity."
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.
Cell 141:668-681(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[31]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"IFN-induced TPR protein IFIT3 potentiates antiviral signaling by bridging MAVS and TBK1."
Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.
J. Immunol. 187:2559-2568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IFIT3 AND TBK1.
[34]"Respiratory syncytial virus NS1 protein colocalizes with mitochondrial antiviral signaling protein MAVS following infection."
Boyapalle S., Wong T., Garay J., Teng M., San Juan-Vergara H., Mohapatra S., Mohapatra S.
PLoS ONE 7:E29386-E29386(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRSV NS1.
[35]"Mitochondrially localised MUL1 is a novel modulator of antiviral signaling."
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.
Immunol. Cell Biol. 91:321-330(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUL1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ174270 mRNA. Translation: AAZ80417.1.
DQ167126 mRNA. Translation: ABA54890.1.
DQ181928 mRNA. Translation: ABA19229.1.
AB232371 mRNA. Translation: BAE79738.1.
EF467323 mRNA. Translation: ABR24161.1.
EF467324 mRNA. Translation: ABR24162.1.
AB033097 mRNA. Translation: BAA86585.1. Different initiation.
AB097003 mRNA. Translation: BAC77356.1.
AK023799 mRNA. Translation: BAB14684.1. Frameshift.
AK123956 mRNA. Translation: BAC85734.1.
AK130992 mRNA. Translation: BAC85473.1.
AK291785 mRNA. Translation: BAF84474.1.
AK296897 mRNA. Translation: BAG59455.1.
AL353194, AL109804 Genomic DNA. Translation: CAI11041.1.
AL109804, AL353194 Genomic DNA. Translation: CAI18851.1.
CH471133 Genomic DNA. Translation: EAX10481.1.
BC044952 mRNA. Translation: AAH44952.1.
CCDSCCDS33437.1. [Q7Z434-1]
CCDS56176.1. [Q7Z434-4]
RefSeqNP_001193420.1. NM_001206491.1. [Q7Z434-4]
NP_065797.2. NM_020746.4. [Q7Z434-1]
UniGeneHs.570362.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VGQX-ray2.10A1-93[»]
3J6Celectron microscopy9.60A3-93[»]
ProteinModelPortalQ7Z434.
SMRQ7Z434. Positions 1-93.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121570. 51 interactions.
DIPDIP-35445N.
IntActQ7Z434. 35 interactions.
MINTMINT-3034048.

PTM databases

PhosphoSiteQ7Z434.

Polymorphism databases

DMDM47115748.

Proteomic databases

MaxQBQ7Z434.
PaxDbQ7Z434.
PeptideAtlasQ7Z434.
PRIDEQ7Z434.

Protocols and materials databases

DNASU57506.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358134; ENSP00000350852; ENSG00000088888. [Q7Z434-5]
ENST00000416600; ENSP00000413749; ENSG00000088888. [Q7Z434-4]
ENST00000428216; ENSP00000401980; ENSG00000088888. [Q7Z434-1]
GeneID57506.
KEGGhsa:57506.
UCSCuc002wjv.3. human. [Q7Z434-2]
uc002wjw.4. human. [Q7Z434-1]

Organism-specific databases

CTD57506.
GeneCardsGC20P003827.
HGNCHGNC:29233. MAVS.
HPACAB009187.
HPA053524.
MIM609676. gene.
neXtProtNX_Q7Z434.
PharmGKBPA164722208.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG79681.
HOVERGENHBG079638.
InParanoidQ7Z434.
KOK12648.
OMAEQDTELG.
OrthoDBEOG71ZP2Z.
PhylomeDBQ7Z434.
TreeFamTF333444.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ7Z434.

Gene expression databases

ArrayExpressQ7Z434.
BgeeQ7Z434.
GenevestigatorQ7Z434.

Family and domain databases

InterProIPR026148. Mt_antiviral_sig_pro.
[Graphical view]
PANTHERPTHR21446. PTHR21446. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMAVS. human.
EvolutionaryTraceQ7Z434.
GeneWikiVISA_(gene).
GenomeRNAi57506.
NextBio35464378.
PMAP-CutDBQ7Z434.
PROQ7Z434.
SOURCESearch...

Entry information

Entry nameMAVS_HUMAN
AccessionPrimary (citable) accession number: Q7Z434
Secondary accession number(s): A8K6X0 expand/collapse secondary AC list , B2BD33, B2BD34, F5H6C8, Q2HWT5, Q3I0Y2, Q5T7I6, Q86VY7, Q9H1H3, Q9H4Y1, Q9H8D3, Q9ULE9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM