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Q7Z434

- MAVS_HUMAN

UniProt

Q7Z434 - MAVS_HUMAN

Protein

Mitochondrial antiviral-signaling protein

Gene

MAVS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
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    Functioni

    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.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei427 – 4282Cleavage; by HHAV protein 3ABC
    Sitei508 – 5092Cleavage; by HCV and hepatitis GB virus B NS3/4A protease complex

    GO - Molecular functioni

    1. CARD domain binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: BHF-UCL
    4. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. activation of innate immune response Source: BHF-UCL
    2. cellular response to exogenous dsRNA Source: BHF-UCL
    3. defense response to bacterium Source: UniProtKB
    4. defense response to virus Source: UniProtKB
    5. innate immune response Source: UniProtKB
    6. negative regulation of type I interferon production Source: Reactome
    7. negative regulation of viral genome replication Source: UniProtKB
    8. positive regulation of chemokine (C-C motif) ligand 5 production Source: BHF-UCL
    9. positive regulation of defense response to virus by host Source: UniProtKB
    10. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    11. positive regulation of interferon-alpha production Source: UniProtKB
    12. positive regulation of interferon-beta production Source: UniProtKB
    13. positive regulation of interleukin-8 production Source: BHF-UCL
    14. positive regulation of IP-10 production Source: BHF-UCL
    15. positive regulation of protein import into nucleus, translocation Source: BHF-UCL
    16. positive regulation of protein phosphorylation Source: BHF-UCL
    17. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    18. positive regulation of transcription factor import into nucleus Source: BHF-UCL
    19. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    20. positive regulation of tumor necrosis factor production Source: BHF-UCL
    21. positive regulation of type I interferon-mediated signaling pathway Source: UniProtKB
    22. regulation of peroxisome organization Source: UniProtKB
    23. RIG-I signaling pathway Source: Ensembl
    24. signal transduction Source: UniProtKB
    25. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Antiviral defense, Host-virus interaction, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
    SignaLinkiQ7Z434.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:MAVS
    Synonyms:IPS1, KIAA1271, VISA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:29233. MAVS.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial membrane Source: UniProtKB
    3. mitochondrial outer membrane Source: BHF-UCL
    4. mitochondrion Source: HPA
    5. peroxisomal membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi54 – 541T → A: Impairs ability to induce IFN-beta. 1 Publication
    Mutagenesisi67 – 693GWV → AAA: Impairs ability to induce IFN-beta.
    Mutagenesisi145 – 1451Q → N: No interaction with TRAF2. 1 Publication
    Mutagenesisi155 – 1551E → D: No interaction with TRAF6; when associated with D-457. 1 Publication
    Mutagenesisi427 – 4271Q → A: No cleavage by HHAV 3ABC. 1 Publication
    Mutagenesisi435 – 4351C → R: No effect on cleavage by NS3/4A protease complex. 1 Publication
    Mutagenesisi452 – 4521C → R: No effect on cleavage by NS3/4A protease complex. 1 Publication
    Mutagenesisi457 – 4571E → D: No interaction with TRAF6; when associated with D-155. 1 Publication
    Mutagenesisi463 – 4631E → A: No effect on cleavage by HHAV 3ABC. 1 Publication
    Mutagenesisi508 – 5081C → A or R: No cleavage by HCV and hepatitis GB virus B NS3/4A protease complex. 3 Publications

    Organism-specific databases

    PharmGKBiPA164722208.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 540540Mitochondrial antiviral-signaling proteinPRO_0000144096Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei152 – 1521Phosphoserine2 Publications
    Modified residuei157 – 1571Phosphoserine1 Publication
    Modified residuei165 – 1651Phosphoserine2 Publications
    Modified residuei222 – 2221Phosphoserine2 Publications
    Modified residuei233 – 2331Phosphoserine1 Publication
    Modified residuei234 – 2341Phosphothreonine1 Publication
    Modified residuei253 – 2531Phosphoserine1 Publication
    Modified residuei258 – 2581Phosphoserine2 Publications
    Modified residuei408 – 4081PhosphoserineBy similarity

    Post-translational modificationi

    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.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ7Z434.
    PaxDbiQ7Z434.
    PeptideAtlasiQ7Z434.
    PRIDEiQ7Z434.

    PTM databases

    PhosphoSiteiQ7Z434.

    Miscellaneous databases

    PMAP-CutDBQ7Z434.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Gene expression databases

    ArrayExpressiQ7Z434.
    BgeeiQ7Z434.
    GenevestigatoriQ7Z434.

    Organism-specific databases

    HPAiCAB009187.
    HPA053524.

    Interactioni

    Subunit structurei

    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.By similarity18 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005196EBI-995373,EBI-375543
    BAG6P463792EBI-995373,EBI-347552
    C1QBPQ070215EBI-995373,EBI-347528
    CALCOCO2Q131373EBI-995373,EBI-739580
    DDX3XO005714EBI-995373,EBI-353779
    DDX58O9578612EBI-995373,EBI-995350
    IFIH1Q9BYX45EBI-995373,EBI-6115771
    IKBKEQ141643EBI-995373,EBI-307369
    IRF5Q135682EBI-995373,EBI-3931258
    M2Q6WB964EBI-995373,EBI-6863628From a different organism.
    MFN1Q8IWA42EBI-995373,EBI-1048197
    NLRP3Q96P204EBI-995373,EBI-6253230
    OAS3Q9Y6K52EBI-995373,EBI-6115729
    RIPK2O433533EBI-995373,EBI-358522
    STAT1P422243EBI-995373,EBI-1057697
    TMEM173Q86WV67EBI-995373,EBI-2800345
    UBE4AQ141392EBI-995373,EBI-1048119
    XQ690272EBI-995373,EBI-3650820From a different organism.

    Protein-protein interaction databases

    BioGridi121570. 51 interactions.
    DIPiDIP-35445N.
    IntActiQ7Z434. 35 interactions.
    MINTiMINT-3034048.

    Structurei

    Secondary structure

    540
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 1414
    Helixi16 – 194
    Helixi24 – 274
    Helixi28 – 303
    Helixi36 – 4914
    Helixi51 – 6212
    Helixi68 – 7811
    Helixi82 – 9211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VGQX-ray2.10A1-93[»]
    3J6Celectron microscopy9.60A3-93[»]
    ProteinModelPortaliQ7Z434.
    SMRiQ7Z434. Positions 1-93.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7Z434.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 513513CytoplasmicCuratedAdd
    BLAST
    Topological domaini535 – 5406Mitochondrial intermembraneCurated

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei514 – 53421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 7768CARDAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni10 – 7768Required for interaction with NLRX1Add
    BLAST
    Regioni143 – 1475Interaction with TRAF2
    Regioni153 – 1586Interaction with TRAF6
    Regioni455 – 4606Interaction with TRAF6

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi103 – 15351Pro-richAdd
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Contains 1 CARD domain.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG79681.
    HOVERGENiHBG079638.
    InParanoidiQ7Z434.
    KOiK12648.
    OMAiEQDTELG.
    OrthoDBiEOG71ZP2Z.
    PhylomeDBiQ7Z434.
    TreeFamiTF333444.

    Family and domain databases

    InterProiIPR026148. Mt_antiviral_sig_pro.
    [Graphical view]
    PANTHERiPTHR21446. PTHR21446. 1 hit.

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z434-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPFAEDKTYK YICRNFSNFC NVDVVEILPY LPCLTARDQD RLRATCTLSG    50
    NRDTLWHLFN TLQRRPGWVE YFIAALRGCE LVDLADEVAS VYQSYQPRTS 100
    DRPPDPLEPP SLPAERPGPP TPAAAHSIPY NSCREKEPSY PMPVQETQAP 150
    ESPGENSEQA LQTLSPRAIP RNPDGGPLES SSDLAALSPL TSSGHQEQDT 200
    ELGSTHTAGA TSSLTPSRGP VSPSVSFQPL ARSTPRASRL PGPTGSVVST 250
    GTSFSSSSPG LASAGAAEGK QGAESDQAEP IICSSGAEAP ANSLPSKVPT 300
    TLMPVNTVAL KVPANPASVS TVPSKLPTSS KPPGAVPSNA LTNPAPSKLP 350
    INSTRAGMVP SKVPTSMVLT KVSASTVPTD GSSRNEETPA APTPAGATGG 400
    SSAWLDSSSE NRGLGSELSK PGVLASQVDS PFSGCFEDLA ISASTSLGMG 450
    PCHGPEENEY KSEGTFGIHV AENPSIQLLE GNPGPPADPD GGPRPQADRK 500
    FQEREVPCHR PSPGALWLQV AVTGVLVVTL LVVLYRRRLH 540
    Length:540
    Mass (Da):56,528
    Last modified:May 10, 2004 - v2
    Checksum:i0E23E3E115941EE8
    GO
    Isoform 2 (identifier: Q7Z434-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         99-131: TSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYN → ERPALALLDPQPAPWPPLSFSLSLYFLPFSVILFLVTVKR
         132-540: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:138
    Mass (Da):15,996
    Checksum:iE05D88F9EA1218AA
    GO
    Isoform 3 (identifier: Q7Z434-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:148
    Mass (Da):17,043
    Checksum:iC1593E51F98F2DCE
    GO
    Isoform 4 (identifier: Q7Z434-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-141: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:399
    Mass (Da):40,468
    Checksum:i4DB7ED11FEA04082
    GO
    Isoform 5 (identifier: Q7Z434-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:124
    Mass (Da):14,385
    Checksum:iEAEB6D179AF1F6A4
    GO
    Isoform 6 (identifier: Q7Z434-6) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:131
    Mass (Da):15,012
    Checksum:iD49F388351EB0ADB
    GO

    Sequence cautioni

    The sequence BAB14684.1 differs from that shown. Reason: Frameshift at position 333.
    The sequence BAA86585.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421L → P in BAC77356. (PubMed:12761501)Curated
    Sequence conflicti191 – 1911T → N in BAF84474. (PubMed:14702039)Curated
    Sequence conflicti356 – 3561A → V in BAC77356. (PubMed:12761501)Curated
    Sequence conflicti373 – 3731S → P in BAC77356. (PubMed:12761501)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791C → F.
    Corresponds to variant rs11905552 [ dbSNP | Ensembl ].
    VAR_048609
    Natural varianti79 – 791C → S.
    Corresponds to variant rs11908032 [ dbSNP | Ensembl ].
    VAR_059197
    Natural varianti93 – 931Q → E.4 Publications
    Corresponds to variant rs17857295 [ dbSNP | Ensembl ].
    VAR_048610
    Natural varianti198 – 1981Q → K.3 Publications
    Corresponds to variant rs7262903 [ dbSNP | Ensembl ].
    VAR_048611
    Natural varianti409 – 4091S → F.3 Publications
    Corresponds to variant rs7269320 [ dbSNP | Ensembl ].
    VAR_018448

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 141141Missing in isoform 4. 1 PublicationVSP_045872Add
    BLAST
    Alternative sequencei40 – 13192DRLRA…SIPYN → GPRTVPQTHWSHRHFLLRGQ GPPHLLRPTASPTTAAERRS QVTPCLSRRPRRQSPQERIQ SKPCRRSAPEPSQGIQMVAP WSPPLTWQPSAL in isoform 6. 1 PublicationVSP_047816Add
    BLAST
    Alternative sequencei64 – 14885RRPGW…VQETQ → LPTWAGEETPGGQSSGRGLD FSSLTSGAVWLWQMSDFWSC FSTWTVSIWLILHWVLLRLN LQVFAKCLAQSKWPLLLPSL SCPTW in isoform 3. 1 PublicationVSP_010261Add
    BLAST
    Alternative sequencei98 – 12427RTSDR…PTPAA → QFRASPADAQPQSHPKESRW WPPGVLL in isoform 5. 2 PublicationsVSP_047817Add
    BLAST
    Alternative sequencei99 – 13133TSDRP…SIPYN → ERPALALLDPQPAPWPPLSF SLSLYFLPFSVILFLVTVKR in isoform 2. 1 PublicationVSP_010262Add
    BLAST
    Alternative sequencei125 – 540416Missing in isoform 5. 2 PublicationsVSP_047818Add
    BLAST
    Alternative sequencei132 – 540409Missing in isoform 2 and isoform 6. 2 PublicationsVSP_010263Add
    BLAST
    Alternative sequencei149 – 540392Missing in isoform 3. 1 PublicationVSP_010264Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS33437.1. [Q7Z434-1]
    CCDS56176.1. [Q7Z434-4]
    RefSeqiNP_001193420.1. NM_001206491.1. [Q7Z434-4]
    NP_065797.2. NM_020746.4. [Q7Z434-1]
    UniGeneiHs.570362.

    Genome annotation databases

    EnsembliENST00000416600; ENSP00000413749; ENSG00000088888. [Q7Z434-4]
    ENST00000428216; ENSP00000401980; ENSG00000088888. [Q7Z434-1]
    GeneIDi57506.
    KEGGihsa:57506.
    UCSCiuc002wjv.3. human. [Q7Z434-2]
    uc002wjw.4. human. [Q7Z434-1]

    Polymorphism databases

    DMDMi47115748.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS33437.1. [Q7Z434-1 ]
    CCDS56176.1. [Q7Z434-4 ]
    RefSeqi NP_001193420.1. NM_001206491.1. [Q7Z434-4 ]
    NP_065797.2. NM_020746.4. [Q7Z434-1 ]
    UniGenei Hs.570362.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VGQ X-ray 2.10 A 1-93 [» ]
    3J6C electron microscopy 9.60 A 3-93 [» ]
    ProteinModelPortali Q7Z434.
    SMRi Q7Z434. Positions 1-93.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121570. 51 interactions.
    DIPi DIP-35445N.
    IntActi Q7Z434. 35 interactions.
    MINTi MINT-3034048.

    PTM databases

    PhosphoSitei Q7Z434.

    Polymorphism databases

    DMDMi 47115748.

    Proteomic databases

    MaxQBi Q7Z434.
    PaxDbi Q7Z434.
    PeptideAtlasi Q7Z434.
    PRIDEi Q7Z434.

    Protocols and materials databases

    DNASUi 57506.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000416600 ; ENSP00000413749 ; ENSG00000088888 . [Q7Z434-4 ]
    ENST00000428216 ; ENSP00000401980 ; ENSG00000088888 . [Q7Z434-1 ]
    GeneIDi 57506.
    KEGGi hsa:57506.
    UCSCi uc002wjv.3. human. [Q7Z434-2 ]
    uc002wjw.4. human. [Q7Z434-1 ]

    Organism-specific databases

    CTDi 57506.
    GeneCardsi GC20P003827.
    HGNCi HGNC:29233. MAVS.
    HPAi CAB009187.
    HPA053524.
    MIMi 609676. gene.
    neXtProti NX_Q7Z434.
    PharmGKBi PA164722208.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG79681.
    HOVERGENi HBG079638.
    InParanoidi Q7Z434.
    KOi K12648.
    OMAi EQDTELG.
    OrthoDBi EOG71ZP2Z.
    PhylomeDBi Q7Z434.
    TreeFami TF333444.

    Enzyme and pathway databases

    Reactomei REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
    SignaLinki Q7Z434.

    Miscellaneous databases

    ChiTaRSi MAVS. human.
    EvolutionaryTracei Q7Z434.
    GeneWikii VISA_(gene).
    GenomeRNAii 57506.
    NextBioi 35464378.
    PMAP-CutDB Q7Z434.
    PROi Q7Z434.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z434.
    Bgeei Q7Z434.
    Genevestigatori Q7Z434.

    Family and domain databases

    InterProi IPR026148. Mt_antiviral_sig_pro.
    [Graphical view ]
    PANTHERi PTHR21446. PTHR21446. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: INTERACTION WITH CYLD.
    18. 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. Cited for: INTERACTION WITH NLRX1.
    21. 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. 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. 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. Cited for: INTERACTION WITH MUL1.

    Entry informationi

    Entry nameiMAVS_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z434
    Secondary accession number(s): A8K6X0
    , B2BD33, B2BD34, F5H6C8, Q2HWT5, Q3I0Y2, Q5T7I6, Q86VY7, Q9H1H3, Q9H4Y1, Q9H8D3, Q9ULE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Cleavage by HCV protease complex leads to inactivation.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3