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Q7Z434

- MAVS_HUMAN

UniProt

Q7Z434 - MAVS_HUMAN

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Protein

Mitochondrial antiviral-signaling protein

Gene

MAVS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 kinase binding Source: BHF-UCL
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
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

BgeeiQ7Z434.
ExpressionAtlasiQ7Z434. baseline and differential.
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. 56 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[»]
3J6Jelectron microscopy3.64A/B/C/D/E/G/I/L1-97[»]
4P4HX-ray3.40I/J/K/L/M/N/O/P1-99[»]
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.
GeneTreeiENSGT00510000049120.
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

        10         20         30         40         50
MPFAEDKTYK YICRNFSNFC NVDVVEILPY LPCLTARDQD RLRATCTLSG
60 70 80 90 100
NRDTLWHLFN TLQRRPGWVE YFIAALRGCE LVDLADEVAS VYQSYQPRTS
110 120 130 140 150
DRPPDPLEPP SLPAERPGPP TPAAAHSIPY NSCREKEPSY PMPVQETQAP
160 170 180 190 200
ESPGENSEQA LQTLSPRAIP RNPDGGPLES SSDLAALSPL TSSGHQEQDT
210 220 230 240 250
ELGSTHTAGA TSSLTPSRGP VSPSVSFQPL ARSTPRASRL PGPTGSVVST
260 270 280 290 300
GTSFSSSSPG LASAGAAEGK QGAESDQAEP IICSSGAEAP ANSLPSKVPT
310 320 330 340 350
TLMPVNTVAL KVPANPASVS TVPSKLPTSS KPPGAVPSNA LTNPAPSKLP
360 370 380 390 400
INSTRAGMVP SKVPTSMVLT KVSASTVPTD GSSRNEETPA APTPAGATGG
410 420 430 440 450
SSAWLDSSSE NRGLGSELSK PGVLASQVDS PFSGCFEDLA ISASTSLGMG
460 470 480 490 500
PCHGPEENEY KSEGTFGIHV AENPSIQLLE GNPGPPADPD GGPRPQADRK
510 520 530 540
FQEREVPCHR PSPGALWLQV AVTGVLVVTL LVVLYRRRLH
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 [» ]
3J6J electron microscopy 3.64 A/B/C/D/E/G/I/L 1-97 [» ]
4P4H X-ray 3.40 I/J/K/L/M/N/O/P 1-99 [» ]
ProteinModelPortali Q7Z434.
SMRi Q7Z434. Positions 1-93.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121570. 56 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.
GeneTreei ENSGT00510000049120.
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

Bgeei Q7Z434.
ExpressionAtlasi Q7Z434. baseline and differential.
Genevestigatori Q7Z434.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 117 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

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