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Protein

Mitochondrial antiviral-signaling protein

Gene

MAVS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Molecular functioni

  • CARD domain binding Source: BHF-UCL
  • protein kinase binding Source: BHF-UCL
  • signal transducer activity Source: UniProtKB

GO - Biological processi

  • activation of innate immune response Source: BHF-UCL
  • cellular response to exogenous dsRNA Source: BHF-UCL
  • cytoplasmic pattern recognition receptor signaling pathway in response to virus Source: GO_Central
  • defense response to bacterium Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • innate immune response Source: UniProtKB
  • negative regulation of type I interferon production Source: Reactome
  • negative regulation of viral genome replication Source: UniProtKB
  • positive regulation of chemokine (C-C motif) ligand 5 production Source: BHF-UCL
  • positive regulation of defense response to virus by host Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of interferon-alpha production Source: UniProtKB
  • positive regulation of interferon-beta production Source: UniProtKB
  • positive regulation of interleukin-8 production Source: BHF-UCL
  • positive regulation of IP-10 production Source: BHF-UCL
  • positive regulation of protein import into nucleus, translocation Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: BHF-UCL
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of transcription factor import into nucleus Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of tumor necrosis factor production Source: BHF-UCL
  • positive regulation of type I interferon-mediated signaling pathway Source: UniProtKB
  • regulation of peroxisome organization Source: UniProtKB
  • RIG-I signaling pathway Source: Ensembl
  • signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiR-HSA-168928. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
R-HSA-5689896. Ovarian tumor domain proteases.
R-HSA-918233. TRAF3-dependent IRF activation pathway.
R-HSA-933541. TRAF6 mediated IRF7 activation.
R-HSA-933542. TRAF6 mediated NF-kB activation.
R-HSA-933543. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
SignaLinkiQ7Z434.
SIGNORiQ7Z434.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:29233. MAVS.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 513CytoplasmicCuratedAdd BLAST513
Transmembranei514 – 534HelicalSequence analysisAdd BLAST21
Topological domaini535 – 540Mitochondrial intermembraneCurated6

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial membrane Source: UniProtKB
  • mitochondrial outer membrane Source: BHF-UCL
  • mitochondrion Source: HPA
  • peroxisomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26E → A or R: Impairs filament formation and abolishes antiviral signaling activity. 1 Publication1
Mutagenesisi54T → A: Impairs ability to induce IFN-beta. 1 Publication1
Mutagenesisi56W → A, E or R: Impairs filament formation and abolishes antiviral signaling activity. 1 Publication1
Mutagenesisi67 – 69GWV → AAA: Impairs ability to induce IFN-beta. 1 Publication3
Mutagenesisi145Q → N: No interaction with TRAF2. 1 Publication1
Mutagenesisi155E → D: No interaction with TRAF6; when associated with D-457. 1 Publication1
Mutagenesisi427Q → A: No cleavage by HHAV 3ABC. 1 Publication1
Mutagenesisi435C → R: No effect on cleavage by NS3/4A protease complex. 1 Publication1
Mutagenesisi452C → R: No effect on cleavage by NS3/4A protease complex. 1 Publication1
Mutagenesisi457E → D: No interaction with TRAF6; when associated with D-155. 1 Publication1
Mutagenesisi463E → A: No effect on cleavage by HHAV 3ABC. 1 Publication1
Mutagenesisi508C → A or R: No cleavage by HCV and hepatitis GB virus B NS3/4A protease complex. 3 Publications1

Organism-specific databases

DisGeNETi57506.
OpenTargetsiENSG00000088888.
PharmGKBiPA164722208.

Polymorphism and mutation databases

BioMutaiMAVS.
DMDMi47115748.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001440961 – 540Mitochondrial antiviral-signaling proteinAdd BLAST540

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei152PhosphoserineCombined sources1
Modified residuei157PhosphoserineCombined sources1
Modified residuei165PhosphoserineCombined sources1
Modified residuei180PhosphoserineCombined sources1
Modified residuei188PhosphoserineCombined sources1
Modified residuei215PhosphothreonineCombined sources1
Modified residuei222PhosphoserineCombined sources1
Modified residuei233PhosphoserineCombined sources1
Modified residuei234PhosphothreonineCombined sources1
Modified residuei236Asymmetric dimethylarginineBy similarity1
Modified residuei253PhosphoserineCombined sources1
Modified residuei258PhosphoserineCombined sources1
Modified residuei408PhosphoserineBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei427 – 428Cleavage; by HHAV protein 3ABC2
Sitei508 – 509Cleavage; by HCV and hepatitis GB virus B NS3/4A protease complex2

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ7Z434.
MaxQBiQ7Z434.
PaxDbiQ7Z434.
PeptideAtlasiQ7Z434.
PRIDEiQ7Z434.

PTM databases

iPTMnetiQ7Z434.
PhosphoSitePlusiQ7Z434.
SwissPalmiQ7Z434.

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

BgeeiENSG00000088888.
GenevisibleiQ7Z434. HS.

Organism-specific databases

HPAiCAB009187.
HPA049850.
HPA053524.

Interactioni

Subunit structurei

Self-associates and polymerizes (via CARD domains) to form 400 nM long three-stranded helical filaments on mitochondria, filament nucleation requires interaction with DDX58/RIG-I whose CARD domains act as a template for filament assembly. Interacts with DDX58/RIG-I, IFIH1/MDA5, TRAF2, TRAF6 and C1QBP (PubMed:17600090). May interact with IRF3, FADD, RIPK1, CHUK and IKBKB. 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 ANKRD17. 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 human respiratory syncytial virus (HRSV) NS1 protein; this interaction disrupts MAVS binding to DDX58/RIG-I.By similarity22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A2T3M44EBI-995373,EBI-9522123From a different organism.
ABL1P005196EBI-995373,EBI-375543
BAG6P463792EBI-995373,EBI-347552
C1QBPQ070215EBI-995373,EBI-347528
CALCOCO2Q131373EBI-995373,EBI-739580
DDX3XO005714EBI-995373,EBI-353779
DDX58O9578613EBI-995373,EBI-995350
IFIH1Q9BYX45EBI-995373,EBI-6115771
IKBKEQ141644EBI-995373,EBI-307369
IRF5Q135682EBI-995373,EBI-3931258
KCNIP3Q9Y2W73EBI-995373,EBI-751501
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
TBK1Q9UHD22EBI-995373,EBI-356402
TMEM173Q86WV67EBI-995373,EBI-2800345
TRAF2Q129333EBI-995373,EBI-355744
UBE4AQ141392EBI-995373,EBI-1048119
XQ690272EBI-995373,EBI-3650820From a different organism.

GO - Molecular functioni

  • CARD domain binding Source: BHF-UCL
  • protein kinase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi121570. 80 interactors.
DIPiDIP-35445N.
IntActiQ7Z434. 43 interactors.
MINTiMINT-3034048.
STRINGi9606.ENSP00000401980.

Structurei

Secondary structure

1540
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 14Combined sources14
Helixi16 – 19Combined sources4
Helixi24 – 27Combined sources4
Helixi28 – 30Combined sources3
Helixi36 – 49Combined sources14
Helixi51 – 62Combined sources12
Helixi68 – 78Combined sources11
Helixi82 – 92Combined sources11
Beta strandi95 – 97Combined sources3
Beta strandi456 – 459Combined sources4
Beta strandi504 – 507Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MS7NMR-A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U1-100[»]
2MS8NMR-A1-100[»]
2VGQX-ray2.10A1-93[»]
3J6Celectron microscopy9.60A3-93[»]
3J6Jelectron microscopy3.64A/B/C/D/E/G/I/L1-97[»]
3RC5X-ray1.60B502-508[»]
4P4HX-ray3.40I/J/K/L/M/N/O/P1-99[»]
4Z8MX-ray2.95C/D450-468[»]
5JEKX-ray2.40C/D433-448[»]
ProteinModelPortaliQ7Z434.
SMRiQ7Z434.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7Z434.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 77CARDAdd BLAST68

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 77Required for interaction with NLRX11 PublicationAdd BLAST68
Regioni143 – 147Interaction with TRAF21 Publication5
Regioni153 – 158Interaction with TRAF66
Regioni455 – 460Interaction with TRAF66

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi103 – 153Pro-richAdd BLAST51

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

eggNOGiENOG410IS5U. Eukaryota.
ENOG410Y2HK. LUCA.
GeneTreeiENSGT00510000049120.
HOGENOMiHOG000056441.
HOVERGENiHBG079638.
InParanoidiQ7Z434.
KOiK12648.
OMAiEQDTELG.
OrthoDBiEOG091G040S.
PhylomeDBiQ7Z434.
TreeFamiTF333444.

Family and domain databases

InterProiIPR031964. CARD_dom.
IPR026148. Mt_antiviral_sig_pro.
[Graphical view]
PANTHERiPTHR21446. PTHR21446. 2 hits.
PfamiPF16739. CARD_2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti42L → P in BAC77356 (PubMed:12761501).Curated1
Sequence conflicti191T → N in BAF84474 (PubMed:14702039).Curated1
Sequence conflicti356A → V in BAC77356 (PubMed:12761501).Curated1
Sequence conflicti373S → P in BAC77356 (PubMed:12761501).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04860979C → F.Corresponds to variant rs11905552dbSNPEnsembl.1
Natural variantiVAR_05919779C → S.Corresponds to variant rs11908032dbSNPEnsembl.1
Natural variantiVAR_04861093Q → E.4 PublicationsCorresponds to variant rs17857295dbSNPEnsembl.1
Natural variantiVAR_048611198Q → K.3 PublicationsCorresponds to variant rs7262903dbSNPEnsembl.1
Natural variantiVAR_018448409S → F.3 PublicationsCorresponds to variant rs7269320dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0458721 – 141Missing in isoform 4. 1 PublicationAdd BLAST141
Alternative sequenceiVSP_04781640 – 131DRLRA…SIPYN → GPRTVPQTHWSHRHFLLRGQ GPPHLLRPTASPTTAAERRS QVTPCLSRRPRRQSPQERIQ SKPCRRSAPEPSQGIQMVAP WSPPLTWQPSAL in isoform 6. 1 PublicationAdd BLAST92
Alternative sequenceiVSP_01026164 – 148RRPGW…VQETQ → LPTWAGEETPGGQSSGRGLD FSSLTSGAVWLWQMSDFWSC FSTWTVSIWLILHWVLLRLN LQVFAKCLAQSKWPLLLPSL SCPTW in isoform 3. 1 PublicationAdd BLAST85
Alternative sequenceiVSP_04781798 – 124RTSDR…PTPAA → QFRASPADAQPQSHPKESRW WPPGVLL in isoform 5. 2 PublicationsAdd BLAST27
Alternative sequenceiVSP_01026299 – 131TSDRP…SIPYN → ERPALALLDPQPAPWPPLSF SLSLYFLPFSVILFLVTVKR in isoform 2. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_047818125 – 540Missing in isoform 5. 2 PublicationsAdd BLAST416
Alternative sequenceiVSP_010263132 – 540Missing in isoform 2 and isoform 6. 2 PublicationsAdd BLAST409
Alternative sequenceiVSP_010264149 – 540Missing in isoform 3. 1 PublicationAdd BLAST392

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
KC415005 mRNA. Translation: AGF94754.1.
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.
UCSCiuc002wjw.5. human. [Q7Z434-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
KC415005 mRNA. Translation: AGF94754.1.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MS7NMR-A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U1-100[»]
2MS8NMR-A1-100[»]
2VGQX-ray2.10A1-93[»]
3J6Celectron microscopy9.60A3-93[»]
3J6Jelectron microscopy3.64A/B/C/D/E/G/I/L1-97[»]
3RC5X-ray1.60B502-508[»]
4P4HX-ray3.40I/J/K/L/M/N/O/P1-99[»]
4Z8MX-ray2.95C/D450-468[»]
5JEKX-ray2.40C/D433-448[»]
ProteinModelPortaliQ7Z434.
SMRiQ7Z434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121570. 80 interactors.
DIPiDIP-35445N.
IntActiQ7Z434. 43 interactors.
MINTiMINT-3034048.
STRINGi9606.ENSP00000401980.

PTM databases

iPTMnetiQ7Z434.
PhosphoSitePlusiQ7Z434.
SwissPalmiQ7Z434.

Polymorphism and mutation databases

BioMutaiMAVS.
DMDMi47115748.

Proteomic databases

EPDiQ7Z434.
MaxQBiQ7Z434.
PaxDbiQ7Z434.
PeptideAtlasiQ7Z434.
PRIDEiQ7Z434.

Protocols and materials databases

DNASUi57506.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000416600; ENSP00000413749; ENSG00000088888. [Q7Z434-4]
ENST00000428216; ENSP00000401980; ENSG00000088888. [Q7Z434-1]
GeneIDi57506.
KEGGihsa:57506.
UCSCiuc002wjw.5. human. [Q7Z434-1]

Organism-specific databases

CTDi57506.
DisGeNETi57506.
GeneCardsiMAVS.
HGNCiHGNC:29233. MAVS.
HPAiCAB009187.
HPA049850.
HPA053524.
MIMi609676. gene.
neXtProtiNX_Q7Z434.
OpenTargetsiENSG00000088888.
PharmGKBiPA164722208.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IS5U. Eukaryota.
ENOG410Y2HK. LUCA.
GeneTreeiENSGT00510000049120.
HOGENOMiHOG000056441.
HOVERGENiHBG079638.
InParanoidiQ7Z434.
KOiK12648.
OMAiEQDTELG.
OrthoDBiEOG091G040S.
PhylomeDBiQ7Z434.
TreeFamiTF333444.

Enzyme and pathway databases

ReactomeiR-HSA-168928. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
R-HSA-5689896. Ovarian tumor domain proteases.
R-HSA-918233. TRAF3-dependent IRF activation pathway.
R-HSA-933541. TRAF6 mediated IRF7 activation.
R-HSA-933542. TRAF6 mediated NF-kB activation.
R-HSA-933543. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
SignaLinkiQ7Z434.
SIGNORiQ7Z434.

Miscellaneous databases

ChiTaRSiMAVS. human.
EvolutionaryTraceiQ7Z434.
GeneWikiiVISA_(gene).
GenomeRNAii57506.
PMAP-CutDBQ7Z434.
PROiQ7Z434.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000088888.
GenevisibleiQ7Z434. HS.

Family and domain databases

InterProiIPR031964. CARD_dom.
IPR026148. Mt_antiviral_sig_pro.
[Graphical view]
PANTHERiPTHR21446. PTHR21446. 2 hits.
PfamiPF16739. CARD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMAVS_HUMAN
AccessioniPrimary (citable) accession number: Q7Z434
Secondary accession number(s): A8K6X0
, B2BD33, B2BD34, F5H6C8, M1P2Z0, 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: November 30, 2016
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.