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Entry version 165 (13 Feb 2019)
Sequence version 2 (10 May 2004)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Required for innate immune defense against viruses. Acts downstream of DHX33, DDX58/RIG-I and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFN-beta and RANTES (CCL5). 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.By similarity7 Publications

Miscellaneous

Cleavage by HCV protease complex leads to inactivation.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processAntiviral defense, Host-virus interaction, Immunity, Innate immunity

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-168928 DDX58/IFIH1-mediated induction of interferon-alpha/beta
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 DDX58/IFIH1 signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q7Z434

SIGNOR Signaling Network Open Resource

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SIGNORi
Q7Z434

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Mitochondrial antiviral-signaling proteinCurated
Short name:
MAVSCurated
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MAVSImported
Synonyms:IPS1, KIAA1271, VISA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000088888.17

Human Gene Nomenclature Database

More...
HGNCi
HGNC:29233 MAVS

Online Mendelian Inheritance in Man (OMIM)

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MIMi
609676 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q7Z434

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 513CytoplasmicCuratedAdd BLAST513
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei514 – 534HelicalSequence analysisAdd BLAST21
Topological domaini535 – 540Mitochondrial intermembraneCurated6

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi26E → A or R: Impairs filament formation and abolishes antiviral signaling activity. 1 Publication1
Mutagenesisi54T → A: Impairs ability to induce IFN-beta. Loss of interaction with the ATG5-ATG12 conjugate. 2 Publications1
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

DisGeNET

More...
DisGeNETi
57506

Open Targets

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OpenTargetsi
ENSG00000088888

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA164722208

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
MAVS

Domain mapping of disease mutations (DMDM)

More...
DMDMi
47115748

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001440961 – 540Mitochondrial antiviral-signaling proteinAdd BLAST540

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

(Microbial infection) Cleaved and degraded by hepatitis A virus (HAV) protein 3ABC allowing the virus to disrupt the activation of host IRF3 through the MDA5 pathway.1 Publication
Ubiquitinated (PubMed:19881509, PubMed:23087404). 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 (PubMed:19881509). Ubiquitinated by RNF125, leading to its degradation by the proteasome (PubMed:17460044). Undergoes 'Lys-48'-linked ubiquitination catalyzed by SMURF1 (PubMed:23087404).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei427 – 428Cleavage; by HAV protein 3ABC1 Publication2
Sitei508 – 509Cleavage; by HCV and hepatitis GB virus B NS3/4A protease complex2

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q7Z434

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q7Z434

MaxQB - The MaxQuant DataBase

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MaxQBi
Q7Z434

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q7Z434

PeptideAtlas

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PeptideAtlasi
Q7Z434

PRoteomics IDEntifications database

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PRIDEi
Q7Z434

ProteomicsDB human proteome resource

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ProteomicsDBi
69137
69138 [Q7Z434-2]
69139 [Q7Z434-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q7Z434

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q7Z434

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q7Z434

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q7Z434

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000088888 Expressed in 229 organ(s), highest expression level in caecum

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q7Z434 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB009187
HPA049850
HPA053524

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 NDFIP1 (PubMed:23087404). Interacts with SMURF1; the interaction is mediated by NDFIP1 and leads to MAVS ubiquitination and degradation (PubMed:23087404). Interacts with UBXN1; this interaction inhibits MAVS-mediated antiviral pathway (PubMed:23545497). Interacts (via C-terminus) with GPATCH3; the interaction is markedly increased upon viral infection (PubMed:28414768). Directly interacts (via CARD domain) with ATG5 and ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5 conjugates (PubMed:17709747). Interacts with DHX33 (via the helicase C-terminal domain) (By similarity).By similarity22 Publications
(Microbial infection) Interacts with hepatitis C/HCV NS3/4A protease; this interaction leads to MAVS cleavage.1 Publication
(Microbial infection) Interacts with hepatitis GB virus B NS3/4A protease; this interaction leads to MAVS cleavage.1 Publication
(Microbial infection) Interacts with human respiratory syncytial virus/HRSV protein NS1; this interaction disrupts MAVS binding to DDX58/RIG-I.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
121570, 109 interactors

Database of interacting proteins

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DIPi
DIP-35445N

Protein interaction database and analysis system

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IntActi
Q7Z434, 61 interactors

Molecular INTeraction database

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MINTi
Q7Z434

STRING: functional protein association networks

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STRINGi
9606.ENSP00000401980

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1540
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q7Z434

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q7Z434

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q7Z434

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini10 – 77CARDAdd BLAST68

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi103 – 153Pro-richAdd BLAST51

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Both CARD and transmembrane domains are essential for antiviral function. The CARD domain is responsible for interaction with DDX58/RIG-I and IFIH1/MDA5.1 Publication
The transmembrane domain and residues 300-444 are essential for its interaction with DHX58/LGP2.1 Publication

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IS5U Eukaryota
ENOG410Y2HK LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00510000049120

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000056441

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG079638

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q7Z434

KEGG Orthology (KO)

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KOi
K12648

Identification of Orthologs from Complete Genome Data

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OMAi
YPMPVQE

Database of Orthologous Groups

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OrthoDBi
887440at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q7Z434

TreeFam database of animal gene trees

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TreeFami
TF333444

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR031964 CARD_dom
IPR026148 Mt_antiviral_sig_pro

The PANTHER Classification System

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PANTHERi
PTHR21446 PTHR21446, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF16739 CARD_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04860979C → F. Corresponds to variant dbSNP:rs11905552Ensembl.1
Natural variantiVAR_05919779C → S. Corresponds to variant dbSNP:rs11908032Ensembl.1
Natural variantiVAR_04861093Q → E4 PublicationsCorresponds to variant dbSNP:rs17857295Ensembl.1
Natural variantiVAR_048611198Q → K3 PublicationsCorresponds to variant dbSNP:rs7262903Ensembl.1
Natural variantiVAR_018448409S → F3 PublicationsCorresponds to variant dbSNP:rs7269320Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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
AL109804 Genomic DNA No translation available.
AL353194 Genomic DNA No translation available.
CH471133 Genomic DNA Translation: EAX10481.1
BC044952 mRNA Translation: AAH44952.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS33437.1 [Q7Z434-1]
CCDS56176.1 [Q7Z434-4]

NCBI Reference Sequences

More...
RefSeqi
NP_001193420.1, NM_001206491.1 [Q7Z434-4]
NP_065797.2, NM_020746.4 [Q7Z434-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.570362

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000416600; ENSP00000413749; ENSG00000088888 [Q7Z434-4]
ENST00000428216; ENSP00000401980; ENSG00000088888 [Q7Z434-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
57506

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:57506

UCSC genome browser

More...
UCSCi
uc002wjw.5 human [Q7Z434-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
AL109804 Genomic DNA No translation available.
AL353194 Genomic DNA No translation available.
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, 109 interactors
DIPiDIP-35445N
IntActiQ7Z434, 61 interactors
MINTiQ7Z434
STRINGi9606.ENSP00000401980

PTM databases

iPTMnetiQ7Z434
PhosphoSitePlusiQ7Z434
SwissPalmiQ7Z434

Polymorphism and mutation databases

BioMutaiMAVS
DMDMi47115748

Proteomic databases

EPDiQ7Z434
jPOSTiQ7Z434
MaxQBiQ7Z434
PaxDbiQ7Z434
PeptideAtlasiQ7Z434
PRIDEiQ7Z434
ProteomicsDBi69137
69138 [Q7Z434-2]
69139 [Q7Z434-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
57506
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

Comparative Toxicogenomics Database

More...
CTDi
57506
DisGeNETi57506
EuPathDBiHostDB:ENSG00000088888.17

GeneCards: human genes, protein and diseases

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GeneCardsi
MAVS
HGNCiHGNC:29233 MAVS
HPAiCAB009187
HPA049850
HPA053524
MIMi609676 gene
neXtProtiNX_Q7Z434
OpenTargetsiENSG00000088888
PharmGKBiPA164722208

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IS5U Eukaryota
ENOG410Y2HK LUCA
GeneTreeiENSGT00510000049120
HOGENOMiHOG000056441
HOVERGENiHBG079638
InParanoidiQ7Z434
KOiK12648
OMAiYPMPVQE
OrthoDBi887440at2759
PhylomeDBiQ7Z434
TreeFamiTF333444

Enzyme and pathway databases

ReactomeiR-HSA-168928 DDX58/IFIH1-mediated induction of interferon-alpha/beta
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 DDX58/IFIH1 signaling
SignaLinkiQ7Z434
SIGNORiQ7Z434

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
MAVS human
EvolutionaryTraceiQ7Z434

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
VISA_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
57506
PMAP-CutDBiQ7Z434

Protein Ontology

More...
PROi
PR:Q7Z434

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000088888 Expressed in 229 organ(s), highest expression level in caecum
GenevisibleiQ7Z434 HS

Family and domain databases

InterProiView protein in InterPro
IPR031964 CARD_dom
IPR026148 Mt_antiviral_sig_pro
PANTHERiPTHR21446 PTHR21446, 1 hit
PfamiView protein in Pfam
PF16739 CARD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMAVS_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q7Z434
Secondary accession number(s): A8K6X0
, B2BD33, B2BD34, F5H6C8, M1P2Z0, Q2HWT5, Q3I0Y2, Q5T7I6, Q86VY7, Q9H1H3, Q9H4Y1, Q9H8D3, Q9ULE9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: February 13, 2019
This is version 165 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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