MAVS
entrez
57506
canonical
uniprot
Q7Z434
canonical
ensembl
ENSG00000088888
resolver
ensp
ENSP00000401980
resolver
ensp
ENSP00000413749
resolver
genesymbol
MAVS
resolver
genesymbol_syn
IPS1
resolver
genesymbol_syn
KIAA1271
resolver
genesymbol_syn
VISA
resolver
hgnc
HGNC:29233
resolver
uniprot
A8K6X0
resolver
uniprot
B2BD33
resolver
uniprot
B2BD34
resolver
uniprot
F5H6C8
resolver
uniprot
M1P2Z0
resolver
uniprot
Q2HWT5
resolver
uniprot
Q3I0Y2
resolver
uniprot
Q5T7I6
resolver
uniprot
Q86VY7
resolver
uniprot
Q9H1H3
resolver
uniprot
Q9H4Y1
resolver
uniprot
Q9H8D3
resolver
uniprot
Q9ULE9
resolver
uniprot_entry
MAVS_HUMAN
resolver
uniprot_sec
A8K6X0
resolver
uniprot_sec
B2BD33
resolver
uniprot_sec
B2BD34
resolver
uniprot_sec
F5H6C8
resolver
uniprot_sec
M1P2Z0
resolver
uniprot_sec
Q2HWT5
resolver
uniprot_sec
Q3I0Y2
resolver
uniprot_sec
Q5T7I6
resolver
uniprot_sec
Q86VY7
resolver
uniprot_sec
Q9H1H3
resolver
uniprot_sec
Q9H4Y1
resolver
uniprot_sec
Q9H8D3
resolver
uniprot_sec
Q9ULE9
resolver
amino_acid_sequence
MPFAEDKTYKYICRNFSNFCNVDVVEILPYLPCLTARDQDRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYNSCREKEPSYPMPVQETQAPESPGENSEQALQTLSPRAIPRNPDGGPLESSSDLAALSPLTSSGHQEQDTELGSTHTAGATSSLTPSRGPVSPSVSFQPLARSTPRASRLPGPTGSVVSTGTSFSSSSPGLASAGAAEGKQGAESDQAEPIICSSGAEAPANSLPSKVPTTLMPVNTVALKVPANPASVSTVPSKLPTSSKPPGAVPSNALTNPAPSKLPINSTRAGMVPSKVPTSMVLTKVSASTVPTDGSSRNEETPAAPTPAGATGGSSAWLDSSSENRGLGSELSKPGVLASQVDSPFSGCFEDLAISASTSLGMGPCHGPEENEYKSEGTFGIHVAENPSIQLLEGNPGPPADPDGGPRPQADRKFQEREVPCHRPSPGALWLQVAVTGVLVVTLLVVLYRRRLH
uniprot
proteins
function
FUNCTION: Adapter required for innate immune defense against viruses (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:21170385, PubMed:23087404, PubMed:27992402, PubMed:33139700, PubMed:37582970, PubMed:39589880, PubMed:38995016). Acts downstream of DHX33, RIGI 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 IFNB and RANTES (CCL5) (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:20628368, PubMed:21170385, PubMed:23087404, PubMed:25636800, PubMed:27736772, PubMed:33110251, PubMed:40042308). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state (PubMed:20451243). 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 (PubMed:20451243). May activate the same pathways following detection of extracellular dsRNA by TLR3 (PubMed:16153868). May protect cells from apoptosis (PubMed:16125763). Involved in NLRP3 inflammasome activation by mediating NLRP3 recruitment to mitochondria (PubMed:23582325). {ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20451243, ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:23087404, ECO:0000269|PubMed:23582325, ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27736772, ECO:0000269|PubMed:27992402, ECO:0000269|PubMed:33110251, ECO:0000269|PubMed:33139700, ECO:0000269|PubMed:37582970, ECO:0000269|PubMed:38995016, ECO:0000269|PubMed:39589880, ECO:0000269|PubMed:40042308}.
uniprot
proteins
mass_dalton
56528
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="K->R: Abolished ubiquitination by MARCHF5; when associated with R-500."; /evidence="ECO:0000269|PubMed:26246171"; MUTAGEN 10; /note="K->R: Abolished ubiquitination by TRIM31; when associated with R-311 and R-461."; /evidence="ECO:0000269|PubMed:23582325"; MUTAGEN 26; /note="E->A,R: Impairs filament formation and abolishes antiviral signaling activity."; /evidence="ECO:0000269|PubMed:24569476"; MUTAGEN 54; /note="T->A: Impairs ability to induce IFN-beta. Loss of interaction with the ATG5-ATG12 conjugate."; /evidence="ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:17709747"; MUTAGEN 56; /note="W->A,E,R: Impairs filament formation and abolishes antiviral signaling activity."; /evidence="ECO:0000269|PubMed:24569476"; MUTAGEN 67..69; /note="GWV->AAA: Impairs ability to induce IFN-beta."; /evidence="ECO:0000269|PubMed:16125763"; MUTAGEN 145; /note="Q->N: No interaction with TRAF2."; /evidence="ECO:0000269|PubMed:16153868"; MUTAGEN 148; /note="Q->A: Complete loss of cleavage by Seneca Valley virus protease 3C."; /evidence="ECO:0000269|PubMed:28566380"; MUTAGEN 155; /note="E->D: No interaction with TRAF6; when associated with D-457."; /evidence="ECO:0000269|PubMed:16153868"; MUTAGEN 159; /note="Q->A: No effect on cleavage by Seneca Valley virus protease 3C."; /evidence="ECO:0000269|PubMed:28566380"; MUTAGEN 162; /note="Q->A: No effect on cleavage by Seneca Valley virus protease 3C."; /evidence="ECO:0000269|PubMed:28566380"; MUTAGEN 196; /note="Q->A: No effect on cleavage by Seneca Valley virus protease 3C."; /evidence="ECO:0000269|PubMed:28566380"; MUTAGEN 198; /note="Q->A: No effect on cleavage by Seneca Valley virus protease 3C."; /evidence="ECO:0000269|PubMed:28566380"; MUTAGEN 209; /note="G->A: Complete loss of cleavage by protease 2A of enterovirus 71."; /evidence="ECO:0000269|PubMed:28253362"; MUTAGEN 251; /note="G->A: Complete loss of cleavage by protease 2A of enterovirus 71."; /evidence="ECO:0000269|PubMed:28253362"; MUTAGEN 265; /note="G->A: Complete loss of cleavage by enterovirus 71."; /evidence="ECO:0000269|PubMed:28253362"; MUTAGEN 311; /note="K->R: Abolished ubiquitination by TRIM31; when associated with R-10 and R-461."; /evidence="ECO:0000269|PubMed:23582325"; MUTAGEN 325; /note="K->R: Abolished ubiquitination by TRIM21."; /evidence="ECO:0000269|PubMed:29743353"; MUTAGEN 427; /note="Q->A: No cleavage by HHAV 3ABC."; /evidence="ECO:0000269|PubMed:17438296"; MUTAGEN 429; /note="D->A: Decreased cleavage by CASP3. Abolished cleavage by CASP3; when associated with A-490."; /evidence="ECO:0000269|PubMed:30878284"; MUTAGEN 435; /note="C->R: No effect on cleavage by NS3/4A protease complex."; /evidence="ECO:0000269|PubMed:16301520"; MUTAGEN 442; /note="S->A: Abolished ability to bind and activate IRF3."; /evidence="ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27302953"; MUTAGEN 452; /note="C->R: No effect on cleavage by NS3/4A protease complex."; /evidence="ECO:0000269|PubMed:16301520"; MUTAGEN 457; /note="E->D: No interaction with TRAF6; when associated with D-155."; /evidence="ECO:0000269|PubMed:16153868"; MUTAGEN 461; /note="K->R: Abolished ubiquitination by TRIM31; when associated with R-10 and R-311. Abolished UFMylation by UFM1."; /evidence="ECO:0000269|PubMed:23582325, ECO:0000269|PubMed:37311461"; MUTAGEN 463; /note="E->A: No effect on cleavage by HHAV 3ABC."; /evidence="ECO:0000269|PubMed:17438296"; MUTAGEN 490; /note="D->A: Decreased cleavage by CASP3. Abolished cleavage by CASP3; when associated with A-429."; /evidence="ECO:0000269|PubMed:30878284"; MUTAGEN 500; /note="K->R: Abolished ubiquitination by MARCH5; when associated with R-7."; /evidence="ECO:0000269|PubMed:26246171"; MUTAGEN 508; /note="C->A,R: No cleavage by HCV and hepatitis GB virus BNS3/4A protease complex."; /evidence="ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:16301520, ECO:0000269|PubMed:17093192
uniprot
proteins
post_translational_modification
PTM: Following activation, phosphorylated by TBK1 at Ser-442 in the pLxIS motif (PubMed:25636800, PubMed:27302953). The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (PubMed:25636800). {ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27302953}.; PTM: Ubiquitinated (PubMed:19881509, PubMed:23087404, PubMed:25636800, PubMed:38016475). 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). Undergoes 'Lys-48'-linked ubiquitination catalyzed by MARCHF5 at Lys-7 and Lys-500, leading to proteasomal degradation (PubMed:26246171). Ubiquitinated via 'Lys-63'-linked ubiquitination at Lys-10, Lys-311 and Lys-461 by UBE2N and TRIM31, promoting MAVS polymerization and formation of three-stranded helical filaments on mitochondria (PubMed:27992402, PubMed:37582970). Undergoes 'Lys-63'-linked ubiquitination leading to enhanced interaction between MAVS and TRAF2 (PubMed:34880843). Undergoes 'Lys-27'-linked ubiquitination by TRIM21 leading to enhanced interaction between MAVS and TBK1 (PubMed:29743353, PubMed:36943869). Deubiquitinated by USP10 leading to attenuation of RIGI-mediated MAVS aggregation and production of type I interferon (PubMed:37582970). Undergoes 'Lys-48'-linked polyubiquitination catalyzed by RNF115 leading to its degradation (PubMed:33139700). Deubiquitinated by USP4 at Lys-461, leading to maintain MAVS protein stability, resulting in increased production of type I interferons (IFN-I) and enhanced antiviral innate immune responses against viral infections (PubMed:39589880). {ECO:0000269|PubMed:17460044, ECO:0000269|PubMed:19881509, ECO:0000269|PubMed:23087404, ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:26246171, ECO:0000269|PubMed:27992402, ECO:0000269|PubMed:29743353, ECO:0000269|PubMed:33139700, ECO:0000269|PubMed:34880843, ECO:0000269|PubMed:36943869, ECO:0000269|PubMed:37582970, ECO:0000269|PubMed:38016475, ECO:0000269|PubMed:39589880}.; PTM: Palmitoylated by ZHDDC4. Palmitoylation promotes MAVS stabilization and activation by inhibiting 'Lys-48'- but facilitating 'Lys-63'-linked ubiquitination. {ECO:0000269|PubMed:38016475}.; PTM: Proteolytically cleaved by apoptotic caspases during apoptosis, leading to its inactivation (PubMed:30878284). Cleavage by CASP3 during virus-induced apoptosis inactivates it, preventing cytokine overproduction (PubMed:30878284). {ECO:0000269|PubMed:30878284}.; PTM: (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. {ECO:0000269|PubMed:17438296}.; PTM: (Microbial infection) Cleaved by the protease 2A of coxsackievirus B3, poliovirus and enterovirus 71 allowing the virus to disrupt the host type I interferon production. {ECO:0000269|PubMed:24390337, ECO:0000269|PubMed:28253362}.; PTM: (Microbial infection) Cleaved by Seneca Valley virus protease 3C allowing the virus to suppress interferon type-I production. {ECO:0000269|PubMed:28566380}.; PTM: (Microbial infection) Cleaved by HCV protease NS3/4A, thereby preventing the establishment of an antiviral state. {ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:16301520}.; PTM: (Microbial infection) UFMylated by ULF1 in association with Epstein-Barr virus BILF1; leading to MAVS routing to the lysosome. {ECO:0000269|PubMed:37311461}.
uniprot
proteins
pubmed
10574462
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
12761501
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16125763
uniprot
proteins
pubmed
16127453
uniprot
proteins
pubmed
16153868
uniprot
proteins
pubmed
16177806
uniprot
proteins
pubmed
16301520
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17020950
uniprot
proteins
pubmed
17093192
uniprot
proteins
pubmed
17438296
uniprot
proteins
pubmed
17460044
uniprot
proteins
pubmed
17600090
uniprot
proteins
pubmed
17709747
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18200010
uniprot
proteins
pubmed
18207245
uniprot
proteins
pubmed
18636086
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19164550
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19416887
uniprot
proteins
pubmed
19419966
uniprot
proteins
pubmed
19631370
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19734229
uniprot
proteins
pubmed
19881509
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20127681
uniprot
proteins
pubmed
20451243
uniprot
proteins
pubmed
20628368
uniprot
proteins
pubmed
21170385
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21436888
uniprot
proteins
pubmed
21813773
uniprot
proteins
pubmed
22383950
uniprot
proteins
pubmed
22427742
uniprot
proteins
pubmed
23087404
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23399697
uniprot
proteins
pubmed
23545497
uniprot
proteins
pubmed
23582325
uniprot
proteins
pubmed
23711367
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24390337
uniprot
proteins
pubmed
24569476
uniprot
proteins
pubmed
25018021
uniprot
proteins
pubmed
25135833
uniprot
proteins
pubmed
25228397
uniprot
proteins
pubmed
25636800
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26246171
uniprot
proteins
pubmed
27302953
uniprot
proteins
pubmed
27736772
uniprot
proteins
pubmed
27980081
uniprot
proteins
pubmed
27992402
uniprot
proteins
pubmed
28011935
uniprot
proteins
pubmed
28253362
uniprot
proteins
pubmed
28414768
uniprot
proteins
pubmed
28566380
uniprot
proteins
pubmed
29743353
uniprot
proteins
pubmed
30878284
uniprot
proteins
pubmed
31390091
uniprot
proteins
pubmed
31522117
uniprot
proteins
pubmed
32321811
uniprot
proteins
pubmed
33110251
uniprot
proteins
pubmed
33139700
uniprot
proteins
pubmed
33232374
uniprot
proteins
pubmed
34880843
uniprot
proteins
pubmed
36943869
uniprot
proteins
pubmed
37311461
uniprot
proteins
pubmed
37316325
uniprot
proteins
pubmed
37582970
uniprot
proteins
pubmed
37656786
uniprot
proteins
pubmed
38016475
uniprot
proteins
pubmed
38995016
uniprot
proteins
pubmed
39037956
uniprot
proteins
pubmed
39589880
uniprot
proteins
pubmed
40042308
uniprot
proteins
pubmed
40105103
uniprot
proteins
sequence_length
540
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:16125763}; Single-pass membrane protein {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:11780052, ECO:0000269|PubMed:17709747, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:23582325, ECO:0000269|PubMed:25135833, ECO:0000269|PubMed:27736772, ECO:0000269|PubMed:37311461, ECO:0000269|PubMed:40042308}. Peroxisome {ECO:0000269|PubMed:20451243}.
uniprot
proteins
transmembrane_region
TRANSMEM 514..534; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins