Q7Z434 (MAVS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MAVS
Synonyms:	IPS1, KIAA1271, VISA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	540 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.2 Ref.3 Ref.4 Ref.21 Ref.28
Subunit structure	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. Ref.1 Ref.2 Ref.3 Ref.4 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.19 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.31
Subcellular location	Mitochondrion outer membrane. Mitochondrion. Peroxisome Ref.1 Ref.28.
Tissue specificity	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. Ref.1 Ref.2 Ref.4
Domain	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.
Post-translational modification	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. Ref.24
Miscellaneous	Cleavage by HCV protease complex leads to inactivation.
Sequence similarities	Contains 1 CARD domain.
Sequence caution	The sequence BAA86585.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB14684.1 differs from that shown. Reason: Frameshift at position 333.

Ontologies

Keywords
Biological process	Antiviral defense Host-virus interaction Immunity Innate immunity
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane Peroxisome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of innate immune response Inferred from mutant phenotype PubMed 18818105. Source: BHF-UCL cellular response to exogenous dsRNA Inferred from mutant phenotype Ref.4. Source: BHF-UCL defense response to bacterium Inferred from mutant phenotype Ref.21. Source: UniProtKB defense response to virus Inferred from direct assay Ref.28. Source: UniProtKB innate immune response Inferred from mutant phenotype PubMed 19609254Ref.21. Source: UniProtKB negative regulation of type I interferon production Traceable author statement. Source: Reactome negative regulation of viral genome replication Inferred from direct assay Ref.28. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of IP-10 production Inferred from direct assay Ref.4. Source: BHF-UCL positive regulation of chemokine (C-C motif) ligand 5 production Inferred from direct assay Ref.4. Source: BHF-UCL positive regulation of defense response to virus by host Inferred from mutant phenotype PubMed 19609254. Source: UniProtKB positive regulation of interferon-alpha production Inferred from mutant phenotype PubMed 19609254. Source: UniProtKB positive regulation of interferon-beta production Inferred from mutant phenotype PubMed 19609254Ref.21. Source: UniProtKB positive regulation of interleukin-8 production Inferred from direct assay Ref.4. Source: BHF-UCL positive regulation of protein import into nucleus, translocation Inferred from direct assay PubMed 18818105. Source: BHF-UCL positive regulation of protein phosphorylation Inferred from direct assay Ref.4. Source: BHF-UCL positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.4. Source: BHF-UCL positive regulation of transcription factor import into nucleus Inferred from direct assay PubMed 18818105. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.4PubMed 18818105. Source: BHF-UCL positive regulation of tumor necrosis factor production Inferred from direct assay Ref.4. Source: BHF-UCL positive regulation of type I interferon-mediated signaling pathway Inferred from direct assay Ref.28. Source: UniProtKB regulation of peroxisome organization Inferred from mutant phenotype Ref.28. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from direct assay PubMed 18818105. Source: BHF-UCL peroxisomal membrane Inferred from direct assay Ref.28. Source: UniProtKB
Molecular_function	signal transducer activity Inferred from mutant phenotype Ref.6Ref.28. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAG6	P46379	2	EBI-995373,EBI-347552
C1QBP	Q07021	5	EBI-995373,EBI-347528
CALCOCO2	Q13137	3	EBI-995373,EBI-739580
DDX3X	O00571	4	EBI-995373,EBI-353779
DDX58	O95786	8	EBI-995373,EBI-995350
IKBKE	Q14164	2	EBI-995373,EBI-307369
IRF5	Q13568	2	EBI-995373,EBI-3931258
OAS3	Q9Y6K5	2	EBI-995373,EBI-6115729
RIPK2	O43353	3	EBI-995373,EBI-358522
STAT1	P42224	3	EBI-995373,EBI-1057697
UBE4A	Q14139	2	EBI-995373,EBI-1048119
X	Q69027	2	EBI-995373,EBI-3650820	From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q7Z434-1)

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.

Isoform 2 (identifier: Q7Z434-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q7Z434-3)

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.

Isoform 4 (identifier: Q7Z434-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 540

540

Mitochondrial antiviral-signaling protein

PRO_0000144096

Regions

Topological domain

1 – 513

513

Cytoplasmic Probable

Transmembrane

514 – 534

21

Helical; Potential

Topological domain

535 – 540

6

Mitochondrial intermembrane Probable

Domain

10 – 77

68

CARD

Region

10 – 77

68

Required for interaction with NLRX1

Region

143 – 147

5

Interaction with TRAF2

Region

153 – 158

6

Interaction with TRAF6

Region

455 – 460

6

Interaction with TRAF6

Compositional bias

103 – 153

51

Pro-rich

Sites

Site

427 – 428

2

Cleavage; by HHAV protein 3ABC

Site

508 – 509

2

Cleavage; by HCV and hepatitis GB virus B NS3/4A protease complex

Amino acid modifications

Modified residue

147

1

Phosphothreonine By similarity

Modified residue

152

1

Phosphoserine Ref.20 Ref.27

Modified residue

157

1

Phosphoserine Ref.20

Modified residue

165

1

Phosphoserine Ref.20 Ref.27

Modified residue

222

1

Phosphoserine Ref.13 Ref.20

Modified residue

233

1

Phosphoserine Ref.20

Modified residue

234

1

Phosphothreonine Ref.20

Modified residue

253

1

Phosphoserine Ref.29

Modified residue

258

1

Phosphoserine Ref.20 Ref.29

Modified residue

373

1

Phosphoserine By similarity

Modified residue

375

1

Phosphoserine By similarity

Modified residue

398

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

1 – 141

141

Missing in isoform 4.

VSP_045872

Alternative sequence

64 – 148

85

RRPGW…VQETQ → LPTWAGEETPGGQSSGRGLD FSSLTSGAVWLWQMSDFWSC FSTWTVSIWLILHWVLLRLN LQVFAKCLAQSKWPLLLPSL SCPTW in isoform 3.

VSP_010261

Alternative sequence

99 – 131

33

TSDRP…SIPYN → ERPALALLDPQPAPWPPLSF SLSLYFLPFSVILFLVTVKR in isoform 2.

VSP_010262

Alternative sequence

132 – 540

409

Missing in isoform 2.

VSP_010263

Alternative sequence

149 – 540

392

Missing in isoform 3.

VSP_010264

Natural variant

79

1

C → F.
Corresponds to variant rs11905552 [ dbSNP | Ensembl ].

VAR_048609

Natural variant

79

1

C → S.
Corresponds to variant rs11908032 [ dbSNP | Ensembl ].

VAR_059197

Natural variant

93

1

Q → E. Ref.2 Ref.4 Ref.7 Ref.10
Corresponds to variant rs17857295 [ dbSNP | Ensembl ].

VAR_048610

Natural variant

198

1

Q → K. Ref.1 Ref.3 Ref.10
Corresponds to variant rs7262903 [ dbSNP | Ensembl ].

VAR_048611

Natural variant

409

1

S → F. Ref.1 Ref.3 Ref.10
Corresponds to variant rs7269320 [ dbSNP | Ensembl ].

VAR_018448

Experimental info

Mutagenesis

54

1

T → A: Impairs ability to induce IFN-beta. Ref.1

Mutagenesis

67 – 69

3

GWV → AAA: Impairs ability to induce IFN-beta. Ref.1

Mutagenesis

145

1

Q → N: No interaction with TRAF2. Ref.2

Mutagenesis

155

1

E → D: No interaction with TRAF6; when associated with D-457. Ref.2

Mutagenesis

427

1

Q → A: No cleavage by HHAV 3ABC. Ref.15

Mutagenesis

435

1

C → R: No effect on cleavage by NS3/4A protease complex. Ref.11

Mutagenesis

452

1

C → R: No effect on cleavage by NS3/4A protease complex. Ref.11

Mutagenesis

457

1

E → D: No interaction with TRAF6; when associated with D-155. Ref.2

Mutagenesis

463

1

E → A: No effect on cleavage by HHAV 3ABC. Ref.15

Mutagenesis

508

1

C → A or R: No cleavage by HCV and hepatitis GB virus B NS3/4A protease complex. Ref.3 Ref.11 Ref.14

Sequence conflict

42

1

L → P in BAC77356. Ref.6

Sequence conflict

191

1

T → N in BAF84474. Ref.7

Sequence conflict

356

1

A → V in BAC77356. Ref.6

Sequence conflict

373

1

S → P in BAC77356. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

540

Helix Strand Turn

Details...

Helix

3 – 14

12

Helix

16 – 19

4

Helix

24 – 27

4

Helix

28 – 30

3

Helix

36 – 49

14

Helix

51 – 62

12

Helix

68 – 78

11

Helix

82 – 92

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2004. Version 2. Checksum: 0E23E3E115941EE8	FASTA	540	56,528
	10 20 30 40 50 60 MPFAEDKTYK YICRNFSNFC NVDVVEILPY LPCLTARDQD RLRATCTLSG NRDTLWHLFN 70 80 90 100 110 120 TLQRRPGWVE YFIAALRGCE LVDLADEVAS VYQSYQPRTS DRPPDPLEPP SLPAERPGPP 130 140 150 160 170 180 TPAAAHSIPY NSCREKEPSY PMPVQETQAP ESPGENSEQA LQTLSPRAIP RNPDGGPLES 190 200 210 220 230 240 SSDLAALSPL TSSGHQEQDT ELGSTHTAGA TSSLTPSRGP VSPSVSFQPL ARSTPRASRL 250 260 270 280 290 300 PGPTGSVVST GTSFSSSSPG LASAGAAEGK QGAESDQAEP IICSSGAEAP ANSLPSKVPT 310 320 330 340 350 360 TLMPVNTVAL KVPANPASVS TVPSKLPTSS KPPGAVPSNA LTNPAPSKLP INSTRAGMVP 370 380 390 400 410 420 SKVPTSMVLT KVSASTVPTD GSSRNEETPA APTPAGATGG SSAWLDSSSE NRGLGSELSK 430 440 450 460 470 480 PGVLASQVDS PFSGCFEDLA ISASTSLGMG PCHGPEENEY KSEGTFGIHV AENPSIQLLE 490 500 510 520 530 540 GNPGPPADPD GGPRPQADRK FQEREVPCHR PSPGALWLQV AVTGVLVVTL LVVLYRRRLH
	Isoform 2 [UniParc]. Checksum: E05D88F9EA1218AA	FASTA	138	15,996
	10 20 30 40 50 60 MPFAEDKTYK YICRNFSNFC NVDVVEILPY LPCLTARDQD RLRATCTLSG NRDTLWHLFN 70 80 90 100 110 120 TLQRRPGWVE YFIAALRGCE LVDLADEVAS VYQSYQPRER PALALLDPQP APWPPLSFSL 130 SLYFLPFSVI LFLVTVKR
	Isoform 3 [UniParc]. Checksum: C1593E51F98F2DCE	FASTA	148	17,043
	10 20 30 40 50 60 MPFAEDKTYK YICRNFSNFC NVDVVEILPY LPCLTARDQD RLRATCTLSG NRDTLWHLFN 70 80 90 100 110 120 TLQLPTWAGE ETPGGQSSGR GLDFSSLTSG AVWLWQMSDF WSCFSTWTVS IWLILHWVLL 130 140 RLNLQVFAKC LAQSKWPLLL PSLSCPTW
	Isoform 4 [UniParc]. Checksum: 4DB7ED11FEA04082	FASTA	399	40,468
	10 20 30 40 50 60 MPVQETQAPE SPGENSEQAL QTLSPRAIPR NPDGGPLESS SDLAALSPLT SSGHQEQDTE 70 80 90 100 110 120 LGSTHTAGAT SSLTPSRGPV SPSVSFQPLA RSTPRASRLP GPTGSVVSTG TSFSSSSPGL 130 140 150 160 170 180 ASAGAAEGKQ GAESDQAEPI ICSSGAEAPA NSLPSKVPTT LMPVNTVALK VPANPASVST 190 200 210 220 230 240 VPSKLPTSSK PPGAVPSNAL TNPAPSKLPI NSTRAGMVPS KVPTSMVLTK VSASTVPTDG 250 260 270 280 290 300 SSRNEETPAA PTPAGATGGS SAWLDSSSEN RGLGSELSKP GVLASQVDSP FSGCFEDLAI 310 320 330 340 350 360 SASTSLGMGP CHGPEENEYK SEGTFGIHVA ENPSIQLLEG NPGPPADPDG GPRPQADRKF 370 380 390 QEREVPCHRP SPGALWLQVA VTGVLVVTLL VVLYRRRLH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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.
[6]	"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.
[7]	"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 AND 4), VARIANT GLU-93. Tissue: Pericardium and Placenta.
[8]	"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].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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.
[15]	"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.
[16]	"The tumour suppressor CYLD is a negative regulator of RIG-I-mediated antiviral response." Friedman C.S., O'Donnell M.A., Legarda-Addison D., Ng A., Cardenas W.B., Yount J.S., Moran T.M., Basler C.F., Komuro A., Horvath C.M., Xavier R., Ting A.T. EMBO Rep. 9:930-936(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CYLD.
[17]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[18]	"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.
[19]	"NLRX1 is a regulator of mitochondrial antiviral immunity." Moore C.B., Bergstralh D.T., Duncan J.A., Lei Y., Morrison T.E., Zimmermann A.G., Accavitti-Loper M.A., Madden V.J., Sun L., Ye Z., Lich J.D., Heise M.T., Chen Z., Ting J.P.-Y. Nature 451:573-577(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NLRX1.
[20]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-157; SER-165; SER-222; SER-233; THR-234 AND SER-258, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[28]	"Peroxisomes are signaling platforms for antiviral innate immunity." Dixit E., Boulant S., Zhang Y., Lee A.S., Odendall C., Shum B., Hacohen N., Chen Z.J., Whelan S.P., Fransen M., Nibert M.L., Superti-Furga G., Kagan J.C. Cell 141:668-681(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[29]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

DQ174270 mRNA. Translation: AAZ80417.1.
DQ167126 mRNA. Translation: ABA54890.1.
DQ181928 mRNA. Translation: ABA19229.1.
AB232371 mRNA. Translation: BAE79738.1.
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.
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.

IPI

IPI00020719.
IPI00411576.
IPI00411577.
IPI01012141.

RefSeq

NP_001193420.1. NM_001206491.1.
NP_065797.2. NM_020746.4.

UniGene

Hs.570362.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VGQ	X-ray	2.10	A	3-93	[»]

ProteinModelPortal

Q7Z434.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35445N.

IntAct

Q7Z434. 26 interactions.

MINT

MINT-3034048.

PTM databases

PhosphoSite

Q7Z434.

Polymorphism databases

DMDM

47115748.

Proteomic databases

PaxDb

Q7Z434.

PeptideAtlas

Q7Z434.

PRIDE

Q7Z434.

Protocols and materials databases

DNASU

57506.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000416600; ENSP00000413749; ENSG00000088888.
ENST00000428216; ENSP00000401980; ENSG00000088888.

GeneID

57506.

KEGG

hsa:57506.

UCSC

uc002wjv.3. human.
uc002wjw.4. human.

Organism-specific databases

CTD

57506.

GeneCards

GC20P003827.

HGNC

HGNC:29233. MAVS.

HPA

CAB009187.

MIM

609676. gene.

neXtProt

NX_Q7Z434.

PharmGKB

PA164722208.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG79681.

HOVERGEN

HBG079638.

InParanoid

Q7Z434.

KO

K12648.

OMA

PINSTRA.

OrthoDB

EOG42BX8F.

PhylomeDB

Q7Z434.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q7Z434.

Bgee

Q7Z434.

Genevestigator

Q7Z434.

GermOnline

ENSG00000088888. Homo sapiens.

Family and domain databases

InterPro

IPR026148. Mt_antiviral_sig_pro.
[Graphical view]

PANTHER

PTHR21446. PTHR21446. 1 hit.

PROSITE

PS50209. CARD. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MAVS. human.

EvolutionaryTrace

Q7Z434.

GenomeRNAi

57506.

NextBio

35464378.

PMAP-CutDB

Q7Z434.

SOURCE

Search...

Entry information

Entry name

MAVS_HUMAN

Accession

Primary (citable) accession number: Q7Z434
Secondary accession number(s): A8K6X0 , F5H6C8, Q2HWT5, Q3I0Y2, Q5T7I6, Q86VY7, Q9H1H3, Q9H4Y1, Q9H8D3, Q9ULE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 10, 2004
Last modified:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.