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Reviewed, UniProtKB/Swiss-Prot Q7Z434 (MAVS_HUMAN)

Last modified January 19, 2010. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mitochondrial antiviral-signaling protein
Alternative name(s):
    Interferon-beta promoter stimulator protein 1
      Short name=IPS-1
    Virus-induced-signaling adapter
    CARD adapter inducing interferon-beta
      Short name=Cardif
    Putative NF-kappa-B-activating protein 031N
Gene names
Name: MAVS
Synonyms: IPS1, KIAA1271, VISA
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required for innate immune defense against viruses. Acts downstream of DDX58 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). 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.22

Subunit structure

Interacts with DDX58, IFIH1, TRAF2 and TRAF6. May interact with IRF3, FADD, RIPK1, IKBKE, CHUK and IKBKB. Does not interact with TBK1. 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. Ref.1 Ref.2 Ref.3 Ref.4 Ref.11 Ref.13 Ref.14 Ref.18

Subcellular location

Mitochondrion outer membrane Ref.1.

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 and IFIH1.

Miscellaneous

Cleavage by HCV protease complex leads to inactivation.

Sequence similarities

Contains 1 CARD domain.

Sequence caution

The sequence BAB14684.1 differs from that shown. Reason: Frameshift at position 333.

Ontologies

Keywords
   Biological processAntiviral defense
Host-virus interaction
Immune response
Innate immunity
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processdefense response to bacterium Ref.22

Inferred from mutant phenotype. Source: UniProtKB

innate immune response Ref.22

Inferred from mutant phenotype. Source: UniProtKB

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of I-kappaB kinase/NF-kappaB cascade Ref.6

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of defense response to virus by host

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of interferon-alpha production

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of interferon-beta production Ref.22

Inferred from mutant phenotype. Source: UniProtKB

response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding Ref.3

Inferred from physical interaction. Source: IntAct

signal transducer activity Ref.6

Inferred from mutant phenotype. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 540540Mitochondrial antiviral-signaling protein
PRO_0000144096

Regions

Topological domain1 – 513513Cytoplasmic Probable
Transmembrane514 – 53421 Potential
Topological domain535 – 5406Mitochondrial intermembrane Probable
Domain10 – 7768CARD
Region10 – 7768Required for interaction with NLRX1
Region143 – 1475Interaction with TRAF2
Region153 – 1586Interaction with TRAF6
Region455 – 4606Interaction with TRAF6
Compositional bias103 – 15351Pro-rich

Sites

Site427 – 4282Cleavage; by HHAV protein 3ABC
Site508 – 5092Cleavage; by HCV and hepatitis GB virus B NS3/4A protease complex

Amino acid modifications

Modified residue1471Phosphothreonine By similarity
Modified residue1521Phosphoserine Ref.17 Ref.19 Ref.24
Modified residue1571Phosphoserine Ref.19
Modified residue1631Phosphothreonine Ref.19
Modified residue1651Phosphoserine Ref.17 Ref.19 Ref.24
Modified residue2221Phosphoserine Ref.17 Ref.19 Ref.24 Ref.12 Ref.15 Ref.16 Ref.21
Modified residue2331Phosphoserine Ref.19
Modified residue2341Phosphothreonine Ref.19
Modified residue2531Phosphoserine Ref.19
Modified residue2581Phosphoserine Ref.19
Modified residue3661Phosphoserine By similarity
Modified residue3731Phosphoserine By similarity
Modified residue3751Phosphoserine By similarity
Modified residue3981Phosphothreonine By similarity

Natural variations

Alternative sequence64 – 14885RRPGW…VQETQ → LPTWAGEETPGGQSSGRGLD FSSLTSGAVWLWQMSDFWSC FSTWTVSIWLILHWVLLRLN LQVFAKCLAQSKWPLLLPSL SCPTW in isoform 3.
VSP_010261
Alternative sequence99 – 13133TSDRP…SIPYN → ERPALALLDPQPAPWPPLSF SLSLYFLPFSVILFLVTVKR in isoform 2.
VSP_010262
Alternative sequence132 – 540409Missing in isoform 2.
VSP_010263
Alternative sequence149 – 540392Missing in isoform 3.
VSP_010264
Natural variant791C → F: dbSNP rs11905552.
VAR_048609
Natural variant791C → S: dbSNP rs11908032.
VAR_059197
Natural variant931Q → E: dbSNP rs17857295. Ref.2 Ref.4 Ref.7 Ref.10
VAR_048610
Natural variant1981Q → K: dbSNP rs7262903. Ref.1 Ref.3 Ref.10
VAR_048611
Natural variant4091S → F: dbSNP rs7269320. Ref.1 Ref.3 Ref.10
VAR_018448

Experimental info

Mutagenesis541T → A: Impairs ability to induce IFN-beta. Ref.1
Mutagenesis67 – 693GWV → AAA: Impairs ability to induce IFN-beta. Ref.1
Mutagenesis1451Q → N: No interaction with TRAF2. Ref.2
Mutagenesis1551E → D: No interaction with TRAF6; when associated with D-457. Ref.2
Mutagenesis4271Q → A: No cleavage by HHAV 3ABC. Ref.14
Mutagenesis4351C → R: No effect on cleavage by NS3/4A protease complex. Ref.11
Mutagenesis4521C → R: No effect on cleavage by NS3/4A protease complex. Ref.11
Mutagenesis4571E → D: No interaction with TRAF6; when associated with D-155. Ref.2
Mutagenesis4631E → A: No effect on cleavage by HHAV 3ABC. Ref.14
Mutagenesis5081C → A or R: No cleavage by HCV and hepatitis GB virus B NS3/4A protease complex. Ref.3 Ref.11 Ref.13
Sequence conflict421L → P in BAC77356. Ref.6
Sequence conflict3561A → V in BAC77356. Ref.6
Sequence conflict3731S → P in BAC77356. Ref.6

Secondary structure

................ 540
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 0E23E3E115941EE8

FASTA54056,528
        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 

« Hide

Isoform 2.

Checksum: E05D88F9EA1218AA
Show »

FASTA13815,996
Isoform 3.

Checksum: C1593E51F98F2DCE
Show »

FASTA14817,043

References

« Hide '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: 16125763] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF THR-54 AND 67-GLY--VAL-69, INTERACTION WITH DDX58 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: 16153868] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH DDX58; 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: 16177806] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDX58; 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: 16127453] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH DDX58; IFIH1; 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: 10574462] [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: 12761501] [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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), 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. expand/collapse author list , 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: 11780052] [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. expand/collapse author list , 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: 15489334] [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: 16301520] [Abstract]
Cited for: INTERACTION WITH HCV NS3/4A PROTEASE, CLEAVAGE SITE, MUTAGENESIS OF CYS-435; CYS-452 AND CYS-508.
[12]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"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: 17093192] [Abstract]
Cited for: INTERACTION WITH HEPATITIS GB VIRUS B NS3/4A PROTEASE, CLEAVAGE SITE, MUTAGENESIS OF CYS-508.
[14]"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: 17438296] [Abstract]
Cited for: INTERACTION WITH HUMAN HEPATITIS A VIRUS PROTEIN 3ABC, CLEAVAGE SITE, MUTAGENESIS OF GLN-427 AND GLU-463.
[15]"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: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, MASS SPECTROMETRY.
Tissue: Platelet.
[16]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, MASS SPECTROMETRY.
[17]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-165 AND SER-222, MASS SPECTROMETRY.
[18]"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: 18200010] [Abstract]
Cited for: INTERACTION WITH NLRX1.
[19]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-157; THR-163; SER-165; SER-222; SER-233; THR-234; SER-253 AND SER-258, MASS SPECTROMETRY.
[20]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, MASS SPECTROMETRY.
[22]"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: 19631370] [Abstract]
Cited for: FUNCTION.
[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: 19734229] [Abstract]
Cited for: INTERACTION WITH PSMA7.
[24]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-165 AND SER-222, MASS SPECTROMETRY.
Tissue: T-cell.
+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.
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.
IPIIPI00020719.
IPI00411576.
IPI00411577.
RefSeqNP_065797.2.
UniGeneHs.570362

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VGQX-ray2.10A3-93[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35445N.
IntActQ7Z434. 4 interactions.
STRINGQ7Z434.

PTM databases

PhosphoSiteQ7Z434.

Proteomic databases

PeptideAtlasQ7Z434.
PRIDEQ7Z434.

Genome annotation databases

EnsemblENST00000428216; ENSP00000401980; ENSG00000088888; Homo sapiens. [Genome view]
GeneID57506.
KEGGhsa:57506.
UCSCuc002wjv.2. human.
uc002wjw.2. human.

Organism-specific databases

CTD57506.
GeneCardsGC20P003782.
HGNCHGNC:29233. MAVS.
HPACAB009187.
MIM609676. gene.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08143.
HOVERGENQ7Z434.
InParanoidQ7Z434.
OMALPINSTR.
OrthoDBEOG91ZHWH.
PhylomeDBQ7Z434.

Gene expression databases

ArrayExpressQ7Z434.
BgeeQ7Z434.
GenevestigatorQ7Z434.
GermOnlineENSG00000088888. Homo sapiens.

Family and domain databases

PROSITEPS50209. CARD. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio63845.
PMAP-CutDBQ7Z434.
SOURCESearch...

Entry information

Entry nameMAVS_HUMAN
AccessionPrimary (citable) accession number: Q7Z434
Secondary accession number(s): Q2HWT5 expand/collapse secondary AC list , 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: January 19, 2010
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents