MAVS_MOUSE - dbPTM
MAVS_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAVS_MOUSE
UniProt AC Q8VCF0
Protein Name Mitochondrial antiviral-signaling protein {ECO:0000305}
Gene Name Mavs {ECO:0000312|MGI:MGI:2444773}
Organism Mus musculus (Mouse).
Sequence Length 503
Subcellular Localization Mitochondrion outer membrane . Mitochondrion . Peroxisome .
Protein Description 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 similarity)..
Protein Sequence MTFAEDKTYKYIRDNHSKFCCVDVLEILPYLSCLTASDQDRLRASYRQIGNRDTLWGLFNNLQRRPGWVEVFIRALQICELPGLADQVTRVYQSYLPPGTSLRSLEPLQLPDFPAAVSGPSAFAPGHNIPDHGLRETPSCPKPVQDTQPPESPVENSEQLLQTNSGAVARMSGGSLIPSPNQQALSPQPSREHQEQEPELGGAHAANVASVPIATYGPVSPTVSFQPLPRTALRTNLLSGVTVSALSADTSLSSSSTGSAFAKGAGDQAKAATCFSTTLTNSVTTSSVPSPRLVPVKTMSSKLPLSSKSTAAMTSTVLTNTAPSKLPSNSVYAGTVPSRVPASVAKAPANTIPPERNSKQAKETPEGPATKVTTGGNQTGPNSSIRSLHSGPEMSKPGVLVSQLDEPFSACSVDLAISPSSSLVSEPNHGPEENEYSSFRIQVDESPSADLLGSPEPLATQQPQEEEEHCASSMPWAKWLGATSALLAVFLAVMLYRSRRLAQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Ubiquitination-MTFAEDKTYKYIRD
-CCCCCCCCHHHHCC		45.30-
7Malonylation-MTFAEDKTYKYIRD
-CCCCCCCCHHHHCC		45.3026320211
7Succinylation-MTFAEDKTYKYIRD
-CCCCCCCCHHHHCC		45.3023954790
30PhosphorylationDVLEILPYLSCLTAS
HHHHHHHHHHHCCCC		14.0623140645
32PhosphorylationLEILPYLSCLTASDQ
HHHHHHHHHCCCCHH		10.9623140645
35PhosphorylationLPYLSCLTASDQDRL
HHHHHHCCCCHHHHH		28.5723140645
37PhosphorylationYLSCLTASDQDRLRA
HHHHCCCCHHHHHHH		30.4823140645
45PhosphorylationDQDRLRASYRQIGNR
HHHHHHHHHHHHCCH		17.8923140645
46PhosphorylationQDRLRASYRQIGNRD
HHHHHHHHHHHCCHH		12.9323140645
79GlutathionylationFIRALQICELPGLAD
HHHHHHHHCCCCHHH		2.5724333276
79S-palmitoylationFIRALQICELPGLAD
HHHHHHHHCCCCHHH		2.5728526873
100PhosphorylationQSYLPPGTSLRSLEP
HHHCCCCCCCCCCCC		30.2923140645
101PhosphorylationSYLPPGTSLRSLEPL
HHCCCCCCCCCCCCC		27.9223140645
137PhosphorylationPDHGLRETPSCPKPV
CCCCCCCCCCCCCCC		17.6725619855
139PhosphorylationHGLRETPSCPKPVQD
CCCCCCCCCCCCCCC		50.9325619855
147PhosphorylationCPKPVQDTQPPESPV
CCCCCCCCCCCCCCC		26.3622942356
152PhosphorylationQDTQPPESPVENSEQ
CCCCCCCCCCCCHHH		39.7725521595
157PhosphorylationPESPVENSEQLLQTN
CCCCCCCHHHHHHHC		17.1425521595
163PhosphorylationNSEQLLQTNSGAVAR
CHHHHHHHCCCCEEE		31.1825619855
165PhosphorylationEQLLQTNSGAVARMS
HHHHHHCCCCEEECC		31.3625619855
172PhosphorylationSGAVARMSGGSLIPS
CCCEEECCCCCCCCC		34.1525619855
175PhosphorylationVARMSGGSLIPSPNQ
EEECCCCCCCCCCCC		27.0125619855
179PhosphorylationSGGSLIPSPNQQALS
CCCCCCCCCCCCCCC		29.5025619855
186PhosphorylationSPNQQALSPQPSREH
CCCCCCCCCCCCHHH		25.2227087446
190PhosphorylationQALSPQPSREHQEQE
CCCCCCCCHHHHHHC		45.0825619855
210PhosphorylationAHAANVASVPIATYG
CCCCCCEECEEEECC		24.9225619855
215PhosphorylationVASVPIATYGPVSPT
CEECEEEECCCCCCC		29.7225619855
216PhosphorylationASVPIATYGPVSPTV
EECEEEECCCCCCCC		15.4825619855
220PhosphorylationIATYGPVSPTVSFQP
EEECCCCCCCCCCCC		20.2726824392
222PhosphorylationTYGPVSPTVSFQPLP
ECCCCCCCCCCCCCC		22.6725619855
224PhosphorylationGPVSPTVSFQPLPRT
CCCCCCCCCCCCCCH		22.2025619855
234MethylationPLPRTALRTNLLSGV
CCCCHHHHHCCCCCC		21.0724129315
234Asymmetric dimethylargininePLPRTALRTNLLSGV
CCCCHHHHHCCCCCC		21.07-
251PhosphorylationSALSADTSLSSSSTG
EEECCCCCCCCCCCC		27.14-
256PhosphorylationDTSLSSSSTGSAFAK
CCCCCCCCCCCHHHC		38.44-
297UbiquitinationSPRLVPVKTMSSKLP
CCCEEECEECCCCCC		32.23-
297MalonylationSPRLVPVKTMSSKLP
CCCEEECEECCCCCC		32.2326320211
298O-linked_GlycosylationPRLVPVKTMSSKLPL
CCEEECEECCCCCCC		23.6355412619
309PhosphorylationKLPLSSKSTAAMTST
CCCCCCCCHHHCCCE		25.8125521595
310PhosphorylationLPLSSKSTAAMTSTV
CCCCCCCHHHCCCEE		23.3619060867
313OxidationSSKSTAAMTSTVLTN
CCCCHHHCCCEEHHC		2.5617242355
315PhosphorylationKSTAAMTSTVLTNTA
CCHHHCCCEEHHCCC		11.9325521595
328PhosphorylationTAPSKLPSNSVYAGT
CCCCCCCCCCEECCC		52.7728725479
330PhosphorylationPSKLPSNSVYAGTVP
CCCCCCCCEECCCCC		22.3525159016
332PhosphorylationKLPSNSVYAGTVPSR
CCCCCCEECCCCCCC		10.1125159016
346MalonylationRVPASVAKAPANTIP
CCCHHHHCCCCCCCC		53.3926320211
364PhosphorylationNSKQAKETPEGPATK
CCHHCCCCCCCCCCE		26.4022871156
370PhosphorylationETPEGPATKVTTGGN
CCCCCCCCEEECCCC		29.2222871156
373O-linked_GlycosylationEGPATKVTTGGNQTG
CCCCCEEECCCCCCC		22.6830059200
374PhosphorylationGPATKVTTGGNQTGP
CCCCEEECCCCCCCC		46.1923140645
379PhosphorylationVTTGGNQTGPNSSIR
EECCCCCCCCCCCHH		59.6229472430
383PhosphorylationGNQTGPNSSIRSLHS
CCCCCCCCCHHCCCC		30.2130352176
384PhosphorylationNQTGPNSSIRSLHSG
CCCCCCCCHHCCCCC		28.7621082442
387PhosphorylationGPNSSIRSLHSGPEM
CCCCCHHCCCCCCCC		28.8529472430
390PhosphorylationSSIRSLHSGPEMSKP
CCHHCCCCCCCCCCC		62.4329472430
395PhosphorylationLHSGPEMSKPGVLVS
CCCCCCCCCCCEEEE		33.7529472430
418PhosphorylationCSVDLAISPSSSLVS
CEEEEEECCCCCCCC		17.08-
446PhosphorylationFRIQVDESPSADLLG
EEEEECCCCCCCCCC		21.4922324799
448PhosphorylationIQVDESPSADLLGSP
EEECCCCCCCCCCCC		43.6322324799
454PhosphorylationPSADLLGSPEPLATQ
CCCCCCCCCCCCCCC		26.5122324799
460PhosphorylationGSPEPLATQQPQEEE
CCCCCCCCCCCHHHH		35.1122324799
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
418SPhosphorylationKinaseTBK1Q9WUN2
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
418SPhosphorylation

-
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MAVS_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMUF1_MOUSESmurf1physical
23087404
ASC_MOUSEPycardphysical
25847972
TRAF3_MOUSETraf3physical
25847972
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MAVS_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147; SER-152; SER-157;SER-309 AND THR-310, AND MASS SPECTROMETRY.

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