IFIH1_MOUSE - dbPTM
IFIH1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFIH1_MOUSE
UniProt AC Q8R5F7
Protein Name Interferon-induced helicase C domain-containing protein 1
Gene Name Ifih1
Organism Mus musculus (Mouse).
Sequence Length 1025
Subcellular Localization Cytoplasm . Nucleus . May be found in the nucleus, during apoptosis.
Protein Description Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include mRNA lacking 2'-O-methylation at their 5' cap and long-dsRNA (>1 kb in length). Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV), mengo encephalomyocarditis virus (ENMG), and theiler's murine encephalomyelitis virus (TMEV). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines..
Protein Sequence MSIVCSAEDSFRNLILFFRPRLKMYIQVEPVLDHLIFLSAETKEQILKKINTCGNTSAAELLLSTLEQGQWPLGWTQMFVEALEHSGNPLAARYVKPTLTDLPSPSSETAHDECLHLLTLLQPTLVDKLLINDVLDTCFEKGLLTVEDRNRISAAGNSGNESGVRELLRRIVQKENWFSTFLDVLRQTGNDALFQELTGGGCPEDNTDLANSSHRDGPAANECLLPAVDESSLETEAWNVDDILPEASCTDSSVTTESDTSLAEGSVSCFDESLGHNSNMGRDSGTMGSDSDESVIQTKRVSPEPELQLRPYQMEVAQPALDGKNIIICLPTGSGKTRVAVYITKDHLDKKKQASESGKVIVLVNKVMLAEQLFRKEFNPYLKKWYRIIGLSGDTQLKISFPEVVKSYDVIISTAQILENSLLNLESGDDDGVQLSDFSLIIIDECHHTNKEAVYNNIMRRYLKQKLRNNDLKKQNKPAIPLPQILGLTASPGVGAAKKQSEAEKHILNICANLDAFTIKTVKENLGQLKHQIKEPCKKFVIADDTRENPFKEKLLEIMASIQTYCQKSPMSDFGTQHYEQWAIQMEKKAAKDGNRKDRVCAEHLRKYNEALQINDTIRMIDAYSHLETFYTDEKEKKFAVLNDSDKSDDEASSCNDQLKGDVKKSLKLDETDEFLMNLFFDNKKMLKKLAENPKYENEKLIKLRNTILEQFTRSEESSRGIIFTKTRQSTYALSQWIMENAKFAEVGVKAHHLIGAGHSSEVKPMTQTEQKEVISKFRTGEINLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYVLVTSSGSGVTEREIVNDFREKMMYKAINRVQNMKPEEYAHKILELQVQSILEKKMKVKRSIAKQYNDNPSLITLLCKNCSMLVCSGENIHVIEKMHHVNMTPEFKGLYIVRENKALQKKFADYQTNGEIICKCGQAWGTMMVHKGLDLPCLKIRNFVVNFKNNSPKKQYKKWVELPIRFPDLDYSEYCLYSDED
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
94PhosphorylationGNPLAARYVKPTLTD
CCCHHHHHCCCCCCC		14.2223984901
98PhosphorylationAARYVKPTLTDLPSP
HHHHCCCCCCCCCCC		36.2523649490
100PhosphorylationRYVKPTLTDLPSPSS
HHCCCCCCCCCCCCC		37.6623984901
104PhosphorylationPTLTDLPSPSSETAH
CCCCCCCCCCCCCHH		44.7223984901
106PhosphorylationLTDLPSPSSETAHDE
CCCCCCCCCCCHHHH		45.1823984901
107PhosphorylationTDLPSPSSETAHDEC
CCCCCCCCCCHHHHH		42.2123649490
109PhosphorylationLPSPSSETAHDECLH
CCCCCCCCHHHHHHH		31.1023984901
119PhosphorylationDECLHLLTLLQPTLV
HHHHHHHHHHCHHHH		31.6123984901
124PhosphorylationLLTLLQPTLVDKLLI
HHHHHCHHHHHHHHH		26.8423984901
284PhosphorylationNSNMGRDSGTMGSDS
CCCCCCCCCCCCCCC		34.5023684622
286PhosphorylationNMGRDSGTMGSDSDE
CCCCCCCCCCCCCCC		23.4725521595
289PhosphorylationRDSGTMGSDSDESVI
CCCCCCCCCCCCCHH		24.1025521595
291PhosphorylationSGTMGSDSDESVIQT
CCCCCCCCCCCHHCC		45.0025521595
294PhosphorylationMGSDSDESVIQTKRV
CCCCCCCCHHCCCCC		29.5227742792
298PhosphorylationSDESVIQTKRVSPEP
CCCCHHCCCCCCCCC		15.0828833060
302PhosphorylationVIQTKRVSPEPELQL
HHCCCCCCCCCCCCC		27.8125521595
312PhosphorylationPELQLRPYQMEVAQP
CCCCCCCEECCCCCC		17.6628833060
334PhosphorylationIICLPTGSGKTRVAV
EEEEECCCCCEEEEE		39.3327357545
392PhosphorylationWYRIIGLSGDTQLKI
HHHHCCCCCCCEEEE		29.43-
395PhosphorylationIIGLSGDTQLKISFP
HCCCCCCCEEEEEHH		39.05-
477UbiquitinationNDLKKQNKPAIPLPQ
CCHHHCCCCCCCHHH		33.08-
523UbiquitinationAFTIKTVKENLGQLK
CCCHHHHHHHHHHHH		46.23-
539MalonylationQIKEPCKKFVIADDT
HCCCCCCCEEECCCC		52.1326320211
569PhosphorylationIQTYCQKSPMSDFGT
HHHHHHHCCCCCCCH		10.4322802335
572PhosphorylationYCQKSPMSDFGTQHY
HHHHCCCCCCCHHHH		32.9222802335
576PhosphorylationSPMSDFGTQHYEQWA
CCCCCCCHHHHHHHH		16.5022802335
579PhosphorylationSDFGTQHYEQWAIQM
CCCCHHHHHHHHHHH		10.4522802335
645PhosphorylationKFAVLNDSDKSDDEA
EEEECCCCCCCCHHH		45.9525521595
648PhosphorylationVLNDSDKSDDEASSC
ECCCCCCCCHHHHHC		56.1125521595
653PhosphorylationDKSDDEASSCNDQLK
CCCCHHHHHCHHHHC		33.1222324799
654PhosphorylationKSDDEASSCNDQLKG
CCCHHHHHCHHHHCC		24.8025266776
695SuccinylationKKLAENPKYENEKLI
HHHHHCCCCCCHHHH		76.4323954790
828PhosphorylationGRARADESTYVLVTS
CCCCCCCCCEEEEEC		26.1130635358
829PhosphorylationRARADESTYVLVTSS
CCCCCCCCEEEEECC		18.6630635358
830PhosphorylationARADESTYVLVTSSG
CCCCCCCEEEEECCC		10.8930635358
834PhosphorylationESTYVLVTSSGSGVT
CCCEEEEECCCCCCC		17.0230635358
835PhosphorylationSTYVLVTSSGSGVTE
CCEEEEECCCCCCCH		25.8130635358
836PhosphorylationTYVLVTSSGSGVTER
CEEEEECCCCCCCHH		27.8430635358
838PhosphorylationVLVTSSGSGVTEREI
EEEECCCCCCCHHHH		31.8530635358
841PhosphorylationTSSGSGVTEREIVND
ECCCCCCCHHHHHHH		32.6130635358
896PhosphorylationKRSIAKQYNDNPSLI
HHHHHHHCCCCHHHH		24.6322871156
904PhosphorylationNDNPSLITLLCKNCS
CCCHHHHHHHCCCCC		20.9722871156
950UbiquitinationENKALQKKFADYQTN
CCHHHHHHHCCCCCC		32.59-
983UbiquitinationGLDLPCLKIRNFVVN
CCCCCEEEEEEEEEE		46.46-
1021PhosphorylationDYSEYCLYSDED---
CHHHHEEECCCC---		15.5429550500
1022PhosphorylationYSEYCLYSDED----
HHHHEEECCCC----		22.9026643407
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
828SPhosphorylationKinaseRIOK3Q9DBU3
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFIH1_MOUSE !!
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 IFIH1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IFIH1_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 SER-302; SER-645 ANDSER-648, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASSSPECTROMETRY.

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