IFIH1_HUMAN - dbPTM
IFIH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFIH1_HUMAN
UniProt AC Q9BYX4
Protein Name Interferon-induced helicase C domain-containing protein 1
Gene Name IFIH1
Organism Homo sapiens (Human).
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) and mengo encephalomyocarditis virus (ENMG). 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 MSNGYSTDENFRYLISCFRARVKMYIQVEPVLDYLTFLPAEVKEQIQRTVATSGNMQAVELLLSTLEKGVWHLGWTREFVEALRRTGSPLAARYMNPELTDLPSPSFENAHDEYLQLLNLLQPTLVDKLLVRDVLDKCMEEELLTIEDRNRIAAAENNGNESGVRELLKRIVQKENWFSAFLNVLRQTGNNELVQELTGSDCSESNAEIENLSQVDGPQVEEQLLSTTVQPNLEKEVWGMENNSSESSFADSSVVSESDTSLAEGSVSCLDESLGHNSNMGSDSGTMGSDSDEENVAARASPEPELQLRPYQMEVAQPALEGKNIIICLPTGSGKTRVAVYIAKDHLDKKKKASEPGKVIVLVNKVLLVEQLFRKEFQPFLKKWYRVIGLSGDTQLKISFPEVVKSCDIIISTAQILENSLLNLENGEDAGVQLSDFSLIIIDECHHTNKEAVYNNIMRHYLMQKLKNNRLKKENKPVIPLPQILGLTASPGVGGATKQAKAEEHILKLCANLDAFTIKTVKENLDQLKNQIQEPCKKFAIADATREDPFKEKLLEIMTRIQTYCQMSPMSDFGTQPYEQWAIQMEKKAAKEGNRKERVCAEHLRKYNEALQINDTIRMIDAYTHLETFYNEEKDKKFAVIEDDSDEGGDDEYCDGDEDEDDLKKPLKLDETDRFLMTLFFENNKMLKRLAENPEYENEKLTKLRNTIMEQYTRTEESARGIIFTKTRQSAYALSQWITENEKFAEVGVKAHHLIGAGHSSEFKPMTQNEQKEVISKFRTGKINLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYVLVAHSGSGVIEHETVNDFREKMMYKAIHCVQNMKPEEYAHKILELQMQSIMEKKMKTKRNIAKHYKNNPSLITFLCKNCSVLACSGEDIHVIEKMHHVNMTPEFKELYIVRENKALQKKCADYQINGEIICKCGQAWGTMMVHKGLDLPCLKIRNFVVVFKNNSTKKQYKKWVELPITFPNLDYSECCLFSDED
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
5Phosphorylation---MSNGYSTDENFR
---CCCCCCCCHHHH		16.7929759185
13PhosphorylationSTDENFRYLISCFRA
CCCHHHHHHHHHHHH		12.3029759185
43SumoylationTFLPAEVKEQIQRTV
HCCCHHHHHHHHHHH		35.09-
86PhosphorylationFVEALRRTGSPLAAR
HHHHHHHHCCCCHHH		35.2628348404
88PhosphorylationEALRRTGSPLAARYM
HHHHHHCCCCHHHHC		19.0027251275
94PhosphorylationGSPLAARYMNPELTD
CCCCHHHHCCHHHCC		9.1220068231
100PhosphorylationRYMNPELTDLPSPSF
HHCCHHHCCCCCCCC		33.5520068231
104PhosphorylationPELTDLPSPSFENAH
HHHCCCCCCCCCCCH		40.2420068231
106PhosphorylationLTDLPSPSFENAHDE
HCCCCCCCCCCCHHH		49.9120068231
114PhosphorylationFENAHDEYLQLLNLL
CCCCHHHHHHHHHHH		13.0523090842
124PhosphorylationLLNLLQPTLVDKLLV
HHHHHCHHHHHHHHH		26.8420068231
128UbiquitinationLQPTLVDKLLVRDVL
HCHHHHHHHHHHHHH		35.92-
137UbiquitinationLVRDVLDKCMEEELL
HHHHHHHHHHHHHCC		31.1829967540
169UbiquitinationSGVRELLKRIVQKEN
HHHHHHHHHHHHHCC		53.3422817900
174UbiquitinationLLKRIVQKENWFSAF
HHHHHHHHCCHHHHH		41.9622817900
174 (in isoform 1)Ubiquitination-41.9621906983
174 (in isoform 2)Ubiquitination-41.9621906983
289PhosphorylationSDSGTMGSDSDEENV
CCCCCCCCCCHHHHH		24.10-
291PhosphorylationSGTMGSDSDEENVAA
CCCCCCCCHHHHHHH		48.93-
301PhosphorylationENVAARASPEPELQL
HHHHHHCCCCCCCCC		25.0129255136
311PhosphorylationPELQLRPYQMEVAQP
CCCCCCCCCHHHCCH		17.6626434776
336PhosphorylationLPTGSGKTRVAVYIA
EECCCCCCEEEEEEE		33.6222210691
341PhosphorylationGKTRVAVYIAKDHLD
CCCEEEEEEEHHHHC		5.8522210691
351AcetylationKDHLDKKKKASEPGK
HHHHCHHHCCCCCCC		60.3512439377
352AcetylationDHLDKKKKASEPGKV
HHHCHHHCCCCCCCE		67.0619825841
354PhosphorylationLDKKKKASEPGKVIV
HCHHHCCCCCCCEEE		53.88-
385PhosphorylationQPFLKKWYRVIGLSG
HHHHHHHHHHCCCCC		12.13-
391PhosphorylationWYRVIGLSGDTQLKI
HHHHCCCCCCCEEEE		29.43-
465UbiquitinationMRHYLMQKLKNNRLK
HHHHHHHHHHHCCCC		47.6829967540
490PhosphorylationQILGLTASPGVGGAT
HHHCCCCCCCCCHHH		19.5625159151
519UbiquitinationNLDAFTIKTVKENLD
CCCCCCHHHHHHHHH		44.1829967540
529UbiquitinationKENLDQLKNQIQEPC
HHHHHHHHHHCHHHH		40.9729967540
538UbiquitinationQIQEPCKKFAIADAT
HCHHHHHHHHHCCCC		46.9029967540
606UbiquitinationVCAEHLRKYNEALQI
HHHHHHHHHHHHHHC		59.8129967540
645PhosphorylationFAVIEDDSDEGGDDE
EEEEECCCCCCCCCC		50.3025849741
653PhosphorylationDEGGDDEYCDGDEDE
CCCCCCCCCCCCCCC		11.6629496963
700UbiquitinationNPEYENEKLTKLRNT
CCCHHHHHHHHHHHH		73.3929967540
726UbiquitinationARGIIFTKTRQSAYA
HCCEEEECCHHHHHH		30.84-
727PhosphorylationRGIIFTKTRQSAYAL
CCEEEECCHHHHHHH		30.7730108239
730PhosphorylationIFTKTRQSAYALSQW
EEECCHHHHHHHHHH		21.6930108239
732PhosphorylationTKTRQSAYALSQWIT
ECCHHHHHHHHHHHH		17.2130108239
735PhosphorylationRQSAYALSQWITENE
HHHHHHHHHHHHCCH		18.4630108239
743UbiquitinationQWITENEKFAEVGVK
HHHHCCHHHHHHHCH		62.5529967540
764UbiquitinationAGHSSEFKPMTQNEQ
CCCCCCCCCCCHHHH		29.8129967540
777UbiquitinationEQKEVISKFRTGKIN
HHHHHHHHHHCCCCC		27.9529967540
828PhosphorylationGRARADESTYVLVAH
CCCCCCCCEEEEEEE		26.1124995871
830PhosphorylationARADESTYVLVAHSG
CCCCCCEEEEEEECC		10.8927642862
865SumoylationIHCVQNMKPEEYAHK
HHHHHHCCHHHHHHH		57.75-
880PhosphorylationILELQMQSIMEKKMK
HHHHHHHHHHHHHHH		20.6829083192
896PhosphorylationKRNIAKHYKNNPSLI
HHHHHHHHHCCHHHH		18.07-
1009PhosphorylationKWVELPITFPNLDYS
HHEECCEECCCCCHH		30.9730108239
1015PhosphorylationITFPNLDYSECCLFS
EECCCCCHHHHCEEC		14.9930108239
1016PhosphorylationTFPNLDYSECCLFSD
ECCCCCHHHHCEECC		24.6730108239
1022PhosphorylationYSECCLFSDED----
HHHHCEECCCC----		27.4330108239
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
828SPhosphorylationKinaseRIOK3O14730
Uniprot
-KUbiquitinationE3 ubiquitin ligaseRNF125Q96EQ8
PMID:17460044
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFIH1_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IDE_HUMANIDEphysical
21903422
MAVS_HUMANMAVSphysical
21903422
PIAS2_HUMANPIAS2physical
21156324
TSN6_HUMANTSPAN6physical
22908223
A4_HUMANAPPphysical
21832049
UBP3_HUMANUSP3physical
24366338
RN123_HUMANRNF123physical
27312109
MAVS_HUMANMAVSphysical
27312109
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610155Diabetes mellitus, insulin-dependent, 19 (IDDM19)
Note=IFIH1 is the CADM-140 autoantigen, involved in clinically amyopathic dermatomyositis (CADM). This is a chronic inflammatory disorder that shows typical skin manifestations of dermatomyositis but has no or little evidence of clinical myositis. Anti-CADM-140 antibodies appear to be specific to dermatomyositis, especially CADM. Patients with anti-CADM-140 antibodies frequently develop life-threatening acute progressive interstitial lung disease (ILD).
615846
182250Singleton-Merten syndrome 1 (SGMRT1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IFIH1_HUMAN

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Related Literatures of Post-Translational Modification

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