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Protein Page:
IFIH1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
IFIH1 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. Monomer in the absence of ligands and homodimerizes in the presence of dsRNA ligands. Can assemble into helical or linear polymeric filaments on long dsRNA. Interacts with MAVS/IPS1. Interacts with V protein of Simian virus 5, Human parainfluenza virus 2, Mumps virus, Sendai virus and Hendra virus. Binding to paramyxoviruses V proteins prevents IFN-beta induction, and the further establishment of an antiviral state. Interacts with PCBP2. Interacts with NLRC5. Interacts with PIAS2-beta. Interacts with DDX60. By interferon (IFN) and TNF. Widely expressed, at a low level. Expression is detected at slightly highest levels in placenta, pancreas and spleen and at barely levels in detectable brain, testis and lung. Belongs to the helicase family. RLR subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.4.13; Helicase; Apoptosis; EC 3.6.1.-
Cellular Component: cytosol; nucleus
Molecular Function: ribonucleoprotein binding; protein binding; single-stranded RNA binding; DNA binding; zinc ion binding; double-stranded RNA binding; helicase activity; ATP binding
Biological Process: regulation of apoptosis; protein sumoylation; viral reproduction; detection of virus; response to virus; positive regulation of interferon-beta production; innate immune response; negative regulation of interferon type I production; positive regulation of interferon-alpha production
Reference #:  Q9BYX4 (UniProtKB)
Alt. Names/Synonyms: DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide; Helicard; Helicase with 2 CARD domains; Hlcd; IDDM19; IFIH1; interferon induced with helicase C domain 1; Interferon-induced helicase C domain-containing protein 1; Interferon-induced with helicase C domain protein 1; MDA-5; MDA5; melanoma differentiation associated protein-5; Melanoma differentiation-associated protein 5; MGC133047; Murabutide down-regulated protein; RH116; RNA helicase-DEAD box protein 116
Gene Symbols: IFIH1
Molecular weight: 116,689 Da
Basal Isoelectric point: 5.38  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

IFIH1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
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Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 S88-p EALRRTGsPLAARYM
1 0 S104-p PELTDLPsPsFENAH
0 1 S106-p LTDLPsPsFENAHDE
0 7 K174-ub LLKRIVQkENWFSAF
0 3 S284 NSNMGSDSGTMGSDS
0 1 T286 NMGSDSGTMGSDSDE
0 9 S289 SDSGTMGSDSDEENV
0 7 S291 SGTMGSDSDEENVAA
0 1 - gap
0 12 S301-p ENVAARAsPEPELQL
0 2 K351-ac KDHLDKKkkAsEPGK
0 1 K352-ac DHLDKKkkAsEPGKV
0 1 S354-p LDKKkkAsEPGKVIV
0 1 Y385-p QPFLKKWyRVIGLsG
0 2 S391-p WyRVIGLsGDTQLKI
0 1 T394 VIGLsGDTQLKISFP
0 1 K476 NRLKKENKPVIPLPQ
0 2 S490-p QILGLTAsPGVGGAT
0 1 K522 AFTIKTVKENLDQLK
0 1 S571 YCQMSPMSDFGTQPY
0 1 T575 SPMSDFGTQPYEQWA
0 1 Y578 SDFGTQPYEQWAIQM
0 6 S645 FAVIEDDSDEGGDDE
0 6 G648 IEDDSDEGGDDEYCD
0 1 E695 KRLAENPEYENEKLT
0 1 Y896-p KRNIAKHyKNNPSLI
0 1 K950 ENKALQKKCADYQIN
0 1 K983 GLDLPCLKIRNFVVV
0 3 S1022 YSECCLFSDED____
  mouse

 
N88 EALEHSGNPLAARYV
S104 PTLTDLPSPSSETAH
S106 LTDLPSPSSETAHDE
K174 LLRRIVQKENWFSTF
S284-p NSNMGRDsGtMGsDs
T286-p NMGRDsGtMGsDsDE
S289-p RDsGtMGsDsDEsVI
S291-p sGtMGsDsDEsVIQT
S294-p MGsDsDEsVIQTKRV
S302-p VIQTKRVsPEPELQL
K352 KDHLDKKKQASESGK
Q353 DHLDKKKQASESGKV
S355 LDKKKQASESGKVIV
Y386 NPYLKKWYRIIGLsG
S392-p WYRIIGLsGDtQLKI
T395-p IIGLsGDtQLKISFP
K477-ub NDLKKQNkPAIPLPQ
S491 QILGLTASPGVGAAK
K523-ub AFTIKTVkENLGQLK
S572-p YCQKSPMsDFGtQHy
T576-p SPMsDFGtQHyEQWA
Y579-p sDFGtQHyEQWAIQM
S645-p KFAVLNDsDKsDDEA
S648-p VLNDsDKsDDEASSC
K695-sc KKLAENPkYENEKLI
Y896 KRSIAKQYNDNPSLI
K950-ub ENKALQKkFADYQTN
K983-ub GLDLPCLkIRNFVVN
S1022-p YSEYCLYsDED____
  rat

 
N88 EALEHSGNPLAARYV
S104 PSLTDLPSPSSETAH
S106 LTDLPSPSSETAHDE
K174 LLRRIVQKENWFSTF
S284 NSNMGRDSGtMGsDs
T286-p NMGRDSGtMGsDsDE
S289-p RDSGtMGsDsDEDTI
S291-p SGtMGsDsDEDTIMG
- gap
S303 IMGTKRASPKPELQL
K353 KDHLDKKKQACESGK
Q354 DHLDKKKQACESGKV
C356 LDKKKQACESGKVIV
Y387 NPFLKKWYRIIGLSG
S393 WYRIIGLSGDTQLKI
T396 IIGLSGDTQLKISFP
K478 HKLKKQNKPTIHLPQ
S492 QILGLTASPGVGAAK
K524 AFTIKTVKENLSQLK
S573 YCQKSPLSDFGTQHY
T577 SPLSDFGTQHYEQWA
Y580 SDFGTQHYEQWAIQM
S646-p KFAALNDsDEsDDDE
S649-p ALNDsDEsDDDEASS
K697 KKLAENPKYENEKLI
Y898 KRSIARQYNSDPSLI
K952 ENKALQMKFADYQTN
K985 GLDLPCLKIRNFVVN
S1024 CSEYCLYSDED____
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