HUMAN:IFIH1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	IFIH1 (synonyms: MDA5, RH116)
Protein Name(s)	Interferon-induced helicase C domain-containing protein 1 Clinically amyopathic dermatomyositis autoantigen 140 kDa CADM-140 autoantigen Helicase with 2 CARD domains Helicard Interferon-induced with helicase C domain protein 1 Melanoma differentiation-associated protein 5 MDA-5 Murabutide down-regulated protein RIG-I-like receptor 2 RLR-2 RNA helicase-DEAD box protein 116
External Links
UniProt	Q9BYX4
EMBL	AF095844 AY017378 BC046208 BC078180 BC111750 AK056293
CCDS	CCDS2217.1
RefSeq	NP_071451.2
UniGene	Hs.163173
PDB	2RQB 3B6E 3GA3 4GL2
PDBsum	2RQB 3B6E 3GA3 4GL2
ProteinModelPortal	Q9BYX4
SMR	Q9BYX4
BioGrid	122082
DIP	DIP-42607N
IntAct	Q9BYX4
MINT	MINT-3381993
STRING	9606.ENSP00000263642
PhosphoSite	Q9BYX4
DMDM	134047802
MaxQB	Q9BYX4
PaxDb	Q9BYX4
PRIDE	Q9BYX4
Ensembl	ENST00000263642 ENST00000421365
GeneID	64135
KEGG	hsa:64135
UCSC	uc002uce.4 uc002ucf.4
CTD	64135
GeneCards	GC02M163123
HGNC	HGNC:18873
HPA	HPA002656
MIM	606951 610155 615846
neXtProt	NX_Q9BYX4
Orphanet	51
PharmGKB	PA134889215
eggNOG	COG1111
GeneTree	ENSGT00510000046789
HOGENOM	HOG000230992
HOVERGEN	HBG106019
InParanoid	Q9BYX4
KO	K12647
OMA	KCGQAWG
OrthoDB	EOG7RV9FC
PhylomeDB	Q9BYX4
TreeFam	TF330258
Reactome	REACT_24938 REACT_24969 REACT_25026 REACT_25039 REACT_25271 REACT_25359
ChiTaRS	IFIH1
EvolutionaryTrace	Q9BYX4
GeneWiki	MDA5
GenomeRNAi	64135
NextBio	66034
PRO	PR:Q9BYX4
Proteomes	UP000005640
Bgee	Q9BYX4
CleanEx	HS_IFIH1
ExpressionAtlas	Q9BYX4
Genevestigator	Q9BYX4
GO	GO:0005829 GO:0005634 GO:0005524 GO:0003677 GO:0003725 GO:0004386 GO:0043021 GO:0003727 GO:0008270 GO:0039528 GO:0009597 GO:0045087 GO:0032480 GO:0032727 GO:0032728 GO:0016925 GO:0042981 GO:0034344 GO:0009615 GO:0016032
Gene3D	1.10.533.10 3.40.50.300
InterPro	IPR001315 IPR011029 IPR006935 IPR014001 IPR001650 IPR027417 IPR021673
Pfam	PF00619 PF00271 PF04851 PF11648
SMART	SM00487 SM00490
SUPFAM	SSF52540
PROSITE	PS51192 PS51194

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0051607	defense response to virus	PMID:21478870^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1902741	positive regulation of interferon-alpha secretion	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0071360	cellular response to exogenous dsRNA	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0060760	positive regulation of response to cytokine stimulus	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0035549	positive regulation of interferon-beta secretion	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1904469	positive regulation of tumor necrosis factor secretion	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:2000778	positive regulation of interleukin-6 secretion	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0039530	MDA-5 signaling pathway	PMID:17600090^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032728	positive regulation of interferon-beta production	PMID:17600090^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0043021	ribonucleoprotein complex binding	PMID:19881509^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q15366	F	Seeded From UniProt	complete
involved_in	GO:0032728	positive regulation of interferon-beta production	PMID:19656871^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032728	positive regulation of interferon-beta production	PMID:19211564^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032727	positive regulation of interferon-alpha production	PMID:19656871^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016925	protein sumoylation	PMID:21156324^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:19380577^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:19531363^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003727	single-stranded RNA binding	PMID:19656871^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:19656871^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25865883^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9BYX4	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22160685^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9BYX4	F	Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R5F7 ensembl:ENSMUSP00000028259	P	Seeded From UniProt	complete
	GO:0032897	negative regulation of viral transcription	PMID:15563593^[12]	ECO:0000314			P	figure 3 electrophoresis inhibiting the promoter for transcription	complete
involved_in	GO:0009615	response to virus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R5F7 ensembl:ENSMUSP00000028259	P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006935	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006935	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006935	F	Seeded From UniProt	complete
involved_in	GO:0032728	positive regulation of interferon-beta production	PMID:17079289^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032727	positive regulation of interferon-alpha production	PMID:17079289^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009597	detection of virus	PMID:17079289^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:17079289^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	PMID:21616437^[14] Reactome:R-HSA-168249	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
	GO:0023014	signal transduction by protein phosphorylation	PMID:26243192^[15]	ECO:0000314			P	S1 shows that IFIH1(referred to here as MDA5) is required for phosporylation of downstream signaling proteins	complete CACAO 11212
involved_in	GO:0039528	cytoplasmic pattern recognition receptor signaling pathway in response to virus	PMID:21616437^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0034344	regulation of type III interferon production	PMID:21616437^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009615	response to virus	PMID:21616437^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032480	negative regulation of type I interferon production	Reactome:R-HSA-936440	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016579	protein deubiquitination	Reactome:R-HSA-5688426	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-NUL-936401 Reactome:R-HSA-990528 Reactome:R-HSA-990526 Reactome:R-HSA-937343 Reactome:R-HSA-936475 Reactome:R-HSA-936381 Reactome:R-HSA-933539 Reactome:R-HSA-933538 Reactome:R-HSA-933537 Reactome:R-HSA-933532 Reactome:R-HSA-933530 Reactome:R-HSA-933527 Reactome:R-HSA-933526 Reactome:R-HSA-933525 Reactome:R-HSA-933523 Reactome:R-HSA-918232 Reactome:R-HSA-918230 Reactome:R-HSA-918229 Reactome:R-HSA-918227 Reactome:R-HSA-918225 Reactome:R-HSA-913725 Reactome:R-HSA-5696600 Reactome:R-HSA-168934 Reactome:R-HSA-168909	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0399	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P	Seeded From UniProt	complete
involved_in	GO:0002376	immune system process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0391	P	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F	Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0051	P	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Schoggins, JW et al. (2011) A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 472 481-5 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Zhang, Z et al. (2011) DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells. J. Immunol. 187 4501-8 PubMed GONUTS page
↑ ^3.0 ^3.1 Diao, F et al. (2007) Negative regulation of MDA5- but not RIG-I-mediated innate antiviral signaling by the dihydroxyacetone kinase. Proc. Natl. Acad. Sci. U.S.A. 104 11706-11 PubMed GONUTS page
↑ You, F et al. (2009) PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4. Nat. Immunol. 10 1300-8 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Pichlmair, A et al. (2009) Activation of MDA5 requires higher-order RNA structures generated during virus infection. J. Virol. 83 10761-9 PubMed GONUTS page
↑ Bamming, D & Horvath, CM (2009) Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2. J. Biol. Chem. 284 9700-12 PubMed GONUTS page
↑ Fu, J et al. (2011) MDA5 is SUMOylated by PIAS2β in the upregulation of type I interferon signaling. Mol. Immunol. 48 415-22 PubMed GONUTS page
↑ Takahasi, K et al. (2009) Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors. J. Biol. Chem. 284 17465-74 PubMed GONUTS page
↑ Li, X et al. (2009) Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5. Arch. Biochem. Biophys. 488 23-33 PubMed GONUTS page
↑ Takashima, K et al. (2015) RIOK3-mediated phosphorylation of MDA5 interferes with its assembly and attenuates the innate immune response. Cell Rep 11 192-200 PubMed GONUTS page
↑ Peisley, A et al. (2011) Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition. Proc. Natl. Acad. Sci. U.S.A. 108 21010-5 PubMed GONUTS page
↑ Andrejeva, J et al. (2004) The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter. Proc. Natl. Acad. Sci. U.S.A. 101 17264-9 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Mibayashi, M et al. (2007) Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus. J. Virol. 81 514-24 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 Loo, YM & Gale, M Jr (2011) Immune signaling by RIG-I-like receptors. Immunity 34 680-92 PubMed GONUTS page
↑ Okazaki, T et al. (2015) The ASK family kinases differentially mediate induction of type I interferon and apoptosis during the antiviral response. Sci Signal 8 ra78 PubMed GONUTS page

[PMID:21478870-1] Schoggins, JW et al. (2011) A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 472 481-5 PubMed GONUTS page

[PMID:21957149-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Zhang, Z et al. (2011) DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells. J. Immunol. 187 4501-8 PubMed GONUTS page

[PMID:17600090-3] 3.0 ^3.1 Diao, F et al. (2007) Negative regulation of MDA5- but not RIG-I-mediated innate antiviral signaling by the dihydroxyacetone kinase. Proc. Natl. Acad. Sci. U.S.A. 104 11706-11 PubMed GONUTS page

[PMID:19881509-4] You, F et al. (2009) PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4. Nat. Immunol. 10 1300-8 PubMed GONUTS page

[PMID:19656871-5] 5.0 ^5.1 ^5.2 ^5.3 Pichlmair, A et al. (2009) Activation of MDA5 requires higher-order RNA structures generated during virus infection. J. Virol. 83 10761-9 PubMed GONUTS page

[PMID:19211564-6] Bamming, D & Horvath, CM (2009) Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2. J. Biol. Chem. 284 9700-12 PubMed GONUTS page

[PMID:21156324-7] Fu, J et al. (2011) MDA5 is SUMOylated by PIAS2β in the upregulation of type I interferon signaling. Mol. Immunol. 48 415-22 PubMed GONUTS page

[PMID:19380577-8] Takahasi, K et al. (2009) Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors. J. Biol. Chem. 284 17465-74 PubMed GONUTS page

[PMID:19531363-9] Li, X et al. (2009) Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5. Arch. Biochem. Biophys. 488 23-33 PubMed GONUTS page

[PMID:25865883-10] Takashima, K et al. (2015) RIOK3-mediated phosphorylation of MDA5 interferes with its assembly and attenuates the innate immune response. Cell Rep 11 192-200 PubMed GONUTS page

[PMID:22160685-11] Peisley, A et al. (2011) Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition. Proc. Natl. Acad. Sci. U.S.A. 108 21010-5 PubMed GONUTS page

[PMID:15563593-12] Andrejeva, J et al. (2004) The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter. Proc. Natl. Acad. Sci. U.S.A. 101 17264-9 PubMed GONUTS page

[PMID:17079289-13] 13.0 ^13.1 ^13.2 ^13.3 Mibayashi, M et al. (2007) Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus. J. Virol. 81 514-24 PubMed GONUTS page

[PMID:21616437-14] 14.0 ^14.1 ^14.2 ^14.3 Loo, YM & Gale, M Jr (2011) Immune signaling by RIG-I-like receptors. Immunity 34 680-92 PubMed GONUTS page

[PMID:26243192-15] Okazaki, T et al. (2015) The ASK family kinases differentially mediate induction of type I interferon and apoptosis during the antiviral response. Sci Signal 8 ra78 PubMed GONUTS page

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HUMAN:IFIH1

Contents

Annotations

Notes

References

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