HUMAN:IRF3

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	IRF3
Protein Name(s)	Interferon regulatory factor 3 IRF-3
External Links
UniProt	Q14653
EMBL	Z56281 AB102884 AB102886 AB102887 AK292027 AK314421 AC011495 CH471177 BC000660 BC071721 U86636
CCDS	CCDS12775.1 CCDS56099.1 CCDS59407.1 CCDS59409.1
RefSeq	NP_001184051.1 NP_001184052.1 NP_001184053.1 NP_001184054.1 NP_001184055.1 NP_001184056.1 NP_001184057.1 NP_001562.1 XP_006723260.1 XP_006723261.1 XP_006723262.1
UniGene	Hs.289052 Hs.731922 Hs.75254
PDB	1J2F 1QWT 1T2K 1ZOQ 2O61 2O6G 2PI0 3A77 3QU6
PDBsum	1J2F 1QWT 1T2K 1ZOQ 2O61 2O6G 2PI0 3A77 3QU6
ProteinModelPortal	Q14653
SMR	Q14653
BioGrid	109869
DIP	DIP-41448N
IntAct	Q14653
MINT	MINT-253351
STRING	9606.ENSP00000310127
PhosphoSite	Q14653
BioMuta	IRF3
DMDM	2497442
MaxQB	Q14653
PaxDb	Q14653
PeptideAtlas	Q14653
PRIDE	Q14653
DNASU	3661
Ensembl	ENST00000309877 ENST00000377139 ENST00000442265 ENST00000596765 ENST00000597198 ENST00000599223 ENST00000600022 ENST00000601291
GeneID	3661
KEGG	hsa:3661
UCSC	uc002pot.2 uc002pou.3 uc002pow.3
CTD	3661
GeneCards	GC19M050162
HGNC	HGNC:6118
HPA	CAB013018 HPA004895
MIM	603734
neXtProt	NX_Q14653
PharmGKB	PA29917
eggNOG	NOG42868
GeneTree	ENSGT00760000119093
HOGENOM	HOG000033705
HOVERGEN	HBG105601
InParanoid	Q14653
KO	K05411
OMA	CHTYWAV
OrthoDB	EOG7CCBR1
PhylomeDB	Q14653
TreeFam	TF328512
Reactome	REACT_115831 REACT_118811 REACT_163743 REACT_163977 REACT_163993 REACT_24938 REACT_24970 REACT_25026 REACT_25078 REACT_25148 REACT_25162 REACT_25271
ChiTaRS	IRF3
EvolutionaryTrace	Q14653
GeneWiki	IRF3
GenomeRNAi	3661
NextBio	14319
PRO	PR:Q14653
Proteomes	UP000005640
Bgee	Q14653
CleanEx	HS_IRF3
ExpressionAtlas	Q14653
Genevisible	Q14653
GO	GO:0005737 GO:0005829 GO:0005654 GO:0005634 GO:0003677 GO:0042802 GO:0042803 GO:0000975 GO:0003700 GO:0003712 GO:0006915 GO:0006974 GO:0071359 GO:0019221 GO:0051607 GO:0045087 GO:0060333 GO:0031663 GO:0071888 GO:0039530 GO:0002756 GO:0032480 GO:0050715 GO:0043123 GO:0032727 GO:0032728 GO:0032481 GO:0060340 GO:0097300 GO:0043330 GO:0034138 GO:0034142 GO:0002224 GO:0006366 GO:0035666 GO:0045351 GO:0060337 GO:0016032
Gene3D	1.10.10.10 2.60.200.10
InterPro	IPR019817 IPR001346 IPR019471 IPR017855 IPR008984 IPR011991
Pfam	PF00605 PF10401
PRINTS	PR00267
SMART	SM00348
SUPFAM	SSF49879
PROSITE	PS00601 PS51507

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:19274049^[1]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:19274049^[1]	ECO:0000255	match to sequence model evidence used in manual assertion	InterPro:IPR001346	F		Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	GO_REF:0000113	ECO:0005556	multiple sequence alignment evidence used in manual assertion	UniProtKB:P15314	F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:22394562^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0035666	TRIF-dependent toll-like receptor signaling pathway	PMID:25636800^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032481	positive regulation of type I interferon production	PMID:25636800^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:11583620^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P45481	F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:9660935^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(NCBI_Gene:3458)	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:17560375^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(NCBI_Gene:15977)	Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	PMID:23332764^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	GO_REF:0000036	ECO:0000305	curator inference used in manual assertion	GO:0043565,GO:0045944	F		Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	PMID:17560375^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_regulation_target:(NCBI_Gene:15977) occurs_at:(SO:0001952)	Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	GO_REF:0000036	ECO:0000305	curator inference used in manual assertion	GO:0000978,GO:0045944	F	occurs_at:(SO:0001952)	Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	PMID:17560375^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_regulation_target:(NCBI_Gene:15977)	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:12062447^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17079289^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:18818105^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17079289^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:18818105^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:12062447^[8]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P70671	P		Seeded From UniProt	complete
involved_in	GO:0032728	positive regulation of interferon-beta production	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P70671	P		Seeded From UniProt	complete
	GO:0039529	RIG-I signaling pathway	PMID:26243192^[11]	ECO:0000314			P		Figure S1 shows lack of IRF3 expression in strains where transcription of RLR pathway intermediates are interfered with (MDA5 and IPS-1)	complete CACAO 11204
involved_in	GO:0032727	positive regulation of interferon-alpha production	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P70671	P		Seeded From UniProt	complete
	GO:0039530	MDA-5 signaling pathway	PMID:26243192^[11]	ECO:0000314			P		Figure S1 shows lack of IRF3 expression when MDA5 expression is inhibited	complete CACAO 11205
part_of	GO:0005634	nucleus	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1096873 MGI:MGI:1859179 MGI:MGI:96395 MGI:MGI:96590 PANTHER:PTN000942746 RGD:2920 UniProtKB:O14896 UniProtKB:P10914 UniProtKB:P14316 UniProtKB:Q02556 UniProtKB:Q13568 UniProtKB:Q14653 UniProtKB:Q15306 UniProtKB:Q92985 ZFIN:ZDB-GENE-041114-13 ZFIN:ZDB-GENE-070912-330	C		Seeded From UniProt	complete
involved_in	GO:0002376	immune system process	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1096873 MGI:MGI:1350924 MGI:MGI:1859179 MGI:MGI:1859212 MGI:MGI:96395 MGI:MGI:96590 PANTHER:PTN000942747 UniProtKB:P10914 UniProtKB:P14316 UniProtKB:Q02556 UniProtKB:Q92985 ZFIN:ZDB-GENE-040718-367 ZFIN:ZDB-GENE-070912-330	P		Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1859212 PANTHER:PTN000942746 UniProtKB:P10914 UniProtKB:P14316 UniProtKB:Q02556 UniProtKB:Q14653 UniProtKB:Q15306 UniProtKB:Q92985 ZFIN:ZDB-GENE-070912-330	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25609649^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23746807^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22728658^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22000020^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21782231^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21102435^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20581830^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20403326^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19454348^[21]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19416887^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18725644^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16301520^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15841462^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071360	cellular response to exogenous dsRNA	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5XIB0 ensembl:ENSRNOP00000027786	P		Seeded From UniProt	complete
involved_in	GO:0050715	positive regulation of cytokine secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5XIB0 ensembl:ENSRNOP00000027786	P		Seeded From UniProt	complete
involved_in	GO:0043123	positive regulation of I-kappaB kinase/NF-kappaB signaling	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5XIB0 ensembl:ENSRNOP00000027786	P		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR019471 InterPro:IPR019817	F		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR019471 InterPro:IPR019817	P		Seeded From UniProt	complete
enables	GO:0044212	transcription regulatory region DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001346	F		Seeded From UniProt	complete
involved_in	GO:0006366	transcription by RNA polymerase II	PMID:8524823^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003712	transcription coregulator activity	PMID:8524823^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0071888	macrophage apoptotic process	PMID:16846591^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0039530	MDA-5 signaling pathway	PMID:16979567^[28]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032728	positive regulation of interferon-beta production	PMID:16979567^[28]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:16979567^[28]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:20049431^[29]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060337	type I interferon signaling pathway	Reactome:R-HSA-909733	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060333	interferon-gamma-mediated signaling pathway	Reactome:R-HSA-877300	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035666	TRIF-dependent toll-like receptor signaling pathway	Reactome:R-HSA-936964 Reactome:R-HSA-9013973	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032481	positive regulation of type I interferon production	Reactome:R-HSA-3270619 Reactome:R-HSA-1834949	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:0032479	regulation of type I interferon production	Reactome:R-HSA-3134975	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-918232 Reactome:R-HSA-918229 Reactome:R-HSA-9013979 Reactome:R-HSA-9013978 Reactome:R-HSA-8948709 Reactome:R-HSA-3249392 Reactome:R-HSA-2396007 Reactome:R-HSA-2396002 Reactome:R-HSA-2395992 Reactome:R-HSA-2032396 Reactome:R-HSA-1834939 Reactome:R-HSA-177671 Reactome:R-HSA-168933 Reactome:R-HSA-166271 Reactome:R-HSA-166245 Reactome:R-HSA-1606327 Reactome:R-HSA-1169394 Reactome:R-HSA-1031716 Reactome:R-HSA-1028821 Reactome:R-HSA-1028816 Reactome:R-HSA-1015702	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-936462 Reactome:R-HSA-936380 Reactome:R-HSA-3134883 Reactome:R-HSA-2032396 Reactome:R-HSA-177671 Reactome:R-HSA-1028820 Reactome:R-HSA-1028819 Reactome:R-HSA-1028817 Reactome:R-HSA-1028816 Reactome:R-HSA-1028815	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		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: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
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: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
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
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:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page
↑ Tanaka, Y & Chen, ZJ (2012) STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway. Sci Signal 5 ra20 PubMed GONUTS page
↑ ^3.0 ^3.1 Liu, S et al. (2015) Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation. Science 347 aaa2630 PubMed GONUTS page
↑ Lin, CH et al. (2001) A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies. Mol. Cell 8 581-90 PubMed GONUTS page
↑ Wathelet, MG et al. (1998) Virus infection induces the assembly of coordinately activated transcription factors on the IFN-beta enhancer in vivo. Mol. Cell 1 507-18 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Escalante, CR et al. (2007) Structure of IRF-3 bound to the PRDIII-I regulatory element of the human interferon-beta enhancer. Mol. Cell 26 703-16 PubMed GONUTS page
↑ Jolma, A et al. (2013) DNA-binding specificities of human transcription factors. Cell 152 327-39 PubMed GONUTS page
↑ ^8.0 ^8.1 Shinobu, N et al. (2002) Involvement of TIRAP/MAL in signaling for the activation of interferon regulatory factor 3 by lipopolysaccharide. FEBS Lett. 517 251-6 PubMed GONUTS page
↑ ^9.0 ^9.1 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
↑ ^10.0 ^10.1 Zhong, B et al. (2008) The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity 29 538-50 PubMed GONUTS page
↑ ^11.0 ^11.1 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
↑ ^12.0 ^12.1 ^12.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Li, X et al. (2015) Proteomic analyses reveal distinct chromatin-associated and soluble transcription factor complexes. Mol. Syst. Biol. 11 775 PubMed GONUTS page
↑ Shu, C et al. (2013) Structural insights into the functions of TBK1 in innate antimicrobial immunity. Structure 21 1137-48 PubMed GONUTS page
↑ Shu, C et al. (2012) Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Nat. Struct. Mol. Biol. 19 722-4 PubMed GONUTS page
↑ Chen, H et al. (2011) Activation of STAT6 by STING is critical for antiviral innate immunity. Cell 147 436-46 PubMed GONUTS page
↑ Hou, F et al. (2011) MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 146 448-61 PubMed GONUTS page
↑ Hayakawa, S et al. (2011) ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses. Nat. Immunol. 12 37-44 PubMed GONUTS page
↑ Kim, H & Seed, B (2010) The transcription factor MafB antagonizes antiviral responses by blocking recruitment of coactivators to the transcription factor IRF3. Nat. Immunol. 11 743-50 PubMed GONUTS page
↑ Zeng, W et al. (2010) Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 141 315-30 PubMed GONUTS page
↑ Gack, MU et al. (2009) Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I. Cell Host Microbe 5 439-49 PubMed GONUTS page
↑ Li, Y et al. (2009) ISG56 is a negative-feedback regulator of virus-triggered signaling and cellular antiviral response. Proc. Natl. Acad. Sci. U.S.A. 106 7945-50 PubMed GONUTS page
↑ Das, K et al. (2008) Structural basis for suppression of a host antiviral response by influenza A virus. Proc. Natl. Acad. Sci. U.S.A. 105 13093-8 PubMed GONUTS page
↑ Li, XD et al. (2005) Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity. Proc. Natl. Acad. Sci. U.S.A. 102 17717-22 PubMed GONUTS page
↑ Otsuka, M et al. (2005) Interaction between the HCV NS3 protein and the host TBK1 protein leads to inhibition of cellular antiviral responses. Hepatology 41 1004-12 PubMed GONUTS page
↑ ^26.0 ^26.1 Au, WC et al. (1995) Identification of a member of the interferon regulatory factor family that binds to the interferon-stimulated response element and activates expression of interferon-induced genes. Proc. Natl. Acad. Sci. U.S.A. 92 11657-61 PubMed GONUTS page
↑ Solis, M et al. (2006) Distinct functions of IRF-3 and IRF-7 in IFN-alpha gene regulation and control of anti-tumor activity in primary macrophages. Biochem. Pharmacol. 72 1469-76 PubMed GONUTS page
↑ ^28.0 ^28.1 ^28.2 Honda, K et al. (2006) Type I interferon [corrected] gene induction by the interferon regulatory factor family of transcription factors. Immunity 25 349-60 PubMed GONUTS page
↑ Savitsky, D et al. (2010) Regulation of immunity and oncogenesis by the IRF transcription factor family. Cancer Immunol. Immunother. 59 489-510 PubMed GONUTS page

[PMID:19274049-1] 1.0 ^1.1 Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page

[PMID:22394562-2] Tanaka, Y & Chen, ZJ (2012) STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway. Sci Signal 5 ra20 PubMed GONUTS page

[PMID:25636800-3] 3.0 ^3.1 Liu, S et al. (2015) Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation. Science 347 aaa2630 PubMed GONUTS page

[PMID:11583620-4] Lin, CH et al. (2001) A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies. Mol. Cell 8 581-90 PubMed GONUTS page

[PMID:9660935-5] Wathelet, MG et al. (1998) Virus infection induces the assembly of coordinately activated transcription factors on the IFN-beta enhancer in vivo. Mol. Cell 1 507-18 PubMed GONUTS page

[PMID:17560375-6] 6.0 ^6.1 ^6.2 Escalante, CR et al. (2007) Structure of IRF-3 bound to the PRDIII-I regulatory element of the human interferon-beta enhancer. Mol. Cell 26 703-16 PubMed GONUTS page

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