IRF3

Summary

IRF3 (interferon regulatory factor 3, HGNC:6118) is a protein-coding gene on chromosome 19q13.33, encoding Interferon regulatory factor 3 (Q14653). Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses.

This gene encodes a member of the interferon regulatory transcription factor (IRF) family. The encoded protein is found in an inactive cytoplasmic form that upon serine/threonine phosphorylation forms a complex with CREBBP. This complex translocates to the nucleus and activates the transcription of interferons alpha and beta, as well as other interferon-induced genes. The protein plays an important role in the innate immune response against DNA and RNA viruses. Mutations in this gene are associated with Encephalopathy, acute, infection-induced, herpes-specific, 7.

Source: NCBI Gene 3661 — RefSeq curated summary.

At a glance

• Gene–disease (curated): herpes simplex encephalitis, susceptibility to, 7 (Moderate, GenCC)
• GWAS associations: 3
• Clinical variants (ClinVar): 110 total — 1 likely-pathogenic
• Phenotypes (HPO): 7
• Druggable target: yes
• Transcription factor: yes — 89 downstream targets (CollecTRI)
• MANE Select transcript: NM_001571

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:6118
Approved symbol	IRF3
Name	interferon regulatory factor 3
Location	19q13.33
Locus type	gene with protein product
Status	Approved
Ensembl gene	ENSG00000126456
Ensembl biotype	protein_coding
OMIM	603734
Entrez	3661

Gene structure

Transcript identifiers

Ensembl transcripts: 40 — 30 protein_coding, 4 retained_intron, 3 nonsense_mediated_decay, 3 protein_coding_CDS_not_defined

ENST00000309877, ENST00000377139, ENST00000442265, ENST00000593337, ENST00000593818, ENST00000593922, ENST00000594387, ENST00000595034, ENST00000595240, ENST00000596644, ENST00000596756, ENST00000596765, ENST00000596788, ENST00000596822, ENST00000597180, ENST00000597198, ENST00000597369, ENST00000597636, ENST00000598108, ENST00000598808, ENST00000599144, ENST00000599223, ENST00000599680, ENST00000600022, ENST00000600453, ENST00000600911, ENST00000601291, ENST00000601373, ENST00000601809, ENST00000602190, ENST00000890747, ENST00000890748, ENST00000890749, ENST00000890750, ENST00000890751, ENST00000921360, ENST00000921361, ENST00000921362, ENST00000942552, ENST00000942553

RefSeq mRNA: 8 — MANE Select: NM_001571 NM_001197122, NM_001197123, NM_001197124, NM_001197125, NM_001197126, NM_001197127, NM_001197128, NM_001571

CCDS: CCDS12775, CCDS56099, CCDS59407, CCDS59408, CCDS59409

Canonical transcript exons

ENST00000377139 — 8 exons

Exon	Start	End
ENSE00002224211	49661948	49662328
ENSE00003468287	49659572	49659833
ENSE00003512840	49663188	49663258
ENSE00003652244	49662425	49662617
ENSE00003656814	49663343	49663514
ENSE00003671030	49660713	49660828
ENSE00003686782	49664674	49664846
ENSE00003849326	49665631	49665857

Expression profiles

Bgee: expression breadth ubiquitous, 266 present calls, max score 98.94.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 21.9312 / max 120.3700, expressed in 1810 samples.

FANTOM5 promoters (4 alternative TSS)

Promoter ID	TPM avg	Samples expressed
182070	13.6132	1789
182069	5.6157	1614
182067	1.6385	669
182068	1.0637	577

Top tissues by expression

289 total, by Bgee expression score (0-100, higher = more expressed):

Tissue	Anatomy ID	Expression score	Quality
granulocyte	CL:0000094	98.94	gold quality
right uterine tube	UBERON:0001302	98.14	gold quality
lower esophagus mucosa	UBERON:0035834	97.80	gold quality
mucosa of transverse colon	UBERON:0004991	97.71	gold quality
spleen	UBERON:0002106	97.46	gold quality
right lobe of thyroid gland	UBERON:0001119	97.44	gold quality
endocervix	UBERON:0000458	97.28	gold quality
small intestine Peyer’s patch	UBERON:0003454	97.27	gold quality
left lobe of thyroid gland	UBERON:0001120	97.26	gold quality
adenohypophysis	UBERON:0002196	97.08	gold quality
lymph node	UBERON:0000029	96.92	gold quality
ectocervix	UBERON:0012249	96.78	gold quality
body of stomach	UBERON:0001161	96.76	gold quality
body of pancreas	UBERON:0001150	96.75	gold quality
metanephros cortex	UBERON:0010533	96.72	gold quality
left uterine tube	UBERON:0001303	96.65	gold quality
right ovary	UBERON:0002118	96.64	gold quality
skin of abdomen	UBERON:0001416	96.49	gold quality
left ovary	UBERON:0002119	96.49	gold quality
body of uterus	UBERON:0009853	96.48	gold quality
transverse colon	UBERON:0001157	96.46	gold quality
minor salivary gland	UBERON:0001830	96.41	gold quality
thyroid gland	UBERON:0002046	96.33	gold quality
skin of leg	UBERON:0001511	96.20	gold quality
pituitary gland	UBERON:0000007	96.16	gold quality
right lobe of liver	UBERON:0001114	96.16	gold quality
olfactory segment of nasal mucosa	UBERON:0005386	96.15	gold quality
small intestine	UBERON:0002108	95.95	gold quality
right adrenal gland	UBERON:0001233	95.87	gold quality
upper lobe of left lung	UBERON:0008952	95.84	gold quality

Single-cell (SCXA)

Detected in 2 experiment(s), a significant marker in 1.

Experiment	Marker?	Max mean expression
E-MTAB-7606	no	1687.70
E-ANND-3	no	0.00

Regulation

Is transcription factor: yes

Downstream targets (CollecTRI)

89 targets.

Target	Regulation
ABCC2	Activation
ADAM2
AKT1
CCL19	Activation
CCL2	Unknown
CCL3	Repression
CCL5	Unknown
CDK2
CDK4
CDKN1A	Unknown
CHUK
CISH
CREBBP
CTNNB1
CXCL1	Unknown
CXCL10	Activation
CXCL14
CXCL8	Activation
DDX3X
FGFR1
GPR146	Activation
IFIT1	Activation
IFIT2	Activation
IFN1@
IFNA1	Activation
IFNA14	Activation
IFNA16
IFNA17
IFNA2	Activation
IFNA4	Activation

JASPAR motifs

Motif	Name	Family
MA1418.1	IRF3	Interferon-regulatory factors
MA1418.2	IRF3	Interferon-regulatory factors

JASPAR matrix evidence (PMIDs): PMID:10938111

Upstream regulators (CollecTRI, top): AHR, CDH8, E2F1, IRF3, IRF4, IRF7, LYAR, MYC, NFKB, NRF1, SP1, SP3, ZNF143

Literature-anchored findings (GeneRIF, showing 40)

• human interferon regulatory factor-3 (IRF-3) gene promoter contains a functional SPH element that is bound by SBF/Staf in vitro and in transfected cells (PMID:11724783)
• Preferential binding sites for interferon regulatory factors 3 and 7 involved in interferon-A gene transcription (PMID:11884139)
• IRF-3 recognizes nucleocapsid structures during measles virus infections and triggers induction of interferon production (PMID:11907205)
• Direct involvement of CREB-binding protein/p300 in sequence-specific DNA binding of virus-activated interferon regulatory factor-3 holocomplex. (PMID:11940575)
• IRF-3-dependent, NFkappa B- and JNK-independent activation of the 561 and IFN-beta genes in response to double-stranded RNA (PMID:11972054)
• IRF3 mediates a TLR3/TLR4-specific antiviral gene program. (PMID:12354379)
• IRF3 binds to p300/CBP and acts as a transcription factor (PMID:12473110)
• Ser(396) within the C-terminal Ser/Thr cluster is targeted in vivo for phosphorylation following virus infection and plays an essential role in IRF-3 activation (PMID:12524442)
• hIRF3 inhibited cell growth, blocked DNA synthesis, and induced apoptosis, while a dominant negative mutant transformed 3T3 cells, implying that IRF3 may function as a tumor suppressor and its dominant negative mutant may have a role in tumorigenesis. (PMID:12582166)
• IKKepsilon and TBK1 have a pivotal role in coordinating the activation of IRF3 and NF-kappaB in the innate immune response. (PMID:12692549)
• In Ebola virus-infected cells, VP35 inhibits the induction of antiviral genes, including the IFN-beta gene, by blocking IRF-3 activation (PMID:12829834)
• Bunyamwera (BUN) NSs protein can delay cell death in the early stages of BUN infection by inhibiting IRF-3-mediated apoptosis. (PMID:12829839)
• LPS-TLR4 signaling to IRF-3/7 and NF-kappaB involves the toll adapters TRAM and TRIF. (PMID:14517278)
• p65 promoted transactivation of gene expression by IRF-3; a dominant negative form of I kappa B kinase 2 and a mutant form of I kappa B, which acts as a super-repressor of NF-kappa B, blocked activation of the ISRE (PMID:14557267)
• Ser-386 is the target of the IRF-3 kinase and critical determinant for the activation of IRF-3 (PMID:14703513)
• herpes simplex virus ICP0 blocks interferon regulatory factor IRF3-mediated activation of interferon-stimulated genes; the RING finger domain of ICP0 is essential for this activity (PMID:14747533)
• enveloped particles from RNA and DNA viruses induce interferon-stimulated genes (ISGs) in the absence of IFN production and virus replication through activation of IRF3 (PMID:14747536)
• double-stranded RNA-induced TLR3/TRIF-mediated NF-kappaB and IRF3 activation diverge at TRIF (PMID:14982987)
• IRF3 activities are essential for the initiation of transcription of the IFNbeta gene (PMID:15107417)
• activated by West Nile Virus (WNV)infection. Irf-3 target genes function to constrain WNV infection and limit cell-to-cell virus spread. (PMID:15220448)
• Cytomegalovirus pp65 prevents activation of IRF-3, a primary mediator of the type I interferon response. (PMID:15452220)
• NF-kappaB and interferon regulatory factor, the two major transcription factors activated by virus infection, were essential for the induction of two sets of genes by Sendai virus (PMID:15767394)
• activation inhibited by Rabies virus P protein (PMID:15919920)
• ArgII gene is an early IRF-3-regulated gene, which participates in the interferon-independent antiviral response through polyamine production and induction of apoptosis. (PMID:15955070)
• JEV and DEN-2 initiate the host innate immune response through a molecular mechanism involving RIG-I/IRF-3 and PI3K/NF-kappaB signaling pathways (PMID:16182584)
• Expression of IKK-i can activate both NFkappaB and IRF3, leading to the production of several cytokines including interferon beta. (PMID:16199137)
• The present study identified a specific interaction between IRF3 and chaperone heat-shock protein of 90 kDa (Hsp90).In addition, TBK1 is found to be a client protein of Hsp90 in vivo. (PMID:16394098)
• West Nile virus avoids IRF3 pathway through RIG-1 dependent and independent pathways early in infection when it is most sensitive to host cell defenses (PMID:16501100)
• IRF3 induces cell growth inhibition and cellular senescence through activation of p53 tumor suppressor (PMID:16513254)
• belongs to one signaling pathway that mediates induction of gene expression, which, in concert, mediates proliferative activity toward endothelial cells (PMID:16537515)
• HCV infection transiently induces RIG-I- and IPS-1-dependent IRF-3 activation (PMID:16585524)
• expression of the LCMV nucleoprotein (NP) is sufficient to inhibit both IFN production and nuclear translocation of IRF-3 (PMID:16940530)
• IPS-1, IRF3, and IFNbeta have critical roles in Legionella infection of lung epithelium (PMID:16984921)
• IRF-3 is a key molecule controlling HCV replication through modulation of host interferon gene responses. (PMID:16988763)
• Transduction of active forms of IRF-3 or IRF-7 differentially modulate the apoptotic and antitumor properties of primary macrophages. (PMID:17079482)
• hypothesized that HSV-1 ICP0 recruits activated IRF-3 & CBP/p300 to nuclear structures, away from host chromatin; this leads to inactivation & accelerated degradation of IRF-3, resulting in reduced transcription of IFN-beta & inhibition of host response (PMID:17126870)
• Both the cytoplasmic and TLR3-mediated dsRNA recognition pathways converge upon NAP1 for the activation of the IRF-3 and IFN-beta promoter. (PMID:17142768)
• ability of bICP0 to reduce IRF3 protein levels is important with respect to disarming the interferon response during productive infection (PMID:17215277)
• proteasome dependent IRF3 degradation in rotavirus infected cells is dependent on the presence of rotavirus NSP1 and the integrity of the N-terminal zinc-binding domain. (PMID:17251580)
• Antiviral gene expression in RA, especially due to TLR ligands and TNFalpha, is dependent on IKKepsilon and IRF-3, and this pathway plays a key role in the production of type I IFNs and chemokines such as RANTES. (PMID:17328045)

Cross-species orthologs

3 orthologs

Organism	Symbol	Gene ID
danio_rerio	irf3	ENSDARG00000076251
mus_musculus	Irf3	ENSMUSG00000003184
rattus_norvegicus	Irf3	ENSRNOG00000043388

Paralogs (8): IRF6 (ENSG00000117595), IRF1 (ENSG00000125347), IRF5 (ENSG00000128604), IRF4 (ENSG00000137265), IRF8 (ENSG00000140968), IRF2 (ENSG00000168310), IRF7 (ENSG00000185507), IRF9 (ENSG00000213928)

Protein

Protein identifiers

Interferon regulatory factor 3 — Q14653 (reviewed: Q14653)

All UniProt accessions (14): Q14653, M0QX56, M0QXC8, M0QYT9, M0QYX3, M0QZB7, M0QZB8, M0R007, M0R0R8, M0R0X9, M0R205, M0R3C2, M0R3E9, M0R3H7

UniProt curated annotations — full annotation on UniProt →

Function. Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages. In response to Sendai virus infection, is recruited by TOMM70:HSP90AA1 to mitochondrion and forms an apoptosis complex TOMM70:HSP90AA1:IRF3:BAX inducing apoptosis. Key transcription factor regulating the IFN response during SARS-CoV-2 infection.

Subunit / interactions. Monomer. Homodimer; phosphorylation-induced. Interacts (when phosphorylated) with CREBBP. Interacts with MAVS (via phosphorylated pLxIS motif). Interacts with TICAM1 (via phosphorylated pLxIS motif). Interacts with STING1 (via phosphorylated pLxIS motif). Interacts with IKBKE and TBK1. Interacts with TICAM2. Interacts with RBCK1. Interacts with HERC5. Interacts with DDX3X (phosphorylated at ‘Ser-102’); the interaction allows the phosphorylation and activation of IRF3 by IKBKE. Interacts with TRIM21 and ULK1, in the presence of TRIM21; this interaction leads to IRF3 degradation by autophagy. Interacts with RIOK3; RIOK3 probably mediates the interaction of TBK1 with IRF3. Interacts with ILRUN; the interaction inhibits IRF3 binding to its DNA consensus sequence. Interacts with LYAR; this interaction impairs IRF3 DNA-binding activity. Interacts with TRAF3. Interacts with ZDHHC11; ZDHHC11 recruits IRF3 to STING1 upon DNA virus infection and thereby promotes IRF3 activation. Interacts with HSP90AA1; the interaction mediates IRF3 association with TOMM70. Interacts with BCL2; the interaction decreases upon Sendai virus infection. Interacts with BAX; the interaction is direct, increases upon Sendai virus infection and mediates the formation of the apoptosis complex TOMM70:HSP90AA1:IRF3:BAX. Interacts with DDX56. Interacts with NBR1. (Microbial infection) Interacts with rotavirus A NSP1 (via pLxIS motif); this interaction leads to the proteasome-dependent degradation of IRF3. (Microbial infection) Interacts with herpes virus 8/HHV-8 protein VIRF1. (Microbial infection) Interacts with Seneca Valley virus protease 3C; this interaction is involved in the suppression of IRF3 expression and phosphorylation by the virus. (Microbial infection) Interacts with herpes virus 2/HHV-2 protein ICP27; this interaction inhibits IRF3 phosphorylation and nuclear translocation. (Microbial infection) Interacts with human cytomegalovirus protein UL44; this interaction prevents IRF3 binding to its promoters. (Microbial infection) Interacts with the two fragments of MERS-COV protein N produced by CASP6 through proteolytic cleavage; both interactions inhibit IRF3 nuclear translocation after activation and IFN signaling.

Subcellular location. Cytoplasm. Nucleus. Mitochondrion.

Tissue specificity. Expressed constitutively in a variety of tissues.

Post-translational modifications. Constitutively phosphorylated on many Ser/Thr residues. Activated following phosphorylation by TBK1 and IKBKE. Innate adapter proteins, such as MAVS, STING1 or TICAM1, are first activated by viral RNA, cytosolic DNA, and bacterial lipopolysaccharide (LPS), respectively, leading to activation of the kinases TBK1 and IKBKE. These kinases then phosphorylate the adapter proteins on the pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1. Phosphorylation at Ser-386 is followed by pyrophosphorylation at the same residue, promoting phosphorylation at Ser-396. Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce IFNs. Phosphorylation of IRF3 at Ser-385 and Ser-386 plays an important role in the PBLD-triggered IFN-I cascade. Pyrophosphorylated by UAP1 following phosphorylation at Ser-386 by TBK1. Pyrophosphorylation promotes subsequent phosphorylation at Ser-396, leading to homodimerization of IRF3. Acetylation at Lys-366 by KAT8 inhibits recruimtent to promoters and transcription factor activity. Acetylation by KAT8 is promoted by phosphorylation at Ser-396. Deamidation of Asn-85 by CTPS1 prevents IRF3 from binding DNA, thereby inhibiting the transcription factor activity. Ubiquitinated; ubiquitination involves RBCK1 leading to proteasomal degradation. Polyubiquitinated; ubiquitination involves TRIM21 leading to proteasomal degradation. Ubiquitinated by UBE3C, leading to its degradation. Deubiquitinated by USP5 on both ‘Lys-48’-linked unanchored and ‘Lys-63’-linked anchored polyubiquitin, leading to inhibition of anti-RNA viral innate immunity. ISGylated by HERC5 resulting in sustained IRF3 activation and in the inhibition of IRF3 ubiquitination by disrupting PIN1 binding. The phosphorylation state of IRF3 does not alter ISGylation. Proteolytically cleaved by apoptotic caspases during apoptosis, leading to its inactivation. Cleavage by CASP3 during virus-induced apoptosis inactivates it, preventing cytokine overproduction. (Microbial infection) ISGylated. ISGylation is cleaved and removed by SARS-COV-2 nsp3 which attenuates type I interferon responses. (Microbial infection) Phosphorylation and subsequent activation of IRF3 is inhibited by vaccinia virus protein E3. (Microbial infection) Phosphorylated by herpes simplex virus 1/HHV-1 US3 at Ser-175 to prevent IRF3 activation.

Disease relevance. Encephalopathy, acute, infection-induced, 7, herpes-specific (IIAE7) [MIM:616532] A rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. It is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome. Disease susceptibility is associated with variants affecting the gene represented in this entry.

Activity regulation. In the absence of viral infection, maintained as a monomer in an autoinhibited state. Phosphorylation by TBK1 and IKBKE disrupts this autoinhibition leading to the liberation of the DNA-binding and dimerization activities and its nuclear localization where it can activate type I IFN and ISG genes. Phosphorylation and activation follow the following steps: innate adapter proteins, such as MAVS, STING1 or TICAM1, are first activated by viral RNA, cytosolic DNA and bacterial lipopolysaccharide (LPS), respectively, leading to activation of the kinases TBK1 and IKBKE. These kinases then phosphorylate the adapter proteins on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1. Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce IFNs. (Microbial infection) Activated upon coronavirus SARS-CoV-2 infection.

Similarity. Belongs to the IRF family.

Isoforms (5)

UniProt ID	Names	Canonical?
Q14653-1	1	yes
Q14653-2	2
Q14653-3	3
Q14653-4	4
Q14653-5	5

RefSeq proteins (8): NP_001184051, NP_001184052, NP_001184053, NP_001184054, NP_001184055, NP_001184056, NP_001184057, NP_001562* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR001346	Interferon_reg_fact_DNA-bd_dom	Domain
IPR008984	SMAD_FHA_dom_sf	Homologous_superfamily
IPR017855	SMAD-like_dom_sf	Homologous_superfamily
IPR019471	Interferon_reg_factor-3	Domain
IPR019817	Interferon_reg_fac_CS	Conserved_site
IPR036388	WH-like_DNA-bd_sf	Homologous_superfamily
IPR036390	WH_DNA-bd_sf	Homologous_superfamily

Pfam: PF00605, PF10401

UniProt features (112 total): strand 27, mutagenesis site 23, modified residue 20, helix 12, sequence variant 10, splice variant 5, region of interest 3, cross-link 3, site 2, chain 1, DNA-binding region 1, disulfide bond 1, short sequence motif 1, compositionally biased region 1, sequence conflict 1, turn 1

Structure

Experimental structures (PDB)

18 structures.

PDB	Method	Resolution (Å)
6SJA	X-RAY DIFFRACTION	1.5
5JEL	X-RAY DIFFRACTION	1.6
7JFL	X-RAY DIFFRACTION	1.68
5JEO	X-RAY DIFFRACTION	1.72
6SIV	X-RAY DIFFRACTION	1.75
3A77	X-RAY DIFFRACTION	1.8
5JEJ	X-RAY DIFFRACTION	2
1QWT	X-RAY DIFFRACTION	2.1
1J2F	X-RAY DIFFRACTION	2.3
3QU6	X-RAY DIFFRACTION	2.3
2PI0	X-RAY DIFFRACTION	2.31
1ZOQ	X-RAY DIFFRACTION	2.37
5JEK	X-RAY DIFFRACTION	2.4
5JEM	X-RAY DIFFRACTION	2.5
2O61	X-RAY DIFFRACTION	2.8
5JER	X-RAY DIFFRACTION	2.91
1T2K	X-RAY DIFFRACTION	3
2O6G	X-RAY DIFFRACTION	3.1

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-Q14653-F1	81.58	0.56

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Catalytic / active sites (2): 121–122 (cleavage; by casp3); 125–126 (cleavage; by casp3)

Post-translational modifications (23): 14, 75, 85, 97, 123, 175, 180, 188, 237, 244, 253, 366, 385, 386, 386, 396, 398, 404, 427, 193 …

Disulfide bonds (1): 267–289

Mutagenesis-validated functional residues (23):

Position	Phenotype
77–78	abolishes nuclear localization.
86–87	no effect on subcellular localization.
116	does not affect cleavage by casp3.
121–125	abolished cleavage by casp3.
139–140	abolishes nuclear export.
193	highly diminished isgylation; when associated with r-360 and r-366.
285	abolished interaction with sting1, mavs or ticam1.
288	decreased interaction with ticam1.
290	decreased interaction with ticam1.
313	abolished interaction with sting1, mavs or ticam1.
360	highly diminished isgylation; when associated with r-193 and r-366.
366	highly diminished isgylation; when associated with r-193 and r-360.
385–386	complete loss of viral infection induced phosphorylation.
385	complete loss of viral infection induced phosphorylation.
385	abolishes pbld-induced ifnb, isg15 and ifitm3 expression during virus infection; when associated with a-386.
386	complete loss of viral infection induced phosphorylation. abolished pyrophosphorylation. abolishes pbld-induced ifnb, is
386	phosphomimetic mutant; interacts with crebbp; when associated with e-396.
390	does not affect pyrophosphorylation.
396–405	complete loss of viral infection induced phosphorylation.
396–405	acts as a constitutively activated irf3.
396–398	complete loss of viral infection induced phosphorylation.
396	phosphomimetic mutant; interacts with crebbp; when associated with e-386.
402–405	complete loss of viral infection induced phosphorylation.

Function

Pathways and Gene Ontology

Reactome pathways

39 pathways

ID	Pathway
R-HSA-1169408	ISG15 antiviral mechanism
R-HSA-1606341	IRF3 mediated activation of type 1 IFN
R-HSA-168928	DDX58/IFIH1-mediated induction of interferon-alpha/beta
R-HSA-3134973	LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-HSA-3134975	Regulation of innate immune responses to cytosolic DNA
R-HSA-3270619	IRF3-mediated induction of type I IFN
R-HSA-877300	Interferon gamma signaling
R-HSA-9013973	TICAM1-dependent activation of IRF3/IRF7
R-HSA-909733	Interferon alpha/beta signaling
R-HSA-918233	TRAF3-dependent IRF activation pathway
R-HSA-933541	TRAF6 mediated IRF7 activation
R-HSA-936440	Negative regulators of DDX58/IFIH1 signaling
R-HSA-936964	Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE)
R-HSA-9692916	SARS-CoV-1 activates/modulates innate immune responses
R-HSA-9705671	SARS-CoV-2 activates/modulates innate and adaptive immune responses
R-HSA-9833109	Evasion by RSV of host interferon responses
R-HSA-1169410	Antimicrobial mechanism of IFN-stimulated genes
R-HSA-1280215	Cytokine Signaling in Immune system
R-HSA-1606322	ZBP1(DAI) mediated induction of type I IFNs
R-HSA-1643685	Disease
R-HSA-166016	Toll Like Receptor 4 (TLR4) Cascade
R-HSA-166166	MyD88-independent TLR4 cascade
R-HSA-168164	Toll Like Receptor 3 (TLR3) Cascade
R-HSA-168249	Innate Immune System
R-HSA-168256	Immune System
R-HSA-168898	Toll-like Receptor Cascades
R-HSA-1834941	STING mediated induction of host immune responses
R-HSA-1834949	Cytosolic sensors of pathogen-associated DNA
R-HSA-5663205	Infectious disease
R-HSA-913531	Interferon Signaling

MSigDB gene sets: 275 (showing top): REACTOME_DDX58_IFIH1_MEDIATED_INDUCTION_OF_INTERFERON_ALPHA_BETA, GOBP_RESPONSE_TO_NITROGEN_COMPOUND, GOBP_CELLULAR_RESPONSE_TO_VIRUS, REACTOME_INNATE_IMMUNE_SYSTEM, GOBP_POSITIVE_REGULATION_OF_TYPE_I_INTERFERON_PRODUCTION, REACTOME_CYTOKINE_SIGNALING_IN_IMMUNE_SYSTEM, GOBP_INFLAMMATORY_RESPONSE, GOBP_RESPONSE_TO_PEPTIDE, GOBP_CELLULAR_RESPONSE_TO_LIPID, GOBP_CELLULAR_RESPONSE_TO_BIOTIC_STIMULUS, GOBP_CANONICAL_NF_KAPPAB_SIGNAL_TRANSDUCTION, GRAESSMANN_APOPTOSIS_BY_DOXORUBICIN_DN, GRAESSMANN_RESPONSE_TO_MC_AND_DOXORUBICIN_DN, GOBP_RESPONSE_TO_TYPE_I_INTERFERON, GOBP_POSITIVE_REGULATION_OF_CYTOKINE_PRODUCTION

GO Biological Process (41): immune system process (GO:0002376), cytoplasmic pattern recognition receptor signaling pathway (GO:0002753), regulation of transcription by RNA polymerase II (GO:0006357), apoptotic process (GO:0006915), DNA damage response (GO:0006974), mRNA transcription (GO:0009299), lipopolysaccharide-mediated signaling pathway (GO:0031663), positive regulation of type I interferon production (GO:0032481), positive regulation of interferon-alpha production (GO:0032727), positive regulation of interferon-beta production (GO:0032728), toll-like receptor 4 signaling pathway (GO:0034142), TRIF-dependent toll-like receptor signaling pathway (GO:0035666), MDA-5 signaling pathway (GO:0039530), regulation of apoptotic process (GO:0042981), positive regulation of canonical NF-kappaB signal transduction (GO:0043123), positive regulation of transcription by RNA polymerase II (GO:0045944), regulation of inflammatory response (GO:0050727), defense response to virus (GO:0051607), type I interferon-mediated signaling pathway (GO:0060337), positive regulation of type I interferon-mediated signaling pathway (GO:0060340), cellular response to exogenous dsRNA (GO:0071360), macrophage apoptotic process (GO:0071888), programmed necrotic cell death (GO:0097300), cellular response to virus (GO:0098586), antiviral innate immune response (GO:0140374), cGAS/STING signaling pathway (GO:0140896), positive regulation of cytokine production involved in inflammatory response (GO:1900017), negative regulation of transcription by RNA polymerase II (GO:0000122), positive regulation of cytokine production (GO:0001819), regulation of DNA-templated transcription (GO:0006355), cell surface receptor signaling pathway (GO:0007166), response to bacterium (GO:0009617), regulation of gene expression (GO:0010468), programmed cell death (GO:0012501), signal transduction involved in regulation of gene expression (GO:0023019), response to lipopolysaccharide (GO:0032496), response to exogenous dsRNA (GO:0043330), innate immune response (GO:0045087), positive regulation of innate immune response (GO:0045089), positive regulation of DNA-templated transcription (GO:0045893)

GO Molecular Function (15): RNA polymerase II cis-regulatory region sequence-specific DNA binding (GO:0000978), DNA-binding transcription factor activity, RNA polymerase II-specific (GO:0000981), DNA-binding transcription activator activity (GO:0001216), DNA-binding transcription repressor activity, RNA polymerase II-specific (GO:0001227), DNA-binding transcription activator activity, RNA polymerase II-specific (GO:0001228), DNA binding (GO:0003677), DNA-binding transcription factor activity (GO:0003700), protein domain specific binding (GO:0019904), identical protein binding (GO:0042802), protein homodimerization activity (GO:0042803), sequence-specific DNA binding (GO:0043565), sequence-specific double-stranded DNA binding (GO:1990837), promoter-specific chromatin binding (GO:1990841), transcription cis-regulatory region binding (GO:0000976), protein binding (GO:0005515)

GO Cellular Component (6): chromatin (GO:0000785), nucleus (GO:0005634), nucleoplasm (GO:0005654), cytoplasm (GO:0005737), mitochondrion (GO:0005739), cytosol (GO:0005829)

Reactome top-level categories

Rollup of top-13 pathways:

Category	Pathways
Cytosolic sensors of pathogen-associated DNA	3
Interferon Signaling	3
DDX58/IFIH1-mediated induction of interferon-alpha/beta	3
Antimicrobial mechanism of IFN-stimulated genes	1
ZBP1(DAI) mediated induction of type I IFNs	1
Innate Immune System	1
STING mediated induction of host immune responses	1
Toll Like Receptor 3 (TLR3) Cascade	1
TRIF (TICAM1)-mediated TLR4 signaling	1
SARS-CoV-1-host interactions	1
SARS-CoV-2-host interactions	1
RSV-host interactions	1
Immune System	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
RNA polymerase II transcription regulatory region sequence-specific DNA binding	4
cellular anatomical structure	4
positive regulation of cytokine production	2
regulation of DNA-templated transcription	2
transcription by RNA polymerase II	2
positive regulation of type I interferon production	2
regulation of transcription by RNA polymerase II	2
positive regulation of DNA-templated transcription	2
DNA-binding transcription factor activity	2
transcription cis-regulatory region binding	2
DNA-binding transcription factor activity, RNA polymerase II-specific	2
protein binding	2
intracellular membrane-bounded organelle	2
cytoplasm	2
biological_process	1
pattern recognition receptor signaling pathway	1
intracellular receptor signaling pathway	1
programmed cell death	1
apoptotic signaling pathway	1
execution phase of apoptosis	1
cellular response to stress	1
DNA-templated transcription	1
mRNA metabolic process	1
cell surface receptor signaling pathway	1
cellular response to lipopolysaccharide	1
regulation of type I interferon production	1
type I interferon production	1
interferon-alpha production	1
regulation of interferon-alpha production	1
interferon-beta production	1
regulation of interferon-beta production	1
cell surface toll-like receptor signaling pathway	1
MyD88-independent toll-like receptor signaling pathway	1
cytoplasmic pattern recognition receptor signaling pathway	1
apoptotic process	1
regulation of programmed cell death	1
canonical NF-kappaB signal transduction	1
regulation of canonical NF-kappaB signal transduction	1
positive regulation of intracellular signal transduction	1
inflammatory response	1

Protein interactions and networks

STRING

3960 interactions, top by confidence (×1000):

Protein A	Protein B	Partner UniProt	Score
IRF3	TBK1	Q9UHD2	999
IRF3	IKBKE	Q14164	995
IRF3	EP300	Q09472	992
IRF3	JUN	P05412	992
IRF3	CREBBP	Q92793	989
IRF3	IRF7	Q92985	988
IRF3	MAVS	Q7Z434	987
IRF3	TRIM21	P19474	960
IRF3	IFNB1	P01574	960
IRF3	TLR3	O15455	959
IRF3	RIGI	O95786	959
IRF3	IFIH1	Q9BYX4	938
IRF3	IFNA13	P01562	924
IRF3	SH2D3A	Q9BRG2	920
IRF3	MYD88	P78397	917

IntAct

109 interactions, top by confidence:

A	B	Type	Score
IRF3	IRF3	psi-mi:“MI:0915”(physical association)	0.970
IRF3	IRF3	psi-mi:“MI:0407”(direct interaction)	0.970
IRF3	CREBBP	psi-mi:“MI:0915”(physical association)	0.930
IRF3	CREBBP	psi-mi:“MI:0407”(direct interaction)	0.930
CREBBP	IRF3	psi-mi:“MI:0914”(association)	0.930
CREBBP	IRF3	psi-mi:“MI:0915”(physical association)	0.930
TBK1	IRF3	psi-mi:“MI:0915”(physical association)	0.920
TBK1	IRF3	psi-mi:“MI:0403”(colocalization)	0.920

BioGRID (365): EP300 (Protein-peptide), EP300 (Affinity Capture-Western), IRF3 (Affinity Capture-Western), IRF3 (Reconstituted Complex), IRF3 (Reconstituted Complex), IRF3 (Affinity Capture-Western), IRF3 (Affinity Capture-Western), IRF3 (Biochemical Activity), AKT1 (Affinity Capture-Western), PRDX1 (Two-hybrid), MAVS (Affinity Capture-Western), TBK1 (Affinity Capture-Western), TRAF2 (Affinity Capture-Western), TRAF6 (Affinity Capture-Western), MAVS (Reconstituted Complex)

ESM2 similar proteins: B5DF93, D2HNW6, O14896, P52633, P56477, P70671, P97431, Q08DD6, Q13568, Q14653, Q15561, Q15562, Q1JPG0, Q3B7M3, Q3TC46, Q3ZBK7, Q4JF28, Q4KLN4, Q53GS7, Q58DJ0, Q5DTY9, Q5R8Q4, Q5RAS2, Q62717, Q68DU8, Q6A0A9, Q6DEZ2, Q6NUQ4, Q7L4E1, Q86TB9, Q86UW7, Q86UW9, Q8AVJ1, Q8BK03, Q8BYR5, Q8CDG3, Q8CF97, Q8CID0, Q8HWS3, Q8IY22

Diamond homologs: A0FIN4, O14896, P10914, P14316, P15314, P23570, P23611, P23906, P56477, P70671, P97431, Q00978, Q02556, Q08DD6, Q13568, Q14653, Q15306, Q3SZP0, Q4JF28, Q58DJ0, Q61179, Q64287, Q764M6, Q8R4E0, Q90643, Q90871, Q90876, Q98925, P70434, Q92985, F5HF68

SIGNOR signaling

58 interactions.

A	Effect	B	Mechanism
PRKDC	up-regulates	IRF3	phosphorylation
TBK1	“up-regulates activity”	IRF3	phosphorylation
MAPK8	up-regulates	IRF3	phosphorylation
IRF3	up-regulates	Immune_response
PIN1	“down-regulates quantity by destabilization”	IRF3	binding
IRF3	“up-regulates quantity by expression”	IFNB1	“transcriptional regulation”
IRF3	“up-regulates quantity by expression”	SOCS2	“transcriptional regulation”
IRF3	“up-regulates quantity by expression”	ABCC2	“transcriptional regulation”
NSD3	“up-regulates activity”	IRF3	methylation
MAVS	“up-regulates activity”	IRF3	binding
8a	“down-regulates activity”	IRF3	binding
8b	“down-regulates activity”	IRF3	binding
“Papain-like proteinase”	“down-regulates activity”	IRF3	deubiquitination
“Papain-like proteinase”	“down-regulates activity”	IRF3	binding
N	“down-regulates activity”	IRF3
3b	“down-regulates activity”	IRF3
6	“down-regulates activity”	IRF3
TRIM59	“down-regulates activity”	IRF3
PPP2CA	“down-regulates activity”	IRF3	dephosphorylation
“Host translation inhibitor nsp1”	“down-regulates activity”	IRF3
KPNA2	“up-regulates activity”	IRF3	relocalization
BRLF1	“down-regulates quantity by repression”	IRF3	“transcriptional regulation”
BGLF4	“down-regulates activity”	IRF3	phosphorylation
CDH8	“up-regulates quantity”	IRF3	“transcriptional regulation”
RBCK1	“down-regulates quantity by destabilization”	IRF3	polyubiquitination
TRIM26	“down-regulates quantity by destabilization”	IRF3	polyubiquitination
PTEN	“up-regulates activity”	IRF3	dephosphorylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 42 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

Pathway	Partners	Fold	FDR
SARS-CoV-1 activates/modulates innate immune responses	5	40.0×	3e-05
DDX58/IFIH1-mediated induction of interferon-alpha/beta	5	37.3×	3e-05
SARS-CoV-2 activates/modulates innate and adaptive immune responses	10	26.2×	1e-09
SARS-CoV-2-host interactions	5	17.5×	5e-04
SARS-CoV-2 Infection	5	11.8×	2e-03
SARS-CoV Infections	5	8.2×	6e-03

GO biological processes:

GO term	Partners	Fold	FDR
positive regulation of type I interferon production	7	81.9×	1e-09
positive regulation of interferon-beta production	6	65.3×	1e-07
defense response to virus	8	15.4×	7e-06
positive regulation of canonical NF-kappaB signal transduction	6	12.1×	7e-04
regulation of cell cycle	5	10.4×	4e-03
intracellular signal transduction	6	6.3×	9e-03

Disease & clinical

Clinical variants and AI predictions

ClinVar

110 variants total. Per-class counts are floors (≥ shown; pagination cap):

Classification	Count (floor)
Pathogenic	0
Likely pathogenic	1
Uncertain significance	62
Likely benign	23
Benign	6

Top pathogenic / likely-pathogenic (1)

Variant ID	HGVS	Classification
1220535	GRCh37/hg19 19q13.33(chr19:50071364-50165942)x1	Likely pathogenic

SpliceAI

1318 predictions. Top by Δscore:

Variant	Effect	Δscore
19:49662420:CTCA:C	donor_loss	1.0000
19:49662421:TCACC:T	donor_loss	1.0000
19:49662422:CAC:C	donor_loss	1.0000
19:49662424:C:CG	donor_loss	1.0000
19:49662614:CTTC:C	acceptor_gain	1.0000
19:49662615:TTC:T	acceptor_gain	1.0000
19:49662616:TC:T	acceptor_gain	1.0000
19:49662617:CC:C	acceptor_gain	1.0000
19:49662617:CCTGG:C	acceptor_loss	1.0000
19:49662618:C:CC	acceptor_gain	1.0000
19:49662618:CT:C	acceptor_loss	1.0000
19:49662619:T:A	acceptor_loss	1.0000
19:49662887:C:CA	donor_gain	1.0000
19:49663183:CTCA:C	donor_loss	1.0000
19:49663184:TCAC:T	donor_loss	1.0000
19:49663185:CACC:C	donor_loss	1.0000
19:49663186:A:C	donor_loss	1.0000
19:49663187:C:A	donor_loss	1.0000
19:49663256:CTC:C	acceptor_gain	1.0000
19:49663355:A:AC	donor_gain	1.0000
19:49663356:C:CC	donor_gain	1.0000
19:49660714:TTG:T	donor_gain	0.9900
19:49660715:TG:T	donor_gain	0.9900
19:49662153:G:C	donor_gain	0.9900
19:49662164:C:A	donor_gain	0.9900
19:49662221:T:TA	donor_gain	0.9900
19:49662235:TCGG:T	donor_gain	0.9900
19:49662338:G:T	acceptor_gain	0.9900
19:49662341:A:T	acceptor_gain	0.9900
19:49662343:C:CT	acceptor_gain	0.9900

AlphaMissense

2763 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
19:49663449:C:A	K77N	0.999
19:49663449:C:G	K77N	0.999
19:49663441:A:G	F80S	0.998
19:49663450:T:G	K77T	0.998
19:49664727:A:G	W38R	0.998
19:49664727:A:T	W38R	0.998
19:49663509:C:A	W57C	0.997
19:49663509:C:G	W57C	0.997
19:49663511:A:G	W57R	0.997
19:49663511:A:T	W57R	0.997
19:49664677:G:C	F54L	0.997
19:49664677:G:T	F54L	0.997
19:49664679:A:G	F54L	0.997
19:49664725:C:A	W38C	0.997
19:49664725:C:G	W38C	0.997
19:49664738:A:G	F34S	0.997
19:49663451:T:C	K77E	0.996
19:49663365:T:A	K105N	0.995
19:49663365:T:G	K105N	0.995
19:49663450:T:A	K77M	0.995
19:49663454:A:G	W76R	0.994
19:49663454:A:T	W76R	0.994
19:49664719:G:C	H40Q	0.994
19:49664719:G:T	H40Q	0.994
19:49664722:C:A	K39N	0.994
19:49664722:C:G	K39N	0.994
19:49664737:G:C	F34L	0.994
19:49664737:G:T	F34L	0.994
19:49664739:A:G	F34L	0.994
19:49663438:C:G	R81P	0.993

dbSNP variants (sampled 300 via entrez): RS1000060931 (19:49665657 G>A,C,T), RS1000090313 (19:49665715 C>G), RS1000505753 (19:49663635 A>G), RS1001101629 (19:49665031 C>T), RS1001282160 (19:49665532 G>A), RS1001282847 (19:49659515 C>T), RS1002002215 (19:49661231 C>T), RS1002530853 (19:49665247 A>G), RS1002619985 (19:49664396 T>C,G), RS1003118991 (19:49660373 T>C), RS1003414486 (19:49660215 A>G,T), RS1003537960 (19:49663772 T>G), RS1003565805 (19:49664039 G>A,C), RS1004004358 (19:49660931 C>T), RS1004024873 (19:49666151 C>G,T)

Disease associations

OMIM: gene MIM:603734 | disease phenotypes: MIM:616532, MIM:616056

GenCC curated gene-disease

Disease	Classification	Inheritance
herpes simplex encephalitis, susceptibility to, 7	Moderate	Autosomal dominant

Mondo (2): herpes simplex encephalitis, susceptibility to, 7 (MONDO:0014680), developmental and epileptic encephalopathy, 26 (MONDO:0014477)

Orphanet (2): Herpes simplex virus encephalitis (Orphanet:1930), Non-specific early-onset epileptic encephalopathy (Orphanet:442835)

HPO phenotypes

7 total (7 of 7 shown, HPO-id order):

HPO	Term
HP:0000006	Autosomal dominant inheritance
HP:0001250	Seizure
HP:0002315	Headache
HP:0003621	Juvenile onset
HP:0012302	Herpes simplex encephalitis
HP:0031179	Nuchal rigidity
HP:0200149	CSF lymphocytic pleiocytosis

GWAS associations

3 associations (top):

Study	Trait	p-value
GCST004785_16	Vitiligo	2.000000e-09
GCST006803_99	Schizophrenia	4.000000e-11
GCST010571_75	Autoimmune thyroid disease	4.000000e-11

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL4523293 (SINGLE PROTEIN)

PharmGKB: 1 entry (VIP=true, CPIC=false)

CTD chemical–gene interactions

57 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
Poly I-C	increases phosphorylation, affects reaction, affects localization, decreases reaction, affects cotreatment (+1 more)	4
Air Pollutants	affects cotreatment, increases abundance, increases expression, increases phosphorylation	3
Particulate Matter	increases abundance, increases expression, increases phosphorylation, affects cotreatment	3
lipopolysaccharide, E coli O55-B5	increases activity, increases phosphorylation	2
Vehicle Emissions	affects cotreatment, increases expression, affects localization	2
Cannabidiol	increases expression, affects cotreatment, affects localization, decreases reaction	2
Lipopolysaccharides	affects cotreatment, affects localization, increases phosphorylation, decreases expression, decreases reaction (+1 more)	2
Dronabinol	affects cotreatment, affects localization, decreases reaction, increases localization, decreases expression	2
aristolochic acid I	decreases expression	1
PAM2-CSK4	affects reaction, increases expression	1
triphenyl phosphate	affects expression	1
alpha-pinene	increases abundance, affects cotreatment, increases expression	1
2,2’-methylenebis(4-methyl-6-tert-butylphenol)	affects response to substance, affects expression	1
beta-lapachone	decreases expression	1
mono-(2-ethylhexyl)phthalate	increases expression	1
nickel chloride	decreases expression, decreases reaction	1
benzo(e)pyrene	increases methylation	1
phenyl-N-tert-butylnitrone	increases phosphorylation, decreases reaction	1
coumarin	increases phosphorylation	1
2-chloroethyl ethyl sulfide	increases expression	1
methacrylaldehyde	affects cotreatment, increases expression, increases abundance	1
cyanoginosin LR	increases expression, increases phosphorylation	1
di-n-butylphosphoric acid	affects expression	1
2,3’,4,4’,5-pentachlorobiphenyl	decreases reaction, increases response to substance, affects cotreatment, affects localization, increases phosphorylation (+1 more)	1
esculentoside A	increases phosphorylation	1
FSL-1 lipoprotein, synthetic	affects reaction, increases expression	1
abrine	increases expression	1
Pam(3)CSK(4) peptide	affects reaction, increases expression	1
Antineoplastic Agents, Immunological	decreases response to substance, increases expression	1
Sunitinib	decreases expression	1

ChEMBL screening assays

7 unique, capped per target: 7 binding

Representative assays (with source publication via chembl_document):

Assay ID	Type	Description	Source paper
CHEMBL4325122	Binding	Induction of IRF3 pathway in STING knockout human THP1 cells measured after 20 hrs by luciferase reporter gene assay	Design, Synthesis, and Biological Evaluation of Amidobenzimidazole Derivatives as Stimulator of Interferon Genes (STING) Receptor Agonists. — J Med Chem

Cellosaurus cell lines

13 cell lines: 8 cancer cell line, 3 embryonic stem cell, 1 induced pluripotent stem cell, 1 transformed cell line

First 10 cell lines (id-ordered, not curated):

Cellosaurus	Name	Category	Sex
CVCL_A0MC	AUi001-A	Induced pluripotent stem cell	Female
CVCL_A3F6	SEES3-1V human IRF3, clone1	Embryonic stem cell	Male
CVCL_A3F7	SEES3-1V human IRF3, clone2	Embryonic stem cell	Male
CVCL_A3F8	SEES3-1V human IRF3, clone3	Embryonic stem cell	Male
CVCL_A8AV	THP1-Dual KO-IRF3	Cancer cell line	Male
CVCL_B1G2	Abcam A-549 IRF3 KO 2	Cancer cell line	Male
CVCL_B1UP	Abcam HeLa IRF3 KO	Cancer cell line	Female
CVCL_B2NK	Abcam A-549 IRF3 KO 1	Cancer cell line	Male
CVCL_C0N2	HEK293-IRF3	Transformed cell line	Female
CVCL_D7SH	Ubigene A-549 IRF3 KO	Cancer cell line	Male

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.