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Interferon regulatory factor 8 (IRF-8) (Interferon consensus sequence-binding protein) (H-ICSBP) (ICSBP)

 IRF8_HUMAN              Reviewed;         426 AA.
Q02556; A0AV82;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 2.
08-MAY-2019, entry version 172.
RecName: Full=Interferon regulatory factor 8;
Short=IRF-8;
AltName: Full=Interferon consensus sequence-binding protein;
Short=H-ICSBP;
Short=ICSBP;
Name=IRF8; Synonyms=ICSBP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY IFNG.
TISSUE=Lung, and Monocyte;
PubMed=1460054;
Weisz A., Marx P., Sharf R., Appella E., Driggers P.H., Ozato K.,
Levi B.-Z.;
"Human interferon consensus sequence binding protein is a negative
regulator of enhancer elements common to interferon-inducible genes.";
J. Biol. Chem. 267:25589-25596(1992).
[2]
SEQUENCE REVISION.
Schmidt M.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH COPS2.
PubMed=10991940; DOI=10.1074/jbc.M004900200;
Cohen H., Azriel A., Cohen T., Meraro D., Hashmueli S.,
Bech-Otschir D., Kraft R., Dubiel W., Levi B.Z.;
"Interaction between interferon consensus sequence-binding protein and
COP9/signalosome subunit CSN2 (Trip15). A possible link between
interferon regulatory factor signaling and the COP9/signalosome.";
J. Biol. Chem. 275:39081-39089(2000).
[5]
INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23166356; DOI=10.1084/jem.20121387;
Basso K., Schneider C., Shen Q., Holmes A.B., Setty M., Leslie C.,
Dalla-Favera R.;
"BCL6 positively regulates AID and germinal center gene expression via
repression of miR-155.";
J. Exp. Med. 209:2455-2465(2012).
[6]
VARIANTS [LARGE SCALE ANALYSIS] LYS-81 AND THR-197.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[7]
VARIANT IMD32A ALA-80, VARIANT IMD32B GLU-108, CHARACTERIZATION OF
VARIANT IMD32A ALA-80, CHARACTERIZATION OF VARIANT IMD32B GLU-108,
INVOLVEMENT IN IMD32A, AND INVOLVEMENT IN IMD32B.
PubMed=21524210; DOI=10.1056/NEJMoa1100066;
Hambleton S., Salem S., Bustamante J., Bigley V., Boisson-Dupuis S.,
Azevedo J., Fortin A., Haniffa M., Ceron-Gutierrez L., Bacon C.M.,
Menon G., Trouillet C., McDonald D., Carey P., Ginhoux F., Alsina L.,
Zumwalt T.J., Kong X.F., Kumararatne D., Butler K., Hubeau M.,
Feinberg J., Al-Muhsen S., Cant A., Abel L., Chaussabel D.,
Doffinger R., Talesnik E., Grumach A., Duarte A., Abarca K.,
Moraes-Vasconcelos D., Burk D., Berghuis A., Geissmann F., Collin M.,
Casanova J.L., Gros P.;
"IRF8 mutations and human dendritic-cell immunodeficiency.";
N. Engl. J. Med. 365:127-138(2011).
[8]
CHARACTERIZATION OF VARIANT IMD32B GLU-108, FUNCTION, SUBCELLULAR
LOCATION, UBIQUITINATION, DESUMOYLATION, AND MUTAGENESIS OF LYS-108.
PubMed=25122610; DOI=10.1182/blood-2014-04-570879;
Salem S., Langlais D., Lefebvre F., Bourque G., Bigley V., Haniffa M.,
Casanova J.L., Burk D., Berghuis A., Butler K.M., Leahy T.R.,
Hambleton S., Gros P.;
"Functional characterization of the human dendritic cell
immunodeficiency associated with the IRF8(K108E) mutation.";
Blood 124:1894-1904(2014).
[9]
FUNCTION.
PubMed=29434592; DOI=10.3389/fimmu.2018.00062;
Agod Z., Pazmandi K., Bencze D., Vereb G., Biro T., Szabo A.,
Rajnavolgyi E., Bacsi A., Engel P., Lanyi A.;
"Signaling lymphocyte activation molecule family 5 enhances autophagy
and fine-tunes cytokine response in monocyte-derived dendritic cells
via stabilization of interferon regulatory factor 8.";
Front. Immunol. 9:62-62(2018).
-!- FUNCTION: Plays a role as a transcriptional activator or repressor
(PubMed:25122610). Specifically binds to the upstream regulatory
region of type I IFN and IFN-inducible MHC class I genes (the
interferon consensus sequence (ICS)). Plays a negative regulatory
role in cells of the immune system. Involved in CD8(+) dendritic
cell differentiation by forming a complex with the BATF-JUNB
heterodimer in immune cells, leading to recognition of AICE
sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory
element, followed by cooperative binding of BATF and IRF8 and
activation of genes (By similarity). Positively regulates
macroautophagy in dendritic cells (PubMed:29434592).
{ECO:0000250|UniProtKB:P23611, ECO:0000269|PubMed:25122610,
ECO:0000269|PubMed:29434592}.
-!- SUBUNIT: Interacts (via C-terminus) with TRIM21 (via C-terminus).
Interacts with the BATF-JUNB heterodimer. Interacts with BATF (via
bZIP domain); the interaction is direct (By similarity). Interacts
with COPS2. {ECO:0000250, ECO:0000269|PubMed:10991940}.
-!- INTERACTION:
O14896:IRF6; NbExp=3; IntAct=EBI-2866563, EBI-6115643;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23166356,
ECO:0000269|PubMed:25122610}. Cytoplasm
{ECO:0000269|PubMed:25122610}. Note=In resting macrophages,
localizes in the cytoplasm. Translocated in the nucleus upon IFN-
gamma induction. {ECO:0000269|PubMed:25122610}.
-!- TISSUE SPECIFICITY: Predominantly expressed in lymphoid tissues.
{ECO:0000269|PubMed:1460054, ECO:0000269|PubMed:23166356}.
-!- INDUCTION: By IFNG/IFN-gamma. Negatively regulated by microRNA-155
(miR155). {ECO:0000269|PubMed:1460054,
ECO:0000269|PubMed:23166356}.
-!- PTM: Ubiquitinated (PubMed:25122610). Ubiquitination by TRIM21 in
macrophages, a process that is strongly increased upon interferon
gamma stimulation, leds to the enhanced transcriptional activity
of target cytokine genes (By similarity). Ubiquitination leads to
its degradation by the proteasome (PubMed:25122610). {ECO:0000250,
ECO:0000269|PubMed:25122610}.
-!- PTM: Sumoylated with SUMO3. Desumoylated by SENP1.
{ECO:0000269|PubMed:25122610}.
-!- DISEASE: Immunodeficiency 32A (IMD32A) [MIM:614893]: An
immunologic disorder characterized by abnormal peripheral blood
myeloid phenotype with a marked loss of CD11C-positive/CD1C
dendritic cells, resulting in selective susceptibility to
mycobacterial infections. {ECO:0000269|PubMed:21524210}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Immunodeficiency 32B (IMD32B) [MIM:226990]: An autosomal
recessive primary immunodeficiency characterized by monocyte and
dendritic cell deficiency, myeloproliferation, and susceptibility
to severe opportunistic infections, including disseminated BCG
infection and oral candidiasis. {ECO:0000269|PubMed:21524210,
ECO:0000269|PubMed:25122610}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
ProRule:PRU00840}.
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EMBL; M91196; AAB63813.1; -; mRNA.
EMBL; BC126247; AAI26248.1; -; mRNA.
CCDS; CCDS10956.1; -.
PIR; A45064; A45064.
RefSeq; NP_002154.1; NM_002163.2.
SMR; Q02556; -.
BioGrid; 109621; 23.
IntAct; Q02556; 11.
STRING; 9606.ENSP00000268638; -.
iPTMnet; Q02556; -.
PhosphoSitePlus; Q02556; -.
BioMuta; IRF8; -.
DMDM; 6016308; -.
jPOST; Q02556; -.
MaxQB; Q02556; -.
PaxDb; Q02556; -.
PeptideAtlas; Q02556; -.
PRIDE; Q02556; -.
ProteomicsDB; 58110; -.
Ensembl; ENST00000268638; ENSP00000268638; ENSG00000140968.
GeneID; 3394; -.
KEGG; hsa:3394; -.
UCSC; uc002fjh.4; human.
CTD; 3394; -.
DisGeNET; 3394; -.
GeneCards; IRF8; -.
HGNC; HGNC:5358; IRF8.
HPA; CAB013480; -.
HPA; HPA002267; -.
HPA; HPA002531; -.
MalaCards; IRF8; -.
MIM; 226990; phenotype.
MIM; 601565; gene.
MIM; 614893; phenotype.
neXtProt; NX_Q02556; -.
OpenTargets; ENSG00000140968; -.
Orphanet; 319600; Mendelian susceptibility to mycobacterial diseases due to partial IRF8 deficiency.
PharmGKB; PA29606; -.
eggNOG; ENOG410IED8; Eukaryota.
eggNOG; ENOG410XNYR; LUCA.
GeneTree; ENSGT00940000158140; -.
HOGENOM; HOG000010107; -.
InParanoid; Q02556; -.
KO; K10155; -.
OMA; QIDSNMY; -.
OrthoDB; 648909at2759; -.
PhylomeDB; Q02556; -.
TreeFam; TF328512; -.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
SignaLink; Q02556; -.
SIGNOR; Q02556; -.
ChiTaRS; IRF8; human.
GeneWiki; IRF8; -.
GenomeRNAi; 3394; -.
PRO; PR:Q02556; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000140968; Expressed in 213 organ(s), highest expression level in tonsil.
ExpressionAtlas; Q02556; baseline and differential.
Genevisible; Q02556; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0002376; P:immune system process; IBA:GO_Central.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0030099; P:myeloid cell differentiation; IEA:Ensembl.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
CDD; cd00103; IRF; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 2.60.200.10; -; 1.
InterPro; IPR019817; Interferon_reg_fac_CS.
InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
InterPro; IPR019471; Interferon_reg_factor-3.
InterPro; IPR017855; SMAD-like_dom_sf.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR11949; PTHR11949; 1.
Pfam; PF00605; IRF; 1.
Pfam; PF10401; IRF-3; 1.
PRINTS; PR00267; INTFRNREGFCT.
SMART; SM00348; IRF; 1.
SMART; SM01243; IRF-3; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS00601; IRF_1; 1.
PROSITE; PS51507; IRF_2; 1.
1: Evidence at protein level;
Activator; Autophagy; Complete proteome; Cytoplasm; Disease mutation;
DNA-binding; Nucleus; Polymorphism; Reference proteome; Repressor;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 426 Interferon regulatory factor 8.
/FTId=PRO_0000154564.
DNA_BIND 7 114 IRF tryptophan pentad repeat.
{ECO:0000255|PROSITE-ProRule:PRU00840}.
VARIANT 80 80 T -> A (in IMD32A; impairs
transcriptional activity by disrupting
the interaction between IRF8 and DNA;
dbSNP:rs397514711).
{ECO:0000269|PubMed:21524210}.
/FTId=VAR_070084.
VARIANT 81 81 R -> K (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036490.
VARIANT 108 108 K -> E (in IMD32B; in resting
macrophages, no effect on cytoplasmic
subcellular localization; loss of nuclear
subcellular localization upon IFN-gamma
induction; decreased protein abundance;
increased proteasome-dependent
degradation; increased ubiquitination and
sumoylation; loss of transcriptional
repressor activity; loss of IRF1-
dependent transcriptional repressor
activity; loss of IRF1-dependent
transcriptional activator activity;
impairs transcriptional activity by
disrupting the interaction between IRF8
and DNA; dbSNP:rs397514710).
{ECO:0000269|PubMed:21524210,
ECO:0000269|PubMed:25122610}.
/FTId=VAR_070085.
VARIANT 197 197 A -> T (in a breast cancer sample;
somatic mutation; dbSNP:rs1372132995).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036491.
MUTAGEN 108 108 K->H: In resting macrophages, no effect
on cytoplasmic subcellular localization.
Decreased nuclear subcellular
localization upon IFN-gamma induction.
Partial loss of IRF1-dependent
transcriptional activator activity.
{ECO:0000269|PubMed:25122610}.
MUTAGEN 108 108 K->Q: In resting macrophages, no effect
on cytoplasmic subcellular localization.
Loss of nuclear subcellular localization
upon IFN-gamma induction. Loss of IRF1-
dependent transcriptional activator
activity. {ECO:0000269|PubMed:25122610}.
MUTAGEN 108 108 K->R: In resting macrophages, no effect
on cytoplasmic subcellular localization.
No effect on nuclear subcellular
localization upon IFN-gamma induction. No
effect on transcriptional activator
activity. No effect on IRF1-dependent
transcriptional activator activity.
{ECO:0000269|PubMed:25122610}.
SEQUENCE 426 AA; 48356 MW; 1535D1B7C83E0355 CRC64;
MCDRNGGRRL RQWLIEQIDS SMYPGLIWEN EEKSMFRIPW KHAGKQDYNQ EVDASIFKAW
AVFKGKFKEG DKAEPATWKT RLRCALNKSP DFEEVTDRSQ LDISEPYKVY RIVPEEEQKC
KLGVATAGCV NEVTEMECGR SEIDELIKEP SVDDYMGMIK RSPSPPEACR SQLLPDWWAQ
QPSTGVPLVT GYTTYDAHHS AFSQMVISFY YGGKLVGQAT TTCPEGCRLS LSQPGLPGTK
LYGPEGLELV RFPPADAIPS ERQRQVTRKL FGHLERGVLL HSSRQGVFVK RLCQGRVFCS
GNAVVCKGRP NKLERDEVVQ VFDTSQFFRE LQQFYNSQGR LPDGRVVLCF GEEFPDMAPL
RSKLILVQIE QLYVRQLAEE AGKSCGAGSV MQAPEEPPPD QVFRMFPDIC ASHQRSFFRE
NQQITV


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WP1836: Interferon gamma signaling
WP619: Type II interferon signaling (IFNG)
WP2292: Chemokine signaling pathway
WP786: Type II interferon signaling (IFNG)
WP900: Type II interferon signaling (IFNG)
WP1350: Type II interferon signaling (IFNG)
WP1493: Carbon assimilation C4 pathway
WP1835: Interferon alpha/beta signaling
WP2113: Type III interferon signaling
WP1017: Type II interferon signaling (IFNG)
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1136: Type II interferon signaling (IFNG)
WP1289: Type II interferon signaling (IFNG)
WP1531: Vitamin D synthesis
WP1837: Interferon Signaling
WP585: Interferon type I
WP1616: ABC transporters
WP1909: Signal regulatory protein (SIRP) family interactions
WP1657: Glycerolipid metabolism
WP1983: Splicing factor NOVA regulated synpatic proteins
WP927: Signaling of Hepatocyte Growth Factor Receptor

Related Genes :
[IRF8 ICSBP1] Interferon regulatory factor 8 (IRF-8) (Interferon consensus sequence-binding protein) (H-ICSBP) (ICSBP)
[Irf8 Icsbp Icsbp1] Interferon regulatory factor 8 (IRF-8) (Interferon consensus sequence-binding protein) (ICSBP)
[IRF8 ICSBP ICSBP1] Interferon regulatory factor 8 (IRF-8) (Interferon consensus sequence-binding protein) (ICSBP)
[IRF3] Interferon regulatory factor 3 (IRF-3)
[Irf3] Interferon regulatory factor 3 (IRF-3)
[IRF7] Interferon regulatory factor 7 (IRF-7)
[IRF1] Interferon regulatory factor 1 (IRF-1)
[IRF9 ISGF3G] Interferon regulatory factor 9 (IRF-9) (IFN-alpha-responsive transcription factor subunit) (ISGF3 p48 subunit) (Interferon-stimulated gene factor 3 gamma) (ISGF-3 gamma) (Transcriptional regulator ISGF3 subunit gamma)
[IRF6] Interferon regulatory factor 6 (IRF-6)
[IRF5] Interferon regulatory factor 5 (IRF-5)
[Irf7] Interferon regulatory factor 7 (IRF-7)
[IRF2BPL C14orf4 EAP1 KIAA1865 My039] Probable E3 ubiquitin-protein ligase IRF2BPL (EC 2.3.2.27) (Enhanced at puberty protein 1) (Interferon regulatory factor 2-binding protein-like)
[IRF3] Interferon regulatory factor 3 (IRF-3)
[TMEM173 ERIS MITA STING] Stimulator of interferon genes protein (hSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (hMITA) (Transmembrane protein 173)
[Irf5] Interferon regulatory factor 5 (IRF-5)
[Tmem173 Eris Mita Mpys Sting] Stimulator of interferon genes protein (mSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (MMITA) (Transmembrane protein 173)
[TICAM1 PRVTIRB TRIF] TIR domain-containing adapter molecule 1 (TICAM-1) (Proline-rich, vinculin and TIR domain-containing protein B) (Putative NF-kappa-B-activating protein 502H) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (MyD88-3) (TIR domain-containing adapter protein inducing IFN-beta)
[EIF2AK2 PKR PRKR] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[IRF3] Interferon regulatory factor 3 (IRF-3)
[PRDM1 BLIMP1] PR domain zinc finger protein 1 (EC 2.1.1.-) (BLIMP-1) (Beta-interferon gene positive regulatory domain I-binding factor) (PR domain-containing protein 1) (Positive regulatory domain I-binding factor 1) (PRDI-BF1) (PRDI-binding factor 1)
[Prdm1 Blimp1] PR domain zinc finger protein 1 (EC 2.1.1.-) (B lymphocyte-induced maturation protein 1) (Blimp-1) (Beta-interferon gene positive regulatory domain I-binding factor) (PR domain-containing protein 1)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[COPS2 CSN2 TRIP15] COP9 signalosome complex subunit 2 (SGN2) (Signalosome subunit 2) (Alien homolog) (JAB1-containing signalosome subunit 2) (Thyroid receptor-interacting protein 15) (TR-interacting protein 15) (TRIP-15)
[ISG15 G1P2 UCRP] Ubiquitin-like protein ISG15 (Interferon-induced 15 kDa protein) (Interferon-induced 17 kDa protein) (IP17) (Ubiquitin cross-reactive protein) (hUCRP)
[IFNAR2 IFNABR IFNARB] Interferon alpha/beta receptor 2 (IFN-R-2) (IFN-alpha binding protein) (IFN-alpha/beta receptor 2) (Interferon alpha binding protein) (Type I interferon receptor 2)
[IFIH1 MDA5 RH116] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (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)
[Eif2ak2 Prkr] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2)
[Mavs Ips1 Visa] Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Virus-induced-signaling adapter) (VISA)
[IFI16 IFNGIP1] Gamma-interferon-inducible protein 16 (Ifi-16) (Interferon-inducible myeloid differentiation transcriptional activator)
[TXNRD1 GRIM12 KDRF] Thioredoxin reductase 1, cytoplasmic (TR) (EC 1.8.1.9) (Gene associated with retinoic and interferon-induced mortality 12 protein) (GRIM-12) (Gene associated with retinoic and IFN-induced mortality 12 protein) (KM-102-derived reductase-like factor) (Thioredoxin reductase TR1)

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