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Interferon regulatory factor 7 (IRF-7)

 IRF7_HUMAN              Reviewed;         503 AA.
Q92985; B9EGL3; O00331; O00332; O00333; O75924; Q9UE79;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
17-JUN-2020, entry version 195.
RecName: Full=Interferon regulatory factor 7;
Short=IRF-7;
Name=IRF7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANT GLU-179.
TISSUE=Spleen;
Grossman A., Nicholl J., Antonio L., Luethy R., Suggs S., Sutherland G.R.,
Mak T.W.;
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
PubMed=9315633; DOI=10.1128/mcb.17.10.5748;
Zhang L., Pagano J.S.;
"IRF-7, a new interferon regulatory factor associated with Epstein-Barr
virus latency.";
Mol. Cell. Biol. 17:5748-5757(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), AND VARIANTS GLU-179 AND ARG-412.
PubMed=9786932; DOI=10.1074/jbc.273.44.29210;
Au W.-C., Moore P.A., LaFleur D.W., Tombal B., Pitha P.M.;
"Characterization of the interferon regulatory factor-7 and its potential
role in the transcription activation of interferon A genes.";
J. Biol. Chem. 273:29210-29217(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
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).
[6]
FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=11073981; DOI=10.1128/mcb.20.23.8803-8814.2000;
Marie I.J., Smith E., Prakash A., Levy D.E.;
"Phosphorylation-induced dimerization of interferon regulatory factor 7
unmasks DNA binding and a bipartite transactivation domain.";
Mol. Cell. Biol. 20:8803-8814(2000).
[7]
INHIBITION OF PHOSPHORYLATION BY VACCINIA VIRUS PROTEIN E3.
PubMed=11124948; DOI=10.1074/jbc.m008717200;
Smith E.J., Marie I.J., Prakash A., Garcia-Sastre A., Levy D.E.;
"IRF3 and IRF7 phosphorylation in virus-infected cells does not require
double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is
blocked by Vaccinia virus E3L protein.";
J. Biol. Chem. 276:8951-8957(2001).
[8]
INTERACTION WITH HHV-8 PROTEIN VIRF1.
PubMed=11314014; DOI=10.1038/sj.onc.1204163;
Lin R., Genin P., Mamane Y., Sgarbanti M., Battistini A.,
Harrington W.J. Jr., Barber G.N., Hiscott J.;
"HHV-8 encoded vIRF-1 represses the interferon antiviral response by
blocking IRF-3 recruitment of the CBP/p300 coactivators.";
Oncogene 20:800-811(2001).
[9]
FUNCTION, ACETYLATION AT LYS-92, MUTAGENESIS OF GLY-90; LYS-92 AND THR-93,
AND PHOSPHORYLATION.
PubMed=12374802; DOI=10.1074/jbc.m207484200;
Caillaud A., Prakash A., Smith E., Masumi A., Hovanessian A.G., Levy D.E.,
Marie I.;
"Acetylation of interferon regulatory factor-7 by p300/CREB-binding protein
(CBP)-associated factor (PCAF) impairs its DNA binding.";
J. Biol. Chem. 277:49417-49421(2002).
[10]
REVIEW ON FUNCTION.
PubMed=11846980; DOI=10.1089/107999002753452700;
Zhang L., Pagano J.S.;
"Structure and function of IRF-7.";
J. Interferon Cytokine Res. 22:95-101(2002).
[11]
INTERACTION WITH HHV-8 PROTEIN ORF45 (MICROBIAL INFECTION).
PubMed=11943871; DOI=10.1073/pnas.082420599;
Zhu F.X., King S.M., Smith E.J., Levy D.E., Yuan Y.;
"A Kaposi's sarcoma-associated herpesviral protein inhibits virus-mediated
induction of type I interferon by blocking IRF-7 phosphorylation and
nuclear accumulation.";
Proc. Natl. Acad. Sci. U.S.A. 99:5573-5578(2002).
[12]
INTERACTION WITH TICAM2.
PubMed=14517278; DOI=10.1084/jem.20031023;
Fitzgerald K.A., Rowe D.C., Barnes B.J., Caffrey D.R., Visintin A.,
Latz E., Monks B., Pitha P.M., Golenbock D.T.;
"LPS-TLR4 signaling to IRF-3/7 and NF-kappaB involves the toll adapters
TRAM and TRIF.";
J. Exp. Med. 198:1043-1055(2003).
[13]
ERRATUM OF PUBMED:14517278.
Fitzgerald K.A., Rowe D.C., Barnes B.J., Caffrey D.R., Visintin A.,
Latz E., Monks B., Pitha P.M., Golenbock D.T.;
J. Exp. Med. 198:1451-1451(2003).
[14]
INTERACTION WITH TICAM1.
PubMed=14739303; DOI=10.1074/jbc.m311629200;
Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.;
"Mechanisms of the TRIF-induced interferon-stimulated response element and
NF-kappaB activation and apoptosis pathways.";
J. Biol. Chem. 279:15652-15661(2004).
[15]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[16]
PHOSPHORYLATION AT SER-477 AND SER-479 BY TBK1 AND IKKE, AND MUTAGENESIS OF
477-SER--SER-479.
PubMed=15367631; DOI=10.1128/jvi.78.19.10636-10649.2004;
tenOever B.R., Sharma S., Zou W., Sun Q., Grandvaux N., Julkunen I.,
Hemmi H., Yamamoto M., Akira S., Yeh W.C., Lin R., Hiscott J.;
"Activation of TBK1 and IKKvarepsilon kinases by vesicular stomatitis virus
infection and the role of viral ribonucleoprotein in the development of
interferon antiviral immunity.";
J. Virol. 78:10636-10649(2004).
[17]
SUBCELLULAR LOCATION, AND INTERACTION WITH MYD88.
PubMed=15492225; DOI=10.1073/pnas.0406933101;
Honda K., Yanai H., Mizutani T., Negishi H., Shimada N., Suzuki N.,
Ohba Y., Takaoka A., Yeh W.C., Taniguchi T.;
"Role of a transductional-transcriptional processor complex involving MyD88
and IRF-7 in Toll-like receptor signaling.";
Proc. Natl. Acad. Sci. U.S.A. 101:15416-15421(2004).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYD88 AND TRAF6.
PubMed=15361868; DOI=10.1038/ni1118;
Kawai T., Sato S., Ishii K.J., Coban C., Hemmi H., Yamamoto M., Terai K.,
Matsuda M., Inoue J., Uematsu S., Takeuchi O., Akira S.;
"Interferon-alpha induction through Toll-like receptors involves a direct
interaction of IRF7 with MyD88 and TRAF6.";
Nat. Immunol. 5:1061-1068(2004).
[19]
PHOSPHORYLATION BY IRAK1.
PubMed=15767370; DOI=10.1084/jem.20042372;
Uematsu S., Sato S., Yamamoto M., Hirotani T., Kato H., Takeshita F.,
Matsuda M., Coban C., Ishii K.J., Kawai T., Takeuchi O., Akira S.;
"Interleukin-1 receptor-associated kinase-1 plays an essential role for
Toll-like receptor (TLR)7- and TLR9-mediated interferon-{alpha}
induction.";
J. Exp. Med. 201:915-923(2005).
[20]
REVIEW ON FUNCTION.
PubMed=16846591; DOI=10.1016/j.bcp.2006.06.002;
Solis M., Goubau D., Romieu-Mourez R., Genin P., Civas A., Hiscott J.;
"Distinct functions of IRF-3 and IRF-7 in IFN-alpha gene regulation and
control of anti-tumor activity in primary macrophages.";
Biochem. Pharmacol. 72:1469-1476(2006).
[21]
REVIEW ON FUNCTION.
PubMed=16979567; DOI=10.1016/j.immuni.2006.08.009;
Honda K., Takaoka A., Taniguchi T.;
"Type I interferon gene induction by the interferon regulatory factor
family of transcription factors.";
Immunity 25:349-360(2006).
[22]
ERRATUM OF PUBMED:16979567.
Honda K., Takaoka A., Taniguchi T.;
Immunity 25:849-849(2006).
[23]
FUNCTION.
PubMed=17404045; DOI=10.1196/annals.1397.036;
Sgarbanti M., Marsili G., Remoli A.L., Orsatti R., Battistini A.;
"IRF-7: new role in the regulation of genes involved in adaptive
immunity.";
Ann. N. Y. Acad. Sci. 1095:325-333(2007).
[24]
INTERACTION WITH ROTAVIRUS A NSP1 (MICROBIAL INFECTION).
PubMed=17301153; DOI=10.1128/jvi.02498-06;
Barro M., Patton J.T.;
"Rotavirus NSP1 inhibits expression of type I interferon by antagonizing
the function of interferon regulatory factors IRF3, IRF5, and IRF7.";
J. Virol. 81:4473-4481(2007).
[25]
INTERACTION WITH EPSTEIN-BARR VIRUS/EBV LMP1 (MICROBIAL INFECTION).
PubMed=19017798; DOI=10.1073/pnas.0809933105;
Song Y.J., Izumi K.M., Shinners N.P., Gewurz B.E., Kieff E.;
"IRF7 activation by Epstein-Barr virus latent membrane protein 1 requires
localization at activation sites and TRAF6, but not TRAF2 or TRAF3.";
Proc. Natl. Acad. Sci. U.S.A. 105:18448-18453(2008).
[26]
INTERACTION WITH EPSTEIN-BARR VIRUS/EBV LF2 (MICROBIAL INFECTION).
PubMed=18987133; DOI=10.1128/jvi.00602-08;
Wu L., Fossum E., Joo C.H., Inn K.S., Shin Y.C., Johannsen E.,
Hutt-Fletcher L.M., Hass J., Jung J.U.;
"Epstein-Barr virus LF2: an antagonist to type I interferon.";
J. Virol. 83:1140-1146(2009).
[27]
REVIEW ON FUNCTION.
PubMed=20049431; DOI=10.1007/s00262-009-0804-6;
Savitsky D., Tamura T., Yanai H., Taniguchi T.;
"Regulation of immunity and oncogenesis by the IRF transcription factor
family.";
Cancer Immunol. Immunother. 59:489-510(2010).
[28]
REVIEW ON FUNCTION.
PubMed=21490621; DOI=10.1038/gene.2011.21;
Ning S., Pagano J.S., Barber G.N.;
"IRF7: activation, regulation, modification and function.";
Genes Immun. 12:399-414(2011).
[29]
SUMOYLATION AT LYS-444 AND LYS-446 BY TRIM28.
PubMed=21940674; DOI=10.4049/jimmunol.1101704;
Liang Q., Deng H., Li X., Wu X., Tang Q., Chang T.H., Peng H.,
Rauscher F.J. III, Ozato K., Zhu F.;
"Tripartite motif-containing protein 28 is a small ubiquitin-related
modifier E3 ligase and negative regulator of IFN regulatory factor 7.";
J. Immunol. 187:4754-4763(2011).
[30]
PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-167 AND
GLN-189.
PubMed=26608321; DOI=10.1128/jvi.02395-15;
Xiang Z., Liu L., Lei X., Zhou Z., He B., Wang J.;
"3C Protease of Enterovirus D68 Inhibits Cellular Defense Mediated by
Interferon Regulatory Factor 7.";
J. Virol. 90:1613-1621(2016).
[31]
INTERACTION WITH HUMAN T-CELL LEUKEMIA VIRUS 1/HTLV-1 PROTEIN HBZ
(MICROBIAL INFECTION).
PubMed=28768861; DOI=10.1128/jvi.00853-17;
Narulla M.S., Alasiri A., Charmier L., Noonan S., Conroy D., Hall W.W.,
Sheehy N.;
"Positive and Negative Regulation of Type I Interferons by the Human T Cell
Leukemia Virus Antisense Protein HBZ.";
J. Virol. 91:0-0(2017).
[32]
PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-151;
GLN-167; GLN-185; GLN-188; GLN-189 AND GLN-215.
PubMed=23175366; DOI=10.1128/jvi.01855-12;
Lei X., Xiao X., Xue Q., Jin Q., He B., Wang J.;
"Cleavage of interferon regulatory factor 7 by enterovirus 71 3C suppresses
cellular responses.";
J. Virol. 87:1690-1698(2013).
[33]
INTERACTION WITH SENECA VALLEY VIRUS PROTEASE 3C (MICROBIAL INFECTION).
PubMed=29427864; DOI=10.1016/j.virol.2018.01.028;
Xue Q., Liu H., Zhu Z., Yang F., Ma L., Cai X., Xue Q., Zheng H.;
"Seneca Valley Virus 3Cpro abrogates the IRF3- and IRF7-mediated innate
immune response by degrading IRF3 and IRF7.";
Virology 518:1-7(2018).
[34]
INVOLVEMENT IN IMD39, VARIANT IMD39 VAL-410, AND CHARACTERIZATION OF
VARIANT IMD39 VAL-410.
PubMed=25814066; DOI=10.1126/science.aaa1578;
Ciancanelli M.J., Huang S.X., Luthra P., Garner H., Itan Y., Volpi S.,
Lafaille F.G., Trouillet C., Schmolke M., Albrecht R.A., Israelsson E.,
Lim H.K., Casadio M., Hermesh T., Lorenzo L., Leung L.W., Pedergnana V.,
Boisson B., Okada S., Picard C., Ringuier B., Troussier F., Chaussabel D.,
Abel L., Pellier I., Notarangelo L.D., Garcia-Sastre A., Basler C.F.,
Geissmann F., Zhang S.Y., Snoeck H.W., Casanova J.L.;
"Infectious disease. Life-threatening influenza and impaired interferon
amplification in human IRF7 deficiency.";
Science 348:448-453(2015).
-!- FUNCTION: Key transcriptional regulator of type I interferon (IFN)-
dependent immune responses and 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. Can efficiently activate both the
IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their
induction via both the virus-activated, MyD88-independent pathway and
the TLR-activated, MyD88-dependent pathway. Induces transcription of
ubiquitin hydrolase USP25 mRNA in response to lipopolysaccharide (LPS)
or viral infection in a type I IFN-dependent manner (By similarity).
Required during both the early and late phases of the IFN gene
induction but is more critical for the late than for the early phase.
Exists in an inactive form in the cytoplasm of uninfected cells and
following viral infection, double-stranded RNA (dsRNA), or toll-like
receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1
kinases. This induces a conformational change, leading to its
dimerization and nuclear localization where along with other
coactivators it can activate transcription of the type I IFN and ISG
genes. Can also play a role in regulating adaptive immune responses by
inducing PSMB9/LMP2 expression, either directly or through induction of
IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1)
and may play a role in the regulation of EBV latency. Can activate
distinct gene expression programs in macrophages and regulate the anti-
tumor properties of primary macrophages. {ECO:0000250|UniProtKB:P70434,
ECO:0000269|PubMed:11073981, ECO:0000269|PubMed:12374802,
ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:17404045}.
-!- ACTIVITY REGULATION: In the absence of viral infection, maintained as a
monomer in an autoinhibited state and phosphorylation 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.
-!- SUBUNIT: Monomer. Homodimer; phosphorylation-induced. Heterodimer with
IRF3. Interacts with TICAM1 and TICAM2. Interacts with MYD88 AND TRAF6.
{ECO:0000269|PubMed:11073981, ECO:0000269|PubMed:11314014,
ECO:0000269|PubMed:14517278, ECO:0000269|PubMed:14739303,
ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:15492225}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus LF2
and LMP1. {ECO:0000269|PubMed:18987133, ECO:0000269|PubMed:19017798}.
-!- SUBUNIT: (Microbial infection) Interacts with rotavirus A NSP1; this
interaction leads to the proteasome-dependent degradation of IRF7.
{ECO:0000269|PubMed:17301153}.
-!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 8/HHV-
8 proteins ORF45 and vIRF-1. {ECO:0000269|PubMed:11943871}.
-!- SUBUNIT: (Microbial infection) Interacts with human T-cell leukemia
virus 1/HTLV-1 protein HBZ. {ECO:0000269|PubMed:28768861}.
-!- SUBUNIT: (Microbial infection) Interacts with Seneca Valley virus
protease 3C; this interaction is involved in the suppression of IRF7
expression and phosphorylation by the virus.
{ECO:0000269|PubMed:29427864}.
-!- INTERACTION:
Q92985; O00170: AIP; NbExp=2; IntAct=EBI-968267, EBI-704197;
Q92985; P10398: ARAF; NbExp=2; IntAct=EBI-968267, EBI-365961;
Q92985; Q96A33: CCDC47; NbExp=2; IntAct=EBI-968267, EBI-720151;
Q92985; O15111: CHUK; NbExp=4; IntAct=EBI-968267, EBI-81249;
Q92985; P51617: IRAK1; NbExp=2; IntAct=EBI-968267, EBI-358664;
Q92985; O94822: LTN1; NbExp=2; IntAct=EBI-968267, EBI-1044684;
Q92985; Q9ULE6: PALD1; NbExp=2; IntAct=EBI-968267, EBI-3957166;
Q92985; Q9UHD2: TBK1; NbExp=2; IntAct=EBI-968267, EBI-356402;
Q92985; Q86UE8: TLK2; NbExp=2; IntAct=EBI-968267, EBI-1047967;
Q92985; Q9BVS5: TRMT61B; NbExp=3; IntAct=EBI-968267, EBI-3197877;
Q92985; P29128: BICP0; Xeno; NbExp=5; IntAct=EBI-968267, EBI-11292028;
Q92985; F5HDE4: ORF45; Xeno; NbExp=3; IntAct=EBI-968267, EBI-8843990;
Q92985; Q77M19: P; Xeno; NbExp=3; IntAct=EBI-968267, EBI-6149376;
Q92985-1; P03230: LMP1; Xeno; NbExp=5; IntAct=EBI-8850881, EBI-6973030;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=The phosphorylated and
active form accumulates selectively in the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=A;
IsoId=Q92985-1; Sequence=Displayed;
Name=B; Synonyms=Beta;
IsoId=Q92985-2; Sequence=VSP_002760;
Name=C; Synonyms=Gamma;
IsoId=Q92985-3; Sequence=VSP_002758, VSP_002759;
Name=D; Synonyms=H;
IsoId=Q92985-4; Sequence=VSP_002757;
-!- TISSUE SPECIFICITY: Expressed predominantly in spleen, thymus and
peripheral blood leukocytes.
-!- INDUCTION: By type I interferon (IFN) and viruses.
-!- PTM: Acetylation inhibits its DNA-binding ability and activity.
{ECO:0000269|PubMed:12374802}.
-!- PTM: In response to a viral infection, phosphorylated on Ser-477 and
Ser-479 by TBK1 and IKBKE1. Phosphorylation, and subsequent activation
is inhibited by vaccinia virus protein E3. In TLR7- and TLR9-mediated
signaling pathway, phosphorylated by IRAK1.
{ECO:0000269|PubMed:11073981, ECO:0000269|PubMed:12374802,
ECO:0000269|PubMed:15367631, ECO:0000269|PubMed:15767370}.
-!- PTM: TRAF6-mediated ubiquitination is required for IRF7 activation.
{ECO:0000250}.
-!- PTM: Sumoylated by TRIM28, which inhibits its transactivation activity.
{ECO:0000269|PubMed:21940674}.
-!- PTM: (Microbial infection) Cleaved and inactivated by the protease 3C
of enterovirus 71 allowing the virus to disrupt the host type I
interferon production. {ECO:0000269|PubMed:23175366}.
-!- PTM: (Microbial infection) Cleaved and inactivated by the protease 3C
of human enterovirus 68D (EV68) allowing the virus to disrupt the host
type I interferon production. {ECO:0000269|PubMed:26608321}.
-!- DISEASE: Immunodeficiency 39 (IMD39) [MIM:616345]: A primary
immunodeficiency causing severe, life-threatening acute respiratory
distress upon infection with H1N1 influenza A.
{ECO:0000269|PubMed:25814066}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- MISCELLANEOUS: [Isoform C]: May be produced at very low levels due to a
premature stop codon in the mRNA, leading to nonsense-mediated mRNA
decay. {ECO:0000305}.
-!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
ProRule:PRU00840}.
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EMBL; U73036; AAB17190.1; -; mRNA.
EMBL; U53830; AAB80686.1; -; mRNA.
EMBL; U53831; AAB80688.1; -; mRNA.
EMBL; U53832; AAB80690.1; -; mRNA.
EMBL; U53832; AAB80691.1; -; mRNA.
EMBL; AF076494; AAC70999.1; -; mRNA.
EMBL; CH471158; EAX02360.1; -; Genomic_DNA.
EMBL; BC136555; AAI36556.1; -; mRNA.
CCDS; CCDS7703.1; -. [Q92985-1]
CCDS; CCDS7704.1; -. [Q92985-2]
CCDS; CCDS7705.1; -. [Q92985-4]
RefSeq; NP_001563.2; NM_001572.3. [Q92985-1]
RefSeq; NP_004020.1; NM_004029.2. [Q92985-2]
RefSeq; NP_004022.2; NM_004031.2. [Q92985-4]
RefSeq; XP_005252963.1; XM_005252906.3.
RefSeq; XP_016873163.1; XM_017017674.1.
PDB; 2O61; X-ray; 2.80 A; A=8-125.
PDBsum; 2O61; -.
SMR; Q92985; -.
BioGRID; 109873; 72.
DIP; DIP-34895N; -.
IntAct; Q92985; 56.
MINT; Q92985; -.
STRING; 9606.ENSP00000380697; -.
iPTMnet; Q92985; -.
PhosphoSitePlus; Q92985; -.
BioMuta; IRF7; -.
DMDM; 116242593; -.
MassIVE; Q92985; -.
MaxQB; Q92985; -.
PaxDb; Q92985; -.
PeptideAtlas; Q92985; -.
PRIDE; Q92985; -.
ProteomicsDB; 75643; -. [Q92985-1]
ProteomicsDB; 75644; -. [Q92985-2]
ProteomicsDB; 75645; -. [Q92985-3]
ProteomicsDB; 75646; -. [Q92985-4]
Antibodypedia; 4325; 585 antibodies.
Ensembl; ENST00000330243; ENSP00000329411; ENSG00000185507. [Q92985-4]
Ensembl; ENST00000348655; ENSP00000331803; ENSG00000185507. [Q92985-2]
Ensembl; ENST00000397566; ENSP00000380697; ENSG00000185507. [Q92985-4]
Ensembl; ENST00000469048; ENSP00000434607; ENSG00000185507. [Q92985-3]
Ensembl; ENST00000525445; ENSP00000434009; ENSG00000185507. [Q92985-1]
Ensembl; ENST00000533182; ENSP00000433903; ENSG00000185507. [Q92985-3]
Ensembl; ENST00000612534; ENSP00000479615; ENSG00000276561. [Q92985-4]
Ensembl; ENST00000621391; ENSP00000480358; ENSG00000276561. [Q92985-1]
Ensembl; ENST00000632827; ENSP00000488039; ENSG00000276561. [Q92985-4]
Ensembl; ENST00000633274; ENSP00000488591; ENSG00000276561. [Q92985-3]
Ensembl; ENST00000633943; ENSP00000488666; ENSG00000276561. [Q92985-2]
Ensembl; ENST00000634105; ENSP00000488581; ENSG00000276561. [Q92985-3]
GeneID; 3665; -.
KEGG; hsa:3665; -.
UCSC; uc001lqg.3; human. [Q92985-1]
CTD; 3665; -.
DisGeNET; 3665; -.
EuPathDB; HostDB:ENSG00000185507.19; -.
GeneCards; IRF7; -.
HGNC; HGNC:6122; IRF7.
HPA; ENSG00000185507; Tissue enhanced (blood).
MalaCards; IRF7; -.
MIM; 605047; gene.
MIM; 616345; phenotype.
neXtProt; NX_Q92985; -.
OpenTargets; ENSG00000185507; -.
PharmGKB; PA29921; -.
eggNOG; ENOG410IWNR; Eukaryota.
eggNOG; ENOG4111G85; LUCA.
GeneTree; ENSGT00940000160931; -.
HOGENOM; CLU_031544_2_0_1; -.
InParanoid; Q92985; -.
KO; K09447; -.
OMA; HYRKKEM; -.
OrthoDB; 648909at2759; -.
PhylomeDB; Q92985; -.
TreeFam; TF328512; -.
Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-9013973; TICAM1-dependent activation of IRF3/IRF7.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
SignaLink; Q92985; -.
SIGNOR; Q92985; -.
BioGRID-ORCS; 3665; 0 hits in 809 CRISPR screens.
ChiTaRS; IRF7; human.
GeneWiki; IRF7; -.
GenomeRNAi; 3665; -.
Pharos; Q92985; Tbio.
PRO; PR:Q92985; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; Q92985; protein.
Bgee; ENSG00000185507; Expressed in right lobe of liver and 185 other tissues.
ExpressionAtlas; Q92985; baseline and differential.
Genevisible; Q92985; HS.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:CACAO.
GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0019043; P:establishment of viral latency; TAS:UniProtKB.
GO; GO:0002376; P:immune system process; IBA:GO_Central.
GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0032607; P:interferon-alpha production; ISS:UniProtKB.
GO; GO:0032608; P:interferon-beta production; ISS:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0039530; P:MDA-5 signaling pathway; TAS:UniProtKB.
GO; GO:2000110; P:negative regulation of macrophage apoptotic process; TAS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:BHF-UCL.
GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:CACAO.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
GO; GO:0002819; P:regulation of adaptive immune response; IDA:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:UniProtKB.
GO; GO:0045655; P:regulation of monocyte differentiation; TAS:UniProtKB.
GO; GO:0034124; P:regulation of MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
GO; GO:0034127; P:regulation of MyD88-independent toll-like receptor signaling pathway; ISS:UniProtKB.
GO; GO:0032479; P:regulation of type I interferon production; TAS:UniProtKB.
GO; GO:0009615; P:response to virus; TAS:UniProtKB.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0045351; P:type I interferon biosynthetic process; IEA:Ensembl.
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.
IDEAL; IID00491; -.
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;
3D-structure; Acetylation; Activator; Alternative splicing;
Antiviral defense; Cytoplasm; Disease mutation; DNA-binding;
Host-virus interaction; Immunity; Innate immunity; Isopeptide bond;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1..503
/note="Interferon regulatory factor 7"
/id="PRO_0000154562"
DNA_BIND 11..126
/note="IRF tryptophan pentad repeat"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
SITE 167..168
/note="(Microbial infection) Cleavage; by viral EV68
protease 3C"
/evidence="ECO:0000269|PubMed:26608321"
SITE 189..190
/note="(Microbial infection) Cleavage; by viral EV 71
protease 3C and EV68 protease 3C"
/evidence="ECO:0000269|PubMed:23175366,
ECO:0000269|PubMed:26608321"
MOD_RES 92
/note="N6-acetyllysine; by KAT2A and KAT2B"
/evidence="ECO:0000269|PubMed:12374802"
MOD_RES 471
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P70434"
MOD_RES 472
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P70434"
MOD_RES 475
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P70434"
MOD_RES 477
/note="Phosphoserine; by TBK1 and IKKE"
/evidence="ECO:0000269|PubMed:15367631"
MOD_RES 479
/note="Phosphoserine; by TBK1 and IKKE"
/evidence="ECO:0000269|PubMed:15367631"
MOD_RES 483
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P70434"
MOD_RES 484
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P70434"
MOD_RES 487
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P70434"
CROSSLNK 444
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
CROSSLNK 446
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
VAR_SEQ 1..6
/note="MALAPE -> MPVPERPAAGPDSPRPGTR (in isoform D)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9786932"
/id="VSP_002757"
VAR_SEQ 152..164
/note="GGPPGPFLAHTHA -> AQGSLLGSCTGGQ (in isoform C)"
/evidence="ECO:0000303|PubMed:9315633"
/id="VSP_002758"
VAR_SEQ 165..503
/note="Missing (in isoform C)"
/evidence="ECO:0000303|PubMed:9315633"
/id="VSP_002759"
VAR_SEQ 228..256
/note="Missing (in isoform B)"
/evidence="ECO:0000303|PubMed:9315633"
/id="VSP_002760"
VARIANT 179
/note="K -> E (in dbSNP:rs1061502)"
/evidence="ECO:0000269|PubMed:9786932, ECO:0000269|Ref.1"
/id="VAR_027957"
VARIANT 204
/note="D -> N (in dbSNP:rs41313489)"
/id="VAR_061273"
VARIANT 410
/note="F -> V (in IMD39; loss of function mutation; shows
abnormal localization to the cytoplasm rather than the
nucleus; dbSNP:rs786205223)"
/evidence="ECO:0000269|PubMed:25814066"
/id="VAR_073779"
VARIANT 412
/note="Q -> R (in dbSNP:rs1131665)"
/evidence="ECO:0000269|PubMed:9786932"
/id="VAR_034017"
MUTAGEN 90
/note="G->T: Loss of acetylation, increased DNA-binding and
activity; when associated with R-93."
/evidence="ECO:0000269|PubMed:12374802"
MUTAGEN 92
/note="K->R: Loss of acetylation, DNA-binding and
activity."
/evidence="ECO:0000269|PubMed:12374802"
MUTAGEN 93
/note="T->R: Loss of acetylation, increased DNA-binding and
activity; when associated with T-90."
/evidence="ECO:0000269|PubMed:12374802"
MUTAGEN 151
/note="Q->A: No effect on cleavage by enterovirus 71."
/evidence="ECO:0000269|PubMed:23175366"
MUTAGEN 167
/note="Q->A: Complete loss of inactivation of IFN-I
production; when associated with R-189."
/evidence="ECO:0000269|PubMed:26608321"
MUTAGEN 167
/note="Q->A: No effect on cleavage by enterovirus 71."
/evidence="ECO:0000269|PubMed:23175366"
MUTAGEN 185
/note="Q->A: No effect on cleavage by enterovirus 71."
/evidence="ECO:0000269|PubMed:23175366"
MUTAGEN 188
/note="Q->A: No effect on cleavage by enterovirus 71."
/evidence="ECO:0000269|PubMed:23175366"
MUTAGEN 189
/note="Q->A: Complete loss of cleavage by enterovirus 71."
/evidence="ECO:0000269|PubMed:23175366"
MUTAGEN 189
/note="Q->R: Complete loss of inactivation of IFN-I
production; when associated with A-167."
/evidence="ECO:0000269|PubMed:26608321"
MUTAGEN 215
/note="Q->A: No effect on cleavage by enterovirus 71."
/evidence="ECO:0000269|PubMed:23175366"
MUTAGEN 477..479
/note="SLS->ALA: Complete loss of TBK1 and IKKE
phosphorylation."
/evidence="ECO:0000269|PubMed:15367631"
HELIX 14..24
/evidence="ECO:0000244|PDB:2O61"
STRAND 31..36
/evidence="ECO:0000244|PDB:2O61"
STRAND 39..43
/evidence="ECO:0000244|PDB:2O61"
HELIX 55..57
/evidence="ECO:0000244|PDB:2O61"
HELIX 58..66
/evidence="ECO:0000244|PDB:2O61"
HELIX 84..102
/evidence="ECO:0000244|PDB:2O61"
STRAND 105..112
/evidence="ECO:0000244|PDB:2O61"
STRAND 119..125
/evidence="ECO:0000244|PDB:2O61"
SEQUENCE 503 AA; 54278 MW; 9863C147514652DE CRC64;
MALAPERAAP RVLFGEWLLG EISSGCYEGL QWLDEARTCF RVPWKHFARK DLSEADARIF
KAWAVARGRW PPSSRGGGPP PEAETAERAG WKTNFRCALR STRRFVMLRD NSGDPADPHK
VYALSRELCW REGPGTDQTE AEAPAAVPPP QGGPPGPFLA HTHAGLQAPG PLPAPAGDKG
DLLLQAVQQS CLADHLLTAS WGADPVPTKA PGEGQEGLPL TGACAGGPGL PAGELYGWAV
ETTPSPGPQP AALTTGEAAA PESPHQAEPY LSPSPSACTA VQEPSPGALD VTIMYKGRTV
LQKVVGHPSC TFLYGPPDPA VRATDPQQVA FPSPAELPDQ KQLRYTEELL RHVAPGLHLE
LRGPQLWARR MGKCKVYWEV GGPPGSASPS TPACLLPRNC DTPIFDFRVF FQELVEFRAR
QRRGSPRYTI YLGFGQDLSA GRPKEKSLVL VKLEPWLCRV HLEGTQREGV SSLDSSSLSL
CLSSANSLYD DIECFLMELE QPA


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Related Genes :
[IRF7] Interferon regulatory factor 7 (IRF-7)
[Irf7] Interferon regulatory factor 7 (IRF-7)
[IRF3] Interferon regulatory factor 3 (IRF-3)
[IRF5] Interferon regulatory factor 5 (IRF-5)
[IRF1] Interferon regulatory factor 1 (IRF-1)
[Irf3] Interferon regulatory factor 3 (IRF-3)
[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)
[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)
[IRF6] Interferon regulatory factor 6 (IRF-6)
[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)
[Irf5] Interferon regulatory factor 5 (IRF-5)
[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)
[STING1 ERIS MITA TMEM173] Stimulator of interferon genes protein (hSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (hMITA) (Transmembrane protein 173)
[Sting1 Eris Mita Mpys Tmem173] Stimulator of interferon genes protein (mSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (MMITA) (Transmembrane protein 173)
[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)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p14); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p66) (p66-HEL); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[IRF3] Interferon regulatory factor 3 (IRF-3)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p14); Non-structural protein 11 (nsp11)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VP1-pX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[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)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)] (Fragment)
[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)
[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)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]
[IRF8 ICSBP ICSBP1] Interferon regulatory factor 8 (IRF-8) (Interferon consensus sequence-binding protein) (ICSBP)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]
[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)

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