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Interferon regulatory factor 4 (IRF-4) (Lymphocyte-specific interferon regulatory factor) (LSIRF) (Multiple myeloma oncogene 1) (NF-EM5)

 IRF4_HUMAN              Reviewed;         451 AA.
Q15306; Q5VUI7; Q99660;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
13-FEB-2019, entry version 191.
RecName: Full=Interferon regulatory factor 4;
Short=IRF-4;
AltName: Full=Lymphocyte-specific interferon regulatory factor;
Short=LSIRF;
AltName: Full=Multiple myeloma oncogene 1;
AltName: Full=NF-EM5;
Name=IRF4; Synonyms=MUM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Spleen;
PubMed=8921401; DOI=10.1006/geno.1996.0547;
Grossman A., Mittrucker H.W., Nicholl J., Suzuki A., Chung S.,
Antonio L., Sugga S., Sutherland G.R., Siderovski D.P., Mak T.W.;
"Cloning of human lymphocyte-specific interferon regulatory factor
(hLSIRF/hIRF4) and mapping of the gene to 6p23-p25.";
Genomics 37:229-233(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN MULTIPLE
MYELOMA.
TISSUE=Spleen;
PubMed=9326949; DOI=10.1038/ng1097-226;
Iida S., Rao P.H., Butler M., Corradini P., Boccadoro M., Klein B.,
Chaganti R.S.K., Dalla-Favera R.;
"Deregulation of MUM1/IRF4 by chromosomal translocation in multiple
myeloma.";
Nat. Genet. 17:226-230(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[5]
INTERACTION WITH SPIB.
PubMed=10196196; DOI=10.1074/jbc.274.16.11115;
Rao S., Matsumura A., Yoon J., Simon M.C.;
"SPI-B activates transcription via a unique proline, serine, and
threonine domain and exhibits DNA binding affinity differences from
PU.1.";
J. Biol. Chem. 274:11115-11124(1999).
[6]
INTERACTION WITH DEF6.
TISSUE=Lymph node;
PubMed=12651066; DOI=10.1016/S0198-8859(03)00024-7;
Gupta S., Lee A.E., Hu C., Fanzo J.C., Goldberg I., Cattoretti G.,
Pernis A.B.;
"Molecular cloning of IBP, a SWAP-70 homologous GEF, which is highly
expressed in the immune system.";
Hum. Immunol. 64:389-401(2003).
[7]
POLYMORPHISM.
PubMed=18483556; DOI=10.1371/journal.pgen.1000074;
Han J., Kraft P., Nan H., Guo Q., Chen C., Qureshi A., Hankinson S.E.,
Hu F.B., Duffy D.L., Zhao Z.Z., Martin N.G., Montgomery G.W.,
Hayward N.K., Thomas G., Hoover R.N., Chanock S., Hunter D.J.;
"A genome-wide association study identifies novel alleles associated
with hair color and skin pigmentation.";
PLoS Genet. 4:E1000074-E1000074(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
POLYMORPHISM.
PubMed=24267888; DOI=10.1016/j.cell.2013.10.022;
Praetorius C., Grill C., Stacey S.N., Metcalf A.M., Gorkin D.U.,
Robinson K.C., Van Otterloo E., Kim R.S., Bergsteinsdottir K.,
Ogmundsdottir M.H., Magnusdottir E., Mishra P.J., Davis S.R., Guo T.,
Zaidi M.R., Helgason A.S., Sigurdsson M.I., Meltzer P.S., Merlino G.,
Petit V., Larue L., Loftus S.K., Adams D.R., Sobhiafshar U.,
Emre N.C., Pavan W.J., Cornell R., Smith A.G., McCallion A.S.,
Fisher D.E., Stefansson K., Sturm R.A., Steingrimsson E.;
"A polymorphism in IRF4 affects human pigmentation through a
tyrosinase-dependent MITF/TFAP2A pathway.";
Cell 155:1022-1033(2013).
[10]
STRUCTURE BY NMR OF 22-130.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the IRF domain of human interferon regulator
factor 4.";
Submitted (OCT-2006) to the PDB data bank.
-!- FUNCTION: Transcriptional activator. Binds to the interferon-
stimulated response element (ISRE) of the MHC class I promoter.
Binds the immunoglobulin lambda light chain enhancer, together
with PU.1. Probably plays a role in ISRE-targeted signal
transduction mechanisms specific to lymphoid cells. 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
IRF4 and activation of genes (By similarity).
{ECO:0000250|UniProtKB:Q64287}.
-!- SUBUNIT: Interacts with the BATF-JUNB heterodimer. Interacts with
BATF (via bZIP domain); the interaction is direct (By similarity).
Interacts with SPIB and DEF6. Directly interacts with NLRP3 in the
nucleus of Th2 cells; this interaction enhances IRF4 ability to
bind to the IL4 promoter and is required for optimal IRF4-
dependent IL4 transcription (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q64287, ECO:0000269|PubMed:10196196,
ECO:0000269|PubMed:12651066}.
-!- INTERACTION:
O95163:ELP1; NbExp=2; IntAct=EBI-751345, EBI-347559;
P51617:IRAK1; NbExp=2; IntAct=EBI-751345, EBI-358664;
Q86UE8:TLK2; NbExp=2; IntAct=EBI-751345, EBI-1047967;
Q9H6S0:YTHDC2; NbExp=2; IntAct=EBI-751345, EBI-1057466;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15306-1; Sequence=Displayed;
Name=2;
IsoId=Q15306-2; Sequence=VSP_002755;
-!- TISSUE SPECIFICITY: Lymphoid cells.
-!- INDUCTION: Not induced by interferons.
-!- PTM: Phosphorylation by ROCK2 regulates IL-17 and IL-21
production. {ECO:0000250}.
-!- POLYMORPHISM: Genetic variants in IRF4 define the skin/hair/eye
pigmentation variation locus 8 (SHEP8) [MIM:611724]. Hair, eye and
skin pigmentation are among the most visible examples of human
phenotypic variation, with a broad normal range that is subject to
substantial geographic stratification. In the case of skin,
individuals tend to have lighter pigmentation with increasing
distance from the equator. By contrast, the majority of variation
in human eye and hair color is found among individuals of European
ancestry, with most other human populations fixed for brown eyes
and black hair. {ECO:0000269|PubMed:18483556,
ECO:0000269|PubMed:24267888}.
-!- DISEASE: Multiple myeloma (MM) [MIM:254500]: A malignant tumor of
plasma cells usually arising in the bone marrow and characterized
by diffuse involvement of the skeletal system, hyperglobulinemia,
Bence-Jones proteinuria and anemia. Complications of multiple
myeloma are bone pain, hypercalcemia, renal failure and spinal
cord compression. The aberrant antibodies that are produced lead
to impaired humoral immunity and patients have a high prevalence
of infection. Amyloidosis may develop in some patients. Multiple
myeloma is part of a spectrum of diseases ranging from monoclonal
gammopathy of unknown significance (MGUS) to plasma cell leukemia.
{ECO:0000269|PubMed:9326949}. Note=The gene represented in this
entry may be involved in disease pathogenesis. A chromosomal
aberration involving IRF4 has been found in multiple myeloma.
Translocation t(6;14)(p25;q32) with the IgH locus.
-!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
ProRule:PRU00840}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/IRF4ID231ch6p25.html";
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EMBL; U52682; AAC50779.1; -; mRNA.
EMBL; U63738; AAB37258.1; -; mRNA.
EMBL; AL365272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL589962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015752; AAH15752.1; -; mRNA.
CCDS; CCDS4469.1; -. [Q15306-1]
RefSeq; NP_001182215.1; NM_001195286.1. [Q15306-2]
RefSeq; NP_002451.2; NM_002460.3. [Q15306-1]
UniGene; Hs.401013; -.
PDB; 2DLL; NMR; -; A=23-130.
PDBsum; 2DLL; -.
ProteinModelPortal; Q15306; -.
SMR; Q15306; -.
BioGrid; 109870; 25.
IntAct; Q15306; 12.
STRING; 9606.ENSP00000370343; -.
iPTMnet; Q15306; -.
PhosphoSitePlus; Q15306; -.
BioMuta; IRF4; -.
DMDM; 2497445; -.
jPOST; Q15306; -.
MaxQB; Q15306; -.
PaxDb; Q15306; -.
PeptideAtlas; Q15306; -.
PRIDE; Q15306; -.
ProteomicsDB; 60524; -.
ProteomicsDB; 60525; -. [Q15306-2]
DNASU; 3662; -.
Ensembl; ENST00000380956; ENSP00000370343; ENSG00000137265. [Q15306-1]
GeneID; 3662; -.
KEGG; hsa:3662; -.
UCSC; uc003msz.5; human. [Q15306-1]
CTD; 3662; -.
DisGeNET; 3662; -.
EuPathDB; HostDB:ENSG00000137265.14; -.
GeneCards; IRF4; -.
HGNC; HGNC:6119; IRF4.
HPA; CAB013508; -.
HPA; HPA002038; -.
HPA; HPA002698; -.
MalaCards; IRF4; -.
MIM; 254500; phenotype.
MIM; 601900; gene.
MIM; 611724; phenotype.
neXtProt; NX_Q15306; -.
OpenTargets; ENSG00000137265; -.
PharmGKB; PA29918; -.
eggNOG; ENOG410IES5; Eukaryota.
eggNOG; ENOG411023V; LUCA.
GeneTree; ENSGT00940000159059; -.
HOGENOM; HOG000010107; -.
HOVERGEN; HBG003072; -.
InParanoid; Q15306; -.
KO; K09445; -.
OMA; RSWREYV; -.
OrthoDB; 648909at2759; -.
PhylomeDB; Q15306; -.
TreeFam; TF328512; -.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
SIGNOR; Q15306; -.
ChiTaRS; IRF4; human.
EvolutionaryTrace; Q15306; -.
GeneWiki; IRF4; -.
GenomeRNAi; 3662; -.
PRO; PR:Q15306; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000137265; Expressed in 116 organ(s), highest expression level in endocervix.
ExpressionAtlas; Q15306; baseline and differential.
Genevisible; Q15306; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0000788; C:nuclear nucleosome; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IC:UniProtKB.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; NAS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0042832; P:defense response to protozoan; ISS:UniProtKB.
GO; GO:0043966; P:histone H3 acetylation; IEA:Ensembl.
GO; GO:0043967; P:histone H4 acetylation; IEA:Ensembl.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IEA:Ensembl.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:0045082; P:positive regulation of interleukin-10 biosynthetic process; IDA:UniProtKB.
GO; GO:0045368; P:positive regulation of interleukin-13 biosynthetic process; IDA:UniProtKB.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IDA:UniProtKB.
GO; GO:0045404; P:positive regulation of interleukin-4 biosynthetic process; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045622; P:regulation of T-helper cell differentiation; NAS:UniProtKB.
GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS: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;
3D-structure; Activator; Alternative splicing;
Chromosomal rearrangement; Complete proteome; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 451 Interferon regulatory factor 4.
/FTId=PRO_0000154556.
DNA_BIND 21 129 IRF tryptophan pentad repeat.
{ECO:0000255|PROSITE-ProRule:PRU00840}.
MOD_RES 447 447 Phosphoserine; by ROCK2.
{ECO:0000250|UniProtKB:Q64287}.
MOD_RES 448 448 Phosphoserine; by ROCK2.
{ECO:0000250|UniProtKB:Q64287}.
VAR_SEQ 165 165 Missing (in isoform 2).
{ECO:0000303|PubMed:8921401}.
/FTId=VSP_002755.
CONFLICT 300 300 Q -> H (in Ref. 2; AAB37258).
{ECO:0000305}.
CONFLICT 306 306 K -> N (in Ref. 2; AAB37258).
{ECO:0000305}.
CONFLICT 333 333 R -> T (in Ref. 2; AAB37258).
{ECO:0000305}.
HELIX 24 34 {ECO:0000244|PDB:2DLL}.
STRAND 37 39 {ECO:0000244|PDB:2DLL}.
STRAND 41 47 {ECO:0000244|PDB:2DLL}.
STRAND 49 53 {ECO:0000244|PDB:2DLL}.
STRAND 60 62 {ECO:0000244|PDB:2DLL}.
HELIX 64 67 {ECO:0000244|PDB:2DLL}.
HELIX 69 78 {ECO:0000244|PDB:2DLL}.
HELIX 90 103 {ECO:0000244|PDB:2DLL}.
STRAND 107 109 {ECO:0000244|PDB:2DLL}.
TURN 111 113 {ECO:0000244|PDB:2DLL}.
STRAND 115 120 {ECO:0000244|PDB:2DLL}.
STRAND 122 127 {ECO:0000244|PDB:2DLL}.
SEQUENCE 451 AA; 51772 MW; 17CD1327C6F5BFFA CRC64;
MNLEGGGRGG EFGMSAVSCG NGKLRQWLID QIDSGKYPGL VWENEEKSIF RIPWKHAGKQ
DYNREEDAAL FKAWALFKGK FREGIDKPDP PTWKTRLRCA LNKSNDFEEL VERSQLDISD
PYKVYRIVPE GAKKGAKQLT LEDPQMSMSH PYTMTTPYPS LPAQQVHNYM MPPLDRSWRD
YVPDQPHPEI PYQCPMTFGP RGHHWQGPAC ENGCQVTGTF YACAPPESQA PGVPTEPSIR
SAEALAFSDC RLHICLYYRE ILVKELTTSS PEGCRISHGH TYDASNLDQV LFPYPEDNGQ
RKNIEKLLSH LERGVVLWMA PDGLYAKRLC QSRIYWDGPL ALCNDRPNKL ERDQTCKLFD
TQQFLSELQA FAHHGRSLPR FQVTLCFGEE FPDPQRQRKL ITAHVEPLLA RQLYYFAQQN
SGHFLRGYDL PEHISNPEDY HRSIRHSSIQ E


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E1776m ELISA kit ICSBP,Icsbp,Icsbp1,Interferon consensus sequence-binding protein,Interferon regulatory factor 8,Irf8,IRF-8,Mouse,Mus musculus 96T
U1776h CLIA H-ICSBP,Homo sapiens,Human,ICSBP,ICSBP1,Interferon consensus sequence-binding protein,Interferon regulatory factor 8,IRF8,IRF-8 96T
E1776h ELISA kit H-ICSBP,Homo sapiens,Human,ICSBP,ICSBP1,Interferon consensus sequence-binding protein,Interferon regulatory factor 8,IRF8,IRF-8 96T
E1776h ELISA H-ICSBP,Homo sapiens,Human,ICSBP,ICSBP1,Interferon consensus sequence-binding protein,Interferon regulatory factor 8,IRF8,IRF-8 96T

Kits Elisa; taq POLYMERASE

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Pathways :
WP1017: Type II interferon signaling (IFNG)
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1136: Type II interferon signaling (IFNG)
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1253: Type II interferon signaling (IFNG)
WP1289: Type II interferon signaling (IFNG)
WP1350: Type II interferon signaling (IFNG)
WP1493: Carbon assimilation C4 pathway
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1835: Interferon alpha/beta signaling
WP1836: Interferon gamma signaling
WP1837: Interferon Signaling
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1901: Regulatory RNA pathways
WP1909: Signal regulatory protein (SIRP) family interactions
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP1983: Splicing factor NOVA regulated synpatic proteins
WP201: Ptf1a related regulatory pathway
WP2113: Type III interferon signaling
WP2119: Interferon induced apoptosis
WP2148: Brain derived neurotrophic factor
WP272: Blood Clotting Cascade
WP313: Signaling of Hepatocyte Growth Factor Receptor

Related Genes :
[IRF3] Interferon regulatory factor 3 (IRF-3)
[IRF8 ICSBP1] Interferon regulatory factor 8 (IRF-8) (Interferon consensus sequence-binding protein) (H-ICSBP) (ICSBP)
[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)
[IRF5] Interferon regulatory factor 5 (IRF-5)
[Irf8 Icsbp Icsbp1] Interferon regulatory factor 8 (IRF-8) (Interferon consensus sequence-binding protein) (ICSBP)
[EGFR ERBB ERBB1 HER1] Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)
[Irf3] Interferon regulatory factor 3 (IRF-3)
[Irf7] Interferon regulatory factor 7 (IRF-7)
[IRF6] Interferon regulatory factor 6 (IRF-6)
[NFKB2 LYT10] Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (H2TF1) (Lymphocyte translocation chromosome 10 protein) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) (Oncogene Lyt-10) (Lyt10) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]
[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)
[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)
[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)
[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)
[MAVS IPS1 KIAA1271 VISA] Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Putative NF-kappa-B-activating protein 031N) (Virus-induced-signaling adapter) (VISA)
[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)
[NFKB1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[Irf5] Interferon regulatory factor 5 (IRF-5)
[RELA NFKB3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[TMEM173 ERIS MITA STING] Stimulator of interferon genes protein (hSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (hMITA) (Transmembrane protein 173)
[Tmem173 Eris Mita Mpys Sting] Stimulator of interferon genes protein (mSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (MMITA) (Transmembrane protein 173)
[IKBKG FIP3 NEMO] NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[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)
[ADAR ADAR1 DSRAD G1P1 IFI4] Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (136 kDa double-stranded RNA-binding protein) (p136) (Interferon-inducible protein 4) (IFI-4) (K88DSRBP)
[TBK1 NAK] Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (NF-kappa-B-activating kinase) (T2K) (TANK-binding kinase 1)
[IFI16 IFNGIP1] Gamma-interferon-inducible protein 16 (Ifi-16) (Interferon-inducible myeloid differentiation transcriptional activator)
[Nfkb1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (NF-kappa-B1 p84/NF-kappa-B1 p98) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[IL18 IGIF IL1F4] Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)

Bibliography :
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