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Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)

 IL18_HUMAN              Reviewed;         193 AA.
Q14116; O75599; Q6FGY3; Q6WWJ7;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-APR-2020, entry version 185.
RecName: Full=Interleukin-18 {ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25261253, ECO:0000303|PubMed:25500532};
Short=IL-18 {ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25261253, ECO:0000303|PubMed:25500532};
AltName: Full=Iboctadekin;
AltName: Full=Interferon gamma-inducing factor {ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25500532};
Short=IFN-gamma-inducing factor {ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25500532};
AltName: Full=Interleukin-1 gamma;
Short=IL-1 gamma;
Flags: Precursor;
Name=IL18 {ECO:0000312|HGNC:HGNC:5986}; Synonyms=IGIF, IL1F4;
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 1).
TISSUE=Liver;
PubMed=8666798;
Ushio S., Namba M., Okura T., Hattori K., Nukada Y., Akita K., Tanabe F.,
Konishi K., Micallef M., Fujii M., Torigoe K., Tanimoto T., Fukuda S.,
Ikeda M., Okamura H., Kurimoto M.;
"Cloning of the cDNA for human IFN-gamma-inducing factor, expression in
Escherichia coli, and studies on the biologic activities of the protein.";
J. Immunol. 156:4274-4279(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEOLYTIC CLEAVAGE, AND
ALTERNATIVE SPLICING.
PubMed=15326478; DOI=10.1038/sj.onc.1208036;
Gaggero A., De Ambrosis A., Mezzanzanica D., Piazza T., Rubartelli A.,
Figini M., Canevari S., Ferrini S.;
"A novel isoform of pro-interleukin-18 expressed in ovarian tumors is
resistant to caspase-1 and -4 processing.";
Oncogene 23:7552-7560(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Yong D., Guixin D., Lihua H., Haitao W.;
"Cloning and sequencing of the cDNA for precursor hIL-18.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Liu J., Peng X., Yuan J., Qiang B.;
"Cloning of human interleukin 18 cDNA.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
Hattori M., Rogers J., Lander E.S., Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Urinary bladder;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-193 (ISOFORM 1).
TISSUE=Peripheral blood;
Conti B., Kim S.J., Tinti C., Chun H.S., Joh T.H.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[10]
FUNCTION.
PubMed=10653850; DOI=10.1093/intimm/12.2.151;
Tominaga K., Yoshimoto T., Torigoe K., Kurimoto M., Matsui K., Hada T.,
Okamura H., Nakanishi K.;
"IL-12 synergizes with IL-18 or IL-1beta for IFN-gamma production from
human T cells.";
Int. Immunol. 12:151-160(2000).
[11]
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).
[12]
INDUCTION BY ENDOCANNABINOID ANANDAMIDE, AND SUBCELLULAR LOCATION.
PubMed=23955712; DOI=10.1038/nm.3265;
Jourdan T., Godlewski G., Cinar R., Bertola A., Szanda G., Liu J., Tam J.,
Han T., Mukhopadhyay B., Skarulis M.C., Ju C., Aouadi M., Czech M.P.,
Kunos G.;
"Activation of the Nlrp3 inflammasome in infiltrating macrophages by
endocannabinoids mediates beta cell loss in type 2 diabetes.";
Nat. Med. 19:1132-1140(2013).
[13]
STRUCTURE BY NMR OF 37-193, FUNCTION, SUBUNIT, AND MUTAGENESIS OF LYS-40;
LEU-41; LYS-44; ARG-49; ASP-53; MET-69; ASP-71; ARG-94; MET-96; LYS-115;
LYS-120; ASP-134; ARG-140 AND ASP-168.
PubMed=14528293; DOI=10.1038/nsb993;
Kato Z., Jee J., Shikano H., Mishima M., Ohki I., Ohnishi H., Li A.,
Hashimoto K., Matsukuma E., Omoya K., Yamamoto Y., Yoneda T., Hara T.,
Kondo N., Shirakawa M.;
"The structure and binding mode of interleukin-18.";
Nat. Struct. Biol. 10:966-971(2003).
[14]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 37-193, PROTEOLYTIC CLEAVAGE, AND
SUBUNIT.
PubMed=25261253; DOI=10.1016/j.febslet.2014.09.019;
Wei H., Wang D., Qian Y., Liu X., Fan S., Yin H.S., Wang X.;
"Structural basis for the specific recognition of IL-18 by its alpha
receptor.";
FEBS Lett. 588:3838-3843(2014).
[15]
X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 37-193, FUNCTION, MUTAGENESIS OF
GLY-144; HIS-145; ASP-146; LYS-148; ARG-183 AND MET-186, AND SUBUNIT.
PubMed=25500532; DOI=10.1038/ncomms6340;
Tsutsumi N., Kimura T., Arita K., Ariyoshi M., Ohnishi H., Yamamoto T.,
Zuo X., Maenaka K., Park E.Y., Kondo N., Shirakawa M., Tochio H., Kato Z.;
"The structural basis for receptor recognition of human interleukin-18.";
Nat. Commun. 5:5340-5340(2014).
-!- FUNCTION: A proinflammatory cytokine primarily involved in polarized T-
helper 1 (Th1) cell and natural killer (NK) cell immune responses
(Probable). Upon binding to IL18R1 and IL18RAP, forms a signaling
ternary complex which activates NF-kappa-B, triggering synthesis of
inflammatory mediators (PubMed:14528293, PubMed:25500532). Synergizes
with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1)
cells and natural killer (NK) cells (Probable) (PubMed:10653850).
{ECO:0000269|PubMed:10653850, ECO:0000269|PubMed:14528293,
ECO:0000269|PubMed:25500532, ECO:0000305}.
-!- SUBUNIT: Forms a ternary complex with ligand-binding receptor subunit
IL18R1 and signaling receptor subunit IL18RAP at the plasma membrane.
Mature IL18 first binds to IL18R1 forming a low affinity binary
complex, which then interacts with IL18RAP to form a high affinity
ternary complex that signals inside the cell (PubMed:25261253,
PubMed:14528293, PubMed:25500532). {ECO:0000269|PubMed:14528293,
ECO:0000269|PubMed:25261253, ECO:0000269|PubMed:25500532}.
-!- INTERACTION:
Q14116; Q9IW12; Xeno; NbExp=2; IntAct=EBI-3910835, EBI-15748155;
Q14116; Q15847: ADIRF; NbExp=3; IntAct=EBI-3910835, EBI-7162516;
Q14116; Q13478: IL18R1; NbExp=2; IntAct=EBI-3910835, EBI-9817499;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23955712}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14116-1; Sequence=Displayed;
Name=2; Synonyms=Delta3pro-IL-18;
IsoId=Q14116-2; Sequence=VSP_044934;
-!- INDUCTION: In macrophages, release is increased by endocannabinoid
anandamide/AEA. {ECO:0000269|PubMed:23955712}.
-!- PTM: The pro-IL-18 precursor is processed by CASP1 or CASP4 to yield
the active form. {ECO:0000269|PubMed:15326478,
ECO:0000269|PubMed:25261253}.
-!- MISCELLANEOUS: [Isoform 2]: Expressed in ovarian carcinoma but
undetectable in normal ovarian epithelial cells. Resistant to
proteolytic activation by caspase-1 and -4. {ECO:0000305}.
-!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-1 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_1";
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EMBL; D49950; BAA08706.1; -; mRNA.
EMBL; AY266351; AAP92112.1; -; mRNA.
EMBL; AF077611; AAC27787.1; -; mRNA.
EMBL; AY044641; AAK95950.1; -; mRNA.
EMBL; CR541973; CAG46771.1; -; mRNA.
EMBL; CR542001; CAG46798.1; -; mRNA.
EMBL; AP002007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67184.1; -; Genomic_DNA.
EMBL; BC007007; AAH07007.1; -; mRNA.
EMBL; BC007461; AAH07461.1; -; mRNA.
EMBL; U90434; AAB50010.1; -; mRNA.
CCDS; CCDS44731.1; -. [Q14116-1]
CCDS; CCDS58180.1; -. [Q14116-2]
RefSeq; NP_001230140.1; NM_001243211.1. [Q14116-2]
RefSeq; NP_001553.1; NM_001562.3. [Q14116-1]
RefSeq; XP_011541107.1; XM_011542805.1. [Q14116-2]
RefSeq; XP_011541108.1; XM_011542806.2. [Q14116-1]
PDB; 1J0S; NMR; -; A=37-193.
PDB; 2VXT; X-ray; 1.49 A; I=37-193.
PDB; 3F62; X-ray; 2.00 A; B=37-193.
PDB; 3WO2; X-ray; 2.33 A; A/B/C/D=37-193.
PDB; 3WO3; X-ray; 3.10 A; A/C/E/G/I/K=37-193.
PDB; 3WO4; X-ray; 3.10 A; A=37-193.
PDB; 4EEE; X-ray; 2.71 A; B/D=37-193.
PDB; 4EKX; X-ray; 1.75 A; B/D=37-193.
PDB; 4HJJ; X-ray; 2.10 A; A=37-192.
PDB; 4R6U; X-ray; 2.80 A; B/D=37-193.
PDB; 4XFS; X-ray; 1.91 A; A/B=37-193.
PDB; 4XFT; X-ray; 2.00 A; A/B=37-193.
PDB; 4XFU; X-ray; 2.85 A; A/B=37-193.
PDBsum; 1J0S; -.
PDBsum; 2VXT; -.
PDBsum; 3F62; -.
PDBsum; 3WO2; -.
PDBsum; 3WO3; -.
PDBsum; 3WO4; -.
PDBsum; 4EEE; -.
PDBsum; 4EKX; -.
PDBsum; 4HJJ; -.
PDBsum; 4R6U; -.
PDBsum; 4XFS; -.
PDBsum; 4XFT; -.
PDBsum; 4XFU; -.
SMR; Q14116; -.
BioGrid; 109819; 13.
DIP; DIP-3785N; -.
IntAct; Q14116; 10.
MINT; Q14116; -.
STRING; 9606.ENSP00000280357; -.
ChEMBL; CHEMBL1741305; -.
iPTMnet; Q14116; -.
PhosphoSitePlus; Q14116; -.
BioMuta; IL18; -.
DMDM; 3219817; -.
OGP; Q14116; -.
CPTAC; CPTAC-1249; -.
CPTAC; CPTAC-1250; -.
CPTAC; CPTAC-1431; -.
CPTAC; CPTAC-1432; -.
CPTAC; CPTAC-1433; -.
CPTAC; CPTAC-1434; -.
CPTAC; CPTAC-1435; -.
CPTAC; CPTAC-705; -.
EPD; Q14116; -.
jPOST; Q14116; -.
MassIVE; Q14116; -.
MaxQB; Q14116; -.
PaxDb; Q14116; -.
PeptideAtlas; Q14116; -.
PRIDE; Q14116; -.
ProteomicsDB; 59823; -. [Q14116-1]
ProteomicsDB; 67779; -.
ABCD; Q14116; -.
Antibodypedia; 1287; 809 antibodies.
DNASU; 3606; -.
Ensembl; ENST00000280357; ENSP00000280357; ENSG00000150782. [Q14116-1]
Ensembl; ENST00000524595; ENSP00000434561; ENSG00000150782. [Q14116-2]
Ensembl; ENST00000528832; ENSP00000434161; ENSG00000150782. [Q14116-1]
GeneID; 3606; -.
KEGG; hsa:3606; -.
UCSC; uc001pnb.2; human. [Q14116-1]
CTD; 3606; -.
DisGeNET; 3606; -.
GeneCards; IL18; -.
HGNC; HGNC:5986; IL18.
HPA; ENSG00000150782; Tissue enhanced (esophagus, skin).
MIM; 600953; gene.
neXtProt; NX_Q14116; -.
OpenTargets; ENSG00000150782; -.
PharmGKB; PA29802; -.
eggNOG; ENOG410J3U9; Eukaryota.
eggNOG; ENOG410ZGS8; LUCA.
GeneTree; ENSGT00390000001053; -.
HOGENOM; CLU_113349_0_0_1; -.
InParanoid; Q14116; -.
KO; K05482; -.
OMA; SVMFTVQ; -.
OrthoDB; 1190337at2759; -.
PhylomeDB; Q14116; -.
TreeFam; TF336297; -.
Reactome; R-HSA-448706; Interleukin-1 processing.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-9012546; Interleukin-18 signaling. [Q14116-2]
SIGNOR; Q14116; -.
EvolutionaryTrace; Q14116; -.
GeneWiki; Interleukin_18; -.
GenomeRNAi; 3606; -.
Pharos; Q14116; Tbio.
PRO; PR:Q14116; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; Q14116; protein.
Bgee; ENSG00000150782; Expressed in lower esophagus mucosa and 193 other tissues.
ExpressionAtlas; Q14116; baseline and differential.
Genevisible; Q14116; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005125; F:cytokine activity; IDA:UniProtKB.
GO; GO:0045515; F:interleukin-18 receptor binding; IDA:UniProtKB.
GO; GO:0032148; P:activation of protein kinase B activity; IDA:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
GO; GO:0042033; P:chemokine biosynthetic process; TAS:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0042253; P:granulocyte macrophage colony-stimulating factor biosynthetic process; TAS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0042095; P:interferon-gamma biosynthetic process; TAS:UniProtKB.
GO; GO:0042231; P:interleukin-13 biosynthetic process; TAS:UniProtKB.
GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0042094; P:interleukin-2 biosynthetic process; TAS:UniProtKB.
GO; GO:0032635; P:interleukin-6 production; IEA:Ensembl.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IEA:Ensembl.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
GO; GO:0042119; P:neutrophil activation; IEA:Ensembl.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:UniProtKB.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISS:BHF-UCL.
GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IDA:BHF-UCL.
GO; GO:0150078; P:positive regulation of neuroinflammatory response; TAS:ARUK-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0051142; P:positive regulation of NK T cell proliferation; IDA:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IDA:UniProtKB.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; ISS:BHF-UCL.
GO; GO:0034105; P:positive regulation of tissue remodeling; IC:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:CACAO.
GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0030431; P:sleep; ISS:UniProtKB.
GO; GO:0035744; P:T-helper 1 cell cytokine production; IEA:Ensembl.
GO; GO:0042088; P:T-helper 1 type immune response; IDA:UniProtKB.
GO; GO:0070328; P:triglyceride homeostasis; ISS:BHF-UCL.
GO; GO:0042092; P:type 2 immune response; TAS:UniProtKB.
InterPro; IPR015529; IL-18.
InterPro; IPR000975; IL-1_fam.
InterPro; IPR008996; IL1/FGF.
Pfam; PF00340; IL1; 1.
PIRSF; PIRSF015162; Interleukin_18; 1.
PRINTS; PR01933; INTRLEUKIN18.
SUPFAM; SSF50353; SSF50353; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cytokine; Inflammatory response;
Reference proteome; Secreted.
PROPEP 1..36
/evidence="ECO:0000250"
/id="PRO_0000015343"
CHAIN 37..193
/note="Interleukin-18"
/id="PRO_0000015344"
VAR_SEQ 27..30
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15326478"
/id="VSP_044934"
MUTAGEN 40
/note="K->A: Reduces binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 41
/note="L->A: Impairs binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 44
/note="K->A: Reduces binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 49
/note="R->A: Reduces binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 53
/note="D->A: Reduces binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 69
/note="M->A: Impairs binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 71
/note="D->A: Impairs binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 94
/note="R->A: Impairs binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 96
/note="M->A: Impairs binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 115
/note="K->A: Reduces binding of the preformed binary
complex of IL18 and IL18R1 to IL18RAP resulting in impaired
IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 120
/note="K->A: Reduces binding of the preformed binary
complex of IL18 and IL18R1 to IL18RAP resulting in impaired
IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 134
/note="D->A: Reduces binding of the preformed binary
complex of IL18 and IL18R1 to IL18RAP resulting in impaired
IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 140
/note="R->A: Reduces binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 144
/note="G->A: Abolishes binding of the preformed binary
complex of IL18 and IL18R1 to IL18RAP."
/evidence="ECO:0000269|PubMed:25500532"
MUTAGEN 145
/note="H->A: Abolishes binding of the preformed binary
complex of IL18 and IL18R1 to IL18RAP."
/evidence="ECO:0000269|PubMed:25500532"
MUTAGEN 146
/note="D->A: Reduces binding of the preformed binary
complex of IL18 and IL18R1 to IL18RAP."
/evidence="ECO:0000269|PubMed:25500532"
MUTAGEN 148
/note="K->A: Abolishes binding of the preformed binary
complex of IL18 and IL18R1 to IL18RAP."
/evidence="ECO:0000269|PubMed:25500532"
MUTAGEN 168
/note="D->A: Reduces binding to IL18R1 and the ability to
induce IFNG production."
/evidence="ECO:0000269|PubMed:14528293"
MUTAGEN 183
/note="R->A: Reduces binding of the preformed binary
complex of IL18 and IL18R1 to IL18RAP."
/evidence="ECO:0000269|PubMed:25500532"
MUTAGEN 186
/note="M->A: Reduces binding of the preformed binary
complex of IL18 and IL18R1 to IL18RAP."
/evidence="ECO:0000269|PubMed:25500532"
CONFLICT 66
/note="F -> L (in Ref. 3; AAC27787)"
/evidence="ECO:0000305"
CONFLICT 86
/note="S -> R (in Ref. 3; AAC27787)"
/evidence="ECO:0000305"
CONFLICT 191
/note="N -> S (in Ref. 3; AAC27787)"
/evidence="ECO:0000305"
STRAND 42..49
/evidence="ECO:0000244|PDB:2VXT"
STRAND 55..58
/evidence="ECO:0000244|PDB:2VXT"
STRAND 64..67
/evidence="ECO:0000244|PDB:2VXT"
HELIX 71..76
/evidence="ECO:0000244|PDB:2VXT"
TURN 77..81
/evidence="ECO:0000244|PDB:2VXT"
STRAND 83..91
/evidence="ECO:0000244|PDB:2VXT"
TURN 92..94
/evidence="ECO:0000244|PDB:2VXT"
STRAND 95..111
/evidence="ECO:0000244|PDB:2VXT"
HELIX 113..115
/evidence="ECO:0000244|PDB:2VXT"
STRAND 118..121
/evidence="ECO:0000244|PDB:2VXT"
STRAND 126..131
/evidence="ECO:0000244|PDB:2VXT"
STRAND 137..142
/evidence="ECO:0000244|PDB:2VXT"
STRAND 145..156
/evidence="ECO:0000244|PDB:2VXT"
STRAND 159..166
/evidence="ECO:0000244|PDB:2VXT"
STRAND 169..176
/evidence="ECO:0000244|PDB:2VXT"
TURN 178..180
/evidence="ECO:0000244|PDB:4HJJ"
HELIX 183..185
/evidence="ECO:0000244|PDB:2VXT"
STRAND 187..191
/evidence="ECO:0000244|PDB:2VXT"
SEQUENCE 193 AA; 22326 MW; 323C62C203788D55 CRC64;
MAAEPVEDNC INFVAMKFID NTLYFIAEDD ENLESDYFGK LESKLSVIRN LNDQVLFIDQ
GNRPLFEDMT DSDCRDNAPR TIFIISMYKD SQPRGMAVTI SVKCEKISTL SCENKIISFK
EMNPPDNIKD TKSDIIFFQR SVPGHDNKMQ FESSSYEGYF LACEKERDLF KLILKKEDEL
GDRSIMFTVQ NED


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Related Genes :
[IL18 IGIF IL1F4] Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[Il18 Igif] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[Il18 Igif] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (EC 3.2.2.6) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (CDw218b) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-1 receptor 7) (IL-1R-7) (IL-1R7) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)
[IL36G IL1E IL1F9 IL1H1 IL1RP2 UNQ2456/PRO5737] Interleukin-36 gamma (IL-1-related protein 2) (IL-1RP2) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 9) (IL-1F9) (Interleukin-1 homolog 1) (IL-1H1)
[IL18R1 IL1RRP] Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (EC 3.2.2.6) (CD218 antigen-like family member A) (CDw218a) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (Interleukin-18 receptor alpha) (IL-18R-alpha) (IL-18Ralpha) (CD antigen CD218a)
[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)
[IL2RG] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[IFNLR1 IL28RA LICR2] Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2)
[IFNL1 IL29 ZCYTO21] Interferon lambda-1 (IFN-lambda-1) (Cytokine Zcyto21) (Interleukin-29) (IL-29)
[IL33 C9orf26 IL1F11 NFHEV] Interleukin-33 (IL-33) (Interleukin-1 family member 11) (IL-1F11) (Nuclear factor from high endothelial venules) (NF-HEV) [Cleaved into: Interleukin-33 (95-270); Interleukin-33 (99-270); Interleukin-33 (109-270)]
[Ticam1 Trif] TIR domain-containing adapter molecule 1 (TICAM-1) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (TIR domain-containing adapter protein inducing IFN-beta)
[Il18r1] Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (EC 3.2.2.6) (CD218 antigen-like family member A) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (Interleukin-18 receptor alpha) (IL-18R-alpha) (IL-18Ralpha) (CD antigen CD218a)
[Il2rg] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[IL1B IL1F2] Interleukin-1 beta (IL-1 beta) (Catabolin)
[IL32 NK4 TAIF] Interleukin-32 (IL-32) (Natural killer cells protein 4) (Tumor necrosis factor alpha-inducing factor)
[IL1R1 IL1R IL1RA IL1RT1] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[IFNG] Interferon gamma (IFN-gamma)
[IFNL3 IL28B IL28C ZCYTO22] Interferon lambda-3 (IFN-lambda-3) (Cytokine Zcyto22) (Interleukin-28B) (IL-28B) (Interleukin-28C) (IL-28C)
[IL36RN FIL1D IL1F5 IL1HY1 IL1L1 IL1RP3 UNQ1896/PRO4342] Interleukin-36 receptor antagonist protein (IL-36Ra) (FIL1 delta) (IL-1-related protein 3) (IL-1RP3) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 receptor antagonist homolog 1) (IL-1ra homolog 1) (Interleukin-1-like protein 1) (IL-1L1)
[IL36RN Fil1d Il1f5 Il1h3 Il1hy1] Interleukin-36 receptor antagonist protein (IL-36Ra) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 homolog 3) (IL-1H3) (Interleukin-1-like protein 1) (IL-1L1)
[IL1RAP C3orf13 IL1R3] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-1 receptor 3) (IL-1R-3) (IL-1R3)
[Il36g Il1f9] Interleukin-36 gamma (Interleukin-1 family member 9) (IL-1F9)
[Ifng] Interferon gamma (IFN-gamma)
[Il1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[Ifng] Interferon gamma (IFN-gamma)

Bibliography :