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Interleukin-1 receptor antagonist protein (IL-1RN) (IL-1ra) (IRAP) (ICIL-1RA) (IL1 inhibitor) (Anakinra)

 IL1RA_HUMAN             Reviewed;         177 AA.
P18510; A8K4G1; Q14628; Q53SC2; Q7RTZ4; Q96GD6; Q9UPC0;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
17-JUN-2020, entry version 217.
RecName: Full=Interleukin-1 receptor antagonist protein;
Short=IL-1RN;
Short=IL-1ra;
Short=IRAP;
AltName: Full=ICIL-1RA;
AltName: Full=IL1 inhibitor;
AltName: INN=Anakinra;
Flags: Precursor;
Name=IL1RN; Synonyms=IL1F3, IL1RA;
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).
PubMed=2139180; DOI=10.1038/344633a0;
Carter D.B., Deibel M.R. Jr., Dunn C.J., Tomich C.S.C., Laborde A.L.,
Slightom J.L., Berger A.E., Bienkowski M.J., Sun F.F., McEwan R.N.,
Harris P.K.W., Yem A.W., Waszak G.A., Chosay J.G., Sieu L.C., Hardee M.M.,
Zurcher-Neely H.A., Reardon I.M., Heinrikson R.L., Truesdell S.E.,
Shelly J.A., Eessalu T.E., Taylor B.M., Tracey D.E.;
"Purification, cloning, expression and biological characterization of an
interleukin-1 receptor antagonist protein.";
Nature 344:633-638(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2137201; DOI=10.1038/343341a0;
Eisenberg S.P., Evans R.J., Arend W.P., Verderber E., Brewer M.T.,
Hannum C.H., Thompson R.C.;
"Primary structure and functional expression from complementary DNA of a
human interleukin-1 receptor antagonist.";
Nature 343:341-346(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=1828896; DOI=10.1073/pnas.88.12.5232;
Eisenberg S.P., Brewer M.T., Verderber E., Heimdal P., Brandhuber B.J.,
Thompson R.C.;
"Interleukin 1 receptor antagonist is a member of the interleukin 1 gene
family: evolution of a cytokine control mechanism.";
Proc. Natl. Acad. Sci. U.S.A. 88:5232-5236(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=1385987; DOI=10.1016/1043-4666(92)90041-o;
Lennard A., Gorman P., Carrier M., Griffiths S., Scotney H., Sheer D.,
Solari R.;
"Cloning and chromosome mapping of the human interleukin-1 receptor
antagonist gene.";
Cytokine 4:83-89(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
PubMed=8992991;
Jenkins J.K., Drong R.F., Shuck M.E., Bienkowski M.J., Slightom J.L.,
Arend W.P., Smith M.F. Jr.;
"Intracellular IL-1 receptor antagonist promoter: cell type-specific and
inducible regulatory regions.";
J. Immunol. 158:748-755(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1827201; DOI=10.1073/pnas.88.9.3681;
Haskill S., Martin G., van Le L., Morris J., Peace A., Bigler C.F.,
Jaffe G.J., Hammerberg C., Sporn S.A., Fong S., Arend W.P., Ralph P.;
"cDNA cloning of an intracellular form of the human interleukin 1 receptor
antagonist associated with epithelium.";
Proc. Natl. Acad. Sci. U.S.A. 88:3681-3685(1991).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=7629520; DOI=10.1084/jem.182.2.623;
Muzio M., Polentarutti N., Sironi M., Poli G., De Gioia L., Introna M.,
Mantovani A., Colotta F.;
"Cloning and characterization of a new isoform of the interleukin 1
receptor antagonist.";
J. Exp. Med. 182:623-628(1995).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Esophagus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[11]
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.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
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).
[13]
PROTEIN SEQUENCE OF 26-45, AND GLYCOSYLATION AT ASN-109.
PubMed=2137200; DOI=10.1038/343336a0;
Hannum C.H., Wilcox C.J., Arend W.P., Joslin F.G., Dripps D.J.,
Heimdal P.L., Armes L.G., Sommer A., Eisenberg S.P., Thompson R.C.;
"Interleukin-1 receptor antagonist activity of a human interleukin-1
inhibitor.";
Nature 343:336-340(1990).
[14]
PROTEIN SEQUENCE OF 26-52.
PubMed=2143761;
Bienkowski M.J., Eessalu T.E., Berger A.E., Truesdell S.E., Shelly J.A.,
Laborde A.L., Zurcher-Neely H.A., Reardon I.M., Heinrikson R.L.,
Chosay J.G., Tracey D.E.;
"Purification and characterization of interleukin 1 receptor level
antagonist proteins from THP-1 cells.";
J. Biol. Chem. 265:14505-14511(1990).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 35-177 (ISOFORM 4).
PubMed=9514884; DOI=10.1006/bbrc.1998.8217;
Weissbach L., Tran K., Colquhoun S.A., Champliaud M.-F., Towle C.A.;
"Detection of an interleukin-1 intracellular receptor antagonist mRNA
variant.";
Biochem. Biophys. Res. Commun. 244:91-95(1998).
[16]
RECEPTOR-BINDING.
PubMed=7989776;
Giri J.G., Wells J., Dower S.K., McCall C.E., Guzman R.N., Slack J.,
Bird T.A., Shanebeck K., Grabstein K.H., Sims J.E., Alderson M.R.;
"Elevated levels of shed type II IL-1 receptor in sepsis. Potential role
for type II receptor in regulation of IL-1 responses.";
J. Immunol. 153:5802-5809(1994).
[17]
FUNCTION.
PubMed=7775431; DOI=10.1074/jbc.270.23.13757;
Greenfeder S.A., Nunes P., Kwee L., Labow M., Chizzonite R.A., Ju G.;
"Molecular cloning and characterization of a second subunit of the
interleukin 1 receptor complex.";
J. Biol. Chem. 270:13757-13765(1995).
[18]
IDENTIFICATION (ISOFORM 2).
PubMed=11991722; DOI=10.1006/geno.2002.6751;
Nicklin M.J.H., Barton J.L., Nguyen M., Fitzgerald M.G., Duff W.G.,
Kornman K.;
"A sequence-based map of the nine genes of the human interleukin-1
cluster.";
Genomics 79:718-725(2002).
[19]
INVOLVEMENT IN MVCD4.
PubMed=8786086; DOI=10.1007/bf02185776;
Blakemore A.I.F., Cox A., Gonzalez A.-M., Maskil J.K., Hughes M.E.,
Wilson R.M., Ward J.D., Duff G.W.;
"Interleukin-1 receptor antagonist allele (IL1RN*2) associated with
nephropathy in diabetes mellitus.";
Hum. Genet. 97:369-374(1996).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[21]
INVOLVEMENT IN DIRA.
PubMed=19494218; DOI=10.1056/nejmoa0807865;
Aksentijevich I., Masters S.L., Ferguson P.J., Dancey P., Frenkel J.,
van Royen-Kerkhoff A., Laxer R., Tedgard U., Cowen E.W., Pham T.H.,
Booty M., Estes J.D., Sandler N.G., Plass N., Stone D.L., Turner M.L.,
Hill S., Butman J.A., Schneider R., Babyn P., El-Shanti H.I., Pope E.,
Barron K., Bing X., Laurence A., Lee C.C., Chapelle D., Clarke G.I.,
Ohson K., Nicholson M., Gadina M., Yang B., Korman B.D., Gregersen P.K.,
van Hagen P.M., Hak A.E., Huizing M., Rahman P., Douek D.C., Remmers E.F.,
Kastner D.L., Goldbach-Mansky R.;
"An autoinflammatory disease with deficiency of the interleukin-1-receptor
antagonist.";
N. Engl. J. Med. 360:2426-2437(2009).
[22]
STRUCTURE BY NMR.
PubMed=1534997; DOI=10.1021/bi00138a001;
Stockman B.J., Scahill T.A., Roy M., Ulrich E.L., Strakalaitis N.A.,
Brunner D.P., Yem A.W., Deibel M.R. Jr.;
"Secondary structure and topology of interleukin-1 receptor antagonist
protein determined by heteronuclear three-dimensional NMR spectroscopy.";
Biochemistry 31:5237-5244(1992).
[23]
STRUCTURE BY NMR.
PubMed=8045306; DOI=10.1016/0014-5793(94)00643-1;
Stockman B.J., Scahill T.A., Strakalaitis N.A., Brunner D.P., Yem A.W.,
Deibel M.R. Jr.;
"Solution structure of human interleukin-1 receptor antagonist protein.";
FEBS Lett. 349:79-83(1994).
[24]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=8175703;
Vigers G.P.A., Caffes P., Evans R.J., Thompson R.C., Eisenberg S.P.,
Brandhuber B.J.;
"X-ray structure of interleukin-1 receptor antagonist at 2.0-A
resolution.";
J. Biol. Chem. 269:12874-12879(1994).
[25]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=7867645; DOI=10.1111/j.1432-1033.1995.tb20209.x;
Schreuder H.A., Rondeau J.-M., Tardif C., Soffientini A., Sarubbi E.,
Akeson A., Bowlin T.L., Yanofsky S., Barrett R.W.;
"Refined crystal structure of the interleukin-1 receptor antagonist.
Presence of a disulfide link and a cis-proline.";
Eur. J. Biochem. 227:838-847(1995).
[26]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 32-177 IN COMPLEX WITH IL1R.
PubMed=9062194; DOI=10.1038/386194a0;
Schreuder H., Tardif C., Trump-Kallmeyer S., Soffientini A., Sarubbi E.,
Akeson A., Bowlin T., Yanofsky S., Barrett R.W.;
"A new cytokine-receptor binding mode revealed by the crystal structure of
the IL-1 receptor with an antagonist.";
Nature 386:194-200(1997).
[27]
VARIANT [LARGE SCALE ANALYSIS] THR-124.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
-!- FUNCTION: Inhibits the activity of interleukin-1 by binding to receptor
IL1R1 and preventing its association with the coreceptor IL1RAP for
signaling. Has no interleukin-1 like activity. Binds functional
interleukin-1 receptor IL1R1 with greater affinity than decoy receptor
IL1R2; however, the physiological relevance of the latter association
is unsure. {ECO:0000269|PubMed:7775431}.
-!- INTERACTION:
P18510; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-1026330, EBI-750109;
-!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
-!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
-!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
-!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P18510-1; Sequence=Displayed;
Name=2; Synonyms=icIL-1ra;
IsoId=P18510-2; Sequence=VSP_002649;
Name=3; Synonyms=icIL-1ra type II;
IsoId=P18510-3; Sequence=VSP_002650;
Name=4;
IsoId=P18510-4; Sequence=VSP_002651;
-!- TISSUE SPECIFICITY: The intracellular form of IL1RN is predominantly
expressed in epithelial cells.
-!- DISEASE: Microvascular complications of diabetes 4 (MVCD4)
[MIM:612628]: Pathological conditions that develop in numerous tissues
and organs as a consequence of diabetes mellitus. They include diabetic
retinopathy, diabetic nephropathy leading to end-stage renal disease,
and diabetic neuropathy. Diabetic retinopathy remains the major cause
of new-onset blindness among diabetic adults. It is characterized by
vascular permeability and increased tissue ischemia and angiogenesis.
{ECO:0000269|PubMed:8786086}. Note=Disease susceptibility is associated
with variations affecting the gene represented in this entry.
-!- DISEASE: Interleukin 1 receptor antagonist deficiency (DIRA)
[MIM:612852]: A rare autoinflammatory disease of skin and bone
resulting in sterile multifocal osteomyelitis, periostitis, and
pustulosis from birth. The term autoinflammatory disease describes a
group of disorders characterized by attacks of seemingly unprovoked
inflammation without significant levels of autoantibodies and
autoreactive T-cells. {ECO:0000269|PubMed:19494218}. Note=The disease
is caused by mutations affecting the gene represented in this entry.
-!- PHARMACEUTICAL: Available under the name Kineret (Amgen). Used for the
reduction in signs and symptoms and slowing the progression of
structural damage in moderately to severely active rheumatoid
arthritis.
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-1 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_1";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il1rn/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=IL1RN";
-!- WEB RESOURCE: Name=Kineret professional medical information;
URL="https://www.rxlist.com/kineret-drug.htm";
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EMBL; X53296; CAA37386.1; -; mRNA.
EMBL; X52015; CAA36262.1; -; mRNA.
EMBL; M63099; AAB41943.1; -; Genomic_DNA.
EMBL; X64532; CAA45832.1; -; Genomic_DNA.
EMBL; U65590; AAB92270.1; -; Genomic_DNA.
EMBL; U65590; AAB92268.1; -; Genomic_DNA.
EMBL; U65590; AAB92269.1; -; Genomic_DNA.
EMBL; M55646; AAA59138.1; -; mRNA.
EMBL; X84348; CAA59087.1; -; mRNA.
EMBL; AY196903; AAN87150.1; -; Genomic_DNA.
EMBL; AK290898; BAF83587.1; -; mRNA.
EMBL; AK290926; BAF83615.1; -; mRNA.
EMBL; AC024704; AAX93278.1; -; Genomic_DNA.
EMBL; CH471217; EAW73625.1; -; Genomic_DNA.
EMBL; BC009745; AAH09745.1; -; mRNA.
EMBL; AF043143; AAC39672.1; -; mRNA.
EMBL; BN000002; CAD29879.1; -; Genomic_DNA.
CCDS; CCDS2113.1; -. [P18510-2]
CCDS; CCDS2114.1; -. [P18510-3]
CCDS; CCDS2115.1; -. [P18510-4]
CCDS; CCDS46396.1; -. [P18510-1]
PIR; A40956; A30368.
PIR; I37893; A39386.
RefSeq; NP_000568.1; NM_000577.4. [P18510-2]
RefSeq; NP_001305843.1; NM_001318914.1. [P18510-4]
RefSeq; NP_776213.1; NM_173841.2. [P18510-3]
RefSeq; NP_776214.1; NM_173842.2. [P18510-1]
RefSeq; NP_776215.1; NM_173843.2. [P18510-4]
RefSeq; XP_005263718.1; XM_005263661.4. [P18510-4]
RefSeq; XP_011509423.1; XM_011511121.1. [P18510-4]
PDB; 1ILR; X-ray; 2.10 A; 1/2=26-177.
PDB; 1ILT; X-ray; 2.00 A; A/B=26-177.
PDB; 1IRA; X-ray; 2.70 A; X=26-177.
PDB; 1IRP; NMR; -; A=26-177.
PDB; 1ITN; Model; -; A=31-177.
PDB; 2IRT; X-ray; 3.20 A; A/B=26-177.
PDBsum; 1ILR; -.
PDBsum; 1ILT; -.
PDBsum; 1IRA; -.
PDBsum; 1IRP; -.
PDBsum; 1ITN; -.
PDBsum; 2IRT; -.
SMR; P18510; -.
BioGRID; 109772; 15.
IntAct; P18510; 8.
STRING; 9606.ENSP00000259206; -.
DrugBank; DB06372; Rilonacept.
DrugCentral; P18510; -.
Allergome; 11858; Hom s Anakinra.
GlyConnect; 1947; -.
iPTMnet; P18510; -.
PhosphoSitePlus; P18510; -.
BioMuta; IL1RN; -.
DMDM; 124312; -.
jPOST; P18510; -.
MassIVE; P18510; -.
MaxQB; P18510; -.
PaxDb; P18510; -.
PeptideAtlas; P18510; -.
PRIDE; P18510; -.
ProteomicsDB; 53572; -. [P18510-1]
ProteomicsDB; 53573; -. [P18510-2]
ProteomicsDB; 53574; -. [P18510-3]
ProteomicsDB; 53575; -. [P18510-4]
Antibodypedia; 806; 847 antibodies.
DNASU; 3557; -.
Ensembl; ENST00000259206; ENSP00000259206; ENSG00000136689. [P18510-3]
Ensembl; ENST00000354115; ENSP00000329072; ENSG00000136689. [P18510-2]
Ensembl; ENST00000361779; ENSP00000354816; ENSG00000136689. [P18510-4]
Ensembl; ENST00000409052; ENSP00000387210; ENSG00000136689. [P18510-4]
Ensembl; ENST00000409930; ENSP00000387173; ENSG00000136689. [P18510-1]
GeneID; 3557; -.
KEGG; hsa:3557; -.
UCSC; uc002tiy.3; human. [P18510-1]
CTD; 3557; -.
DisGeNET; 3557; -.
EuPathDB; HostDB:ENSG00000136689.18; -.
GeneCards; IL1RN; -.
HGNC; HGNC:6000; IL1RN.
HPA; ENSG00000136689; Tissue enhanced (esophagus, lymphoid tissue, tongue).
MalaCards; IL1RN; -.
MIM; 147679; gene.
MIM; 612628; phenotype.
MIM; 612852; phenotype.
neXtProt; NX_P18510; -.
OpenTargets; ENSG00000136689; -.
Orphanet; 210115; Sterile multifocal osteomyelitis with periostitis and pustulosis.
PharmGKB; PA29816; -.
eggNOG; ENOG410IZQ4; Eukaryota.
eggNOG; ENOG41119SQ; LUCA.
GeneTree; ENSGT00950000182943; -.
HOGENOM; CLU_095373_2_0_1; -.
InParanoid; P18510; -.
KO; K05481; -.
OMA; WYLCTAL; -.
OrthoDB; 1410755at2759; -.
PhylomeDB; P18510; -.
TreeFam; TF300203; -.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
SIGNOR; P18510; -.
BioGRID-ORCS; 3557; 1 hit in 790 CRISPR screens.
ChiTaRS; IL1RN; human.
EvolutionaryTrace; P18510; -.
GeneWiki; Interleukin_1_receptor_antagonist; -.
GenomeRNAi; 3557; -.
Pharos; P18510; Tchem.
PRO; PR:P18510; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; P18510; protein.
Bgee; ENSG00000136689; Expressed in lower esophagus mucosa and 162 other tissues.
ExpressionAtlas; P18510; baseline and differential.
Genevisible; P18510; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005125; F:cytokine activity; IEA:InterPro.
GO; GO:0005152; F:interleukin-1 receptor antagonist activity; IDA:BHF-UCL.
GO; GO:0005149; F:interleukin-1 receptor binding; IDA:BHF-UCL.
GO; GO:0045352; F:interleukin-1 type I receptor antagonist activity; IDA:BHF-UCL.
GO; GO:0045353; F:interleukin-1 type II receptor antagonist activity; IDA:BHF-UCL.
GO; GO:0005150; F:interleukin-1, type I receptor binding; IPI:BHF-UCL.
GO; GO:0005151; F:interleukin-1, type II receptor binding; IPI:BHF-UCL.
GO; GO:0006953; P:acute-phase response; IDA:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IBA:GO_Central.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0051384; P:response to glucocorticoid; IDA:BHF-UCL.
InterPro; IPR020877; IL-1_CS.
InterPro; IPR000975; IL-1_fam.
InterPro; IPR003297; IL-1RA/IL-36.
InterPro; IPR008996; IL1/FGF.
InterPro; IPR039348; IL1RA.
PANTHER; PTHR10078; PTHR10078; 1.
PANTHER; PTHR10078:SF28; PTHR10078:SF28; 1.
Pfam; PF00340; IL1; 1.
PRINTS; PR00264; INTERLEUKIN1.
PRINTS; PR01360; INTRLEUKIN1X.
SUPFAM; SSF50353; SSF50353; 1.
PROSITE; PS00253; INTERLEUKIN_1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
Disulfide bond; Glycoprotein; Pharmaceutical; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1..25
/evidence="ECO:0000269|PubMed:2137200,
ECO:0000269|PubMed:2143761"
CHAIN 26..177
/note="Interleukin-1 receptor antagonist protein"
/id="PRO_0000015328"
CARBOHYD 109
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:2137200"
DISULFID 91..141
VAR_SEQ 1..34
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:9514884"
/id="VSP_002651"
VAR_SEQ 1..21
/note="MEICRGLRSHLITLLLFLFHS -> MAL (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1827201"
/id="VSP_002649"
VAR_SEQ 1..21
/note="MEICRGLRSHLITLLLFLFHS -> MALADLYEEGGGGGGEGEDNADSK
(in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7629520"
/id="VSP_002650"
VARIANT 124
/note="A -> T (in dbSNP:rs45507693)"
/evidence="ECO:0000269|PubMed:18987736"
/id="VAR_049573"
STRAND 36..42
/evidence="ECO:0000244|PDB:1ILR"
TURN 43..45
/evidence="ECO:0000244|PDB:1IRP"
STRAND 47..51
/evidence="ECO:0000244|PDB:1ILR"
STRAND 54..58
/evidence="ECO:0000244|PDB:1ILR"
HELIX 62..67
/evidence="ECO:0000244|PDB:1ILR"
STRAND 71..76
/evidence="ECO:0000244|PDB:1ILR"
TURN 77..79
/evidence="ECO:0000244|PDB:1ILR"
STRAND 80..85
/evidence="ECO:0000244|PDB:1ILR"
TURN 86..89
/evidence="ECO:0000244|PDB:1ILR"
STRAND 90..97
/evidence="ECO:0000244|PDB:1ILR"
STRAND 100..106
/evidence="ECO:0000244|PDB:1ILR"
HELIX 110..112
/evidence="ECO:0000244|PDB:1ILR"
HELIX 118..123
/evidence="ECO:0000244|PDB:1ILR"
STRAND 124..130
/evidence="ECO:0000244|PDB:1ILR"
STRAND 133..141
/evidence="ECO:0000244|PDB:1ILR"
STRAND 145..151
/evidence="ECO:0000244|PDB:1ILR"
STRAND 157..160
/evidence="ECO:0000244|PDB:1ILR"
STRAND 162..168
/evidence="ECO:0000244|PDB:1ILR"
STRAND 171..175
/evidence="ECO:0000244|PDB:1ILR"
SEQUENCE 177 AA; 20055 MW; D1690776A7394057 CRC64;
MEICRGLRSH LITLLLFLFH SETICRPSGR KSSKMQAFRI WDVNQKTFYL RNNQLVAGYL
QGPNVNLEEK IDVVPIEPHA LFLGIHGGKM CLSCVKSGDE TRLQLEAVNI TDLSENRKQD
KRFAFIRSDS GPTTSFESAA CPGWFLCTAM EADQPVSLTN MPDEGVMVTK FYFQEDE


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Related Genes :
[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)]
[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)
[Il1r1 Il-1r1 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)]
[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)]
[IL37 FIL1Z IL1F7 IL1H4 IL1RP1] Interleukin-37 (FIL1 zeta) (IL-1X) (Interleukin-1 family member 7) (IL-1F7) (Interleukin-1 homolog 4) (IL-1H) (IL-1H4) (Interleukin-1 zeta) (IL-1 zeta) (Interleukin-1-related protein) (IL-1RP1) (Interleukin-23) (IL-37)
[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] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[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)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6)
[IL1RAP] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6)
[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)
[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)
[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)
[Il36a Fil1e Il1e Il1f6 Il1h1] Interleukin-36 alpha (FIL1 epsilon) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 6) (IL-1F6) (Interleukin-1 homolog 1) (IL-1H1)
[Il1rl2] Interleukin-1 receptor-like 2 (EC 3.2.2.6) (IL-36 receptor) (Interleukin-1 receptor-related protein 2) (IL-1Rrp2) (IL1R-rp2)
[IL1RAPL1 OPHN4] Interleukin-1 receptor accessory protein-like 1 (IL-1-RAPL-1) (IL-1RAPL-1) (IL1RAPL-1) (EC 3.2.2.6) (Oligophrenin-4) (Three immunoglobulin domain-containing IL-1 receptor-related 2) (TIGIRR-2) (X-linked interleukin-1 receptor accessory protein-like 1)
[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)
[IL36B IL1F8 IL1H2] Interleukin-36 beta (FIL1 eta) (Interleukin-1 eta) (IL-1 eta) (Interleukin-1 family member 8) (IL-1F8) (Interleukin-1 homolog 2) (IL-1H2)
[IL36A FIL1E IL1E IL1F6] Interleukin-36 alpha (FIL1 epsilon) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 6) (IL-1F6)
[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)]
[IL1B IL1F2] Interleukin-1 beta (IL-1 beta) (Catabolin)
[IL18 IGIF IL1F4] Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL1A IL1F1] Interleukin-1 alpha (IL-1 alpha) (Hematopoietin-1)
[CARD16 COP COP1] Caspase recruitment domain-containing protein 16 (Caspase recruitment domain-only protein 1) (CARD-only protein 1) (Caspase-1 inhibitor COP) (Pseudo interleukin-1 beta converting enzyme) (Pseudo-ICE) (Pseudo-IL1B-converting enzyme)
[Il1rl1 Ly84 St2 Ste2] Interleukin-1 receptor-like 1 (EC 3.2.2.6) (Interleukin-33 receptor alpha chain) (Lymphocyte antigen 84) (Protein ST2) (Protein T1)
[Sigirr Tir8] Single Ig IL-1-related receptor (Single Ig IL-1R-related molecule) (Single immunoglobulin domain-containing IL1R-related protein) (Toll/interleukin-1 receptor 8) (TIR8)
[Il1b] Interleukin-1 beta (IL-1 beta)
[Il1b] Interleukin-1 beta (IL-1 beta)
[IL1B] Interleukin-1 beta (IL-1 beta)
[Il1a] Interleukin-1 alpha (IL-1 alpha)

Bibliography :