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P18510 (IL1RA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-1 receptor antagonist protein

Short name=IL-1RN
Short name=IL-1ra
Short name=IRAP
Alternative name(s):
ICIL-1RA
IL1 inhibitor
INN=Anakinra
Gene names
Name:IL1RN
Synonyms:IL1F3, IL1RA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.17

Subcellular location

Isoform 1: Secreted.

Isoform 2: Cytoplasm.

Isoform 3: Cytoplasm.

Isoform 4: Cytoplasm.

Tissue specificity

The intracellular form of IL1RN is predominantly expressed in epithelial cells.

Involvement in 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Pharmaceutical use

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.

Ontologies

Keywords
   Cellular componentCytoplasm
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from direct assay PubMed 9185517. Source: BHF-UCL

carboxylic acid metabolic process

Inferred from electronic annotation. Source: Ensembl

chronic inflammatory response to antigenic stimulus

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

fever generation

Inferred from electronic annotation. Source: Ensembl

immune response

Non-traceable author statement Ref.7. Source: UniProtKB

insulin secretion

Inferred from electronic annotation. Source: Ensembl

lipid metabolic process

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytokine-mediated signaling pathway

Inferred from direct assay Ref.13. Source: GOC

negative regulation of glutamate secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of heterotypic cell-cell adhesion

Inferred from direct assay Ref.1. Source: BHF-UCL

negative regulation of interleukin-1-mediated signaling pathway

Inferred from direct assay Ref.13Ref.1. Source: BHF-UCL

negative regulation of membrane potential

Inferred from electronic annotation. Source: Ensembl

positive regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from direct assay PubMed 10443688. Source: BHF-UCL

response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from direct assay PubMed 10443688PubMed 12483741Ref.13PubMed 9185517. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

intracellular

Non-traceable author statement Ref.7. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioninterleukin-1 Type I receptor antagonist activity

Inferred from direct assay PubMed 1828071. Source: BHF-UCL

interleukin-1 Type II receptor antagonist activity

Inferred from direct assay PubMed 1830582. Source: BHF-UCL

interleukin-1 receptor antagonist activity

Inferred from direct assay Ref.13. Source: BHF-UCL

interleukin-1 receptor binding

Inferred from direct assay Ref.13. Source: BHF-UCL

interleukin-1, Type I receptor binding

Inferred from physical interaction PubMed 1828071. Source: BHF-UCL

interleukin-1, Type II receptor binding

Inferred from physical interaction PubMed 1830582. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P18510-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P18510-2)

Also known as: icIL-1ra;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEICRGLRSHLITLLLFLFHS → MAL
Isoform 3 (identifier: P18510-3)

Also known as: icIL-1ra type II;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEICRGLRSHLITLLLFLFHS → MALADLYEEGGGGGGEGEDNADSK
Isoform 4 (identifier: P18510-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.13 Ref.14
Chain26 – 177152Interleukin-1 receptor antagonist protein Ref.1
PRO_0000015328

Amino acid modifications

Glycosylation1091N-linked (GlcNAc...) Ref.13 Ref.20
Disulfide bond91 ↔ 141

Natural variations

Alternative sequence1 – 3434Missing in isoform 4.
VSP_002651
Alternative sequence1 – 2121MEICR…FLFHS → MAL in isoform 2.
VSP_002649
Alternative sequence1 – 2121MEICR…FLFHS → MALADLYEEGGGGGGEGEDN ADSK in isoform 3.
VSP_002650
Natural variant1241A → T. Ref.27
Corresponds to variant rs45507693 [ dbSNP | Ensembl ].
VAR_049573

Secondary structure

................................. 177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: D1690776A7394057

FASTA17720,055
        10         20         30         40         50         60 
MEICRGLRSH LITLLLFLFH SETICRPSGR KSSKMQAFRI WDVNQKTFYL RNNQLVAGYL 

        70         80         90        100        110        120 
QGPNVNLEEK IDVVPIEPHA LFLGIHGGKM CLSCVKSGDE TRLQLEAVNI TDLSENRKQD 

       130        140        150        160        170 
KRFAFIRSDS GPTTSFESAA CPGWFLCTAM EADQPVSLTN MPDEGVMVTK FYFQEDE 

« Hide

Isoform 2 (icIL-1ra) [UniParc].

Checksum: C1D66CDF0D2F7B44
Show »

FASTA15917,888
Isoform 3 (icIL-1ra type II) [UniParc].

Checksum: 624A1574C2334229
Show »

FASTA18019,897
Isoform 4 [UniParc].

Checksum: 4CAD6784B890906B
Show »

FASTA14316,142

References

« Hide 'large scale' references
[1]"Purification, cloning, expression and biological characterization of an interleukin-1 receptor antagonist protein."
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. expand/collapse author list , Heinrikson R.L., Truesdell S.E., Shelly J.A., Eessalu T.E., Taylor B.M., Tracey D.E.
Nature 344:633-638(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Primary structure and functional expression from complementary DNA of a human interleukin-1 receptor antagonist."
Eisenberg S.P., Evans R.J., Arend W.P., Verderber E., Brewer M.T., Hannum C.H., Thompson R.C.
Nature 343:341-346(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Interleukin 1 receptor antagonist is a member of the interleukin 1 gene family: evolution of a cytokine control mechanism."
Eisenberg S.P., Brewer M.T., Verderber E., Heimdal P., Brandhuber B.J., Thompson R.C.
Proc. Natl. Acad. Sci. U.S.A. 88:5232-5236(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]"Cloning and chromosome mapping of the human interleukin-1 receptor antagonist gene."
Lennard A., Gorman P., Carrier M., Griffiths S., Scotney H., Sheer D., Solari R.
Cytokine 4:83-89(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]"Intracellular IL-1 receptor antagonist promoter: cell type-specific and inducible regulatory regions."
Jenkins J.K., Drong R.F., Shuck M.E., Bienkowski M.J., Slightom J.L., Arend W.P., Smith M.F. Jr.
J. Immunol. 158:748-755(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
[6]"cDNA cloning of an intracellular form of the human interleukin 1 receptor antagonist associated with epithelium."
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.
Proc. Natl. Acad. Sci. U.S.A. 88:3681-3685(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]"Cloning and characterization of a new isoform of the interleukin 1 receptor antagonist."
Muzio M., Polentarutti N., Sironi M., Poli G., De Gioia L., Introna M., Mantovani A., Colotta F.
J. Exp. Med. 182:623-628(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[8]SeattleSNPs variation discovery resource
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Esophagus.
[10]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Pancreas.
[13]"Interleukin-1 receptor antagonist activity of a human interleukin-1 inhibitor."
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.
Nature 343:336-340(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-45, GLYCOSYLATION AT ASN-109.
[14]"Purification and characterization of interleukin 1 receptor level antagonist proteins from THP-1 cells."
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.
J. Biol. Chem. 265:14505-14511(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-52.
[15]"Detection of an interleukin-1 intracellular receptor antagonist mRNA variant."
Weissbach L., Tran K., Colquhoun S.A., Champliaud M.-F., Towle C.A.
Biochem. Biophys. Res. Commun. 244:91-95(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-177 (ISOFORM 4).
[16]"Elevated levels of shed type II IL-1 receptor in sepsis. Potential role for type II receptor in regulation of IL-1 responses."
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.
J. Immunol. 153:5802-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: RECEPTOR-BINDING.
[17]"Molecular cloning and characterization of a second subunit of the interleukin 1 receptor complex."
Greenfeder S.A., Nunes P., Kwee L., Labow M., Chizzonite R.A., Ju G.
J. Biol. Chem. 270:13757-13765(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"A sequence-based map of the nine genes of the human interleukin-1 cluster."
Nicklin M.J.H., Barton J.L., Nguyen M., Fitzgerald M.G., Duff W.G., Kornman K.
Genomics 79:718-725(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORM 2).
[19]"Interleukin-1 receptor antagonist allele (IL1RN*2) associated with nephropathy in diabetes mellitus."
Blakemore A.I.F., Cox A., Gonzalez A.-M., Maskil J.K., Hughes M.E., Wilson R.M., Ward J.D., Duff G.W.
Hum. Genet. 97:369-374(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DIABETIC NEPHROPATHY SUSCEPTIBILITY.
[20]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109.
Tissue: Plasma.
[21]"An autoinflammatory disease with deficiency of the interleukin-1-receptor antagonist."
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. expand/collapse author list , 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.
N. Engl. J. Med. 360:2426-2437(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DIRA.
[22]"Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy."
Stockman B.J., Scahill T.A., Roy M., Ulrich E.L., Strakalaitis N.A., Brunner D.P., Yem A.W., Deibel M.R. Jr.
Biochemistry 31:5237-5244(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[23]"Solution structure of human interleukin-1 receptor antagonist protein."
Stockman B.J., Scahill T.A., Strakalaitis N.A., Brunner D.P., Yem A.W., Deibel M.R. Jr.
FEBS Lett. 349:79-83(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[24]"X-ray structure of interleukin-1 receptor antagonist at 2.0-A resolution."
Vigers G.P.A., Caffes P., Evans R.J., Thompson R.C., Eisenberg S.P., Brandhuber B.J.
J. Biol. Chem. 269:12874-12879(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[25]"Refined crystal structure of the interleukin-1 receptor antagonist. Presence of a disulfide link and a cis-proline."
Schreuder H.A., Rondeau J.-M., Tardif C., Soffientini A., Sarubbi E., Akeson A., Bowlin T.L., Yanofsky S., Barrett R.W.
Eur. J. Biochem. 227:838-847(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[26]"A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist."
Schreuder H., Tardif C., Trump-Kallmeyer S., Soffientini A., Sarubbi E., Akeson A., Bowlin T., Yanofsky S., Barrett R.W.
Nature 386:194-200(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 32-177 IN COMPLEX WITH IL1R.
[27]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
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. expand/collapse author list , 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.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-124.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53296 mRNA. Translation: CAA37386.1.
X52015 mRNA. Translation: CAA36262.1.
M63099 Genomic DNA. Translation: AAB41943.1.
X64532 Genomic DNA. Translation: CAA45832.1.
U65590 Genomic DNA. Translation: AAB92270.1.
U65590 Genomic DNA. Translation: AAB92268.1.
U65590 Genomic DNA. Translation: AAB92269.1.
M55646 mRNA. Translation: AAA59138.1.
X84348 mRNA. Translation: CAA59087.1.
AY196903 Genomic DNA. Translation: AAN87150.1.
AK290898 mRNA. Translation: BAF83587.1.
AK290926 mRNA. Translation: BAF83615.1.
AC024704 Genomic DNA. Translation: AAX93278.1.
CH471217 Genomic DNA. Translation: EAW73625.1.
BC009745 mRNA. Translation: AAH09745.1.
AF043143 mRNA. Translation: AAC39672.1.
BN000002 Genomic DNA. Translation: CAD29879.1.
PIRA30368. A40956.
A39386. I37893.
RefSeqNP_000568.1. NM_000577.4.
NP_776213.1. NM_173841.2.
NP_776214.1. NM_173842.2.
NP_776215.1. NM_173843.2.
XP_005263718.1. XM_005263661.2.
UniGeneHs.81134.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ILRX-ray2.101/226-177[»]
1ILTX-ray2.00A/B26-177[»]
1IRAX-ray2.70X26-177[»]
1IRPNMR-A26-177[»]
1ITNmodel-A31-177[»]
2IRTX-ray3.20A/B26-177[»]
ProteinModelPortalP18510.
SMRP18510. Positions 33-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109772. 4 interactions.
DIPDIP-3513N.
IntActP18510. 1 interaction.
MINTMINT-1522172.
STRING9606.ENSP00000259206.

Chemistry

DrugBankDB00026. Anakinra.

Polymorphism databases

DMDM124312.

Proteomic databases

PaxDbP18510.
PRIDEP18510.

Protocols and materials databases

DNASU3557.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259206; ENSP00000259206; ENSG00000136689. [P18510-3]
ENST00000354115; ENSP00000329072; ENSG00000136689. [P18510-2]
ENST00000361779; ENSP00000354816; ENSG00000136689. [P18510-4]
ENST00000409052; ENSP00000387210; ENSG00000136689. [P18510-4]
ENST00000409930; ENSP00000387173; ENSG00000136689. [P18510-1]
GeneID3557.
KEGGhsa:3557.
UCSCuc002tiy.3. human. [P18510-1]
uc002tiz.3. human. [P18510-3]
uc002tja.3. human. [P18510-2]

Organism-specific databases

CTD3557.
GeneCardsGC02P113864.
HGNCHGNC:6000. IL1RN.
HPACAB009633.
HPA001482.
MIM147679. gene.
612628. phenotype.
612852. phenotype.
neXtProtNX_P18510.
Orphanet210115. Sterile multifocal osteomyelitis with periostitis and pustulosis.
PharmGKBPA29816.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46710.
HOGENOMHOG000231506.
HOVERGENHBG052099.
KOK05481.
OMAIHGGKLC.
OrthoDBEOG7X6M1M.
PhylomeDBP18510.
TreeFamTF300203.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP18510.
BgeeP18510.
CleanExHS_IL1RN.
GenevestigatorP18510.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR000975. IL-1.
IPR020877. IL-1_CS.
IPR027166. IL-1RA.
IPR003297. IL-1RA/IL-36.
[Graphical view]
PANTHERPTHR10078:SF6. PTHR10078:SF6. 1 hit.
PfamPF00340. IL1. 1 hit.
[Graphical view]
PRINTSPR00264. INTERLEUKIN1.
PR01360. INTRLEUKIN1X.
SMARTSM00125. IL1. 1 hit.
[Graphical view]
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIL1RN. human.
EvolutionaryTraceP18510.
GeneWikiInterleukin_1_receptor_antagonist.
GenomeRNAi3557.
NextBio13886.
PROP18510.
SOURCESearch...

Entry information

Entry nameIL1RA_HUMAN
AccessionPrimary (citable) accession number: P18510
Secondary accession number(s): A8K4G1 expand/collapse secondary AC list , Q14628, Q53SC2, Q7RTZ4, Q96GD6, Q9UPC0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM