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P18510

- IL1RA_HUMAN

UniProt

P18510 - IL1RA_HUMAN

Protein

Interleukin-1 receptor antagonist protein

Gene

IL1RN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. interleukin-1, Type II receptor binding Source: BHF-UCL
    2. interleukin-1, Type I receptor binding Source: BHF-UCL
    3. interleukin-1 receptor antagonist activity Source: BHF-UCL
    4. interleukin-1 receptor binding Source: BHF-UCL
    5. interleukin-1 Type II receptor antagonist activity Source: BHF-UCL
    6. interleukin-1 Type I receptor antagonist activity Source: BHF-UCL

    GO - Biological processi

    1. acute-phase response Source: BHF-UCL
    2. carboxylic acid metabolic process Source: Ensembl
    3. chronic inflammatory response to antigenic stimulus Source: Ensembl
    4. female pregnancy Source: Ensembl
    5. fever generation Source: Ensembl
    6. immune response Source: UniProtKB
    7. insulin secretion Source: Ensembl
    8. lipid metabolic process Source: Ensembl
    9. memory Source: Ensembl
    10. negative regulation of apoptotic process Source: Ensembl
    11. negative regulation of cell migration Source: Ensembl
    12. negative regulation of cytokine-mediated signaling pathway Source: GOC
    13. negative regulation of glutamate secretion Source: Ensembl
    14. negative regulation of heterotypic cell-cell adhesion Source: BHF-UCL
    15. negative regulation of interleukin-1-mediated signaling pathway Source: BHF-UCL
    16. negative regulation of membrane potential Source: Ensembl
    17. positive regulation of JUN kinase activity Source: Ensembl
    18. response to drug Source: Ensembl
    19. response to glucocorticoid Source: BHF-UCL
    20. response to interleukin-4 Source: Ensembl
    21. response to lipopolysaccharide Source: Ensembl
    22. response to organonitrogen compound Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_22442. Interleukin-1 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:IL1RN
    Synonyms:IL1F3, IL1RA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6000. IL1RN.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. intracellular Source: UniProtKB
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    Pathology & Biotechi

    Involvement in diseasei

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

    Pharmaceutical usei

    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.

    Organism-specific databases

    MIMi612628. phenotype.
    612852. phenotype.
    Orphaneti210115. Sterile multifocal osteomyelitis with periostitis and pustulosis.
    PharmGKBiPA29816.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25252 PublicationsAdd
    BLAST
    Chaini26 – 177152Interleukin-1 receptor antagonist proteinPRO_0000015328Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi91 ↔ 141
    Glycosylationi109 – 1091N-linked (GlcNAc...)2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP18510.
    PaxDbiP18510.
    PRIDEiP18510.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP18510.
    BgeeiP18510.
    CleanExiHS_IL1RN.
    GenevestigatoriP18510.

    Organism-specific databases

    HPAiCAB009633.
    HPA001482.

    Interactioni

    Protein-protein interaction databases

    BioGridi109772. 4 interactions.
    DIPiDIP-3513N.
    IntActiP18510. 1 interaction.
    MINTiMINT-1522172.
    STRINGi9606.ENSP00000259206.

    Structurei

    Secondary structure

    1
    177
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 427
    Turni43 – 453
    Beta strandi47 – 515
    Beta strandi54 – 585
    Helixi62 – 676
    Beta strandi71 – 766
    Turni77 – 793
    Beta strandi80 – 856
    Turni86 – 894
    Beta strandi90 – 978
    Beta strandi100 – 1067
    Helixi110 – 1123
    Helixi118 – 1236
    Beta strandi124 – 1307
    Beta strandi133 – 1419
    Beta strandi145 – 1517
    Beta strandi157 – 1604
    Beta strandi162 – 1687
    Beta strandi171 – 1755

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP18510.
    SMRiP18510. Positions 33-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18510.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG46710.
    HOGENOMiHOG000231506.
    HOVERGENiHBG052099.
    KOiK05481.
    OMAiQSIYGRR.
    OrthoDBiEOG7X6M1M.
    PhylomeDBiP18510.
    TreeFamiTF300203.

    Family and domain databases

    InterProiIPR008996. Cytokine_IL1-like.
    IPR020877. IL-1_CS.
    IPR000975. IL-1_fam.
    IPR027166. IL-1RA.
    IPR003297. IL-1RA/IL-36.
    [Graphical view]
    PANTHERiPTHR10078:SF6. PTHR10078:SF6. 1 hit.
    PfamiPF00340. IL1. 1 hit.
    [Graphical view]
    PRINTSiPR00264. INTERLEUKIN1.
    PR01360. INTRLEUKIN1X.
    SUPFAMiSSF50353. SSF50353. 1 hit.
    PROSITEiPS00253. INTERLEUKIN_1. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P18510-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEICRGLRSH LITLLLFLFH SETICRPSGR KSSKMQAFRI WDVNQKTFYL    50
    RNNQLVAGYL QGPNVNLEEK IDVVPIEPHA LFLGIHGGKM CLSCVKSGDE 100
    TRLQLEAVNI TDLSENRKQD KRFAFIRSDS GPTTSFESAA CPGWFLCTAM 150
    EADQPVSLTN MPDEGVMVTK FYFQEDE 177
    Length:177
    Mass (Da):20,055
    Last modified:November 1, 1990 - v1
    Checksum:iD1690776A7394057
    GO
    Isoform 2 (identifier: P18510-2) [UniParc]FASTAAdd to Basket

    Also known as: icIL-1ra

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MEICRGLRSHLITLLLFLFHS → MAL

    Show »
    Length:159
    Mass (Da):17,888
    Checksum:iC1D66CDF0D2F7B44
    GO
    Isoform 3 (identifier: P18510-3) [UniParc]FASTAAdd to Basket

    Also known as: icIL-1ra type II

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MEICRGLRSHLITLLLFLFHS → MALADLYEEGGGGGGEGEDNADSK

    Show »
    Length:180
    Mass (Da):19,897
    Checksum:i624A1574C2334229
    GO
    Isoform 4 (identifier: P18510-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:143
    Mass (Da):16,142
    Checksum:i4CAD6784B890906B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti124 – 1241A → T.1 Publication
    Corresponds to variant rs45507693 [ dbSNP | Ensembl ].
    VAR_049573

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3434Missing in isoform 4. 1 PublicationVSP_002651Add
    BLAST
    Alternative sequencei1 – 2121MEICR…FLFHS → MAL in isoform 2. 2 PublicationsVSP_002649Add
    BLAST
    Alternative sequencei1 – 2121MEICR…FLFHS → MALADLYEEGGGGGGEGEDN ADSK in isoform 3. 2 PublicationsVSP_002650Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2113.1. [P18510-2]
    CCDS2114.1. [P18510-3]
    CCDS2115.1. [P18510-4]
    CCDS46396.1. [P18510-1]
    PIRiA40956. A30368.
    I37893. A39386.
    RefSeqiNP_000568.1. NM_000577.4. [P18510-2]
    NP_776213.1. NM_173841.2. [P18510-3]
    NP_776214.1. NM_173842.2. [P18510-1]
    NP_776215.1. NM_173843.2. [P18510-4]
    XP_005263718.1. XM_005263661.2. [P18510-4]
    XP_006712560.1. XM_006712497.1. [P18510-4]
    UniGeneiHs.81134.

    Genome annotation databases

    EnsembliENST00000259206; ENSP00000259206; ENSG00000136689. [P18510-3]
    ENST00000354115; ENSP00000329072; ENSG00000136689. [P18510-2]
    ENST00000361779; ENSP00000354816; ENSG00000136689. [P18510-4]
    ENST00000409052; ENSP00000387210; ENSG00000136689. [P18510-4]
    ENST00000409930; ENSP00000387173; ENSG00000136689. [P18510-1]
    GeneIDi3557.
    KEGGihsa:3557.
    UCSCiuc002tiy.3. human. [P18510-1]
    uc002tiz.3. human. [P18510-3]
    uc002tja.3. human. [P18510-2]

    Polymorphism databases

    DMDMi124312.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    R&D Systems' cytokine source book: IL-1ra
    Wikipedia

    Interleukin-1 entry

    SeattleSNPs
    SHMPD

    The Singapore human mutation and polymorphism database

    Kineret professional medical information"

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2113.1. [P18510-2 ]
    CCDS2114.1. [P18510-3 ]
    CCDS2115.1. [P18510-4 ]
    CCDS46396.1. [P18510-1 ]
    PIRi A40956. A30368.
    I37893. A39386.
    RefSeqi NP_000568.1. NM_000577.4. [P18510-2 ]
    NP_776213.1. NM_173841.2. [P18510-3 ]
    NP_776214.1. NM_173842.2. [P18510-1 ]
    NP_776215.1. NM_173843.2. [P18510-4 ]
    XP_005263718.1. XM_005263661.2. [P18510-4 ]
    XP_006712560.1. XM_006712497.1. [P18510-4 ]
    UniGenei Hs.81134.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ILR X-ray 2.10 1/2 26-177 [» ]
    1ILT X-ray 2.00 A/B 26-177 [» ]
    1IRA X-ray 2.70 X 26-177 [» ]
    1IRP NMR - A 26-177 [» ]
    1ITN model - A 31-177 [» ]
    2IRT X-ray 3.20 A/B 26-177 [» ]
    ProteinModelPortali P18510.
    SMRi P18510. Positions 33-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109772. 4 interactions.
    DIPi DIP-3513N.
    IntActi P18510. 1 interaction.
    MINTi MINT-1522172.
    STRINGi 9606.ENSP00000259206.

    Chemistry

    DrugBanki DB00026. Anakinra.

    Polymorphism databases

    DMDMi 124312.

    Proteomic databases

    MaxQBi P18510.
    PaxDbi P18510.
    PRIDEi P18510.

    Protocols and materials databases

    DNASUi 3557.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259206 ; ENSP00000259206 ; ENSG00000136689 . [P18510-3 ]
    ENST00000354115 ; ENSP00000329072 ; ENSG00000136689 . [P18510-2 ]
    ENST00000361779 ; ENSP00000354816 ; ENSG00000136689 . [P18510-4 ]
    ENST00000409052 ; ENSP00000387210 ; ENSG00000136689 . [P18510-4 ]
    ENST00000409930 ; ENSP00000387173 ; ENSG00000136689 . [P18510-1 ]
    GeneIDi 3557.
    KEGGi hsa:3557.
    UCSCi uc002tiy.3. human. [P18510-1 ]
    uc002tiz.3. human. [P18510-3 ]
    uc002tja.3. human. [P18510-2 ]

    Organism-specific databases

    CTDi 3557.
    GeneCardsi GC02P113864.
    HGNCi HGNC:6000. IL1RN.
    HPAi CAB009633.
    HPA001482.
    MIMi 147679. gene.
    612628. phenotype.
    612852. phenotype.
    neXtProti NX_P18510.
    Orphaneti 210115. Sterile multifocal osteomyelitis with periostitis and pustulosis.
    PharmGKBi PA29816.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46710.
    HOGENOMi HOG000231506.
    HOVERGENi HBG052099.
    KOi K05481.
    OMAi QSIYGRR.
    OrthoDBi EOG7X6M1M.
    PhylomeDBi P18510.
    TreeFami TF300203.

    Enzyme and pathway databases

    Reactomei REACT_22442. Interleukin-1 signaling.

    Miscellaneous databases

    ChiTaRSi IL1RN. human.
    EvolutionaryTracei P18510.
    GeneWikii Interleukin_1_receptor_antagonist.
    GenomeRNAii 3557.
    NextBioi 13886.
    PROi P18510.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P18510.
    Bgeei P18510.
    CleanExi HS_IL1RN.
    Genevestigatori P18510.

    Family and domain databases

    InterProi IPR008996. Cytokine_IL1-like.
    IPR020877. IL-1_CS.
    IPR000975. IL-1_fam.
    IPR027166. IL-1RA.
    IPR003297. IL-1RA/IL-36.
    [Graphical view ]
    PANTHERi PTHR10078:SF6. PTHR10078:SF6. 1 hit.
    Pfami PF00340. IL1. 1 hit.
    [Graphical view ]
    PRINTSi PR00264. INTERLEUKIN1.
    PR01360. INTRLEUKIN1X.
    SUPFAMi SSF50353. SSF50353. 1 hit.
    PROSITEi PS00253. INTERLEUKIN_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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.
      , 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-124.

    Entry informationi

    Entry nameiIL1RA_HUMAN
    AccessioniPrimary (citable) accession number: P18510
    Secondary accession number(s): A8K4G1
    , Q14628, Q53SC2, Q7RTZ4, Q96GD6, Q9UPC0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 170 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3