Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27930

- IL1R2_HUMAN

UniProt

P27930 - IL1R2_HUMAN

Protein

Interleukin-1 receptor type 2

Gene

IL1R2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors.4 Publications

    GO - Molecular functioni

    1. interleukin-1, Type II, blocking receptor activity Source: InterPro
    2. interleukin-1 receptor activity Source: ProtInc
    3. protein binding Source: BHF-UCL

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: GOC
    2. immune response Source: ProtInc

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_22442. Interleukin-1 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interleukin-1 receptor type 2
    Short name:
    IL-1R-2
    Short name:
    IL-1RT-2
    Short name:
    IL-1RT2
    Alternative name(s):
    CD121 antigen-like family member B
    CDw121b
    IL-1 type II receptor
    Interleukin-1 receptor beta
    Short name:
    IL-1R-beta
    Interleukin-1 receptor type II
    CD_antigen: CD121b
    Cleaved into the following 2 chains:
    Interleukin-1 receptor type 2, membrane form
    Short name:
    mIL-1R2
    Short name:
    mIL-1RII
    Interleukin-1 receptor type 2, soluble form
    Short name:
    sIL-1R2
    Short name:
    sIL-1RII
    Gene namesi
    Name:IL1R2
    Synonyms:IL1RB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:5994. IL1R2.

    Subcellular locationi

    Isoform Short : Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29810.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1313Sequence AnalysisAdd
    BLAST
    Chaini14 – 398385Interleukin-1 receptor type 2, membrane formPRO_0000015439Add
    BLAST
    Chaini14 – ?Interleukin-1 receptor type 2, soluble formPRO_0000415348

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 1161 PublicationPROSITE-ProRule annotation
    Disulfide bondi50 ↔ 1081 PublicationPROSITE-ProRule annotation
    Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi112 – 1121N-linked (GlcNAc...)1 Publication
    Disulfide bondi152 ↔ 2071 PublicationPROSITE-ProRule annotation
    Glycosylationi219 – 2191N-linked (GlcNAc...)1 Publication
    Disulfide bondi258 ↔ 3261 PublicationPROSITE-ProRule annotation
    Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    A soluble form (sIL1R2) can also be produced by proteolytic cleavage at the cell surface (shedding) involving a metalloproteinase; hovever, several sIL1R2 forms ranging from 45 and 60 kDa are reported.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP27930.
    PRIDEiP27930.

    PTM databases

    PhosphoSiteiP27930.

    Expressioni

    Gene expression databases

    ArrayExpressiP27930.
    BgeeiP27930.
    CleanExiHS_IL1R2.
    GenevestigatoriP27930.

    Organism-specific databases

    HPAiHPA027597.
    HPA027598.

    Interactioni

    Subunit structurei

    Associates with IL1RAP to form a non-signaling interleukin-1 receptor complex.1 Publication

    Protein-protein interaction databases

    BioGridi113605. 1 interaction.
    IntActiP27930. 4 interactions.
    STRINGi9606.ENSP00000330959.

    Structurei

    Secondary structure

    1
    398
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 335
    Beta strandi38 – 414
    Beta strandi47 – 493
    Beta strandi70 – 734
    Beta strandi82 – 843
    Beta strandi86 – 894
    Beta strandi92 – 987
    Beta strandi104 – 1074
    Beta strandi110 – 1123
    Beta strandi115 – 12612
    Helixi130 – 1323
    Helixi133 – 1364
    Beta strandi138 – 1436
    Beta strandi148 – 1514
    Turni156 – 1583
    Beta strandi161 – 1633
    Beta strandi170 – 1734
    Beta strandi181 – 1855
    Beta strandi189 – 1968
    Helixi199 – 2013
    Beta strandi203 – 2108
    Beta strandi219 – 22911
    Beta strandi260 – 2656
    Beta strandi271 – 2799
    Beta strandi281 – 2855
    Beta strandi287 – 2893
    Beta strandi301 – 3033
    Beta strandi305 – 3084
    Beta strandi325 – 3306
    Beta strandi333 – 3353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O4OX-ray3.30C14-343[»]
    ProteinModelPortaliP27930.
    SMRiP27930. Positions 28-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27930.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini14 – 343330ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini370 – 39829CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei344 – 36926HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 124107Ig-like C2-type 1Add
    BLAST
    Domaini134 – 22390Ig-like C2-type 2Add
    BLAST
    Domaini237 – 349113Ig-like C2-type 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni329 – 34315Contains proteolytic cleavage siteCuratedAdd
    BLAST

    Sequence similaritiesi

    Belongs to the interleukin-1 receptor family.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG44340.
    HOGENOMiHOG000113036.
    HOVERGENiHBG052104.
    InParanoidiP27930.
    KOiK04387.
    OMAiRQEYSEN.
    OrthoDBiEOG77HDDW.
    PhylomeDBiP27930.
    TreeFamiTF325519.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR015621. IL-1_rcpt_fam.
    IPR004074. IL-1_rcpt_I/II-typ.
    IPR004077. IL-1_rcpt_II-typ.
    IPR013151. Immunoglobulin.
    [Graphical view]
    PANTHERiPTHR11890. PTHR11890. 1 hit.
    PfamiPF00047. ig. 1 hit.
    [Graphical view]
    PRINTSiPR01539. INTRLEUKN1R2.
    PR01536. INTRLKN1R12F.
    SMARTiSM00409. IG. 3 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P27930-1) [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

    MLRLYVLVMG VSAFTLQPAA HTGAARSCRF RGRHYKREFR LEGEPVALRC    50
    PQVPYWLWAS VSPRINLTWH KNDSARTVPG EEETRMWAQD GALWLLPALQ 100
    EDSGTYVCTT RNASYCDKMS IELRVFENTD AFLPFISYPQ ILTLSTSGVL 150
    VCPDLSEFTR DKTDVKIQWY KDSLLLDKDN EKFLSVRGTT HLLVHDVALE 200
    DAGYYRCVLT FAHEGQQYNI TRSIELRIKK KKEETIPVII SPLKTISASL 250
    GSRLTIPCKV FLGTGTPLTT MLWWTANDTH IESAYPGGRV TEGPRQEYSE 300
    NNENYIEVPL IFDPVTREDL HMDFKCVVHN TLSFQTLRTT VKEASSTFSW 350
    GIVLAPLSLA FLVLGGIWMH RRCKHRTGKA DGLTVLWPHH QDFQSYPK 398
    Length:398
    Mass (Da):45,421
    Last modified:August 1, 1992 - v1
    Checksum:i2C2A03ADA6F3AC5B
    GO
    Isoform Short (identifier: P27930-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         297-398: Missing.

    Show »
    Length:296
    Mass (Da):33,622
    Checksum:i581AA026BB7DACD5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti123 – 1231L → F in AAD00242. (PubMed:8702856)Curated
    Sequence conflicti171 – 1711K → R in AAD00242. (PubMed:8702856)Curated
    Sequence conflicti199 – 1991L → Q in AAD00242. (PubMed:8702856)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti181 – 1811E → K.1 Publication
    Corresponds to variant rs28385682 [ dbSNP | Ensembl ].
    VAR_019132
    Natural varianti292 – 2921E → K.1 Publication
    Corresponds to variant rs3218976 [ dbSNP | Ensembl ].
    VAR_019133

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei297 – 398102Missing in isoform Short. 1 PublicationVSP_042222Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59770 mRNA. Translation: CAA42441.1.
    U64094 mRNA. Translation: AAB05878.1.
    U74649 mRNA. Translation: AAD00242.1.
    AY124010 Genomic DNA. Translation: AAM64221.1.
    AC007165 Genomic DNA. Translation: AAK52072.1.
    CH471127 Genomic DNA. Translation: EAX01800.1.
    CH471127 Genomic DNA. Translation: EAX01801.1.
    CH471127 Genomic DNA. Translation: EAX01802.1.
    CH471127 Genomic DNA. Translation: EAX01803.1.
    BC039031 mRNA. Translation: AAH39031.1.
    CCDSiCCDS2054.1. [P27930-1]
    CCDS58719.1. [P27930-2]
    PIRiS17428.
    RefSeqiNP_001248348.1. NM_001261419.1. [P27930-2]
    NP_004624.1. NM_004633.3. [P27930-1]
    XP_006712797.1. XM_006712734.1. [P27930-1]
    UniGeneiHs.25333.

    Genome annotation databases

    EnsembliENST00000332549; ENSP00000330959; ENSG00000115590. [P27930-1]
    ENST00000393414; ENSP00000377066; ENSG00000115590. [P27930-1]
    ENST00000441002; ENSP00000414611; ENSG00000115590. [P27930-2]
    GeneIDi7850.
    KEGGihsa:7850.
    UCSCiuc002tbm.3. human. [P27930-1]

    Polymorphism databases

    DMDMi124310.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59770 mRNA. Translation: CAA42441.1 .
    U64094 mRNA. Translation: AAB05878.1 .
    U74649 mRNA. Translation: AAD00242.1 .
    AY124010 Genomic DNA. Translation: AAM64221.1 .
    AC007165 Genomic DNA. Translation: AAK52072.1 .
    CH471127 Genomic DNA. Translation: EAX01800.1 .
    CH471127 Genomic DNA. Translation: EAX01801.1 .
    CH471127 Genomic DNA. Translation: EAX01802.1 .
    CH471127 Genomic DNA. Translation: EAX01803.1 .
    BC039031 mRNA. Translation: AAH39031.1 .
    CCDSi CCDS2054.1. [P27930-1 ]
    CCDS58719.1. [P27930-2 ]
    PIRi S17428.
    RefSeqi NP_001248348.1. NM_001261419.1. [P27930-2 ]
    NP_004624.1. NM_004633.3. [P27930-1 ]
    XP_006712797.1. XM_006712734.1. [P27930-1 ]
    UniGenei Hs.25333.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3O4O X-ray 3.30 C 14-343 [» ]
    ProteinModelPortali P27930.
    SMRi P27930. Positions 28-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113605. 1 interaction.
    IntActi P27930. 4 interactions.
    STRINGi 9606.ENSP00000330959.

    Chemistry

    DrugBanki DB00026. Anakinra.

    PTM databases

    PhosphoSitei P27930.

    Polymorphism databases

    DMDMi 124310.

    Proteomic databases

    PaxDbi P27930.
    PRIDEi P27930.

    Protocols and materials databases

    DNASUi 7850.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332549 ; ENSP00000330959 ; ENSG00000115590 . [P27930-1 ]
    ENST00000393414 ; ENSP00000377066 ; ENSG00000115590 . [P27930-1 ]
    ENST00000441002 ; ENSP00000414611 ; ENSG00000115590 . [P27930-2 ]
    GeneIDi 7850.
    KEGGi hsa:7850.
    UCSCi uc002tbm.3. human. [P27930-1 ]

    Organism-specific databases

    CTDi 7850.
    GeneCardsi GC02P102608.
    HGNCi HGNC:5994. IL1R2.
    HPAi HPA027597.
    HPA027598.
    MIMi 147811. gene.
    neXtProti NX_P27930.
    PharmGKBi PA29810.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44340.
    HOGENOMi HOG000113036.
    HOVERGENi HBG052104.
    InParanoidi P27930.
    KOi K04387.
    OMAi RQEYSEN.
    OrthoDBi EOG77HDDW.
    PhylomeDBi P27930.
    TreeFami TF325519.

    Enzyme and pathway databases

    Reactomei REACT_22442. Interleukin-1 signaling.

    Miscellaneous databases

    EvolutionaryTracei P27930.
    GeneWikii Interleukin_1_receptor,_type_II.
    GenomeRNAii 7850.
    NextBioi 30276.
    PROi P27930.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27930.
    Bgeei P27930.
    CleanExi HS_IL1R2.
    Genevestigatori P27930.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR015621. IL-1_rcpt_fam.
    IPR004074. IL-1_rcpt_I/II-typ.
    IPR004077. IL-1_rcpt_II-typ.
    IPR013151. Immunoglobulin.
    [Graphical view ]
    PANTHERi PTHR11890. PTHR11890. 1 hit.
    Pfami PF00047. ig. 1 hit.
    [Graphical view ]
    PRINTSi PR01539. INTRLEUKN1R2.
    PR01536. INTRLKN1R12F.
    SMARTi SM00409. IG. 3 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types."
      McMahan C.J., Slack J.L., Mosley B., Cosman D., Lupton S.D., Brunton L.L., Grubin C.E., Wignall J.M., Jenkins N.A., Brannan C.I., Copeland N.G., Huebner K., Croce C.M., Cannizzarro L.A., Benjamin D., Dower S.K., Spriggs M.K., Sims J.E.
      EMBO J. 10:2821-2832(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: B-cell.
    2. "Cloning and characterization of an alternatively processed human type II interleukin-1 receptor mRNA."
      Liu C., Hart R.P., Liu X.J., Clevenger W., Maki R.A., Souza E.B.
      J. Biol. Chem. 271:20965-20972(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), IL1B-BINDING, SUBCELLULAR LOCATION (ISOFORM SHORT).
    3. "Complete nucleotide sequence and expression of the human interleukin-1 receptor type II in human gingival fibroblasts."
      Chou H.-H., Takashiba T., Takigawa M., Maeda H., Asahara Y., Nishimura F., Arai H., Murayama Y.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    4. SeattleSNPs variation discovery resource
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-181 AND LYS-292.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 LONG).
      Tissue: Ovary.
    8. "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: FUNCTION, PROTEOLYTIC PROCESSING, LIGAND-BINDING.
    9. "Soluble type II interleukin 1 (IL-1) receptor binds and blocks processing of IL-1 beta precursor and loses affinity for IL-1 receptor antagonist."
      Symons J.A., Young P.R., Duff G.W.
      Proc. Natl. Acad. Sci. U.S.A. 92:1714-1718(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIGAND-BINDING.
    10. "Role of metalloproteases in the release of the IL-1 type II decoy receptor."
      Orlando S., Sironi M., Bianchi G., Drummond A.H., Boraschi D., Yabes D., Mantovani A.
      J. Biol. Chem. 272:31764-31769(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    11. "The type II IL-1 receptor interacts with the IL-1 receptor accessory protein: a novel mechanism of regulation of IL-1 responsiveness."
      Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D., Martin M.U.
      J. Immunol. 161:6871-6877(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IL1RAP.
    12. "The membrane form of the type II IL-1 receptor accounts for inhibitory function."
      Neumann D., Kollewe C., Martin M.U., Boraschi D.
      J. Immunol. 165:3350-3357(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS DECOY RECEPTOR.
    13. "The soluble form of IL-1 receptor accessory protein enhances the ability of soluble type II IL-1 receptor to inhibit IL-1 action."
      Smith D.E., Hanna R., Friend D., Moore H., Chen H., Farese A.M., MacVittie T.J., Virca G.D., Sims J.E.
      Immunity 18:87-96(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS DECOY RECEPTOR.
    14. "Structural insights into the assembly and activation of IL-1beta with its receptors."
      Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.
      Nat. Immunol. 11:905-911(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 14-343 IN COMPLEX WITH IL1RAP AND IL1B, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-112 AND ASN-219.

    Entry informationi

    Entry nameiIL1R2_HUMAN
    AccessioniPrimary (citable) accession number: P27930
    Secondary accession number(s): D3DVJ5, Q6LCE6, Q9UE68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 144 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, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3