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P14778

- IL1R1_HUMAN

UniProt

P14778 - IL1R1_HUMAN

Protein

Interleukin-1 receptor type 1

Gene

IL1R1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 181 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the corecptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex.1 Publication

    GO - Molecular functioni

    1. interleukin-1, Type I, activating receptor activity Source: ProtInc
    2. interleukin-1 receptor activity Source: BHF-UCL
    3. platelet-derived growth factor receptor binding Source: BHF-UCL
    4. protein binding Source: IntAct
    5. signal transducer activity Source: ProtInc
    6. transmembrane signaling receptor activity Source: ProtInc

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. immune response Source: ProtInc
    3. interleukin-1-mediated signaling pathway Source: BHF-UCL
    4. regulation of inflammatory response Source: Ensembl
    5. response to interleukin-1 Source: BHF-UCL

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_22442. Interleukin-1 signaling.
    SignaLinkiP14778.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interleukin-1 receptor type 1
    Short name:
    IL-1R-1
    Short name:
    IL-1RT-1
    Short name:
    IL-1RT1
    Alternative name(s):
    CD121 antigen-like family member A
    Interleukin-1 receptor alpha
    Short name:
    IL-1R-alpha
    Interleukin-1 receptor type I
    p80
    CD_antigen: CD121a
    Cleaved into the following 2 chains:
    Interleukin-1 receptor type 1, membrane form
    Short name:
    mIL-1R1
    Short name:
    mIL-1RI
    Interleukin-1 receptor type 1, soluble form
    Short name:
    sIL-1R1
    Short name:
    sIL-1RI
    Gene namesi
    Name:IL1R1
    Synonyms:IL1R, IL1RA, IL1RT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:5993. IL1R1.

    Subcellular locationi

    Membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cell membrane 1 Publication. Secreted 1 Publication

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. extracellular region Source: UniProtKB-SubCell
    3. integral component of plasma membrane Source: ProtInc
    4. membrane Source: BHF-UCL
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi369 – 3691D → A: Reduces NF-kappa-B activation. 1 Publication
    Mutagenesisi428 – 4281R → A: Reduces NF-kappa-B activation and receptor-associated kinase activation. 1 Publication

    Organism-specific databases

    PharmGKBiPA29809.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Add
    BLAST
    Chaini18 – 569552Interleukin-1 receptor type 1, membrane formPRO_0000015435Add
    BLAST
    Chaini18 – ?Interleukin-1 receptor type 1, soluble formPRO_0000415344

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 104
    Disulfide bondi44 ↔ 96
    Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi121 ↔ 164
    Disulfide bondi142 ↔ 196
    Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi248 ↔ 312
    Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
    Modified residuei496 – 4961Phosphotyrosine1 Publication

    Post-translational modificationi

    A soluble form (sIL1R1) is probably produced by proteolytic cleavage at the cell surface (shedding).1 Publication
    Rapidly phosphorylated on Tyr-496 in response to IL-1, which creates a SH2 binding site for the PI 3-kinase regulatory subunit PIK3R1.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP14778.
    PRIDEiP14778.

    PTM databases

    PhosphoSiteiP14778.

    Expressioni

    Gene expression databases

    ArrayExpressiP14778.
    BgeeiP14778.
    CleanExiHS_IL1R1.
    GenevestigatoriP14778.

    Organism-specific databases

    HPAiCAB007779.

    Interactioni

    Subunit structurei

    The interleukin-1 receptor complex is a heterodimer of IL1R1 and IL1RAP. Interacts with PIK3R1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TRAF6Q9Y4K32EBI-525905,EBI-359276

    Protein-protein interaction databases

    BioGridi109770. 18 interactions.
    DIPiDIP-93N.
    IntActiP14778. 6 interactions.
    MINTiMINT-262640.
    STRINGi9606.ENSP00000233946.

    Structurei

    Secondary structure

    1
    569
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 274
    Beta strandi32 – 354
    Beta strandi40 – 434
    Helixi48 – 503
    Beta strandi56 – 594
    Beta strandi72 – 776
    Beta strandi80 – 834
    Helixi88 – 903
    Beta strandi92 – 976
    Beta strandi100 – 1023
    Beta strandi105 – 11410
    Beta strandi120 – 1223
    Helixi124 – 1263
    Beta strandi127 – 1337
    Beta strandi135 – 1373
    Beta strandi138 – 1414
    Helixi146 – 1483
    Turni151 – 1533
    Beta strandi159 – 1624
    Beta strandi171 – 1777
    Beta strandi180 – 1834
    Helixi188 – 1903
    Beta strandi192 – 20211
    Beta strandi205 – 21814
    Beta strandi227 – 2304
    Beta strandi233 – 2375
    Beta strandi240 – 2423
    Beta strandi244 – 2529
    Beta strandi256 – 2627
    Beta strandi272 – 28110
    Helixi287 – 2893
    Beta strandi290 – 30011
    Helixi303 – 3064
    Beta strandi310 – 3167
    Beta strandi319 – 32810

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G0YX-ray3.00R21-332[»]
    1IRAX-ray2.70Y18-336[»]
    1ITBX-ray2.50B18-332[»]
    4DEPX-ray3.10B/E18-336[»]
    4GAFX-ray2.15B18-336[»]
    ProteinModelPortaliP14778.
    SMRiP14778. Positions 23-332, 383-539.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14778.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 336319ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini357 – 569213CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei337 – 35620HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 11088Ig-like C2-type 1Add
    BLAST
    Domaini118 – 21093Ig-like C2-type 2Add
    BLAST
    Domaini226 – 328103Ig-like C2-type 3Add
    BLAST
    Domaini383 – 541159TIRPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the interleukin-1 receptor family.Curated
    Contains 1 TIR domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG40914.
    HOGENOMiHOG000253916.
    HOVERGENiHBG052103.
    InParanoidiP14778.
    KOiK04386.
    OMAiIQDYEKM.
    OrthoDBiEOG7H1JK3.
    PhylomeDBiP14778.
    TreeFamiTF325519.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    3.40.50.10140. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR015621. IL-1_rcpt_fam.
    IPR004076. IL-1_rcpt_I-typ.
    IPR004074. IL-1_rcpt_I/II-typ.
    IPR000157. TIR_dom.
    [Graphical view]
    PANTHERiPTHR11890. PTHR11890. 1 hit.
    PfamiPF07679. I-set. 1 hit.
    PF01582. TIR. 1 hit.
    [Graphical view]
    PRINTSiPR01538. INTRLEUKN1R1.
    PR01536. INTRLKN1R12F.
    SMARTiSM00409. IG. 2 hits.
    SM00255. TIR. 1 hit.
    [Graphical view]
    SUPFAMiSSF52200. SSF52200. 1 hit.
    PROSITEiPS50835. IG_LIKE. 3 hits.
    PS50104. TIR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14778-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVLLRLICF IALLISSLEA DKCKEREEKI ILVSSANEID VRPCPLNPNE    50
    HKGTITWYKD DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN 100
    SSYCLRIKIS AKFVENEPNL CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN 150
    ENNELPKLQW YKDCKPLLLD NIHFSGVKDR LIVMNVAEKH RGNYTCHASY 200
    TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL GSQIQLICNV 250
    TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE 300
    IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKHMIG ICVTLTVIIV 350
    CSVFIYKIFK IDIVLWYRDS CYDFLPIKAS DGKTYDAYIL YPKTVGEGST 400
    SDCDIFVFKV LPEVLEKQCG YKLFIYGRDD YVGEDIVEVI NENVKKSRRL 450
    IIILVRETSG FSWLGGSSEE QIAMYNALVQ DGIKVVLLEL EKIQDYEKMP 500
    ESIKFIKQKH GAIRWSGDFT QGPQSAKTRF WKNVRYHMPV QRRSPSSKHQ 550
    LLSPATKEKL QREAHVPLG 569
    Length:569
    Mass (Da):65,402
    Last modified:April 1, 1990 - v1
    Checksum:i5BAA83F8F0225C25
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti124 – 1241A → G.1 Publication
    Corresponds to variant rs2228139 [ dbSNP | Ensembl ].
    VAR_019131
    Natural varianti344 – 3441T → M.
    Corresponds to variant rs28362304 [ dbSNP | Ensembl ].
    VAR_029189

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16896 mRNA. Translation: CAA34773.1.
    M27492 mRNA. Translation: AAA59137.1.
    AF531102 Genomic DNA. Translation: AAM88423.1.
    AC007271 Genomic DNA. Translation: AAX81988.1.
    CH471127 Genomic DNA. Translation: EAX01799.1.
    BC067506 mRNA. Translation: AAH67506.1.
    BC075062 mRNA. Translation: AAH75062.1.
    BC075063 mRNA. Translation: AAH75063.1.
    CCDSiCCDS2055.1.
    PIRiA36187.
    RefSeqiNP_000868.1. NM_000877.3.
    NP_001275635.1. NM_001288706.1.
    XP_005263986.1. XM_005263929.1.
    XP_005263987.1. XM_005263930.2.
    XP_005263988.1. XM_005263931.1.
    XP_005263989.1. XM_005263932.1.
    XP_005263990.1. XM_005263933.2.
    XP_005263991.1. XM_005263934.2.
    UniGeneiHs.701982.

    Genome annotation databases

    EnsembliENST00000410023; ENSP00000386380; ENSG00000115594.
    GeneIDi3554.
    KEGGihsa:3554.
    UCSCiuc002tbq.3. human.

    Polymorphism databases

    DMDMi124308.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16896 mRNA. Translation: CAA34773.1 .
    M27492 mRNA. Translation: AAA59137.1 .
    AF531102 Genomic DNA. Translation: AAM88423.1 .
    AC007271 Genomic DNA. Translation: AAX81988.1 .
    CH471127 Genomic DNA. Translation: EAX01799.1 .
    BC067506 mRNA. Translation: AAH67506.1 .
    BC075062 mRNA. Translation: AAH75062.1 .
    BC075063 mRNA. Translation: AAH75063.1 .
    CCDSi CCDS2055.1.
    PIRi A36187.
    RefSeqi NP_000868.1. NM_000877.3.
    NP_001275635.1. NM_001288706.1.
    XP_005263986.1. XM_005263929.1.
    XP_005263987.1. XM_005263930.2.
    XP_005263988.1. XM_005263931.1.
    XP_005263989.1. XM_005263932.1.
    XP_005263990.1. XM_005263933.2.
    XP_005263991.1. XM_005263934.2.
    UniGenei Hs.701982.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G0Y X-ray 3.00 R 21-332 [» ]
    1IRA X-ray 2.70 Y 18-336 [» ]
    1ITB X-ray 2.50 B 18-332 [» ]
    4DEP X-ray 3.10 B/E 18-336 [» ]
    4GAF X-ray 2.15 B 18-336 [» ]
    ProteinModelPortali P14778.
    SMRi P14778. Positions 23-332, 383-539.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109770. 18 interactions.
    DIPi DIP-93N.
    IntActi P14778. 6 interactions.
    MINTi MINT-262640.
    STRINGi 9606.ENSP00000233946.

    Chemistry

    ChEMBLi CHEMBL1959.
    DrugBanki DB00026. Anakinra.

    PTM databases

    PhosphoSitei P14778.

    Polymorphism databases

    DMDMi 124308.

    Proteomic databases

    PaxDbi P14778.
    PRIDEi P14778.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000410023 ; ENSP00000386380 ; ENSG00000115594 .
    GeneIDi 3554.
    KEGGi hsa:3554.
    UCSCi uc002tbq.3. human.

    Organism-specific databases

    CTDi 3554.
    GeneCardsi GC02P102681.
    HGNCi HGNC:5993. IL1R1.
    HPAi CAB007779.
    MIMi 147810. gene.
    neXtProti NX_P14778.
    PharmGKBi PA29809.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40914.
    HOGENOMi HOG000253916.
    HOVERGENi HBG052103.
    InParanoidi P14778.
    KOi K04386.
    OMAi IQDYEKM.
    OrthoDBi EOG7H1JK3.
    PhylomeDBi P14778.
    TreeFami TF325519.

    Enzyme and pathway databases

    Reactomei REACT_22442. Interleukin-1 signaling.
    SignaLinki P14778.

    Miscellaneous databases

    ChiTaRSi IL1R1. human.
    EvolutionaryTracei P14778.
    GeneWikii Interleukin_1_receptor,_type_I.
    GenomeRNAii 3554.
    NextBioi 13876.
    PROi P14778.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14778.
    Bgeei P14778.
    CleanExi HS_IL1R1.
    Genevestigatori P14778.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    3.40.50.10140. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR015621. IL-1_rcpt_fam.
    IPR004076. IL-1_rcpt_I-typ.
    IPR004074. IL-1_rcpt_I/II-typ.
    IPR000157. TIR_dom.
    [Graphical view ]
    PANTHERi PTHR11890. PTHR11890. 1 hit.
    Pfami PF07679. I-set. 1 hit.
    PF01582. TIR. 1 hit.
    [Graphical view ]
    PRINTSi PR01538. INTRLEUKN1R1.
    PR01536. INTRLKN1R12F.
    SMARTi SM00409. IG. 2 hits.
    SM00255. TIR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52200. SSF52200. 1 hit.
    PROSITEi PS50835. IG_LIKE. 3 hits.
    PS50104. TIR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the cDNA for the human fibroblast type interleukin-1 receptor."
      Chua A.O., Gubler U.
      Nucleic Acids Res. 17:10114-10114(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: T-cell.
    3. SeattleSNPs variation discovery resource
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-124.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Brain.
    7. "Specific binding of interleukin 1 (IL-1) beta and IL-1 receptor antagonist (IL-1ra) to human serum. High-affinity binding of IL-1ra to soluble IL-1 receptor type I."
      Svenson M., Hansen M.B., Heegaard P., Abell K., Bendtzen K.
      Cytokine 5:427-435(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
    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: LIGAND-BINDING.
    9. "Recruitment of IRAK to the interleukin 1 receptor complex requires interleukin 1 receptor accessory protein."
      Huang J., Gao X., Li S., Cao Z.
      Proc. Natl. Acad. Sci. U.S.A. 94:12829-12832(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IL1RAP AND IRAK1.
      Tissue: Placenta.
    10. "Phosphatidylinositol 3-kinase is recruited to a specific site in the activated IL-1 receptor I."
      Marmiroli S., Bavelloni A., Faenza I., Sirri A., Ognibene A., Cenni V., Tsukada J., Koyama Y., Ruzzene M., Ferri A., Auron P.E., Toker A., Maraldi N.M.
      FEBS Lett. 438:49-54(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-496, INTERACTION WITH PIK3R1.
    11. "Identification of two major sites in the type I interleukin-1 receptor cytoplasmic region responsible for coupling to pro-inflammatory signaling pathways."
      Slack J.L., Schooley K., Bonnert T.P., Mitcham J.L., Qwarnstrom E.E., Sims J.E., Dower S.K.
      J. Biol. Chem. 275:4670-4678(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-369 AND ARG-428.
    12. "Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta."
      Vigers G.P.A., Anderson L.J., Caffes P., Brandhuber B.J.
      Nature 386:190-194(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-332 IN COMPLEX WITH IL1B.
    13. "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 21-331 IN COMPLEX WITH IL1RA.
    14. "X-ray crystal structure of a small antagonist peptide bound to interleukin-1 receptor type 1."
      Vigers G.P.A., Dripps D.J., Edwards C.K. III, Brandhuber B.J.
      J. Biol. Chem. 275:36927-36933(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 4-315 IN COMPLEX WITH THE ANTAGONIST PEPTIDE AF10847.

    Entry informationi

    Entry nameiIL1R1_HUMAN
    AccessioniPrimary (citable) accession number: P14778
    Secondary accession number(s): Q587I7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 181 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