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Protein

Interleukin-1 receptor type 1

Gene

IL1R1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • interleukin-1, Type I, activating receptor activity Source: ProtInc
  • interleukin-1 receptor activity Source: BHF-UCL
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • signal transducer activity Source: ProtInc
  • transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  • cell surface receptor signaling pathway Source: ProtInc
  • immune response Source: ProtInc
  • interleukin-1-mediated signaling pathway Source: BHF-UCL
  • regulation of inflammatory response Source: Ensembl
  • response to interleukin-1 Source: BHF-UCL
Complete GO annotation...

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 Componenti: 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 336319ExtracellularSequence AnalysisAdd
BLAST
Transmembranei337 – 35620HelicalSequence AnalysisAdd
BLAST
Topological domaini357 – 569213CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: Ensembl
  • extracellular region Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: ProtInc
  • membrane Source: BHF-UCL
  • plasma membrane Source: Reactome
Complete GO annotation...

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.

Chemistry

DrugBankiDB00026. Anakinra.

Polymorphism and mutation databases

BioMutaiIL1R1.
DMDMi124308.

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

MaxQBiP14778.
PaxDbiP14778.
PRIDEiP14778.

PTM databases

PhosphoSiteiP14778.

Expressioni

Gene expression databases

BgeeiP14778.
CleanExiHS_IL1R1.
ExpressionAtlasiP14778. baseline and differential.
GenevisibleiP14778. HS.

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 – 274Combined sources
Beta strandi32 – 354Combined sources
Beta strandi40 – 434Combined sources
Helixi48 – 503Combined sources
Beta strandi56 – 594Combined sources
Beta strandi72 – 776Combined sources
Beta strandi80 – 834Combined sources
Helixi88 – 903Combined sources
Beta strandi92 – 976Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi105 – 11410Combined sources
Beta strandi120 – 1223Combined sources
Helixi124 – 1263Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi138 – 1414Combined sources
Helixi146 – 1483Combined sources
Turni151 – 1533Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi171 – 1777Combined sources
Beta strandi180 – 1834Combined sources
Helixi188 – 1903Combined sources
Beta strandi192 – 20211Combined sources
Beta strandi205 – 21814Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi233 – 2375Combined sources
Beta strandi240 – 2423Combined sources
Beta strandi244 – 2529Combined sources
Beta strandi256 – 2627Combined sources
Beta strandi272 – 28110Combined sources
Helixi287 – 2893Combined sources
Beta strandi290 – 30011Combined sources
Helixi303 – 3064Combined sources
Beta strandi310 – 3167Combined sources
Beta strandi319 – 32810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00760000119071.
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

        10         20         30         40         50
MKVLLRLICF IALLISSLEA DKCKEREEKI ILVSSANEID VRPCPLNPNE
60 70 80 90 100
HKGTITWYKD DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN
110 120 130 140 150
SSYCLRIKIS AKFVENEPNL CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN
160 170 180 190 200
ENNELPKLQW YKDCKPLLLD NIHFSGVKDR LIVMNVAEKH RGNYTCHASY
210 220 230 240 250
TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL GSQIQLICNV
260 270 280 290 300
TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE
310 320 330 340 350
IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKHMIG ICVTLTVIIV
360 370 380 390 400
CSVFIYKIFK IDIVLWYRDS CYDFLPIKAS DGKTYDAYIL YPKTVGEGST
410 420 430 440 450
SDCDIFVFKV LPEVLEKQCG YKLFIYGRDD YVGEDIVEVI NENVKKSRRL
460 470 480 490 500
IIILVRETSG FSWLGGSSEE QIAMYNALVQ DGIKVVLLEL EKIQDYEKMP
510 520 530 540 550
ESIKFIKQKH GAIRWSGDFT QGPQSAKTRF WKNVRYHMPV QRRSPSSKHQ
560
LLSPATKEKL QREAHVPLG
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:
EMBLi
GenBanki
DDBJi
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_005263930.3.
XP_005263988.1. XM_005263931.1.
XP_005263989.1. XM_005263932.1.
XP_005263990.1. XM_005263933.3.
XP_005263991.1. XM_005263934.3.
UniGeneiHs.701982.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005263930.3.
XP_005263988.1. XM_005263931.1.
XP_005263989.1. XM_005263932.1.
XP_005263990.1. XM_005263933.3.
XP_005263991.1. XM_005263934.3.
UniGeneiHs.701982.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL1959.
DrugBankiDB00026. Anakinra.

PTM databases

PhosphoSiteiP14778.

Polymorphism and mutation databases

BioMutaiIL1R1.
DMDMi124308.

Proteomic databases

MaxQBiP14778.
PaxDbiP14778.
PRIDEiP14778.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3554.
GeneCardsiGC02P102681.
HGNCiHGNC:5993. IL1R1.
HPAiCAB007779.
MIMi147810. gene.
neXtProtiNX_P14778.
PharmGKBiPA29809.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40914.
GeneTreeiENSGT00760000119071.
HOGENOMiHOG000253916.
HOVERGENiHBG052103.
InParanoidiP14778.
KOiK04386.
OMAiIQDYEKM.
OrthoDBiEOG7H1JK3.
PhylomeDBiP14778.
TreeFamiTF325519.

Enzyme and pathway databases

ReactomeiREACT_22442. Interleukin-1 signaling.
SignaLinkiP14778.

Miscellaneous databases

ChiTaRSiIL1R1. human.
EvolutionaryTraceiP14778.
GeneWikiiInterleukin_1_receptor,_type_I.
GenomeRNAii3554.
NextBioi13876.
PROiP14778.
SOURCEiSearch...

Gene expression databases

BgeeiP14778.
CleanExiHS_IL1R1.
ExpressionAtlasiP14778. baseline and differential.
GenevisibleiP14778. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 187 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.