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Reviewed, UniProtKB/Swiss-Prot P14778 (IL1R1_HUMAN)

Last modified February 9, 2010. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Interleukin-1 receptor type 1
      Short name=IL-1RT-1
      Short name=IL-1RT1
      Short name=IL-1R-1
Alternative name(s):
    Interleukin-1 receptor type I
    Interleukin-1 receptor alpha
      Short name=IL-1R-alpha
    p80
    CD121 antigen-like family member A
    CD_antigen=CD121a
Gene names
Name: IL1R1
Synonyms: IL1R, IL1RA, IL1RT1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Receptor for interleukin-1 alpha (IL-1A), beta (IL-1B), and interleukin-1 receptor antagonist protein (IL-1RA). Binding to the agonist leads to the activation of NF-kappa-B. Signaling involves formation of a ternary complex containing IL1RAP, TOLLIP, MYD88, and IRAK1 or IRAK2.

Subunit structure

Binds IL1RAP.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the interleukin-1 receptor family.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 TIR domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717
Chain18 – 569552Interleukin-1 receptor type 1
PRO_0000015435

Regions

Topological domain18 – 336319Extracellular Potential
Transmembrane337 – 35620 Potential
Topological domain357 – 569213Cytoplasmic Potential
Domain23 – 11088Ig-like C2-type 1
Domain118 – 21093Ig-like C2-type 2
Domain226 – 328103Ig-like C2-type 3
Domain383 – 541159TIR

Amino acid modifications

Modified residue5561Phosphothreonine Ref.6
Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation2631N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Disulfide bond23 ↔ 104
Disulfide bond44 ↔ 96
Disulfide bond121 ↔ 164
Disulfide bond142 ↔ 196
Disulfide bond248 ↔ 312

Natural variations

Natural variant1241A → G: dbSNP rs2228139. Ref.3
VAR_019131
Natural variant3441T → M: dbSNP rs28362304.
VAR_029189

Secondary structure

........................................................... 569
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14778-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 5BAA83F8F0225C25

FASTA56965,402
        10         20         30         40         50         60 
MKVLLRLICF IALLISSLEA DKCKEREEKI ILVSSANEID VRPCPLNPNE HKGTITWYKD 

        70         80         90        100        110        120 
DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN SSYCLRIKIS AKFVENEPNL 

       130        140        150        160        170        180 
CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN ENNELPKLQW YKDCKPLLLD NIHFSGVKDR 

       190        200        210        220        230        240 
LIVMNVAEKH RGNYTCHASY TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL 

       250        260        270        280        290        300 
GSQIQLICNV TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE 

       310        320        330        340        350        360 
IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKHMIG ICVTLTVIIV CSVFIYKIFK 

       370        380        390        400        410        420 
IDIVLWYRDS CYDFLPIKAS DGKTYDAYIL YPKTVGEGST SDCDIFVFKV LPEVLEKQCG 

       430        440        450        460        470        480 
YKLFIYGRDD YVGEDIVEVI NENVKKSRRL IIILVRETSG FSWLGGSSEE QIAMYNALVQ 

       490        500        510        520        530        540 
DGIKVVLLEL EKIQDYEKMP ESIKFIKQKH GAIRWSGDFT QGPQSAKTRF WKNVRYHMPV 

       550        560 
QRRSPSSKHQ LLSPATKEKL QREAHVPLG 

« Hide

References

« Hide 'large scale' references
[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: 2532321] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Cloning the interleukin 1 receptor from human T cells."
Sims J.E., Acres R.B., Grubin C.E., McMahan C.J., Wignall J.M., March C.J., Dower S.K.
Proc. Natl. Acad. Sci. U.S.A. 86:8946-8950(1989) [PubMed: 2530587] [Abstract]
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]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"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: 9371760] [Abstract]
Cited for: INTERACTION WITH IL1RAP AND IRAK1.
Tissue: Placenta.
[6]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-556, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"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: 9062193] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-332 IN COMPLEX WITH IL1B.
[8]"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: 9062194] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-331 IN COMPLEX WITH IL1RA.
[9]"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: 10903327] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 4-315 IN COMPLEX WITH THE ANTAGONIST PEPTIDE AF10847.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16896 mRNA. Translation: CAA34773.1.
M27492 mRNA. Translation: AAA59137.1.
AF531102 Genomic DNA. Translation: AAM88423.1.
BC067506 mRNA. Translation: AAH67506.1.
BC075062 mRNA. Translation: AAH75062.1.
BC075063 mRNA. Translation: AAH75063.1.
IPIIPI00027508.
PIRA36187.
RefSeqNP_000868.1.
UniGeneHs.701982

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G0YX-ray3.00R21-332[»]
1IRAX-ray2.70Y18-336[»]
1ITBX-ray2.50B18-332[»]
SMRP14778. Positions 42-370, 151-401, 383-540.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-93N.
IntActP14778. 5 interactions.
STRINGP14778.

PTM databases

PhosphoSiteP14778.

Proteomic databases

PRIDEP14778.

Genome annotation databases

EnsemblENST00000233946; ENSP00000233946; ENSG00000115594; Homo sapiens. [Genome view]
ENST00000410023; ENSP00000386380; ENSG00000115594; Homo sapiens. [Genome view]
GeneID3554.
KEGGhsa:3554.
UCSCuc002tbq.1. human.

Organism-specific databases

CTD3554.
GeneCardsGC02P102053.
H-InvDBHIX0002331.
HGNCHGNC:5993. IL1R1.
HPACAB007779.
MIM147810. gene.
PharmGKBPA29809.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG19194.
HOGENOMHBG282747.
HOVERGENP14778.
InParanoidP14778.
OMASEEQIAM.
OrthoDBEOG92RGSG.
PhylomeDBP14778.

Enzyme and pathway databases

Pathway_Interaction_DBil1pathway. IL1-mediated signaling events.
il12_2pathway. IL12-mediated signaling events.

Gene expression databases

ArrayExpressP14778.
BgeeP14778.
CleanExHS_IL1R1.
GenevestigatorP14778.
GermOnlineENSG00000115594. Homo sapiens.

Family and domain databases

InterProIPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR015621. IL1-receptor.
IPR004075. IL1_rcpt_1.
IPR004074. IL1_rcpt_I/II.
IPR004076. IL1R_rcpt.
IPR000157. Toll-Interleukin_rcpt.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 3 hits.
PANTHERPTHR11890. IL1-receptor. 1 hit.
PfamPF01582. TIR. 1 hit.
[Graphical view]
PRINTSPR01538. INTRLEUKN1R1.
PR01536. INTRLKN1R12F.
PR01537. INTRLKN1R1F.
SMARTSM00409. IG. 2 hits.
SM00255. TIR. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00026. Anakinra.
NextBio13876.
SOURCESearch...

Entry information

Entry nameIL1R1_HUMAN
AccessionPrimary (citable) accession number: P14778
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: February 9, 2010
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents