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P18510

- IL1RA_HUMAN

UniProt

P18510 - IL1RA_HUMAN

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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

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
Complete GO annotation...

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-KW
  2. extracellular space Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. intracellular Source: UniProtKB
  5. plasma membrane Source: Reactome
Complete GO annotation...

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

BgeeiP18510.
CleanExiHS_IL1RN.
ExpressionAtlasiP18510. baseline and differential.
GenevestigatoriP18510.

Organism-specific databases

HPAiCAB009633.
HPA001482.

Interactioni

Protein-protein interaction databases

BioGridi109772. 5 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 – 427Combined sources
Turni43 – 453Combined sources
Beta strandi47 – 515Combined sources
Beta strandi54 – 585Combined sources
Helixi62 – 676Combined sources
Beta strandi71 – 766Combined sources
Turni77 – 793Combined sources
Beta strandi80 – 856Combined sources
Turni86 – 894Combined sources
Beta strandi90 – 978Combined sources
Beta strandi100 – 1067Combined sources
Helixi110 – 1123Combined sources
Helixi118 – 1236Combined sources
Beta strandi124 – 1307Combined sources
Beta strandi133 – 1419Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi157 – 1604Combined sources
Beta strandi162 – 1687Combined sources
Beta strandi171 – 1755Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000062899.
HOGENOMiHOG000231506.
HOVERGENiHBG052099.
InParanoidiP18510.
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

        10         20         30         40         50
MEICRGLRSH LITLLLFLFH SETICRPSGR KSSKMQAFRI WDVNQKTFYL
60 70 80 90 100
RNNQLVAGYL QGPNVNLEEK IDVVPIEPHA LFLGIHGGKM CLSCVKSGDE
110 120 130 140 150
TRLQLEAVNI TDLSENRKQD KRFAFIRSDS GPTTSFESAA CPGWFLCTAM
160 170
EADQPVSLTN MPDEGVMVTK FYFQEDE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 5 interactions.
DIPi DIP-3513N.
IntActi P18510. 1 interaction.
MINTi MINT-1522172.
STRINGi 9606.ENSP00000259206.

Chemistry

DrugBanki DB06372. Rilonacept.

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.
GeneTreei ENSGT00530000062899.
HOGENOMi HOG000231506.
HOVERGENi HBG052099.
InParanoidi P18510.
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

Bgeei P18510.
CleanExi HS_IL1RN.
ExpressionAtlasi P18510. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 172 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