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P27930

- IL1R2_HUMAN

UniProt

P27930 - IL1R2_HUMAN

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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

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

GO - Biological processi

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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini14 – 343330ExtracellularSequence AnalysisAdd
BLAST
Transmembranei344 – 36926HelicalSequence AnalysisAdd
BLAST
Topological domaini370 – 39829CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

BgeeiP27930.
CleanExiHS_IL1R2.
ExpressionAtlasiP27930. baseline and differential.
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 – 335Combined sources
Beta strandi38 – 414Combined sources
Beta strandi47 – 493Combined sources
Beta strandi70 – 734Combined sources
Beta strandi82 – 843Combined sources
Beta strandi86 – 894Combined sources
Beta strandi92 – 987Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi115 – 12612Combined sources
Helixi130 – 1323Combined sources
Helixi133 – 1364Combined sources
Beta strandi138 – 1436Combined sources
Beta strandi148 – 1514Combined sources
Turni156 – 1583Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi181 – 1855Combined sources
Beta strandi189 – 1968Combined sources
Helixi199 – 2013Combined sources
Beta strandi203 – 2108Combined sources
Beta strandi219 – 22911Combined sources
Beta strandi260 – 2656Combined sources
Beta strandi271 – 2799Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi301 – 3033Combined sources
Beta strandi305 – 3084Combined sources
Beta strandi325 – 3306Combined sources
Beta strandi333 – 3353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O4OX-ray3.30C14-343[»]
ProteinModelPortaliP27930.
SMRiP27930. Positions 28-377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27930.

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.
GeneTreeiENSGT00760000119071.
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

        10         20         30         40         50
MLRLYVLVMG VSAFTLQPAA HTGAARSCRF RGRHYKREFR LEGEPVALRC
60 70 80 90 100
PQVPYWLWAS VSPRINLTWH KNDSARTVPG EEETRMWAQD GALWLLPALQ
110 120 130 140 150
EDSGTYVCTT RNASYCDKMS IELRVFENTD AFLPFISYPQ ILTLSTSGVL
160 170 180 190 200
VCPDLSEFTR DKTDVKIQWY KDSLLLDKDN EKFLSVRGTT HLLVHDVALE
210 220 230 240 250
DAGYYRCVLT FAHEGQQYNI TRSIELRIKK KKEETIPVII SPLKTISASL
260 270 280 290 300
GSRLTIPCKV FLGTGTPLTT MLWWTANDTH IESAYPGGRV TEGPRQEYSE
310 320 330 340 350
NNENYIEVPL IFDPVTREDL HMDFKCVVHN TLSFQTLRTT VKEASSTFSW
360 370 380 390
GIVLAPLSLA FLVLGGIWMH RRCKHRTGKA DGLTVLWPHH QDFQSYPK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3O4O X-ray 3.30 C 14-343 [» ]
ProteinModelPortali P27930.
SMRi P27930. Positions 28-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

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

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.
GeneTreei ENSGT00760000119071.
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

Bgeei P27930.
CleanExi HS_IL1R2.
ExpressionAtlasi P27930. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 146 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