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Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (Interleukin-33 receptot beta chain)

 IL1AP_MOUSE             Reviewed;         570 AA.
Q61730; Q3UVZ1; Q8VCB9;
22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-APR-2020, entry version 181.
RecName: Full=Interleukin-1 receptor accessory protein;
Short=IL-1 receptor accessory protein;
Short=IL-1RAcP;
EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
AltName: Full=Interleukin-33 receptot beta chain {ECO:0000303|PubMed:18003919};
Flags: Precursor;
Name=Il1rap;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH IL1R1,
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Fibroblast;
PubMed=7775431; DOI=10.1074/jbc.270.23.13757;
Greenfeder S.A., Nunes P., Kwee L., Labow M., Chizzonite R.A., Ju G.;
"Molecular cloning and characterization of a second subunit of the
interleukin 1 receptor complex.";
J. Biol. Chem. 270:13757-13765(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Brain, Diencephalon, and Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH IL1R2.
PubMed=9862719;
Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D.,
Martin M.U.;
"The type II IL-1 receptor interacts with the IL-1 receptor accessory
protein: a novel mechanism of regulation of IL-1 responsiveness.";
J. Immunol. 161:6871-6877(1998).
[6]
INTERACTION WITH TOLLIP.
PubMed=10854325; DOI=10.1038/35014038;
Burns K., Clatworthy J., Martin L., Martinon F., Plumpton C., Maschera B.,
Lewis A., Ray K., Tschopp J., Volpe F.;
"Tollip, a new component of the IL-1R1 pathway, links IRAK to the IL-1
receptor.";
Nat. Cell Biol. 2:346-351(2000).
[7]
MUTAGENESIS OF 527-LYS--PRO-534, INTERACTION WITH MYD88, AND FUNCTION.
PubMed=11880380; DOI=10.1074/jbc.m201000200;
Radons J., Gabler S., Wesche H., Korherr C., Hofmeister R., Falk W.;
"Identification of essential regions in the cytoplasmic tail of
interleukin-1 receptor accessory protein critical for interleukin-1
signaling.";
J. Biol. Chem. 277:16456-16463(2002).
[8]
INTERACTION WITH IRAK2.
PubMed=12659850; DOI=10.1016/s0006-291x(03)00385-1;
Boch J.A., Yoshida Y., Koyama Y., Wara-Aswapati N., Peng H., Unlu S.,
Auron P.E.;
"Characterization of a cascade of protein interactions initiated at the IL-
1 receptor.";
Biochem. Biophys. Res. Commun. 303:525-531(2003).
[9]
FUNCTION.
PubMed=15986350; DOI=10.1002/art.21108;
Smeets R.L., Joosten L.A., Arntz O.J., Bennink M.B., Takahashi N.,
Carlsen H., Martin M.U., van den Berg W.B., van de Loo F.A.;
"Soluble interleukin-1 receptor accessory protein ameliorates collagen-
induced arthritis by a different mode of action from that of interleukin-1
receptor antagonist.";
Arthritis Rheum. 52:2202-2211(2005).
[10]
FUNCTION, AND SUBUNIT.
PubMed=17675517; DOI=10.4049/jimmunol.179.4.2551;
Chackerian A.A., Oldham E.R., Murphy E.E., Schmitz J., Pflanz S.,
Kastelein R.A.;
"IL-1 receptor accessory protein and ST2 comprise the IL-33 receptor
complex.";
J. Immunol. 179:2551-2555(2007).
[11]
FUNCTION, AND INTERACTION WITH IL1RL1.
PubMed=18003919; DOI=10.1073/pnas.0705939104;
Ali S., Huber M., Kollewe C., Bischoff S.C., Falk W., Martin M.U.;
"IL-1 receptor accessory protein is essential for IL-33-induced activation
of T lymphocytes and mast cells.";
Proc. Natl. Acad. Sci. U.S.A. 104:18660-18665(2007).
[12]
FUNCTION, AND INTERACTION WITH IL1RL1.
PubMed=18450470; DOI=10.1016/j.cyto.2008.03.008;
Palmer G., Lipsky B.P., Smithgall M.D., Meininger D., Siu S.,
Talabot-Ayer D., Gabay C., Smith D.E.;
"The IL-1 receptor accessory protein (AcP) is required for IL-33 signaling
and soluble AcP enhances the ability of soluble ST2 to inhibit IL-33.";
Cytokine 42:358-364(2008).
[13]
ALTERNATIVE SPLICING (ISOFORM 3), AND TISSUE SPECIFICITY (ISOFORM 3).
PubMed=19481478; DOI=10.1016/j.immuni.2009.03.020;
Smith D.E., Lipsky B.P., Russell C., Ketchem R.R., Kirchner J., Hensley K.,
Huang Y., Friedman W.J., Boissonneault V., Plante M.M., Rivest S.,
Sims J.E.;
"A central nervous system-restricted isoform of the interleukin-1 receptor
accessory protein modulates neuronal responses to interleukin-1.";
Immunity 30:817-831(2009).
[14]
INTERACTION WITH KIT, AND SUBUNIT.
PubMed=20200353; DOI=10.1182/blood-2009-10-247411;
Drube S., Heink S., Walter S., Loehn T., Grusser M., Gerbaulet A.,
Berod L., Schons J., Dudeck A., Freitag J., Grotha S., Reich D.,
Rudeschko O., Norgauer J., Hartmann K., Roers A., Kamradt T.;
"The receptor tyrosine kinase c-Kit controls IL-33 receptor signaling in
mast cells.";
Blood 115:3899-3906(2010).
[15]
TISSUE SPECIFICITY.
PubMed=21349253; DOI=10.1016/j.brainres.2011.02.045;
Yasuoka S., Kawanokuchi J., Parajuli B., Jin S., Doi Y., Noda M.,
Sonobe Y., Takeuchi H., Mizuno T., Suzumura A.;
"Production and functions of IL-33 in the central nervous system.";
Brain Res. 1385:8-17(2011).
[16]
INTERACTION WITH IL1RL2, AND SUBUNIT.
PubMed=21965679; DOI=10.1074/jbc.m111.267922;
Towne J.E., Renshaw B.R., Douangpanya J., Lipsky B.P., Shen M., Gabel C.A.,
Sims J.E.;
"Interleukin-36 (IL-36) ligands require processing for full agonist (IL-
36alpha, IL-36beta, and IL-36gamma) or antagonist (IL-36Ra) activity.";
J. Biol. Chem. 286:42594-42602(2011).
[17]
FUNCTION (ISOFORM 3), AND TISSUE SPECIFICITY (ISOFORM 3).
PubMed=22159118; DOI=10.1523/jneurosci.4067-11.2011;
Huang Y., Smith D.E., Ibanez-Sandoval O., Sims J.E., Friedman W.J.;
"Neuron-specific effects of interleukin-1beta are mediated by a novel
isoform of the IL-1 receptor accessory protein.";
J. Neurosci. 31:18048-18059(2011).
[18]
FUNCTION (ISOFORM 3).
PubMed=22778412; DOI=10.1073/pnas.1205207109;
Qian J., Zhu L., Li Q., Belevych N., Chen Q., Zhao F., Herness S., Quan N.;
"Interleukin-1R3 mediates interleukin-1-induced potassium current increase
through fast activation of Akt kinase.";
Proc. Natl. Acad. Sci. U.S.A. 109:12189-12194(2012).
[19] {ECO:0000244|PDB:4YFD}
X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 21-351 IN COMPLEX WITH PTPRD,
DISULFIDE BONDS, GLYCOSYLATION AT ASN-57; ASN-107; ASN-111; ASN-118 AND
ASN-209, INTERACTION WITH PTPRD, FUNCTION, MUTAGENESIS OF TRP-27; ASP-30;
69-ILE--TYR-71; 82-PRO--PHE-85 AND LYS-94, AND REGION.
PubMed=25908590; DOI=10.1038/ncomms7926;
Yamagata A., Yoshida T., Sato Y., Goto-Ito S., Uemura T., Maeda A.,
Shiroshima T., Iwasawa-Okamoto S., Mori H., Mishina M., Fukai S.;
"Mechanisms of splicing-dependent trans-synaptic adhesion by PTPdelta-
IL1RAPL1/IL-1RAcP for synaptic differentiation.";
Nat. Commun. 6:6926-6926(2015).
-!- FUNCTION: Coreceptor for IL1RL2 in the IL-36 signaling system.
Coreceptor with IL1R1 in the IL-1 signaling system. Associates with
IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor
complex which mediates interleukin-1-dependent activation of NF-kappa-B
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. Recruits TOLLIP to the
signaling complex. Does not bind to interleukin-1 alone; binding of
IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling
complex. The cellular response is modulated through a non-signaling
association with the membrane IL1R2 decoy receptor. Secreted forms
(isoforms 2 and 3) associate with secreted ligand-bound IL1R2 and
increase the affinity of secreted IL1R2 for IL1B; this complex
formation may be the dominant mechanism for neutralization of IL1B by
secreted/soluble receptors. Coreceptor for IL1RL1 in the IL-33
signaling system. Can bidirectionally induce pre- and postsynaptic
differentiation of neurons by trans-synaptically binding to PTPRD
(PubMed:25908590). May play a role in IL1B-mediated costimulation of
IFNG production from T-helper 1 (Th1) cells (By similarity).
{ECO:0000250|UniProtKB:Q9NPH3, ECO:0000269|PubMed:11880380,
ECO:0000269|PubMed:15986350, ECO:0000269|PubMed:17675517,
ECO:0000269|PubMed:18003919, ECO:0000269|PubMed:18450470,
ECO:0000269|PubMed:25908590, ECO:0000303|PubMed:21965679}.
-!- FUNCTION: [Isoform 2]: Associates with secreted ligand-bound IL1R2 and
increases the affinity of secreted IL1R2 for IL1B; this complex
formation may be the dominant mechanism for neutralization of IL1B by
secreted/soluble receptors. Enhances the ability of secreted IL1R1 to
inhibit IL-33 signaling. {ECO:0000269|PubMed:15986350,
ECO:0000269|PubMed:18450470}.
-!- FUNCTION: [Isoform 3]: Required for Src phosphorylation by IL1B.
Required for IL1B-potentiated NMDA-induced calcium influx in neurons
acting in cooperation with IL1R1 isoform 2 to mediate Akt kinase
activation. {ECO:0000269|PubMed:22159118, ECO:0000269|PubMed:22778412}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
-!- SUBUNIT: The interleukin-36 receptor complex is a heterodimer of IL1RL2
and IL1RAP; the association is inhibited by IL36RN. The interleukin-1
receptor complex is a heterodimer of IL1R1 and IL1RAP. Associates with
IL1R2 to form a non-signaling interleukin-1 receptor complex. Interacts
with IL-33-bound IL1RL1 to form the minimal interleukin-33 signaling
complex with a 1:1:1 stoichiometry. Interacts with KIT (independently
of stimulation with KITLG/SCF). A mast cell-specific KITLG/SCF-induced
interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and
MYD88. Interacts (via the first immunoglobilin domain) with PTPRD (via
the third immunoglobilin domain); induces pre- and postsynaptic
differentiation of neurons (PubMed:25908590).
{ECO:0000269|PubMed:17675517, ECO:0000269|PubMed:18003919,
ECO:0000269|PubMed:20200353, ECO:0000269|PubMed:21965679,
ECO:0000269|PubMed:25908590, ECO:0000269|PubMed:9862719}.
-!- INTERACTION:
Q61730; P14719: Il1rl1; NbExp=3; IntAct=EBI-525035, EBI-525078;
Q61730; Q9QZ06: Tollip; NbExp=2; IntAct=EBI-525035, EBI-74272;
-!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=MuIL-1R AcP;
IsoId=Q61730-1; Sequence=Displayed;
Name=2; Synonyms=SmuIL-1R AcP;
IsoId=Q61730-2; Sequence=VSP_008054, VSP_008055;
Name=3; Synonyms=IL-1RAcPb;
IsoId=Q61730-3; Sequence=VSP_058171;
-!- TISSUE SPECIFICITY: Detected in lung, brain, spleen, thymus and liver.
Expressed in brain endothelial cells, astrocytes, microglia and
neurons. Isoform 3 is predominantly expressed in brain; expressed in
hippocampal neurons. {ECO:0000269|PubMed:19481478,
ECO:0000269|PubMed:21349253, ECO:0000269|PubMed:22159118,
ECO:0000269|PubMed:7775431}.
-!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
Self-association of TIR domains is required for NADase activity.
{ECO:0000255|PROSITE-ProRule:PRU00204}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
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EMBL; X85999; CAA59991.1; -; mRNA.
EMBL; AK039582; BAC30392.1; -; mRNA.
EMBL; AK045686; BAC32457.1; -; mRNA.
EMBL; AK136782; BAE23128.1; -; mRNA.
EMBL; AC154234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC154601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CT009561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC021159; AAH21159.1; -; mRNA.
CCDS; CCDS28089.1; -. [Q61730-1]
CCDS; CCDS49815.1; -. [Q61730-3]
CCDS; CCDS57023.1; -. [Q61730-2]
PIR; A57535; A57535.
RefSeq; NP_001152790.1; NM_001159318.1. [Q61730-3]
RefSeq; NP_032390.1; NM_008364.2. [Q61730-1]
RefSeq; NP_598864.1; NM_134103.2. [Q61730-2]
PDB; 4YFD; X-ray; 3.25 A; B=21-351.
PDB; 5VI4; X-ray; 2.79 A; C/F=21-350.
PDBsum; 4YFD; -.
PDBsum; 5VI4; -.
SMR; Q61730; -.
BioGrid; 200628; 3.
CORUM; Q61730; -.
DIP; DIP-296N; -.
IntAct; Q61730; 3.
iPTMnet; Q61730; -.
PhosphoSitePlus; Q61730; -.
CPTAC; non-CPTAC-3320; -.
EPD; Q61730; -.
jPOST; Q61730; -.
PeptideAtlas; Q61730; -.
PRIDE; Q61730; -.
ABCD; Q61730; -.
Antibodypedia; 19361; 367 antibodies.
DNASU; 16180; -.
Ensembl; ENSMUST00000023156; ENSMUSP00000023156; ENSMUSG00000022514. [Q61730-1]
Ensembl; ENSMUST00000096129; ENSMUSP00000093843; ENSMUSG00000022514. [Q61730-3]
Ensembl; ENSMUST00000174202; ENSMUSP00000134202; ENSMUSG00000022514. [Q61730-2]
GeneID; 16180; -.
KEGG; mmu:16180; -.
UCSC; uc007yve.2; mouse. [Q61730-1]
UCSC; uc007yvg.2; mouse.
CTD; 3556; -.
MGI; MGI:104975; Il1rap.
eggNOG; ENOG410IEPH; Eukaryota.
eggNOG; ENOG410ZRCQ; LUCA.
GeneTree; ENSGT00980000198494; -.
HOGENOM; CLU_025552_3_2_1; -.
InParanoid; Q61730; -.
KO; K04723; -.
OMA; KSPRWSS; -.
PhylomeDB; Q61730; -.
TreeFam; TF325519; -.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-9014826; Interleukin-36 pathway.
Reactome; R-MMU-9014843; Interleukin-33 signaling.
Reactome; R-MMU-9020702; Interleukin-1 signaling.
ChiTaRS; Il1rap; mouse.
PRO; PR:Q61730; -.
Proteomes; UP000000589; Chromosome 16.
RNAct; Q61730; protein.
Bgee; ENSMUSG00000022514; Expressed in liver and 227 other tissues.
ExpressionAtlas; Q61730; baseline and differential.
Genevisible; Q61730; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0004908; F:interleukin-1 receptor activity; IDA:MGI.
GO; GO:0005149; F:interleukin-1 receptor binding; ISO:MGI.
GO; GO:0002114; F:interleukin-33 receptor activity; IMP:UniProtKB.
GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0042094; P:interleukin-2 biosynthetic process; IDA:MGI.
GO; GO:0038172; P:interleukin-33-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0072602; P:interleukin-4 secretion; IMP:UniProtKB.
GO; GO:1900006; P:positive regulation of dendrite development; IDA:MGI.
GO; GO:0032736; P:positive regulation of interleukin-13 production; IMP:UniProtKB.
GO; GO:0032754; P:positive regulation of interleukin-5 production; IMP:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
GO; GO:0099545; P:trans-synaptic signaling by trans-synaptic complex; IDA:SynGO.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR041416; Ig_6.
InterPro; IPR003599; Ig_sub.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR004074; IL-1_rcpt_I/II-typ.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF13895; Ig_2; 1.
Pfam; PF18452; Ig_6; 1.
Pfam; PF01582; TIR; 1.
PRINTS; PR01536; INTRLKN1R12F.
SMART; SM00409; IG; 3.
SMART; SM00255; TIR; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
Glycoprotein; Hydrolase; Immunity; Immunoglobulin domain;
Inflammatory response; Innate immunity; Membrane; NAD; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1..20
/evidence="ECO:0000255"
CHAIN 21..570
/note="Interleukin-1 receptor accessory protein"
/id="PRO_0000015452"
TOPO_DOM 21..367
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 368..388
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 389..570
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 21..128
/note="Ig-like C2-type 1"
DOMAIN 139..230
/note="Ig-like C2-type 2"
DOMAIN 243..348
/note="Ig-like C2-type 3"
DOMAIN 403..546
/note="TIR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
REGION 69..85
/note="Essential for interaction with PTPRD"
/evidence="ECO:0000269|PubMed:25908590"
ACT_SITE 482
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
CARBOHYD 57
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:4YFD,
ECO:0000269|PubMed:25908590"
CARBOHYD 107
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:4YFD,
ECO:0000269|PubMed:25908590"
CARBOHYD 111
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:4YFD,
ECO:0000269|PubMed:25908590"
CARBOHYD 118
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:4YFD,
ECO:0000269|PubMed:25908590"
CARBOHYD 196
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 209
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:4YFD,
ECO:0000269|PubMed:25908590"
CARBOHYD 299
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 24..122
/evidence="ECO:0000244|PDB:4YFD, ECO:0000255|PROSITE-
ProRule:PRU00114, ECO:0000269|PubMed:25908590"
DISULFID 47..114
/evidence="ECO:0000244|PDB:4YFD, ECO:0000255|PROSITE-
ProRule:PRU00114, ECO:0000269|PubMed:25908590"
DISULFID 137..181
/evidence="ECO:0000244|PDB:4YFD, ECO:0000255|PROSITE-
ProRule:PRU00114, ECO:0000269|PubMed:25908590"
DISULFID 160..212
/evidence="ECO:0000244|PDB:4YFD, ECO:0000255|PROSITE-
ProRule:PRU00114, ECO:0000269|PubMed:25908590"
DISULFID 266..332
/evidence="ECO:0000244|PDB:4YFD, ECO:0000255|PROSITE-
ProRule:PRU00114, ECO:0000269|PubMed:25908590"
VAR_SEQ 351..359
/note="VIPPRYTVE -> GNGCTEPMTL (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7775431"
/id="VSP_008054"
VAR_SEQ 360..570
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7775431"
/id="VSP_008055"
VAR_SEQ 449..570
/note="IVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLENMASRGNINVIL
VQYKAVKDMKVKELKRAKTVLTVIKWKGEKSKYPQGRFWKQLQVAMPVKKSPRWSSNDK
QGLSYSSLKNV -> NTVEAVFDFIQRSRRMIVVLSPDYVTEKSISMLEFKLGVMCQNS
IATKLIVVEYRPLEQPHPGIMQLKESVSFVSWKGEKSKHSGSKFWKALRLALPLRSLSA
SSGWNESCSSQSDISLDHVQRRSRLKEPPELRSSERVSGAEPAPGTMSKHRGKPSAACR
CCVTYCEGESHLRSKSRAEMHTHPQWETHLCKPPLQESESQWIQNGTRPEPAPQISALA
LRHFTDLSNNNDFYIL (in isoform 3)"
/id="VSP_058171"
MUTAGEN 27
/note="W->A: Reduces affinity for PTPRD."
/evidence="ECO:0000269|PubMed:25908590"
MUTAGEN 30
/note="D->A: Does not affect affinity for PTPRD."
/evidence="ECO:0000269|PubMed:25908590"
MUTAGEN 69..71
/note="IWY->AWA: Abolishes interaction with PTPRD; when
associates with 82-A--A-85. Significantly reduces
synaptogenesis; when associates with 82-A--A-85."
/evidence="ECO:0000269|PubMed:25908590"
MUTAGEN 82..85
/note="PINF->AINA: Abolishes interaction with PTPRD; when
associates with 69-A--A-71 Significantly reduces
synaptogenesis; when associates with 82-A--A-85."
/evidence="ECO:0000269|PubMed:25908590"
MUTAGEN 94
/note="K->A: Reduces affinity for PTPRD."
/evidence="ECO:0000269|PubMed:25908590"
MUTAGEN 527..534
/note="KGEKSKYP->AAAAAAAA: Abolishes interaction with MYD88
and IL-1-dependent activation of NF-kappa-B."
/evidence="ECO:0000269|PubMed:11880380"
STRAND 26..30
/evidence="ECO:0000244|PDB:5VI4"
STRAND 35..38
/evidence="ECO:0000244|PDB:5VI4"
STRAND 43..46
/evidence="ECO:0000244|PDB:5VI4"
HELIX 49..52
/evidence="ECO:0000244|PDB:5VI4"
HELIX 58..63
/evidence="ECO:0000244|PDB:5VI4"
STRAND 67..74
/evidence="ECO:0000244|PDB:5VI4"
STRAND 85..87
/evidence="ECO:0000244|PDB:4YFD"
HELIX 88..90
/evidence="ECO:0000244|PDB:4YFD"
STRAND 91..95
/evidence="ECO:0000244|PDB:5VI4"
STRAND 98..103
/evidence="ECO:0000244|PDB:5VI4"
HELIX 106..108
/evidence="ECO:0000244|PDB:5VI4"
STRAND 110..117
/evidence="ECO:0000244|PDB:5VI4"
STRAND 122..132
/evidence="ECO:0000244|PDB:5VI4"
STRAND 146..150
/evidence="ECO:0000244|PDB:5VI4"
STRAND 156..159
/evidence="ECO:0000244|PDB:5VI4"
STRAND 174..179
/evidence="ECO:0000244|PDB:5VI4"
STRAND 182..185
/evidence="ECO:0000244|PDB:5VI4"
STRAND 188..193
/evidence="ECO:0000244|PDB:5VI4"
STRAND 196..201
/evidence="ECO:0000244|PDB:5VI4"
HELIX 204..206
/evidence="ECO:0000244|PDB:5VI4"
STRAND 208..218
/evidence="ECO:0000244|PDB:5VI4"
STRAND 221..234
/evidence="ECO:0000244|PDB:5VI4"
HELIX 237..239
/evidence="ECO:0000244|PDB:5VI4"
STRAND 244..248
/evidence="ECO:0000244|PDB:5VI4"
STRAND 250..252
/evidence="ECO:0000244|PDB:4YFD"
STRAND 264..270
/evidence="ECO:0000244|PDB:5VI4"
STRAND 279..286
/evidence="ECO:0000244|PDB:5VI4"
STRAND 296..299
/evidence="ECO:0000244|PDB:4YFD"
STRAND 300..304
/evidence="ECO:0000244|PDB:5VI4"
STRAND 310..316
/evidence="ECO:0000244|PDB:5VI4"
TURN 325..327
/evidence="ECO:0000244|PDB:5VI4"
STRAND 330..336
/evidence="ECO:0000244|PDB:5VI4"
STRAND 339..345
/evidence="ECO:0000244|PDB:5VI4"
SEQUENCE 570 AA; 65741 MW; 4D4B07E0310AFDC5 CRC64;
MGLLWYLMSL SFYGILQSHA SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKYNYST
AHSSGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT
YCSKVAFPLE VVQKDSCFNS AMRFPVHKMY IEHGIHKITC PNVDGYFPSS VKPSVTWYKG
CTEIVDFHNV LPEGMNLSFF IPLVSNNGNY TCVVTYPENG RLFHLTRTVT VKVVGSPKDA
LPPQIYSPND RVVYEKEPGE ELVIPCKVYF SFIMDSHNEV WWTIDGKKPD DVTVDITINE
SVSYSSTEDE TRTQILSIKK VTPEDLRRNY VCHARNTKGE AEQAAKVKQK VIPPRYTVEL
ACGFGATVFL VVVLIVVYHV YWLEMVLFYR AHFGTDETIL DGKEYDIYVS YARNVEEEEF
VLLTLRGVLE NEFGYKLCIF DRDSLPGGIV TDETLSFIQK SRRLLVVLSP NYVLQGTQAL
LELKAGLENM ASRGNINVIL VQYKAVKDMK VKELKRAKTV LTVIKWKGEK SKYPQGRFWK
QLQVAMPVKK SPRWSSNDKQ GLSYSSLKNV


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Related Genes :
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[IL1RAP C3orf13 IL1R3] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-1 receptor 3) (IL-1R-3) (IL-1R3)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6)
[IL1RAP] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6)
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (EC 3.2.2.6) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (CDw218b) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-1 receptor 7) (IL-1R-7) (IL-1R7) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)
[IL1RAPL1 OPHN4] Interleukin-1 receptor accessory protein-like 1 (IL-1-RAPL-1) (IL-1RAPL-1) (IL1RAPL-1) (EC 3.2.2.6) (Oligophrenin-4) (Three immunoglobulin domain-containing IL-1 receptor-related 2) (TIGIRR-2) (X-linked interleukin-1 receptor accessory protein-like 1)
[Il1rl1 Ly84 St2 Ste2] Interleukin-1 receptor-like 1 (EC 3.2.2.6) (Interleukin-33 receptor alpha chain) (Lymphocyte antigen 84) (Protein ST2) (Protein T1)
[IL1R1 IL1R IL1RA IL1RT1] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[IL2RB IL15RB] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (Interleukin-15 receptor subunit beta) (p70-75) (p75) (CD antigen CD122)
[IL33 C9orf26 IL1F11 NFHEV] Interleukin-33 (IL-33) (Interleukin-1 family member 11) (IL-1F11) (Nuclear factor from high endothelial venules) (NF-HEV) [Cleaved into: Interleukin-33 (95-270); Interleukin-33 (99-270); Interleukin-33 (109-270)]
[IFNLR1 IL28RA LICR2] Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2)
[IL36RN FIL1D IL1F5 IL1HY1 IL1L1 IL1RP3 UNQ1896/PRO4342] Interleukin-36 receptor antagonist protein (IL-36Ra) (FIL1 delta) (IL-1-related protein 3) (IL-1RP3) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 receptor antagonist homolog 1) (IL-1ra homolog 1) (Interleukin-1-like protein 1) (IL-1L1)
[IL13RA1 IL13R IL13RA] Interleukin-13 receptor subunit alpha-1 (IL-13 receptor subunit alpha-1) (IL-13R subunit alpha-1) (IL-13R-alpha-1) (IL-13RA1) (Cancer/testis antigen 19) (CT19) (CD antigen CD213a1)
[IL2RG] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[IL12RB1 IL12R IL12RB] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12RB1) (IL-12 receptor beta component) (CD antigen CD212)
[Il3ra Sut-1] Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (Interleukin-3 receptor class II alpha chain) (CD antigen CD123)
[Il12rb1 Il12rb] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12 receptor beta component) (CD antigen CD212)
[Il1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[IL1RL1 DER4 ST2 T1] Interleukin-1 receptor-like 1 (EC 3.2.2.6) (Protein ST2)
[IL36RN Fil1d Il1f5 Il1h3 Il1hy1] Interleukin-36 receptor antagonist protein (IL-36Ra) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 homolog 3) (IL-1H3) (Interleukin-1-like protein 1) (IL-1L1)
[IL18R1 IL1RRP] Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (EC 3.2.2.6) (CD218 antigen-like family member A) (CDw218a) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (Interleukin-18 receptor alpha) (IL-18R-alpha) (IL-18Ralpha) (CD antigen CD218a)
[IL10RB CRFB4 D21S58 D21S66] Interleukin-10 receptor subunit beta (IL-10 receptor subunit beta) (IL-10R subunit beta) (IL-10RB) (Cytokine receptor class-II member 4) (Cytokine receptor family 2 member 4) (CRF2-4) (Interleukin-10 receptor subunit 2) (IL-10R subunit 2) (IL-10R2) (CD antigen CDw210b)
[IL4R IL4RA 582J2.1] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[Il1r1 Il-1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL6ST] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (CDw130) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL10RA IL10R] Interleukin-10 receptor subunit alpha (IL-10 receptor subunit alpha) (IL-10R subunit alpha) (IL-10RA) (CDw210a) (Interleukin-10 receptor subunit 1) (IL-10R subunit 1) (IL-10R1) (CD antigen CD210)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[Il1rl2] Interleukin-1 receptor-like 2 (EC 3.2.2.6) (IL-36 receptor) (Interleukin-1 receptor-related protein 2) (IL-1Rrp2) (IL1R-rp2)
[Il18r1] Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (EC 3.2.2.6) (CD218 antigen-like family member A) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (Interleukin-18 receptor alpha) (IL-18R-alpha) (IL-18Ralpha) (CD antigen CD218a)

Bibliography :