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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)

 I10R1_HUMAN             Reviewed;         578 AA.
Q13651; A8K6I0; B0YJ27;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 2.
12-AUG-2020, entry version 175.
RecName: Full=Interleukin-10 receptor subunit alpha;
Short=IL-10 receptor subunit alpha;
Short=IL-10R subunit alpha;
Short=IL-10RA;
AltName: Full=CDw210a;
AltName: Full=Interleukin-10 receptor subunit 1;
Short=IL-10R subunit 1;
Short=IL-10R1;
AltName: CD_antigen=CD210;
Flags: Precursor;
Name=IL10RA; Synonyms=IL10R;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-351.
TISSUE=Lymphoma;
PubMed=8120391;
Liu Y., Wei S.H.-Y., Ho A.S.-Y., de Waal Malefyt R., Moore K.W.;
"Expression cloning and characterization of a human IL-10 receptor.";
J. Immunol. 152:1821-1829(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-61; ILE-113; GLY-159;
GLN-212; GLY-351 AND LEU-420.
SeattleSNPs variation discovery resource;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-351.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
Hattori M., Rogers J., Lander E.S., Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-351.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-351.
TISSUE=Blood;
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).
[8]
PROTEIN SEQUENCE OF 22-36.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified
cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[9]
FUNCTION, AND INTERACTION WITH JAK1.
PubMed=12133952; DOI=10.4049/jimmunol.169.3.1302;
Usacheva A., Kotenko S., Witte M.M., Colamonici O.R.;
"Two distinct domains within the N-terminal region of Janus kinase 1
interact with cytokine receptors.";
J. Immunol. 169:1302-1308(2002).
[10]
FUNCTION, AND INTERACTION WITH IL10 AND IL10RB.
PubMed=16982608; DOI=10.1074/jbc.m606791200;
Yoon S.I., Logsdon N.J., Sheikh F., Donnelly R.P., Walter M.R.;
"Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding
to IL-10 and assembly of the signaling complex.";
J. Biol. Chem. 281:35088-35096(2006).
[11]
INTERACTION WITH BTRC, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=22087322; DOI=10.1371/journal.pone.0027464;
Jiang H., Lu Y., Yuan L., Liu J.;
"Regulation of interleukin-10 receptor ubiquitination and stability by
beta-TrCP-containing ubiquitin E3 ligase.";
PLoS ONE 6:E27464-E27464(2011).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26962683; DOI=10.1038/cddis.2016.44;
Shi J., Wang H., Guan H., Shi S., Li Y., Wu X., Li N., Yang C., Bai X.,
Cai W., Yang F., Wang X., Su L., Zheng Z., Hu D.;
"IL10 inhibits starvation-induced autophagy in hypertrophic scar
fibroblasts via cross talk between the IL10-IL10R-STAT3 and IL10-AKT-mTOR
pathways.";
Cell Death Dis. 7:E2133-E2133(2016).
[13]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-235 IN COMPLEX WITH IL10, AND
DISULFIDE BONDS.
PubMed=11485736; DOI=10.1016/s1074-7613(01)00169-8;
Josephson K., Logsdon N.J., Walter M.R.;
"Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor
binding site.";
Immunity 15:35-46(2001).
[14]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-235 IN COMPLEX WITH
CYTOMEGALOVIRUS IL10 (MICROBIAL INFECTION).
PubMed=12093920; DOI=10.1073/pnas.152147499;
Jones B.C., Logsdon N.J., Josephson K., Cook J., Barry P.A., Walter M.R.;
"Crystal structure of human cytomegalovirus IL-10 bound to soluble human
IL-10R1.";
Proc. Natl. Acad. Sci. U.S.A. 99:9404-9409(2002).
[15]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-335 IN COMPLEX WITH IL10 AND
EPSTEIN-BARR VIRUS IL10 (MICROBIAL INFECTION).
PubMed=15837194; DOI=10.1016/j.str.2005.01.016;
Yoon S.I., Jones B.C., Logsdon N.J., Walter M.R.;
"Same structure, different function crystal structure of the Epstein-Barr
virus IL-10 bound to the soluble IL-10R1 chain.";
Structure 13:551-564(2005).
[16]
VARIANTS IBD28 ILE-84 AND ARG-141.
PubMed=19890111; DOI=10.1056/nejmoa0907206;
Glocker E.O., Kotlarz D., Boztug K., Gertz E.M., Schaffer A.A., Noyan F.,
Perro M., Diestelhorst J., Allroth A., Murugan D., Hatscher N., Pfeifer D.,
Sykora K.W., Sauer M., Kreipe H., Lacher M., Nustede R., Woellner C.,
Baumann U., Salzer U., Koletzko S., Shah N., Segal A.W., Sauerbrey A.,
Buderus S., Snapper S.B., Grimbacher B., Klein C.;
"Inflammatory bowel disease and mutations affecting the interleukin-10
receptor.";
N. Engl. J. Med. 361:2033-2045(2009).
[17]
VARIANTS IBD28 CYS-91; TRP-101; HIS-117 AND CYS-262.
PubMed=23839161; DOI=10.1097/meg.0b013e328361a4f9;
Shim J.O., Hwang S., Yang H.R., Moon J.S., Chang J.Y., Ko J.S., Park S.S.,
Kang G.H., Kim W.S., Seo J.K.;
"Interleukin-10 receptor mutations in children with neonatal-onset Crohn's
disease and intractable ulcerating enterocolitis.";
Eur. J. Gastroenterol. Hepatol. 25:1235-1240(2013).
[18]
VARIANTS IBD28 ARG-69; CYS-91; TRP-101; HIS-117 AND CYS-262.
PubMed=24785691; DOI=10.1038/jhg.2014.32;
Shim J.O., Seo J.K.;
"Very early-onset inflammatory bowel disease (IBD) in infancy is a
different disease entity from adult-onset IBD; one form of interleukin-10
receptor mutations.";
J. Hum. Genet. 59:337-341(2014).
-!- FUNCTION: Cell surface receptor for the cytokine IL10 that participates
in IL10-mediated anti-inflammatory functions, limiting excessive tissue
disruption caused by inflammation. Upon binding to IL10, induces a
conformational change in IL10RB, allowing IL10RB to bind IL10 as well
(PubMed:16982608). In turn, the heterotetrameric assembly complex,
composed of two subunits of IL10RA and IL10RB, activates the kinases
JAK1 and TYK2 that are constitutively associated with IL10RA and IL10RB
respectively (PubMed:12133952). These kinases then phosphorylate
specific tyrosine residues in the intracellular domain in IL10RA
leading to the recruitment and subsequent phosphorylation of STAT3.
Once phosphorylated, STAT3 homodimerizes, translocates to the nucleus
and activates the expression of anti-inflammatory genes. In addition,
IL10RA-mediated activation of STAT3 inhibits starvation-induced
autophagy (PubMed:26962683). {ECO:0000269|PubMed:12133952,
ECO:0000269|PubMed:16982608, ECO:0000269|PubMed:26962683}.
-!- SUBUNIT: Interacts with IL10 (PubMed:16982608, PubMed:15837194).
Interacts with IL10RB (PubMed:16982608). Interacts (via its cytoplasmic
domain) with JAK1 (via N-terminus) (PubMed:12133952). Interacts with
BTRC; this interaction leads to IL10RA ubiquitination and subsequent
degradation (PubMed:22087322). Interacts with STAT3 (By similarity).
{ECO:0000250|UniProtKB:Q61727, ECO:0000269|PubMed:12133952,
ECO:0000269|PubMed:15837194, ECO:0000269|PubMed:16982608,
ECO:0000269|PubMed:22087322}.
-!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
protein IL10. {ECO:0000269|PubMed:12093920}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
protein IL10. {ECO:0000269|PubMed:15837194}.
-!- INTERACTION:
Q13651; P27449: ATP6V0C; NbExp=3; IntAct=EBI-1031656, EBI-721179;
Q13651; Q9Y297: BTRC; NbExp=6; IntAct=EBI-1031656, EBI-307461;
Q13651; Q96GQ5: C16orf58; NbExp=3; IntAct=EBI-1031656, EBI-8636004;
Q13651; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-1031656, EBI-12062109;
Q13651; Q8IX05: CD302; NbExp=3; IntAct=EBI-1031656, EBI-14259393;
Q13651; O95674: CDS2; NbExp=3; IntAct=EBI-1031656, EBI-3913685;
Q13651; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-1031656, EBI-7247651;
Q13651; P02724: GYPA; NbExp=3; IntAct=EBI-1031656, EBI-702665;
Q13651; B0YJ81: HACD1; NbExp=3; IntAct=EBI-1031656, EBI-12051643;
Q13651; Q6Y1H2: HACD2; NbExp=3; IntAct=EBI-1031656, EBI-530257;
Q13651; P22301: IL10; NbExp=9; IntAct=EBI-1031656, EBI-1031632;
Q13651; P21145: MAL; NbExp=3; IntAct=EBI-1031656, EBI-3932027;
Q13651; Q0D2K0: NIPAL4; NbExp=3; IntAct=EBI-1031656, EBI-9550165;
Q13651; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-1031656, EBI-11721828;
Q13651; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-1031656, EBI-9679163;
Q13651; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-1031656, EBI-8644112;
Q13651; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-1031656, EBI-10314552;
Q13651; Q8N2U9: SLC66A2; NbExp=3; IntAct=EBI-1031656, EBI-3907610;
Q13651; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-1031656, EBI-5235586;
Q13651; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-1031656, EBI-8640191;
Q13651; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-1031656, EBI-10315004;
Q13651; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-1031656, EBI-2852148;
Q13651; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-1031656, EBI-2820477;
Q13651; O95183: VAMP5; NbExp=3; IntAct=EBI-1031656, EBI-10191195;
Q13651; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-1031656, EBI-751210;
Q13651; P03180: BCRF1; Xeno; NbExp=4; IntAct=EBI-1031656, EBI-1042167;
Q13651; P03495: NS; Xeno; NbExp=2; IntAct=EBI-1031656, EBI-2548993;
Q13651; P17150: UL111A; Xeno; NbExp=2; IntAct=EBI-1031656, EBI-1033736;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22087322,
ECO:0000269|PubMed:26962683}; Single-pass type I membrane protein.
Cytoplasm {ECO:0000269|PubMed:26962683}.
-!- TISSUE SPECIFICITY: Primarily expressed in hematopoetic cells including
B-cells, T-cells, NK cells, monocytes and macrophages. Not expressed in
non-hematopoetic cells such as fibroblasts or endothelial cells.
-!- PTM: Phosphorylated. Phosphorylation of the cytoplasmic tail induced
STAT3 activation. {ECO:0000250|UniProtKB:Q61727}.
-!- PTM: Ubiquitinated by BTRC; ubiquitination leads to endocytosis and
subsequent degradation of IL10RA. {ECO:0000269|PubMed:22087322}.
-!- DISEASE: Inflammatory bowel disease 28 (IBD28) [MIM:613148]: A chronic,
relapsing inflammation of the gastrointestinal tract with a complex
etiology. It is subdivided into Crohn disease and ulcerative colitis
phenotypes. Crohn disease may affect any part of the gastrointestinal
tract from the mouth to the anus, but most frequently it involves the
terminal ileum and colon. Bowel inflammation is transmural and
discontinuous; it may contain granulomas or be associated with
intestinal or perianal fistulas. In contrast, in ulcerative colitis,
the inflammation is continuous and limited to rectal and colonic
mucosal layers; fistulas and granulomas are not observed. Both diseases
include extraintestinal inflammation of the skin, eyes, or joints.
{ECO:0000269|PubMed:19890111, ECO:0000269|PubMed:23839161,
ECO:0000269|PubMed:24785691}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type II cytokine receptor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il10ra/";
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EMBL; U00672; AAA17896.1; -; mRNA.
EMBL; AY195619; AAN86349.1; -; Genomic_DNA.
EMBL; EF444988; ACA06005.1; -; Genomic_DNA.
EMBL; AK291645; BAF84334.1; -; mRNA.
EMBL; AP002962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67343.1; -; Genomic_DNA.
EMBL; BC028082; AAH28082.1; -; mRNA.
CCDS; CCDS8388.1; -.
PIR; I56215; I56215.
RefSeq; NP_001549.2; NM_001558.3.
PDB; 1J7V; X-ray; 2.90 A; R=22-235.
PDB; 1LQS; X-ray; 2.70 A; R/S=22-235.
PDB; 1Y6K; X-ray; 2.52 A; R=22-235.
PDB; 1Y6M; X-ray; 2.80 A; R=22-235.
PDB; 1Y6N; X-ray; 2.70 A; R=22-235.
PDB; 5IXI; X-ray; 2.57 A; B=263-303.
PDBsum; 1J7V; -.
PDBsum; 1LQS; -.
PDBsum; 1Y6K; -.
PDBsum; 1Y6M; -.
PDBsum; 1Y6N; -.
PDBsum; 5IXI; -.
SMR; Q13651; -.
BioGRID; 109801; 4.
CORUM; Q13651; -.
DIP; DIP-3512N; -.
IntAct; Q13651; 32.
MINT; Q13651; -.
STRING; 9606.ENSP00000227752; -.
GuidetoPHARMACOLOGY; 1727; -.
GlyGen; Q13651; 6 sites.
iPTMnet; Q13651; -.
PhosphoSitePlus; Q13651; -.
BioMuta; IL10RA; -.
DMDM; 322510034; -.
PaxDb; Q13651; -.
PeptideAtlas; Q13651; -.
PRIDE; Q13651; -.
ProteomicsDB; 59648; -.
Antibodypedia; 18560; 830 antibodies.
DNASU; 3587; -.
Ensembl; ENST00000227752; ENSP00000227752; ENSG00000110324.
GeneID; 3587; -.
KEGG; hsa:3587; -.
UCSC; uc001prv.5; human.
CTD; 3587; -.
DisGeNET; 3587; -.
EuPathDB; HostDB:ENSG00000110324.9; -.
GeneCards; IL10RA; -.
HGNC; HGNC:5964; IL10RA.
HPA; ENSG00000110324; Tissue enhanced (lymphoid).
MalaCards; IL10RA; -.
MIM; 146933; gene.
MIM; 613148; phenotype.
neXtProt; NX_Q13651; -.
OpenTargets; ENSG00000110324; -.
Orphanet; 238569; Immune dysregulation-inflammatory bowel disease-arthritis-recurrent infections syndrome.
PharmGKB; PA29779; -.
eggNOG; ENOG502S2PS; Eukaryota.
GeneTree; ENSGT00510000048847; -.
HOGENOM; CLU_033904_0_0_1; -.
InParanoid; Q13651; -.
KO; K05134; -.
OMA; EAEFFHH; -.
OrthoDB; 1456451at2759; -.
PhylomeDB; Q13651; -.
TreeFam; TF334107; -.
PathwayCommons; Q13651; -.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
SignaLink; Q13651; -.
SIGNOR; Q13651; -.
BioGRID-ORCS; 3587; 4 hits in 874 CRISPR screens.
ChiTaRS; IL10RA; human.
EvolutionaryTrace; Q13651; -.
GeneWiki; Interleukin_10_receptor,_alpha_subunit; -.
GenomeRNAi; 3587; -.
Pharos; Q13651; Tbio.
PRO; PR:Q13651; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; Q13651; protein.
Bgee; ENSG00000110324; Expressed in granulocyte and 194 other tissues.
ExpressionAtlas; Q13651; baseline and differential.
Genevisible; Q13651; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
GO; GO:0019969; F:interleukin-10 binding; IEA:Ensembl.
GO; GO:0004920; F:interleukin-10 receptor activity; TAS:ProtInc.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0010507; P:negative regulation of autophagy; IDA:UniProtKB.
GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:UniProtKB.
GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0070086; P:ubiquitin-dependent endocytosis; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
Pfam; PF01108; Tissue_fac; 1.
SUPFAM; SSF49265; SSF49265; 2.
1: Evidence at protein level;
3D-structure; Cell membrane; Cytoplasm; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1..21
/evidence="ECO:0000269|PubMed:15340161"
CHAIN 22..578
/note="Interleukin-10 receptor subunit alpha"
/id="PRO_0000011012"
TOPO_DOM 22..235
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 236..256
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 257..578
/note="Cytoplasmic"
/evidence="ECO:0000255"
MOTIF 318..323
/note="BTRC recognition motif"
/evidence="ECO:0000269|PubMed:22087322"
CARBOHYD 50
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 74
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 110
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 154
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 177
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 189
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 56..75
/evidence="ECO:0000269|PubMed:11485736"
DISULFID 202..223
/evidence="ECO:0000269|PubMed:11485736"
VARIANT 61
/note="L -> V (in dbSNP:rs4252250)"
/evidence="ECO:0000269|Ref.2"
/id="VAR_016294"
VARIANT 69
/note="W -> R (in IBD28; dbSNP:rs1343534194)"
/evidence="ECO:0000269|PubMed:24785691"
/id="VAR_071663"
VARIANT 84
/note="T -> I (in IBD28; dbSNP:rs137853580)"
/evidence="ECO:0000269|PubMed:19890111"
/id="VAR_063542"
VARIANT 91
/note="Y -> C (in IBD28)"
/evidence="ECO:0000269|PubMed:23839161,
ECO:0000269|PubMed:24785691"
/id="VAR_071664"
VARIANT 101
/note="R -> W (in IBD28; dbSNP:rs368287711)"
/evidence="ECO:0000269|PubMed:23839161,
ECO:0000269|PubMed:24785691"
/id="VAR_071665"
VARIANT 113
/note="V -> I (in dbSNP:rs4252303)"
/evidence="ECO:0000269|Ref.2"
/id="VAR_016295"
VARIANT 117
/note="R -> H (in IBD28; dbSNP:rs199989396)"
/evidence="ECO:0000269|PubMed:23839161,
ECO:0000269|PubMed:24785691"
/id="VAR_071666"
VARIANT 141
/note="G -> R (in IBD28; dbSNP:rs137853579)"
/evidence="ECO:0000269|PubMed:19890111"
/id="VAR_063543"
VARIANT 159
/note="S -> G (in dbSNP:rs3135932)"
/evidence="ECO:0000269|Ref.2"
/id="VAR_016296"
VARIANT 212
/note="R -> Q (in dbSNP:rs4252273)"
/evidence="ECO:0000269|Ref.2"
/id="VAR_016297"
VARIANT 224
/note="I -> V (in dbSNP:rs2228055)"
/id="VAR_020004"
VARIANT 262
/note="R -> C (in IBD28; dbSNP:rs149491038)"
/evidence="ECO:0000269|PubMed:23839161,
ECO:0000269|PubMed:24785691"
/id="VAR_071667"
VARIANT 351
/note="R -> G (in dbSNP:rs2229113)"
/evidence="ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8120391,
ECO:0000269|Ref.2, ECO:0000269|Ref.6"
/id="VAR_016298"
VARIANT 353
/note="P -> S (in dbSNP:rs35235073)"
/id="VAR_049175"
VARIANT 420
/note="S -> L (in dbSNP:rs2229114)"
/evidence="ECO:0000269|Ref.2"
/id="VAR_016299"
STRAND 32..37
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 40..45
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 56..63
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 70..82
/evidence="ECO:0000244|PDB:1Y6K"
HELIX 84..87
/evidence="ECO:0000244|PDB:1Y6K"
HELIX 90..92
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 96..104
/evidence="ECO:0000244|PDB:1Y6K"
HELIX 120..122
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 123..125
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 128..134
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 136..144
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 149..151
/evidence="ECO:0000244|PDB:1Y6K"
HELIX 157..160
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 165..176
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 181..193
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 199..209
/evidence="ECO:0000244|PDB:1Y6K"
STRAND 222..225
/evidence="ECO:0000244|PDB:1Y6K"
HELIX 268..270
/evidence="ECO:0000244|PDB:5IXI"
SEQUENCE 578 AA; 63003 MW; 54B183ABE84808DB CRC64;
MLPCLVVLLA ALLSLRLGSD AHGTELPSPP SVWFEAEFFH HILHWTPIPN QSESTCYEVA
LLRYGIESWN SISNCSQTLS YDLTAVTLDL YHSNGYRARV RAVDGSRHSN WTVTNTRFSV
DEVTLTVGSV NLEIHNGFIL GKIQLPRPKM APANDTYESI FSHFREYEIA IRKVPGNFTF
THKKVKHENF SLLTSGEVGE FCVQVKPSVA SRSNKGMWSK EECISLTRQY FTVTNVIIFF
AFVLLLSGAL AYCLALQLYV RRRKKLPSVL LFKKPSPFIF ISQRPSPETQ DTIHPLDEEA
FLKVSPELKN LDLHGSTDSG FGSTKPSLQT EEPQFLLPDP HPQADRTLGN REPPVLGDSC
SSGSSNSTDS GICLQEPSLS PSTGPTWEQQ VGSNSRGQDD SGIDLVQNSE GRAGDTQGGS
ALGHHSPPEP EVPGEEDPAA VAFQGYLRQT RCAEEKATKT GCLEEESPLT DGLGPKFGRC
LVDEAGLHPP ALAKGYLKQD PLEMTLASSG APTGQWNQPT EEWSLLALSS CSDLGISDWS
FAHDLAPLGC VAAPGGLLGS FNSDLVTLPL ISSLQSSE


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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP1566: Citrate cycle (TCA cycle)
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WP1655: Geraniol degradation
WP2292: Chemokine signaling pathway
WP1963: The effect of Glucocorticoids on target gene expression
WP566: canonical wnt - zebrafish
WP1644: DNA replication
WP1671: Methane metabolism
WP1693: Purine metabolism
WP1718: Vitamin B6 metabolism
WP1634: Butanoate metabolism
WP1663: Homologous recombination
WP1680: Oxidative phosphorylation
WP1711: Trinitrotoluene degradation
WP1626: Benzoate degradation via CoA ligation
WP1672: Mismatch repair
WP1694: Pyrimidine metabolism
WP2328: Allograft rejection
WP1003: Ovarian Infertility Genes
WP1348: Androgen Receptor Signaling Pathway
WP262: EBV LMP1 signaling
WP774: Kit Receptor Signaling Pathway
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1618: alpha-Linolenic acid metabolism

Related Genes :
[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)
[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)]
[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)
[IL6R] Interleukin-6 receptor subunit alpha (IL-6 receptor subunit alpha) (IL-6R subunit alpha) (IL-6R-alpha) (IL-6RA) (IL-6R 1) (Membrane glycoprotein 80) (gp80) (CD antigen CD126) [Cleaved into: Soluble interleukin-6 receptor subunit alpha (sIL6R)]
[Il4r Il4ra] 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)]
[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)
[IL15RA] Interleukin-15 receptor subunit alpha (IL-15 receptor subunit alpha) (IL-15R-alpha) (IL-15RA) (CD antigen CD215) [Cleaved into: Soluble interleukin-15 receptor subunit alpha (sIL-15 receptor subunit alpha) (sIL-15R-alpha) (sIL-15RA)]
[Il11ra1 Etl2 Il11ra] Interleukin-11 receptor subunit alpha-1 (IL-11 receptor subunit alpha-1) (IL-11R subunit alpha-1) (IL-11R-alpha-1) (IL-11RA1) (Enhancer trap locus homolog 2) (Etl-2) (Novel cytokine receptor 1) (NR-1) (NR1) [Cleaved into: Soluble interleukin-11 receptor subunit alpha (sIL-11R) (sIL-11RA) (sIL11RA)]
[IL7R] Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CDw127) (CD antigen CD127)
[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)
[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)
[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)
[IL13RA2 IL13R] Interleukin-13 receptor subunit alpha-2 (IL-13 receptor subunit alpha-2) (IL-13R subunit alpha-2) (IL-13R-alpha-2) (IL-13RA2) (Interleukin-13-binding protein) (CD antigen CD213a2)
[IL3RA IL3R] Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (CD antigen CD123)
[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)
[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)]
[Il4r Il4ra] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124)
[IL5RA IL5R] Interleukin-5 receptor subunit alpha (IL-5 receptor subunit alpha) (IL-5R subunit alpha) (IL-5R-alpha) (IL-5RA) (CDw125) (CD antigen CD125)
[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)]
[Il7r] Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CD antigen CD127)
[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)]
[IL11RA] Interleukin-11 receptor subunit alpha (IL-11 receptor subunit alpha) (IL-11R subunit alpha) (IL-11R-alpha) (IL-11RA) [Cleaved into: Soluble interleukin-11 receptor subunit alpha (sIL-11R) (sIL-11RA) (sIL11RA)]
[IL27RA CRL1 TCCR WSX1 UNQ296/PRO336] Interleukin-27 receptor subunit alpha (IL-27 receptor subunit alpha) (IL-27R subunit alpha) (IL-27R-alpha) (IL-27RA) (Cytokine receptor WSX-1) (Cytokine receptor-like 1) (Type I T-cell cytokine receptor) (TCCR) (ZcytoR1)
[IL31RA CRL3 GPL UNQ6368/PRO21073/PRO21384] Interleukin-31 receptor subunit alpha (IL-31 receptor subunit alpha) (IL-31R subunit alpha) (IL-31R-alpha) (IL-31RA) (Cytokine receptor-like 3) (GLM-R) (hGLM-R) (Gp130-like monocyte receptor) (Gp130-like receptor) (ZcytoR17)
[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)
[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)
[Il27ra Tccr Wsx1] Interleukin-27 receptor subunit alpha (IL-27 receptor subunit alpha) (IL-27R subunit alpha) (IL-27R-alpha) (IL-27RA) (Type I T-cell cytokine receptor) (TCCR) (WSX-1)
[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)
[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)

Bibliography :