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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)

 IL6RA_HUMAN             Reviewed;         468 AA.
P08887; A8KAE8; B2R6V4; Q16202; Q53EQ7; Q5FWG2; Q5VZ23;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
17-JUN-2020, entry version 228.
RecName: Full=Interleukin-6 receptor subunit alpha;
Short=IL-6 receptor subunit alpha;
Short=IL-6R subunit alpha;
Short=IL-6R-alpha;
Short=IL-6RA;
AltName: Full=IL-6R 1;
AltName: Full=Membrane glycoprotein 80;
Short=gp80;
AltName: CD_antigen=CD126;
Flags: Precursor;
Name=IL6R;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3136546; DOI=10.1126/science.3136546;
Yamasaki K., Taga T., Hirata Y., Yawata H., Kawanishi Y., Seed B.,
Taniguchi T., Hirano T., Kishimoto T.;
"Cloning and expression of the human interleukin-6 (BSF-2/IFN beta 2)
receptor.";
Science 241:825-828(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Yamasaki K., Taga T., Hirata Y., Yawata H., Kawanishi Y., Seed B.,
Taniguchi T., Hirano T., Kishimoto T.;
"Molecular structure of interleukin 6 receptor.";
Proc. Jpn. Acad., B, Phys. Biol. Sci. 64:209-211(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1872801; DOI=10.1042/bj2770659;
Schooltink H., Stoyan T., Lenz D., Schmitz H., Hirano T., Kishimoto T.,
Heinrich P.C., Rose-John S.;
"Structural and functional studies on the human hepatic interleukin-6
receptor. Molecular cloning and overexpression in HepG2 cells.";
Biochem. J. 277:659-664(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ALA-358.
TISSUE=Trachea;
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 MRNA] (ISOFORM 1).
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 313-365 (ISOFORM 2).
PubMed=8056053; DOI=10.1002/eji.1830240837;
Horiuchi S., Koyanagi Y., Zhou Y., Miyamoto H., Tanaka Y., Waki M.,
Matsumoto A., Yamamoto M., Yamamoto N.;
"Soluble interleukin-6 receptors released from T cell or
granulocyte/macrophage cell lines and human peripheral blood mononuclear
cells are generated through an alternative splicing mechanism.";
Eur. J. Immunol. 24:1945-1948(1994).
[10]
PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-55; ASN-93 AND ASN-221, LACK
OF GLYCOSYLATION AT ASN-245, AND DISULFIDE BONDS.
PubMed=10066782; DOI=10.1074/jbc.274.11.7207;
Cole A.R., Hall N.E., Treutlein H.R., Eddes J.S., Reid G.E., Moritz R.L.,
Simpson R.J.;
"Disulfide bond structure and N-glycosylation sites of the extracellular
domain of the human interleukin-6 receptor.";
J. Biol. Chem. 274:7207-7215(1999).
[11]
PROTEIN SEQUENCE OF 20-49, AND SUBCELLULAR LOCATION.
PubMed=2529343; DOI=10.1084/jem.170.4.1409;
Novick D., Engelmann H., Wallach D., Rubinstein M.;
"Soluble cytokine receptors are present in normal human urine.";
J. Exp. Med. 170:1409-1414(1989).
[12]
MUTAGENESIS.
PubMed=8467812; DOI=10.1002/j.1460-2075.1993.tb05815.x;
Yawata H., Yasukawa K., Natsuka S., Murakami M., Yamasaki K., Hibi M.,
Taga T., Kishimoto T.;
"Structure-function analysis of human IL-6 receptor: dissociation of amino
acid residues required for IL-6-binding and for IL-6 signal transduction
through gp130.";
EMBO J. 12:1705-1712(1993).
[13]
FUNCTION.
PubMed=11017875;
Martens A.S., Bode J.G., Heinrich P.C., Graeve L.;
"The cytoplasmic domain of the interleukin-6 receptor gp80 mediates its
basolateral sorting in polarized Madin-Darby canine kidney cells.";
J. Cell Sci. 113:3593-3602(2000).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16270750; DOI=10.1016/j.ejcb.2005.06.001;
Buk D.M., Renner O., Graeve L.;
"Increased association with detergent-resistant membranes/lipid rafts of
apically targeted mutants of the interleukin-6 receptor gp80.";
Eur. J. Cell Biol. 84:819-831(2005).
[15]
FUNCTION, AND INTERACTION WITH SORL1.
PubMed=28265003; DOI=10.1128/mcb.00641-16;
Larsen J.V., Petersen C.M.;
"SorLA in Interleukin-6 Signaling and Turnover.";
Mol. Cell. Biol. 37:0-0(2017).
[16]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-344.
PubMed=12461182; DOI=10.1073/pnas.232432399;
Varghese J.N., Moritz R.L., Lou M.-Z., Van Donkelaar A., Ji H., Ivancic N.,
Branson K.M., Hall N.E., Simpson R.J.;
"Structure of the extracellular domains of the human interleukin-6 receptor
alpha-chain.";
Proc. Natl. Acad. Sci. U.S.A. 99:15959-15964(2002).
[17]
X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS) OF 115-315.
PubMed=12829785; DOI=10.1126/science.1083901;
Boulanger M.J., Chow D.-C., Brevnova E.E., Garcia K.C.;
"Hexameric structure and assembly of the interleukin-6/IL-6 alpha-
receptor/gp130 complex.";
Science 300:2101-2104(2003).
[18]
POLYMORPHISM, VARIANT ALA-358, AND ASSOCIATION OF VARIANT ALA-358 WITH IL6
AND SOLUBLE IL6R SERUM LEVELS.
PubMed=17357077; DOI=10.1086/513206;
Health, Aging and Body Composition (Health ABC) Study;
Reich D., Patterson N., Ramesh V., De Jager P.L., McDonald G.J., Tandon A.,
Choy E., Hu D., Tamraz B., Pawlikowska L., Wassel-Fyr C., Huntsman S.,
Waliszewska A., Rossin E., Li R., Garcia M., Reiner A., Ferrell R.,
Cummings S., Kwok P.Y., Harris T., Zmuda J.M., Ziv E.;
"Admixture mapping of an allele affecting interleukin 6 soluble receptor
and interleukin 6 levels.";
Am. J. Hum. Genet. 80:716-726(2007).
-!- FUNCTION: Part of the receptor for interleukin 6. Binds to IL6 with low
affinity, but does not transduce a signal (PubMed:28265003). Signal
activation necessitate an association with IL6ST. Activation may lead
to the regulation of the immune response, acute-phase reactions and
hematopoiesis. {ECO:0000269|PubMed:28265003}.
-!- FUNCTION: Low concentration of a soluble form of IL6 receptor acts as
an agonist of IL6 activity.
-!- SUBUNIT: Hexamer of two molecules each of IL6, IL6R and IL6ST
(PubMed:28265003). Interacts (via N-terminal ectodomain) with SORL1;
this interaction may affect IL6-binding to IL6R, hence decrease IL6
cis-signaling (PubMed:28265003). The soluble form of IL6R also
interacts with SORL1; this interaction leads to soluble IL6R
internalization (PubMed:28265003). May form a trimeric complex with the
soluble SORL1 ectodomain and circulating IL6 receptor; this interaction
might stabilize circulating IL6, hence promote IL6 trans signaling
(PubMed:28265003). {ECO:0000269|PubMed:28265003}.
-!- INTERACTION:
P08887; P05231: IL6; NbExp=7; IntAct=EBI-299383, EBI-720533;
P08887; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-299383, EBI-744081;
P08887; Q92673: SORL1; NbExp=7; IntAct=EBI-299383, EBI-1171329;
P08887; Q2HRC7: K2; Xeno; NbExp=3; IntAct=EBI-299383, EBI-9007403;
P08887-2; O00233: PSMD9; NbExp=3; IntAct=EBI-16630231, EBI-750973;
-!- SUBCELLULAR LOCATION: [Isoform 1]: Basolateral cell membrane; Single-
pass type I membrane protein.
-!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=P08887-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P08887-2; Sequence=VSP_001682, VSP_001683;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed in peripheral blood
mononuclear cells and weakly found in urine and serum.
-!- DOMAIN: The two fibronectin type-III-like domains, contained in the N-
terminal part, form together a cytokine-binding domain.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-surface
receptor binding.
-!- PTM: A short soluble form may also be released from the membrane by
proteolysis.
-!- POLYMORPHISM: Genetic variations in IL6R determine soluble IL6R serum
levels [MIM:614689].
-!- POLYMORPHISM: Genetic variations in IL6R define the IL6 serum level
quantitative trait locus [MIM:614752].
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
subfamily. {ECO:0000305}.
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EMBL; X12830; CAA31312.1; -; mRNA.
EMBL; X58298; CAA41231.1; -; mRNA.
EMBL; AK293013; BAF85702.1; -; mRNA.
EMBL; AK312730; BAG35601.1; -; mRNA.
EMBL; AK223582; BAD97302.1; -; mRNA.
EMBL; AL162591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53200.1; -; Genomic_DNA.
EMBL; BC089410; AAH89410.1; -; mRNA.
EMBL; S72848; AAC60635.1; -; mRNA.
CCDS; CCDS1067.1; -. [P08887-1]
CCDS; CCDS1068.1; -. [P08887-2]
PIR; A41242; A41242.
RefSeq; NP_000556.1; NM_000565.3. [P08887-1]
RefSeq; NP_001193795.1; NM_001206866.1.
RefSeq; NP_852004.1; NM_181359.2. [P08887-2]
PDB; 1N26; X-ray; 2.40 A; A=20-344.
PDB; 1N2Q; Model; -; C/D=20-344.
PDB; 1P9M; X-ray; 3.65 A; C=115-315.
PDB; 2ARW; NMR; -; A=212-336.
PDB; 5FUC; X-ray; 2.70 A; C/D=111-322.
PDBsum; 1N26; -.
PDBsum; 1N2Q; -.
PDBsum; 1P9M; -.
PDBsum; 2ARW; -.
PDBsum; 5FUC; -.
SMR; P08887; -.
BioGRID; 109784; 19.
DIP; DIP-162N; -.
ELM; P08887; -.
IntAct; P08887; 18.
MINT; P08887; -.
STRING; 9606.ENSP00000357470; -.
ChEMBL; CHEMBL2364155; -.
DrugBank; DB11767; Sarilumab.
DrugBank; DB06273; Tocilizumab.
DrugCentral; P08887; -.
GuidetoPHARMACOLOGY; 1708; -.
iPTMnet; P08887; -.
PhosphoSitePlus; P08887; -.
BioMuta; IL6R; -.
DMDM; 124343; -.
MassIVE; P08887; -.
MaxQB; P08887; -.
PaxDb; P08887; -.
PeptideAtlas; P08887; -.
PRIDE; P08887; -.
ProteomicsDB; 52171; -. [P08887-1]
ProteomicsDB; 52172; -. [P08887-2]
ABCD; P08887; 121 sequenced antibodies.
Antibodypedia; 20397; 952 antibodies.
DNASU; 3570; -.
Ensembl; ENST00000344086; ENSP00000340589; ENSG00000160712. [P08887-2]
Ensembl; ENST00000368485; ENSP00000357470; ENSG00000160712. [P08887-1]
GeneID; 3570; -.
KEGG; hsa:3570; -.
UCSC; uc001fez.2; human. [P08887-1]
CTD; 3570; -.
DisGeNET; 3570; -.
EuPathDB; HostDB:ENSG00000160712.12; -.
GeneCards; IL6R; -.
HGNC; HGNC:6019; IL6R.
HPA; ENSG00000160712; Tissue enhanced (skeletal).
MalaCards; IL6R; -.
MIM; 147880; gene.
MIM; 614689; phenotype.
MIM; 614752; phenotype.
neXtProt; NX_P08887; -.
OpenTargets; ENSG00000160712; -.
PharmGKB; PA29835; -.
eggNOG; ENOG410II5K; Eukaryota.
eggNOG; ENOG4111XGC; LUCA.
GeneTree; ENSGT00940000161919; -.
HOGENOM; CLU_051451_0_0_1; -.
InParanoid; P08887; -.
KO; K05055; -.
OrthoDB; 783799at2759; -.
PhylomeDB; P08887; -.
TreeFam; TF331210; -.
Reactome; R-HSA-1059683; Interleukin-6 signaling.
Reactome; R-HSA-110056; MAPK3 (ERK1) activation.
Reactome; R-HSA-112411; MAPK1 (ERK2) activation.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
SignaLink; P08887; -.
SIGNOR; P08887; -.
BioGRID-ORCS; 3570; 3 hits in 787 CRISPR screens.
ChiTaRS; IL6R; human.
EvolutionaryTrace; P08887; -.
GeneWiki; Interleukin-6_receptor; -.
GenomeRNAi; 3570; -.
Pharos; P08887; Tclin.
PRO; PR:P08887; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; P08887; protein.
Bgee; ENSG00000160712; Expressed in blood and 217 other tissues.
ExpressionAtlas; P08887; baseline and differential.
Genevisible; P08887; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; IDA:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005896; C:interleukin-6 receptor complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0070119; F:ciliary neurotrophic factor binding; IPI:BHF-UCL.
GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0019981; F:interleukin-6 binding; IPI:BHF-UCL.
GO; GO:0004915; F:interleukin-6 receptor activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0006953; P:acute-phase response; TAS:BHF-UCL.
GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0050829; P:defense response to Gram-negative bacterium; TAS:BHF-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; NAS:BHF-UCL.
GO; GO:0031018; P:endocrine pancreas development; IMP:BHF-UCL.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; TAS:BHF-UCL.
GO; GO:0002384; P:hepatic immune response; TAS:BHF-UCL.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0002548; P:monocyte chemotaxis; IC:BHF-UCL.
GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IDA:BHF-UCL.
GO; GO:0032717; P:negative regulation of interleukin-8 production; NAS:BHF-UCL.
GO; GO:0002446; P:neutrophil mediated immunity; TAS:BHF-UCL.
GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL.
GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IMP:ARUK-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; TAS:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; TAS:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:BHF-UCL.
GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003530; Hematopoietin_rcpt_L_F3_CS.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR015321; TypeI_recpt_CBD.
Pfam; PF00047; ig; 1.
Pfam; PF09240; IL6Ra-bind; 1.
SMART; SM00060; FN3; 1.
SMART; SM00409; IG; 1.
SMART; SM00408; IGc2; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 2.
PROSITE; PS01354; HEMATOPO_REC_L_F3; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1..19
/evidence="ECO:0000269|PubMed:2529343"
CHAIN 20..468
/note="Interleukin-6 receptor subunit alpha"
/id="PRO_0000010895"
TOPO_DOM 20..365
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 366..386
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 387..468
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 26..112
/note="Ig-like C2-type"
DOMAIN 113..217
/note="Fibronectin type-III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 218..316
/note="Fibronectin type-III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
MOTIF 303..307
/note="WSXWS motif"
SITE 245
/note="Not glycosylated"
/evidence="ECO:0000269|PubMed:10066782"
CARBOHYD 55
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:10066782"
CARBOHYD 93
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:10066782"
CARBOHYD 221
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:10066782"
DISULFID 25..193
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10066782"
DISULFID 47..96
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10066782"
DISULFID 121..132
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10066782"
DISULFID 165..176
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10066782"
VAR_SEQ 356..365
/note="VQDSSSVPLP -> GSRRRGSCGL (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8056053"
/id="VSP_001682"
VAR_SEQ 366..468
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8056053"
/id="VSP_001683"
VARIANT 358
/note="D -> A (significantly associated with circulating
levels of IL6 and soluble IL6R; dbSNP:rs2228145)"
/evidence="ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17357077"
/id="VAR_021995"
VARIANT 385
/note="V -> I (in dbSNP:rs2228146)"
/id="VAR_049166"
MUTAGEN 121
/note="C->S: Complete loss of ligand-binding."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 122
/note="F->A: No change of ligand-binding and IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 132
/note="C->A: Complete loss of ligand-binding."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 134
/note="W->L: Complete loss of ligand-binding."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 140
/note="P->G: No change of ligand-binding and IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 153
/note="F->L: No change of ligand-binding and IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 165
/note="C->L: Complete loss of ligand-binding."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 174
/note="F->L: No change of ligand-binding and IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 176
/note="C->A: Complete loss of ligand-binding."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 184
/note="D->T: 30% decrease of ligand-binding and IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 190
/note="V->G: 80% decrease of ligand-binding and no IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 193
/note="C->D: Complete loss of ligand-binding."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 211
/note="C->A: No change of ligand-binding and IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 217
/note="D->V: Complete loss of ligand-binding."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 232
/note="R->S: 30% decrease of ligand-binding and IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 233
/note="W->Q: 30% decrease of ligand-binding and increase of
IL6 signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 254
/note="E->A: 50% decrease of ligand-binding and IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 277
/note="C->D: 30% increase of ligand-binding and 100%
increase in IL6 signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 278
/note="V->N: 50% Decrease of ligand-binding and 50%
increase in IL6 signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 279
/note="I->D: Complete loss of ligand-binding."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 280
/note="H->I: No change of ligand-binding and no IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 281
/note="D->G: 70% decrease of ligand-binding and no IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 285
/note="G->D: 80% decrease of ligand-binding and no IL6
signaling."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 291
/note="Q->K: Complete loss of ligand-binding."
/evidence="ECO:0000269|PubMed:8467812"
MUTAGEN 293
/note="R->G: Complete loss of ligand-binding."
/evidence="ECO:0000269|PubMed:8467812"
CONFLICT 210
/note="G -> D (in Ref. 5; BAD97302)"
/evidence="ECO:0000305"
STRAND 34..37
/evidence="ECO:0000244|PDB:1N26"
STRAND 43..46
/evidence="ECO:0000244|PDB:1N26"
STRAND 56..63
/evidence="ECO:0000244|PDB:1N26"
STRAND 65..68
/evidence="ECO:0000244|PDB:1N26"
STRAND 72..83
/evidence="ECO:0000244|PDB:1N26"
HELIX 88..90
/evidence="ECO:0000244|PDB:1N26"
STRAND 92..101
/evidence="ECO:0000244|PDB:1N26"
STRAND 105..110
/evidence="ECO:0000244|PDB:1N26"
STRAND 120..125
/evidence="ECO:0000244|PDB:1N26"
STRAND 130..134
/evidence="ECO:0000244|PDB:1N26"
STRAND 145..157
/evidence="ECO:0000244|PDB:1N26"
STRAND 159..168
/evidence="ECO:0000244|PDB:1N26"
TURN 169..172
/evidence="ECO:0000244|PDB:1N26"
STRAND 173..178
/evidence="ECO:0000244|PDB:1N26"
STRAND 187..196
/evidence="ECO:0000244|PDB:1N26"
STRAND 199..202
/evidence="ECO:0000244|PDB:1N26"
STRAND 206..209
/evidence="ECO:0000244|PDB:1N26"
TURN 210..212
/evidence="ECO:0000244|PDB:1N26"
STRAND 220..226
/evidence="ECO:0000244|PDB:1N26"
STRAND 234..239
/evidence="ECO:0000244|PDB:1N26"
STRAND 247..249
/evidence="ECO:0000244|PDB:1N26"
STRAND 251..259
/evidence="ECO:0000244|PDB:1N26"
STRAND 266..269
/evidence="ECO:0000244|PDB:1N26"
HELIX 271..273
/evidence="ECO:0000244|PDB:1N26"
STRAND 275..281
/evidence="ECO:0000244|PDB:1N26"
STRAND 288..296
/evidence="ECO:0000244|PDB:1N26"
TURN 297..299
/evidence="ECO:0000244|PDB:1N26"
STRAND 310..312
/evidence="ECO:0000244|PDB:1N26"
SEQUENCE 468 AA; 51548 MW; 62AA239FA14F1B8B CRC64;
MLAVGCALLA ALLAAPGAAL APRRCPAQEV ARGVLTSLPG DSVTLTCPGV EPEDNATVHW
VLRKPAAGSH PSRWAGMGRR LLLRSVQLHD SGNYSCYRAG RPAGTVHLLV DVPPEEPQLS
CFRKSPLSNV VCEWGPRSTP SLTTKAVLLV RKFQNSPAED FQEPCQYSQE SQKFSCQLAV
PEGDSSFYIV SMCVASSVGS KFSKTQTFQG CGILQPDPPA NITVTAVARN PRWLSVTWQD
PHSWNSSFYR LRFELRYRAE RSKTFTTWMV KDLQHHCVIH DAWSGLRHVV QLRAQEEFGQ
GEWSEWSPEA MGTPWTESRS PPAENEVSTP MQALTTNKDD DNILFRDSAN ATSLPVQDSS
SVPLPTFLVA GGSLAFGTLL CIAIVLRFKK TWKLRALKEG KTSMHPPYSL GQLVPERPRP
TPVLVPLISP PVSPSSLGSD NTSSHNRPDA RDPRSPYDIS NTDYFFPR


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Related Genes :
[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)
[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)
[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 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)]
[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)]
[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)]
[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)
[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)]
[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)
[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)]
[Il7r] Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CD antigen CD127)
[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)
[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)
[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)
[IL3RA IL3R] Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (CD antigen CD123)
[IL7R] Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CDw127) (CD antigen CD127)
[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)
[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)
[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)
[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)]
[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] 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)
[Il4r Il4ra] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124)
[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)
[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)
[IL11RA] Interleukin-11 receptor subunit alpha (IL-11 receptor subunit alpha) (IL-11R subunit alpha) (IL-11R-alpha) (IL-11RA)
[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 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)
[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)

Bibliography :