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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.
12-AUG-2020, entry version 229.
RecName: Full=Interleukin-6 receptor subunit alpha {ECO:0000305};
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;
Contains:
RecName: Full=Soluble interleukin-6 receptor subunit alpha {ECO:0000305};
Short=sIL6R {ECO:0000303|PubMed:12794819, ECO:0000303|PubMed:26876177, ECO:0000303|PubMed:28060820};
Flags: Precursor;
Name=IL6R {ECO:0000312|HGNC:HGNC:6019};
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.
PubMed=12794819; DOI=10.1002/art.11143;
Nakahara H., Song J., Sugimoto M., Hagihara K., Kishimoto T., Yoshizaki K.,
Nishimoto N.;
"Anti-interleukin-6 receptor antibody therapy reduces vascular endothelial
growth factor production in rheumatoid arthritis.";
Arthritis Rheum. 48:1521-1529(2003).
[15]
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).
[16]
FUNCTION, AND ACTIVITY REGULATION.
PubMed=21990364; DOI=10.1074/jbc.m111.295758;
Garbers C., Thaiss W., Jones G.W., Waetzig G.H., Lorenzen I., Guilhot F.,
Lissilaa R., Ferlin W.G., Groetzinger J., Jones S.A., Rose-John S.,
Scheller J.;
"Inhibition of classic signaling is a novel function of soluble
glycoprotein 130 (sgp130), which is controlled by the ratio of interleukin
6 and soluble interleukin 6 receptor.";
J. Biol. Chem. 286:42959-42970(2011).
[17]
FUNCTION, AND PROTEOLYTIC CLEAVAGE.
PubMed=26876177; DOI=10.1016/j.celrep.2016.01.053;
Lokau J., Nitz R., Agthe M., Monhasery N., Aparicio-Siegmund S.,
Schumacher N., Wolf J., Moeller-Hackbarth K., Waetzig G.H., Groetzinger J.,
Mueller-Newen G., Rose-John S., Scheller J., Garbers C.;
"Proteolytic Cleavage Governs Interleukin-11 Trans-signaling.";
Cell Rep. 14:1761-1773(2016).
[18]
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).
[19]
FUNCTION, PROTEOLYTIC CLEAVAGE, TISSUE SPECIFICITY (ISOFORM 2),
GLYCOSYLATION AT ASN-55; ASN-93; ASN-221; ASN-245; ASN-350 AND THR-352,
MUTAGENESIS OF ASN-55; THR-57; ASN-93; ASN-221; ASN-245; ASN-350; THR-352;
355-PRO-VAL-356; PRO-355 AND VAL-356, CHARACTERIZATION OF VARIANT ALA-358,
AND SUBCELLULAR LOCATION.
PubMed=28060820; DOI=10.1371/journal.pbio.2000080;
Riethmueller S., Somasundaram P., Ehlers J.C., Hung C.W., Flynn C.M.,
Lokau J., Agthe M., Duesterhoeft S., Zhu Y., Groetzinger J., Lorenzen I.,
Koudelka T., Yamamoto K., Pickhinke U., Wichert R., Becker-Pauly C.,
Raedisch M., Albrecht A., Hessefort M., Stahnke D., Unverzagt C.,
Rose-John S., Tholey A., Garbers C.;
"Proteolytic Origin of the Soluble Human IL-6R In Vivo and a Decisive Role
of N-Glycosylation.";
PLoS Biol. 15:e2000080-e2000080(2017).
[20]
REVIEW ON FUNCTION.
PubMed=30995492; DOI=10.1016/j.immuni.2019.03.026;
Kang S., Tanaka T., Narazaki M., Kishimoto T.;
"Targeting Interleukin-6 Signaling in Clinic.";
Immunity 50:1007-1023(2019).
[21]
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).
[22] {ECO:0000244|PDB:1P9M}
X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS) OF 115-315 IN COMPLEX WITH IL6 AND
IL6ST, AND SUBUNIT.
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).
[23]
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 leads to
the regulation of the immune response, acute-phase reactions and
hematopoiesis (Probable). The interaction with membrane-bound IL6R and
IL6ST stimulates 'classic signaling', the restricted expression of the
IL6R limits classic IL6 signaling to only a few tissues such as the
liver and some cells of the immune system. Whereas the binding of IL6
and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively,
'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on
transmitter cells activate IL6ST receptors on neighboring receiver
cells (Probable). {ECO:0000269|PubMed:28265003,
ECO:0000305|PubMed:30995492}.
-!- FUNCTION: [Isoform 1]: Signaling via the membrane-bound IL6R is mostly
regenerative and anti-inflammatory (Probable). Drives naive CD4(+) T
cells to the Th17 lineage, through 'cluster signaling' by dendritic
cells (By similarity). {ECO:0000250|UniProtKB:P22272,
ECO:0000305|PubMed:30995492}.
-!- FUNCTION: [Isoform 2]: Soluble form of IL6 receptor (sIL6R) that acts
as an agonist of IL6 activity (PubMed:21990364). The IL6:sIL6R complex
(hyper-IL6) binds to IL6ST/gp130 on cell surfaces and induces signaling
also on cells that do not express membrane-bound IL6R in a process
called IL6 'trans-signaling'. sIL6R is causative for the
proinflammatory properties of IL6 and an important player in the
development of chronic inflammatory diseases (PubMed:21990364). In
complex with IL6, is required for induction of VEGF production
(PubMed:12794819). Plays a protective role during liver injury, being
required for maintenance of tissue regeneration (By similarity).
'Trans-signaling' in central nervous system regulates energy and
glucose homeostasis (By similarity). {ECO:0000250|UniProtKB:P22272,
ECO:0000269|PubMed:12794819, ECO:0000269|PubMed:21990364}.
-!- FUNCTION: [Soluble interleukin-6 receptor subunit alpha]: Soluble form
of IL6 receptor (sIL6R) that acts as an agonist of IL6 activity
(PubMed:21990364). The IL6:sIL6R complex (hyper-IL6) binds to
IL6ST/gp130 on cell surfaces and induces signaling also on cells that
do not express membrane-bound IL6R in a process called IL6 'trans-
signaling'. sIL6R is causative for the proinflammatory properties of
IL6 and an important player in the development of chronic inflammatory
diseases (PubMed:21990364). In complex with IL6, is required for
induction of VEGF production (PubMed:12794819). Plays a protective role
during liver injury, being required for maintenance of tissue
regeneration (By similarity). 'Trans-signaling' in central nervous
system regulates energy and glucose homeostasis (By similarity).
{ECO:0000250|UniProtKB:P22272, ECO:0000269|PubMed:12794819,
ECO:0000269|PubMed:21990364}.
-!- ACTIVITY REGULATION: Classic and trans-signaling are both inhibited by
tocilizumab, a humanized monoclonal antibody that blocks interleukin
IL6R signaling. {ECO:0000269|PubMed:21990364}.
-!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R and
IL6ST; first binds to IL6 to associate with the signaling subunit IL6ST
(PubMed:12829785, PubMed:28265003). Interacts (via N-terminal
ectodomain) with SORL1; this interaction may affect IL6-binding to
IL6R, hence decrease IL6 'classic-signaling' (PubMed:28265003).
{ECO:0000269|PubMed:12829785, ECO:0000269|PubMed:28265003}.
-!- SUBUNIT: [Isoform 2]: Also interacts with SORL1; this interaction leads
to soluble IL6R internalization. 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,.
{ECO:0000269|PubMed:28265003}.
-!- SUBUNIT: [Soluble interleukin-6 receptor subunit alpha]: Also interacts
with SORL1; this interaction leads to soluble IL6R internalization. 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,.
{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]: Cell membrane
{ECO:0000250|UniProtKB:P22272}; Single-pass type I membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
{ECO:0000269|PubMed:28060820}.
-!- SUBCELLULAR LOCATION: [Soluble interleukin-6 receptor subunit alpha]:
Secreted {ECO:0000269|PubMed:28060820}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long, mIL6R {ECO:0000303|PubMed:26876177};
IsoId=P08887-1; Sequence=Displayed;
Name=2; Synonyms=Short, sIL6R {ECO:0000303|PubMed:21990364};
IsoId=P08887-2; Sequence=VSP_001682, VSP_001683;
-!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in peripheral blood
mononuclear cells and weakly found in urine and serum. 1%-20% of the
total sIL6R in plasma is generated by alternative splicing
(PubMed:28060820). {ECO:0000269|PubMed:28060820}.
-!- 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 is released from the membrane by proteolysis
(PubMed:26876177). The sIL6R is formed mostly by limited proteolysis of
membrane-bound receptors, a process referred to as ectodomain shedding,
but is also directly secreted from the cells after alternative mRNA
splicing (PubMed:26876177, PubMed:28060820). mIL6R is cleaved by the
proteases ADAM10 and ADAM17 (PubMed:26876177, PubMed:28060820).
{ECO:0000269|PubMed:26876177, ECO:0000269|PubMed:28060820}.
-!- PTM: Glycosylated. Glycosylation is dispensable for transport,
signaling, and cell-surface turnover. Glycosylation at Asn-55 is a
protease-regulatory exosite. Glycosylation is required for ADAM17-
mediated proteolysis. {ECO:0000269|PubMed:28060820}.
-!- 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; -.
GlyGen; P08887; 6 sites, 2 O-linked glycans (2 sites).
iPTMnet; P08887; -.
PhosphoSitePlus; P08887; -.
BioMuta; IL6R; -.
DMDM; 124343; -.
jPOST; P08887; -.
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; 967 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; ENOG502RY0M; Eukaryota.
GeneTree; ENSGT00940000161919; -.
HOGENOM; CLU_051451_0_0_1; -.
InParanoid; P08887; -.
KO; K05055; -.
OrthoDB; 783799at2759; -.
PhylomeDB; P08887; -.
TreeFam; TF331210; -.
PathwayCommons; P08887; -.
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; 4 hits in 876 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 liver and 228 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"
CHAIN 20..355
/note="Soluble interleukin-6 receptor subunit alpha"
/id="PRO_0000450730"
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"
SITE 355..356
/note="Cleavage; by ADAM10 and ADAM17"
/evidence="ECO:0000269|PubMed:28060820"
CARBOHYD 55
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:10066782,
ECO:0000269|PubMed:28060820"
CARBOHYD 93
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:10066782,
ECO:0000269|PubMed:28060820"
CARBOHYD 221
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:10066782,
ECO:0000269|PubMed:28060820"
CARBOHYD 245
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:28060820"
CARBOHYD 350
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:28060820"
CARBOHYD 352
/note="O-linked (GlcNAc) threonine"
/evidence="ECO:0000269|PubMed:28060820"
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; increases cleavage by
ADAM17; dbSNP:rs2228145)"
/evidence="ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17357077, ECO:0000269|PubMed:28060820"
/id="VAR_021995"
VARIANT 385
/note="V -> I (in dbSNP:rs2228146)"
/id="VAR_049166"
MUTAGEN 55
/note="N->A: Strongly induces cleavage and sIL6R levels. No
effect on IL6R signaling; when associated with A-93, A-221,
A-245 and A-350. Loss of cleavage by ADAM17; when
associated with A-93, A-221, A-245 and A-350."
/evidence="ECO:0000269|PubMed:28060820"
MUTAGEN 57
/note="T->A: Strongly induces cleavage and sIL6R levels."
/evidence="ECO:0000269|PubMed:28060820"
MUTAGEN 93
/note="N->A: No effect on cleavage or sIL6R levels. No
effect on IL6R signaling; when associated with A-55, A-221,
A-245 and A-350. Loss of cleavage by ADAM17; when
associated with A-55, A-221, A-245 and A-350."
/evidence="ECO:0000269|PubMed:28060820"
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 221
/note="N->A: No effect on cleavage or sIL6R levels. No
effect on IL6R signaling; when associated with A-55, A-93,
A-245 and A-350. Loss of cleavage by ADAM17; when
associated with A-55, A-93, A-245 and A-350."
/evidence="ECO:0000269|PubMed:28060820"
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 245
/note="N->A: Slightly induces cleavage and sIL6R levels.No
effect on IL6R signaling; when associated with A-55, A-93,
A-221 and A-350. Loss of cleavage by ADAM17; when
associated with A-55, A-93, A-221 and A-350."
/evidence="ECO:0000269|PubMed:28060820"
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"
MUTAGEN 350
/note="N->A: No effect on IL6R signaling; when associated
with A-55, A-93, A-221 and A-245. Loss of cleavage by
ADAM17; when associated with A-55, A-93, A-221 and A-245."
/evidence="ECO:0000269|PubMed:28060820"
MUTAGEN 352
/note="T->A: No effect on IL6R signaling."
/evidence="ECO:0000269|PubMed:28060820"
MUTAGEN 355..356
/note="PV->IE: Abolishes cleavage by ADAM17."
/evidence="ECO:0000269|PubMed:28060820"
MUTAGEN 355
/note="P->I,D: Reduces cleavage by ADAM17."
/evidence="ECO:0000269|PubMed:28060820"
MUTAGEN 356
/note="V->E,G: Abolishes cleavage by ADAM17."
/evidence="ECO:0000269|PubMed:28060820"
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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U2031r CLIA kit IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Rat,Rattus norvegicus 96T
U1815r CLIA kit IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Rat,Rattus norvegicus 96T
E1815r ELISA IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Rat,Rattus norvegicus 96T
U1815m CLIA kit IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Mouse,Mus musculus 96T
E2031m ELISA kit IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Mouse,Mus musculus 96T
U2031m CLIA kit IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Mouse,Mus musculus 96T
U1815r CLIA IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Rat,Rattus norvegicus 96T
U2031r CLIA IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Rat,Rattus norvegicus 96T
Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP1566: Citrate cycle (TCA cycle)
WP566: canonical wnt - zebrafish
WP1963: The effect of Glucocorticoids on target gene expression
WP2272: Pathogenic Escherichia coli infection
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP1584: Type II diabetes mellitus
WP1904: RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways
WP1003: Ovarian Infertility Genes
WP537: Translation Factors
WP1369: TNF-alpha NF-kB Signaling Pathway
WP231: TNF alpha Signaling Pathway
WP811: TNF-alpha NF-kB Signaling Pathway
WP1225: estrogen signalling
WP34: Ovarian Infertility Genes
WP1835: Interferon alpha/beta signaling
WP246: TNF-alpha NF-kB Signaling Pathway
WP2100: AhR pathway
WP402: ERK1 - ERK2 MAPK cascade
WP215: noncanonical wnt pathway
WP773: Ovarian Infertility Genes
WP1571: EBV LMP1 signaling
WP273: Ovarian Infertility Genes

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) [Cleaved into: Soluble interleukin-6 receptor subunit alpha (sIL6R)]
[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)
[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)]
[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)
[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)
[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)
[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 :