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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)

 IL6RB_HUMAN             Reviewed;         918 AA.
P40189; A0N0L4; Q5FC04; Q9UQ41;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
17-JUN-2020, entry version 226.
RecName: Full=Interleukin-6 receptor subunit beta;
Short=IL-6 receptor subunit beta;
Short=IL-6R subunit beta;
Short=IL-6R-beta;
Short=IL-6RB;
AltName: Full=CDw130;
AltName: Full=Interleukin-6 signal transducer;
AltName: Full=Membrane glycoprotein 130;
Short=gp130;
AltName: Full=Oncostatin-M receptor subunit alpha;
AltName: CD_antigen=CD130;
Flags: Precursor;
Name=IL6ST;
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), FUNCTION, TISSUE SPECIFICITY, AND
VARIANT VAL-8.
TISSUE=Myeloma, and Placenta;
PubMed=2261637; DOI=10.1016/0092-8674(90)90411-7;
Hibi M., Murakami M., Saito M., Hirano T., Taga T., Kishimoto T.;
"Molecular cloning and expression of an IL-6 signal transducer, gp130.";
Cell 63:1149-1157(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-8.
TISSUE=Synovium;
PubMed=10880057; DOI=10.1172/jci7479;
Tanaka M., Kishimura M., Ozaki S., Osakada F., Hashimoto H., Okubo M.,
Murakami M., Nakao K.;
"Cloning of novel soluble gp130 and detection of its neutralizing
autoantibodies in rheumatoid arthritis.";
J. Clin. Invest. 106:137-144(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Hayashi A., Sameshima E., Tabata Y., Iida K., Mitsuyama M., Kanai S.,
Furuya T., Saito T.;
"IL6ST mRNA, nirs splice variant 4.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-43;
ASN-83; ASN-131; ASN-157; ASN-227; ASN-379; ASN-383; ASN-553 AND ASN-564.
PubMed=11098061; DOI=10.1074/jbc.m009979200;
Moritz R.L., Hall N.E., Connolly L.M., Simpson R.J.;
"Determination of the disulfide structure and N-glycosylation sites of the
extracellular domain of the human signal transducer gp130.";
J. Biol. Chem. 276:8244-8253(2001).
[8]
SUBUNIT, AND INDUCTION.
PubMed=8999038; DOI=10.1074/jbc.271.51.32635;
Mosley B., De Imus C., Friend D., Boiani N., Thoma B., Park L.S.,
Cosman D.;
"Dual oncostatin M (OSM) receptors. Cloning and characterization of an
alternative signaling subunit conferring OSM-specific receptor
activation.";
J. Biol. Chem. 271:32635-32643(1996).
[9]
INTERACTION WITH HCK.
PubMed=9406996;
Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S., von Bubnoff N.,
de Vos G., Druker B.J., Yasukawa K., Griffin J.D., Emmerich B.;
"Signal transduction of interleukin-6 involves tyrosine phosphorylation of
multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck,
and Lyn in multiple myeloma cell lines.";
Exp. Hematol. 25:1367-1377(1997).
[10]
PHOSPHORYLATION AT SER-782, MUTAGENESIS OF SER-782, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=10811661; DOI=10.1074/jbc.m907658199;
Gibson R.M., Schiemann W.P., Prichard L.B., Reno J.M., Ericsson L.H.,
Nathanson N.M.;
"Phosphorylation of human gp130 at Ser-782 adjacent to the di-leucine
internalization motif. Effects on expression and signaling.";
J. Biol. Chem. 275:22574-22582(2000).
[11]
INTERACTION WITH HERPES VIRUS-8/HHV-8 PROTEIN VIL6 (MICROBIAL INFECTION).
PubMed=11238858; DOI=10.1128/jvi.75.7.3325-3334.2001;
Li H., Wang H., Nicholas J.;
"Detection of direct binding of human herpesvirus 8-encoded interleukin-6
(vIL-6) to both gp130 and IL-6 receptor (IL-6R) and identification of amino
acid residues of vIL-6 important for IL-6R-dependent and -independent
signaling.";
J. Virol. 75:3325-3334(2001).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-379 AND ASN-383.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227 AND ASN-390.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple
enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[17]
GLYCOSYLATION AT ASN-390.
PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core fucosylated
glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=19915009; DOI=10.1074/jbc.m109.075952;
Waetzig G.H., Chalaris A., Rosenstiel P., Suthaus J., Holland C., Karl N.,
Valles Uriarte L., Till A., Scheller J., Grotzinger J., Schreiber S.,
Rose-John S., Seegert D.;
"N-linked glycosylation is essential for the stability but not the
signaling function of the interleukin-6 signal transducer glycoprotein
130.";
J. Biol. Chem. 285:1781-1789(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
FUNCTION, AND MUTAGENESIS OF CYS-172; 186-TYR--TYR-190; VAL-189; TYR-190;
ASP-215 AND VAL-252.
PubMed=23294003; DOI=10.1042/bj20121660;
Schutt A., Zacharias M., Schneider N., Horn S., Grotzinger J.,
Rose-John S., Schmidt-Arras D.;
"gp130 activation is regulated by D2-D3 interdomain connectivity.";
Biochem. J. 450:487-496(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667 AND SER-839, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661 AND SER-667, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 122-325.
PubMed=9501088; DOI=10.1093/emboj/17.6.1665;
Bravo J., Staunton D., Heath J.K., Jones E.Y.;
"Crystal structure of a cytokine-binding region of gp130.";
EMBO J. 17:1665-1674(1998).
[24]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-325 IN COMPLEX WITH HERPES
VIRUS-8/HHV-8 PROTEIN VIL6 (MICROBIAL INFECTION), SUBUNIT, AND
GLYCOSYLATION.
PubMed=11251120; DOI=10.1126/science.1058308;
Chow D.-C., He X.-L., Snow A.L., Rose-John S., Garcia K.C.;
"Structure of an extracellular gp130 cytokine receptor signaling complex.";
Science 291:2150-2155(2001).
[25]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 123-323 IN COMPLEX WITH LIF.
PubMed=14527405; DOI=10.1016/s1097-2765(03)00365-4;
Boulanger M.J., Bankovich A.J., Kortemme T., Baker D., Garcia K.C.;
"Convergent mechanisms for recognition of divergent cytokines by the shared
signaling receptor gp130.";
Mol. Cell 12:577-589(2003).
[26]
X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS) OF 23-321 IN COMPLEX WITH IL6 AND
IL6R, 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).
[27]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-612, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-43; ASN-83; ASN-227; ASN-383 AND ASN-553.
PubMed=20489211; DOI=10.1074/jbc.c110.129502;
Xu Y., Kershaw N.J., Luo C.S., Soo P., Pocock M.J., Czabotar P.E.,
Hilton D.J., Nicola N.A., Garrett T.P., Zhang J.G.;
"Crystal structure of the entire ectodomain of gp130: insights into the
molecular assembly of the tall cytokine receptor complexes.";
J. Biol. Chem. 285:21214-21218(2010).
[28]
VARIANT [LARGE SCALE ANALYSIS] ILE-415.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
[29]
VARIANT GLY-200.
PubMed=25242236; DOI=10.1016/j.cancergen.2014.07.003;
Sun L., Sui L., Cong X., Ma K., Ma X., Huang Y., Fan C., Fu X., Ma K.;
"Low incidence of IL6ST (gp130) mutations in exon 6 in lung cancer of a
Chinese cohort.";
Cancer Genet. 207:291-298(2014).
[30]
VARIANT ARG-148, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=24629561; DOI=10.1016/j.metabol.2014.02.005;
Wonnerth A., Katsaros K.M., Krychtiuk K.A., Speidl W.S., Kaun C.,
Thaler K., Huber K., Wojta J., Maurer G., Seljeflot I., Arnesen H.,
Weiss T.W.;
"Glycoprotein 130 polymorphism predicts soluble glycoprotein 130 levels.";
Metabolism 63:647-653(2014).
[31]
VARIANT HIES4 TYR-404, INVOLVEMENT IN HIES4, FUNCTION, AND CHARACTERIZATION
OF VARIANT HIES4 TYR-404.
PubMed=28747427; DOI=10.1084/jem.20161810;
Schwerd T., Twigg S.R.F., Aschenbrenner D., Manrique S., Miller K.A.,
Taylor I.B., Capitani M., McGowan S.J., Sweeney E., Weber A., Chen L.,
Bowness P., Riordan A., Cant A., Freeman A.F., Milner J.D., Holland S.M.,
Frede N., Mueller M., Schmidt-Arras D., Grimbacher B., Wall S.A.,
Jones E.Y., Wilkie A.O.M., Uhlig H.H.;
"A biallelic mutation in IL6ST encoding the GP130 co-receptor causes
immunodeficiency and craniosynostosis.";
J. Exp. Med. 214:2547-2562(2017).
[32]
VARIANT HIES4 LEU-498, INVOLVEMENT IN HIES4, FUNCTION, AND CHARACTERIZATION
OF VARIANT HIES4 LEU-498.
PubMed=30309848; DOI=10.3324/haematol.2018.194233;
Shahin T., Aschenbrenner D., Cagdas D., Bal S.K., Conde C.D., Garncarz W.,
Medgyesi D., Schwerd T., Karaatmaca B., Cetinkaya P.G., Esenboga S.,
Twigg S.R.F., Cant A., Wilkie A.O.M., Tezcan I., Uhlig H.H., Boztug K.;
"Selective loss of function variants in IL6ST cause Hyper-IgE syndrome with
distinct impairments of T-cell phenotype and function.";
Haematologica 104:609-621(2019).
-!- FUNCTION: Signal-transducing molecule. The receptor systems for IL6,
LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for initiating
signal transmission. Binding of IL6 to IL6R induces IL6ST
homodimerization and formation of a high-affinity receptor complex,
which activates Janus kinases (PubMed:2261637). That causes
phosphorylation of IL6ST tyrosine residues which in turn activates
STAT3 (PubMed:19915009, PubMed:23294003). Mediates signals which
regulate immune response, hematopoiesis, pain control and bone
metabolism (By similarity). Has a role in embryonic development (By
similarity). Does not bind IL6 (PubMed:2261637). Essential for survival
of motor and sensory neurons and for differentiation of astrocytes (By
similarity). Required for expression of TRPA1 in nociceptive neurons
(By similarity). Required for the maintenance of PTH1R expression in
the osteoblast lineage and for the stimulation of PTH-induced
osteoblast differentiation (By similarity). Required for normal
trabecular bone mass and cortical bone composition (By similarity).
{ECO:0000250|UniProtKB:Q00560, ECO:0000269|PubMed:19915009,
ECO:0000269|PubMed:2261637, ECO:0000269|PubMed:23294003,
ECO:0000269|PubMed:28747427, ECO:0000269|PubMed:30309848}.
-!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R and
IL6ST (PubMed:12829785). Forms heterodimers composed of LIFR and IL6ST
(type I OSM receptor) which are activated by LIF and OSM
(PubMed:8999038). Also forms heterodimers composed of OSMR and IL6ST
(type II receptor) which are activated by OSM but not by LIF
(PubMed:8999038). Homodimer. Interacts with HCK (PubMed:9406996).
Interacts with INPP5D/SHIP1 (By similarity).
{ECO:0000250|UniProtKB:Q00560, ECO:0000269|PubMed:12829785,
ECO:0000269|PubMed:14527405, ECO:0000269|PubMed:8999038,
ECO:0000269|PubMed:9406996}.
-!- SUBUNIT: (Microbial infection) The homodimer binds two molecules of
herpes virus 8/HHV-8 protein vIL-6. {ECO:0000269|PubMed:11238858,
ECO:0000269|PubMed:11251120}.
-!- INTERACTION:
P40189; P26441: CNTF; NbExp=10; IntAct=EBI-1030834, EBI-1050897;
P40189; P40189: IL6ST; NbExp=2; IntAct=EBI-1030834, EBI-1030834;
P40189; Q9NZI2-2: KCNIP1; NbExp=3; IntAct=EBI-1030834, EBI-22452746;
P40189; Q9Y2W7: KCNIP3; NbExp=7; IntAct=EBI-1030834, EBI-751501;
P40189; P15018: LIF; NbExp=2; IntAct=EBI-1030834, EBI-1037189;
P40189; P43364: MAGEA11; NbExp=3; IntAct=EBI-1030834, EBI-739552;
P40189; P13725: OSM; NbExp=2; IntAct=EBI-1030834, EBI-6595724;
P40189; Q99650: OSMR; NbExp=2; IntAct=EBI-1030834, EBI-2804080;
P40189; O43765: SGTA; NbExp=3; IntAct=EBI-1030834, EBI-347996;
P40189; Q96EQ0: SGTB; NbExp=4; IntAct=EBI-1030834, EBI-744081;
P40189; Q2HRC7: K2; Xeno; NbExp=2; IntAct=EBI-1030834, EBI-9007403;
P40189; P42227: Stat3; Xeno; NbExp=4; IntAct=EBI-1030834, EBI-602878;
P40189-1; P23458: JAK1; NbExp=3; IntAct=EBI-15742214, EBI-1383438;
-!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
{ECO:0000269|PubMed:19915009}; Single-pass type I membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
{ECO:0000269|PubMed:24629561}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P40189-1; Sequence=Displayed;
Name=2; Synonyms=GP130-RAPS;
IsoId=P40189-2; Sequence=VSP_001684, VSP_001685;
Name=3;
IsoId=P40189-3; Sequence=VSP_043716;
-!- TISSUE SPECIFICITY: Found in all the tissues and cell lines examined
(PubMed:2261637). Expression not restricted to IL6 responsive cells
(PubMed:2261637). Expressed in blood serum (at protein level)
(PubMed:24629561). {ECO:0000269|PubMed:2261637,
ECO:0000269|PubMed:24629561}.
-!- INDUCTION: LIF and OSM activate the type I OSM receptor while only OSM
can activate the type II OSM receptor. {ECO:0000269|PubMed:8999038}.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-surface
receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- PTM: Phosphorylation of Ser-782 down-regulates cell surface expression.
{ECO:0000269|PubMed:10811661}.
-!- PTM: Heavily N-glycosylated (PubMed:11098061, PubMed:16335952,
PubMed:19159218, PubMed:19139490, PubMed:11251120). Glycosylation is
required for protein stability and localization in plasma membrane but
not for ligand binding (PubMed:19915009). {ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:11251120, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19915009}.
-!- DISEASE: Hyper-IgE recurrent infection syndrome 4, autosomal recessive
(HIES4) [MIM:618523]: An immunologic disorder characterized by
recurrent infections, mainly affecting the respiratory tract, skin and
eye, and skeletal abnormalities including craniosynostosis and
scoliosis. Immunologic workup shows increased serum IgE, intermittent
eosinophilia, impaired development of certain B- and T-cell
populations, as well as impaired acute-phase response. Disease onset is
in early childhood. {ECO:0000269|PubMed:28747427,
ECO:0000269|PubMed:30309848}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
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EMBL; M57230; AAA59155.1; -; mRNA.
EMBL; AB015706; BAA78112.1; -; mRNA.
EMBL; AB102802; BAD89393.1; -; mRNA.
EMBL; EF064722; ABK41905.1; -; Genomic_DNA.
EMBL; AC008914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC016596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471123; EAW54936.1; -; Genomic_DNA.
CCDS; CCDS3971.1; -. [P40189-1]
CCDS; CCDS47209.1; -. [P40189-2]
CCDS; CCDS54856.1; -. [P40189-3]
PIR; A36337; A36337.
RefSeq; NP_001177910.1; NM_001190981.1. [P40189-3]
RefSeq; NP_002175.2; NM_002184.3. [P40189-1]
RefSeq; NP_786943.1; NM_175767.2. [P40189-2]
PDB; 1BJ8; NMR; -; A=219-325.
PDB; 1BQU; X-ray; 2.00 A; A/B=122-333.
PDB; 1I1R; X-ray; 2.40 A; A=23-325.
PDB; 1N2Q; Model; -; A/B=23-324.
PDB; 1P9M; X-ray; 3.65 A; A=23-321.
PDB; 1PVH; X-ray; 2.50 A; A/C=123-323.
PDB; 3L5H; X-ray; 3.60 A; A=24-612.
PDB; 3L5I; X-ray; 1.90 A; A=323-612.
PDB; 3L5J; X-ray; 3.04 A; A/B=323-610.
PDBsum; 1BJ8; -.
PDBsum; 1BQU; -.
PDBsum; 1I1R; -.
PDBsum; 1N2Q; -.
PDBsum; 1P9M; -.
PDBsum; 1PVH; -.
PDBsum; 3L5H; -.
PDBsum; 3L5I; -.
PDBsum; 3L5J; -.
SMR; P40189; -.
BioGRID; 109786; 36.
CORUM; P40189; -.
DIP; DIP-95N; -.
IntAct; P40189; 23.
MINT; P40189; -.
STRING; 9606.ENSP00000370698; -.
BindingDB; P40189; -.
ChEMBL; CHEMBL3124734; -.
DrugCentral; P40189; -.
GuidetoPHARMACOLOGY; 2317; -.
GlyConnect; 649; -.
iPTMnet; P40189; -.
PhosphoSitePlus; P40189; -.
SwissPalm; P40189; -.
UniCarbKB; P40189; -.
BioMuta; IL6ST; -.
DMDM; 215273999; -.
EPD; P40189; -.
jPOST; P40189; -.
MassIVE; P40189; -.
MaxQB; P40189; -.
PaxDb; P40189; -.
PeptideAtlas; P40189; -.
PRIDE; P40189; -.
ProteomicsDB; 55338; -. [P40189-1]
ProteomicsDB; 55339; -. [P40189-2]
ProteomicsDB; 55340; -. [P40189-3]
Antibodypedia; 2448; 744 antibodies.
DNASU; 3572; -.
Ensembl; ENST00000336909; ENSP00000338799; ENSG00000134352. [P40189-1]
Ensembl; ENST00000381287; ENSP00000370687; ENSG00000134352. [P40189-2]
Ensembl; ENST00000381294; ENSP00000370694; ENSG00000134352. [P40189-3]
Ensembl; ENST00000381298; ENSP00000370698; ENSG00000134352. [P40189-1]
Ensembl; ENST00000502326; ENSP00000462158; ENSG00000134352. [P40189-1]
Ensembl; ENST00000522633; ENSP00000435399; ENSG00000134352. [P40189-2]
GeneID; 3572; -.
KEGG; hsa:3572; -.
UCSC; uc003jqq.4; human. [P40189-1]
CTD; 3572; -.
DisGeNET; 3572; -.
EuPathDB; HostDB:ENSG00000134352.19; -.
GeneCards; IL6ST; -.
HGNC; HGNC:6021; IL6ST.
HPA; ENSG00000134352; Low tissue specificity.
MalaCards; IL6ST; -.
MIM; 600694; gene.
MIM; 618523; phenotype.
neXtProt; NX_P40189; -.
OpenTargets; ENSG00000134352; -.
PharmGKB; PA29837; -.
eggNOG; ENOG410IF1N; Eukaryota.
eggNOG; ENOG410YNQ4; LUCA.
GeneTree; ENSGT00940000159608; -.
HOGENOM; CLU_017990_0_0_1; -.
InParanoid; P40189; -.
KO; K05060; -.
OMA; YLITVYP; -.
PhylomeDB; P40189; -.
TreeFam; TF338122; -.
Reactome; R-HSA-1059683; Interleukin-6 signaling.
Reactome; R-HSA-110056; MAPK3 (ERK1) activation. [P40189-1]
Reactome; R-HSA-112411; MAPK1 (ERK2) activation. [P40189-1]
Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions.
Reactome; R-HSA-8984722; Interleukin-35 Signalling.
Reactome; R-HSA-9020956; Interleukin-27 signaling.
SignaLink; P40189; -.
SIGNOR; P40189; -.
BioGRID-ORCS; 3572; 19 hits in 795 CRISPR screens.
ChiTaRS; IL6ST; human.
EvolutionaryTrace; P40189; -.
GeneWiki; Glycoprotein_130; -.
GenomeRNAi; 3572; -.
Pharos; P40189; Tclin.
PRO; PR:P40189; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P40189; protein.
Bgee; ENSG00000134352; Expressed in female gonad and 247 other tissues.
ExpressionAtlas; P40189; baseline and differential.
Genevisible; P40189; HS.
GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; IDA:BHF-UCL.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005896; C:interleukin-6 receptor complex; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005900; C:oncostatin-M receptor complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; IDA:BHF-UCL.
GO; GO:0005127; F:ciliary neurotrophic factor receptor 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:0019838; F:growth factor binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019970; F:interleukin-11 binding; IEA:Ensembl.
GO; GO:0004921; F:interleukin-11 receptor activity; IEA:Ensembl.
GO; GO:0045509; F:interleukin-27 receptor activity; IC:BHF-UCL.
GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0005977; P:glycogen metabolic process; IEA:Ensembl.
GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0070757; P:interleukin-35-mediated signaling pathway; TAS:Reactome.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; IDA:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:BHF-UCL.
GO; GO:0070104; P:negative regulation of interleukin-6-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0002675; P:positive regulation of acute inflammatory response; IC:BHF-UCL.
GO; GO:0002821; P:positive regulation of adaptive immune response; IC:BHF-UCL.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IEA:Ensembl.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; TAS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:BHF-UCL.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; TAS:BHF-UCL.
GO; GO:0008593; P:regulation of Notch signaling pathway; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR010457; IgC2-like_lig-bd.
InterPro; IPR015321; TypeI_recpt_CBD.
Pfam; PF00041; fn3; 2.
Pfam; PF09240; IL6Ra-bind; 1.
Pfam; PF06328; Lep_receptor_Ig; 1.
SMART; SM00060; FN3; 5.
SUPFAM; SSF49265; SSF49265; 5.
PROSITE; PS50853; FN3; 4.
PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane;
Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein;
Host-virus interaction; Immunoglobulin domain; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1..22
CHAIN 23..918
/note="Interleukin-6 receptor subunit beta"
/id="PRO_0000010899"
TOPO_DOM 23..619
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 620..641
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 642..918
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 26..120
/note="Ig-like C2-type"
DOMAIN 125..216
/note="Fibronectin type-III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 224..324
/note="Fibronectin type-III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 329..424
/note="Fibronectin type-III 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 426..517
/note="Fibronectin type-III 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 518..613
/note="Fibronectin type-III 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
MOTIF 310..314
/note="WSXWS motif"
MOTIF 651..659
/note="Box 1 motif"
COMPBIAS 725..755
/note="Ser-rich"
MOD_RES 661
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 667
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 782
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:10811661"
MOD_RES 789
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q00560"
MOD_RES 829
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983"
MOD_RES 839
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
CARBOHYD 43
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211"
CARBOHYD 83
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211"
CARBOHYD 131
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:11098061"
CARBOHYD 157
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:11098061"
CARBOHYD 227
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20489211"
CARBOHYD 379
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:16335952"
CARBOHYD 383
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:20489211"
CARBOHYD 390
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218"
CARBOHYD 553
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211"
CARBOHYD 564
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:11098061"
DISULFID 28..54
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211"
DISULFID 48..103
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211"
DISULFID 134..144
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211"
DISULFID 172..182
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211"
DISULFID 458..466
/evidence="ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211"
VAR_SEQ 325..329
/note="RPSKA -> NIASF (in isoform 2)"
/evidence="ECO:0000303|PubMed:10880057"
/id="VSP_001684"
VAR_SEQ 330..918
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:10880057"
/id="VSP_001685"
VAR_SEQ 423..483
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|Ref.3"
/id="VSP_043716"
VARIANT 8
/note="L -> V (in dbSNP:rs1063560)"
/evidence="ECO:0000269|PubMed:10880057,
ECO:0000269|PubMed:2261637"
/id="VAR_047782"
VARIANT 148
/note="G -> R (polymorphism; associated with increased
levels of soluble IL6RB in blood serum; dbSNP:rs2228044)"
/evidence="ECO:0000269|PubMed:24629561"
/id="VAR_047783"
VARIANT 200
/note="A -> G (found in patient with lung cancer; unknown
pathological significance; dbSNP:rs199905033)"
/evidence="ECO:0000269|PubMed:25242236"
/id="VAR_074654"
VARIANT 397
/note="L -> V (in dbSNP:rs2228043)"
/id="VAR_047784"
VARIANT 404
/note="N -> Y (in HIES4; results in defective cytokine-
mediated signaling pathway)"
/evidence="ECO:0000269|PubMed:28747427"
/id="VAR_083197"
VARIANT 415
/note="T -> I (in a colorectal cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036165"
VARIANT 454
/note="I -> T (in dbSNP:rs2228046)"
/id="VAR_047785"
VARIANT 498
/note="P -> L (in HIES4; results in defective cytokine-
mediated signaling pathway)"
/evidence="ECO:0000269|PubMed:30309848"
/id="VAR_083198"
VARIANT 499
/note="V -> I (in dbSNP:rs34417936)"
/id="VAR_047786"
MUTAGEN 172
/note="C->S: Induces ligand-independent activation."
/evidence="ECO:0000269|PubMed:23294003"
MUTAGEN 186..190
/note="Missing: Induces ligand-independent activation."
/evidence="ECO:0000269|PubMed:23294003"
MUTAGEN 189
/note="V->G: Does not induce ligand-independent
activation."
/evidence="ECO:0000269|PubMed:23294003"
MUTAGEN 190
/note="Y->G: Does not induce ligand-independent
activation."
/evidence="ECO:0000269|PubMed:23294003"
MUTAGEN 215
/note="D->G: Induces ligand-independent activation."
/evidence="ECO:0000269|PubMed:23294003"
MUTAGEN 252
/note="V->G: Induces ligand-independent activation."
/evidence="ECO:0000269|PubMed:23294003"
MUTAGEN 782
/note="S->A: Increases cell surface expression."
/evidence="ECO:0000269|PubMed:10811661"
STRAND 28..35
/evidence="ECO:0000244|PDB:1I1R"
STRAND 37..39
/evidence="ECO:0000244|PDB:1I1R"
STRAND 44..50
/evidence="ECO:0000244|PDB:1I1R"
HELIX 52..58
/evidence="ECO:0000244|PDB:1I1R"
HELIX 62..64
/evidence="ECO:0000244|PDB:1I1R"
STRAND 65..69
/evidence="ECO:0000244|PDB:1I1R"
HELIX 76..78
/evidence="ECO:0000244|PDB:1I1R"
STRAND 80..83
/evidence="ECO:0000244|PDB:1I1R"
STRAND 86..91
/evidence="ECO:0000244|PDB:1I1R"
STRAND 97..107
/evidence="ECO:0000244|PDB:1I1R"
TURN 108..110
/evidence="ECO:0000244|PDB:1I1R"
STRAND 111..123
/evidence="ECO:0000244|PDB:1I1R"
STRAND 130..137
/evidence="ECO:0000244|PDB:1BQU"
STRAND 143..147
/evidence="ECO:0000244|PDB:1BQU"
STRAND 157..164
/evidence="ECO:0000244|PDB:1BQU"
STRAND 176..178
/evidence="ECO:0000244|PDB:1PVH"
STRAND 181..183
/evidence="ECO:0000244|PDB:1BQU"
STRAND 194..202
/evidence="ECO:0000244|PDB:1BQU"
STRAND 205..208
/evidence="ECO:0000244|PDB:1BQU"
STRAND 212..214
/evidence="ECO:0000244|PDB:1BQU"
HELIX 216..218
/evidence="ECO:0000244|PDB:1BQU"
STRAND 219..221
/evidence="ECO:0000244|PDB:1BQU"
STRAND 226..231
/evidence="ECO:0000244|PDB:1BQU"
STRAND 234..238
/evidence="ECO:0000244|PDB:1I1R"
STRAND 240..245
/evidence="ECO:0000244|PDB:1BQU"
HELIX 248..251
/evidence="ECO:0000244|PDB:1BQU"
STRAND 255..263
/evidence="ECO:0000244|PDB:1BQU"
HELIX 274..277
/evidence="ECO:0000244|PDB:1BQU"
STRAND 282..286
/evidence="ECO:0000244|PDB:1BQU"
STRAND 291..303
/evidence="ECO:0000244|PDB:1BQU"
STRAND 317..321
/evidence="ECO:0000244|PDB:1BQU"
HELIX 325..331
/evidence="ECO:0000244|PDB:1BQU"
STRAND 332..338
/evidence="ECO:0000244|PDB:3L5I"
STRAND 345..351
/evidence="ECO:0000244|PDB:3L5I"
HELIX 356..359
/evidence="ECO:0000244|PDB:3L5I"
STRAND 363..372
/evidence="ECO:0000244|PDB:3L5I"
STRAND 378..391
/evidence="ECO:0000244|PDB:3L5I"
STRAND 396..406
/evidence="ECO:0000244|PDB:3L5I"
STRAND 412..416
/evidence="ECO:0000244|PDB:3L5I"
STRAND 428..435
/evidence="ECO:0000244|PDB:3L5I"
STRAND 438..444
/evidence="ECO:0000244|PDB:3L5I"
STRAND 452..460
/evidence="ECO:0000244|PDB:3L5I"
STRAND 462..464
/evidence="ECO:0000244|PDB:3L5I"
STRAND 469..474
/evidence="ECO:0000244|PDB:3L5I"
STRAND 478..481
/evidence="ECO:0000244|PDB:3L5I"
STRAND 491..500
/evidence="ECO:0000244|PDB:3L5I"
STRAND 508..515
/evidence="ECO:0000244|PDB:3L5I"
STRAND 525..530
/evidence="ECO:0000244|PDB:3L5I"
STRAND 535..539
/evidence="ECO:0000244|PDB:3L5I"
HELIX 544..547
/evidence="ECO:0000244|PDB:3L5I"
STRAND 553..560
/evidence="ECO:0000244|PDB:3L5I"
STRAND 566..571
/evidence="ECO:0000244|PDB:3L5I"
STRAND 575..579
/evidence="ECO:0000244|PDB:3L5I"
STRAND 587..596
/evidence="ECO:0000244|PDB:3L5I"
STRAND 599..602
/evidence="ECO:0000244|PDB:3L5I"
STRAND 606..609
/evidence="ECO:0000244|PDB:3L5I"
SEQUENCE 918 AA; 103537 MW; 6510A4409FFCF08C CRC64;
MLTLQTWLVQ ALFIFLTTES TGELLDPCGY ISPESPVVQL HSNFTAVCVL KEKCMDYFHV
NANYIVWKTN HFTIPKEQYT IINRTASSVT FTDIASLNIQ LTCNILTFGQ LEQNVYGITI
ISGLPPEKPK NLSCIVNEGK KMRCEWDGGR ETHLETNFTL KSEWATHKFA DCKAKRDTPT
SCTVDYSTVY FVNIEVWVEA ENALGKVTSD HINFDPVYKV KPNPPHNLSV INSEELSSIL
KLTWTNPSIK SVIILKYNIQ YRTKDASTWS QIPPEDTAST RSSFTVQDLK PFTEYVFRIR
CMKEDGKGYW SDWSEEASGI TYEDRPSKAP SFWYKIDPSH TQGYRTVQLV WKTLPPFEAN
GKILDYEVTL TRWKSHLQNY TVNATKLTVN LTNDRYLATL TVRNLVGKSD AAVLTIPACD
FQATHPVMDL KAFPKDNMLW VEWTTPRESV KKYILEWCVL SDKAPCITDW QQEDGTVHRT
YLRGNLAESK CYLITVTPVY ADGPGSPESI KAYLKQAPPS KGPTVRTKKV GKNEAVLEWD
QLPVDVQNGF IRNYTIFYRT IIGNETAVNV DSSHTEYTLS SLTSDTLYMV RMAAYTDEGG
KDGPEFTFTT PKFAQGEIEA IVVPVCLAFL LTTLLGVLFC FNKRDLIKKH IWPNVPDPSK
SHIAQWSPHT PPRHNFNSKD QMYSDGNFTD VSVVEIEAND KKPFPEDLKS LDLFKKEKIN
TEGHSSGIGG SSCMSSSRPS ISSSDENESS QNTSSTVQYS TVVHSGYRHQ VPSVQVFSRS
ESTQPLLDSE ERPEDLQLVD HVDGGDGILP RQQYFKQNCS QHESSPDISH FERSKQVSSV
NEEDFVRLKQ QISDHISQSC GSGQMKMFQE VSAADAFGPG TEGQVERFET VGMEAATDEG
MPKSYLPQTV RQGGYMPQ


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E0046h ELISA kit CDw130,gp130,Homo sapiens,Human,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,IL6ST,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprote 96T
U0046r CLIA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Oncostatin-M receptor sub 96T
E0046r ELISA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Oncostatin-M receptor su 96T
20-272-190538 CD130 ( gp130 ) - Mouse monoclonal [B - T2] to CD130 ( gp130 ); IL-6R-beta; Interleukin-6 signal transducer; Membrane glycoprotein 130; gp130; Oncostatin-M receptor alpha subunit; CD130 antigen; CDw13 0.05 mg
U0046m CLIA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Mouse,Mus musculus,Oncost 96T
E0046m ELISA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Mouse,Mus musculus,Oncos 96T
E0046m ELISA kit gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Mouse,Mus musculus, 96T
20-272-190537 CD130 ( gp130 ) ( FITC ) - Mouse monoclonal [B - R3] to CD130 ( gp130 ) ( FITC ); IL-6R-beta; Interleukin-6 signal transducer; Membrane glycoprotein 130; gp130; Oncostatin-M receptor alpha subunit; CD 0.5 ml
E1761h ELISA Homo sapiens,Human,IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,OSMR,OSMRB 96T
E1761h ELISA kit Homo sapiens,Human,IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,OSMR,OSMRB 96T
U1761h CLIA Homo sapiens,Human,IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,OSMR,OSMRB 96T
E1761r ELISA IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb,Rat,Rattus norvegicus 96T
U1761m CLIA IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Mouse,Mus musculus,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb 96T
U1761r CLIA IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb,Rat,Rattus norvegicus 96T
E1761m ELISA IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Mouse,Mus musculus,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb 96T
E1761r ELISA kit IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb,Rat,Rattus norvegicus 96T
E1761m ELISA kit IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Mouse,Mus musculus,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb 96T
U1837h CLIA kit High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T
U1837h CLIA High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T
E1837h ELISA kit High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T
E1837h ELISA High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T
E1837r ELISA High affinity IL-2 receptor subunit beta,IL-2 receptor subunit beta,IL-2R subunit beta,Il2rb,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,Rat,Rattus norvegicus 96T
Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP1566: Citrate cycle (TCA cycle)
WP566: canonical wnt - zebrafish
WP2292: Chemokine signaling pathway
WP258: TGF-beta Receptor Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP2272: Pathogenic Escherichia coli infection
WP809: TGF-beta Receptor Signaling Pathway
WP362: TGF-beta Receptor Signaling Pathway
WP1367: TGF-beta Receptor Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP244: Alpha 6 Beta 4 signaling pathway
WP215: noncanonical wnt pathway
WP210: Cytoplasmic Ribosomal Proteins
WP537: Translation Factors
WP1434: Osteopontin Signaling
WP433: tRNA Synthetases
WP1225: estrogen signalling
WP1835: Interferon alpha/beta signaling
WP1571: EBV LMP1 signaling
WP1904: RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways
WP1224: EBV LMP1 signaling
WP219: Cytoplasmic tRNA Synthetases

Related Genes :
[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)
[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)
[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)
[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)
[OSMR OSMRB] Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB)
[Osmr Osmrb] Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB)
[Il12rb2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[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)
[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)
[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)
[IL12RB2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[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)
[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)
[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)]
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[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)
[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)]
[Il7r] Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CD antigen CD127)
[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)
[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)]
[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)
[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)
[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)]
[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)
[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)
[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)]
[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)]
[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)

Bibliography :