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P40189 (IL6RB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-6 receptor subunit beta

Short name=IL-6 receptor subunit beta
Short name=IL-6R subunit beta
Short name=IL-6R-beta
Short name=IL-6RB
Alternative name(s):
CDw130
Interleukin-6 signal transducer
Membrane glycoprotein 130
Short name=gp130
Oncostatin-M receptor subunit alpha
CD_antigen=CD130
Gene names
Name:IL6ST
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length918 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Signal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize gp130 for initiating signal transmission. Binds to IL6/IL6R (alpha chain) complex, resulting in the formation of high-affinity IL6 binding sites, and transduces the signal. Does not bind IL6. May have a role in embryonic development By similarity. The type I OSM receptor is capable of transducing OSM-specific signaling events.

Subunit structure

Interacts with INPP5D/SHIP1 By similarity. Forms heterodimers composed of LIPR and IL6ST (type I OSM receptor). Also forms heterodimers composed of OSMR and IL6ST (type II OSM receptor). Homodimer. The homodimer binds two molecules of herpes virus 8/HHV-8 protein vIL-6. Component of a hexamer of two molecules each of IL6, IL6R and IL6ST. Interacts with HCK. Ref.8 Ref.9 Ref.11 Ref.20 Ref.22

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein.

Isoform 2: Secreted.

Tissue specificity

Found in all the tissues and cell lines examined. Expression not restricted to IL6 responsive cells.

Induction

LIF and OSM activate the type I OSM receptor while only OSM can activate the type II OSM receptor. Ref.8

Domain

The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.

The box 1 motif is required for JAK interaction and/or activation.

Post-translational modification

Phosphorylation of Ser-782 down-regulates cell surface expression.

Heavily N-glycosylated. Ref.7 Ref.17 Ref.20

Sequence similarities

Belongs to the type I cytokine receptor family. Type 2 subfamily.

Contains 5 fibronectin type-III domains.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycogen metabolic process

Inferred from electronic annotation. Source: Ensembl

interleukin-6-mediated signaling pathway

Inferred from mutant phenotype PubMed 12643274Ref.1. Source: BHF-UCL

leukemia inhibitory factor signaling pathway

Inferred from genetic interaction PubMed 12643274Ref.8. Source: BHF-UCL

negative regulation of apoptotic process

Traceable author statement PubMed 17530315. Source: BHF-UCL

negative regulation of interleukin-6-mediated signaling pathway

Inferred from direct assay PubMed 8353278. Source: BHF-UCL

oncostatin-M-mediated signaling pathway

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

positive regulation of T cell proliferation

Inferred from mutant phenotype PubMed 14764690. Source: BHF-UCL

positive regulation of acute inflammatory response

Inferred by curator Ref.8. Source: BHF-UCL

positive regulation of adaptive immune response

Inferred by curator PubMed 14764690. Source: BHF-UCL

positive regulation of astrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cardiac muscle hypertrophy

Traceable author statement PubMed 10744750. Source: BHF-UCL

positive regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 12372336. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of Stat1 protein

Inferred from mutant phenotype PubMed 14764690. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of Stat3 protein

Inferred from mutant phenotype PubMed 14764690. Source: BHF-UCL

positive regulation vascular endothelial growth factor production

Traceable author statement PubMed 10744750. Source: BHF-UCL

regulation of Notch signaling pathway

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentciliary neurotrophic factor receptor complex

Inferred from direct assay PubMed 12707266. Source: BHF-UCL

dendrite

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 8353278. Source: BHF-UCL

interleukin-6 receptor complex

Inferred from direct assay Ref.22Ref.1. Source: BHF-UCL

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

oncostatin-M receptor complex

Inferred from direct assay Ref.8. Source: BHF-UCL

   Molecular_functionciliary neurotrophic factor receptor activity

Inferred from direct assay PubMed 12643274. Source: BHF-UCL

interleukin-11 receptor activity

Inferred from electronic annotation. Source: Ensembl

interleukin-27 receptor activity

Inferred by curator PubMed 14764690. Source: BHF-UCL

protein homodimerization activity

Traceable author statement PubMed 8390097. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

K2Q2HRC72EBI-1030834,EBI-9007403From a different organism.
Stat3P422276EBI-1030834,EBI-602878From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P40189-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P40189-2)

Also known as: GP130-RAPS;

The sequence of this isoform differs from the canonical sequence as follows:
     325-329: RPSKA → NIASF
     330-918: Missing.
Isoform 3 (identifier: P40189-3)

The sequence of this isoform differs from the canonical sequence as follows:
     423-483: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 918896Interleukin-6 receptor subunit beta
PRO_0000010899

Regions

Topological domain23 – 619597Extracellular Potential
Transmembrane620 – 64122Helical; Potential
Topological domain642 – 918277Cytoplasmic Potential
Domain26 – 12095Ig-like C2-type
Domain125 – 21692Fibronectin type-III 1
Domain224 – 324101Fibronectin type-III 2
Domain329 – 42496Fibronectin type-III 3
Domain426 – 51792Fibronectin type-III 4
Domain518 – 61396Fibronectin type-III 5
Motif310 – 3145WSXWS motif
Motif651 – 6599Box 1 motif
Compositional bias725 – 75531Ser-rich

Amino acid modifications

Modified residue6671Phosphoserine Ref.14 Ref.18
Modified residue7821Phosphoserine Ref.10
Modified residue8291Phosphoserine Ref.13
Glycosylation431N-linked (GlcNAc...) Ref.7
Glycosylation831N-linked (GlcNAc...) Ref.7
Glycosylation1311N-linked (GlcNAc...) Ref.7
Glycosylation1571N-linked (GlcNAc...) Ref.7
Glycosylation2271N-linked (GlcNAc...) Ref.7 Ref.16
Glycosylation3791N-linked (GlcNAc...) Ref.7 Ref.12
Glycosylation3831N-linked (GlcNAc...) Ref.7 Ref.12
Glycosylation3901N-linked (GlcNAc...) (complex) Ref.16 Ref.17
Glycosylation5531N-linked (GlcNAc...) Ref.7
Glycosylation5641N-linked (GlcNAc...) Ref.7
Disulfide bond28 ↔ 54 Ref.7
Disulfide bond48 ↔ 103 Ref.7
Disulfide bond134 ↔ 144 Ref.7
Disulfide bond172 ↔ 182 Ref.7
Disulfide bond458 ↔ 466 Ref.7

Natural variations

Alternative sequence325 – 3295RPSKA → NIASF in isoform 2.
VSP_001684
Alternative sequence330 – 918589Missing in isoform 2.
VSP_001685
Alternative sequence423 – 48361Missing in isoform 3.
VSP_043716
Natural variant81L → V. Ref.1 Ref.2
Corresponds to variant rs1063560 [ dbSNP | Ensembl ].
VAR_047782
Natural variant1481G → R.
Corresponds to variant rs2228044 [ dbSNP | Ensembl ].
VAR_047783
Natural variant3971L → V.
Corresponds to variant rs2228043 [ dbSNP | Ensembl ].
VAR_047784
Natural variant4151T → I in a colorectal cancer sample; somatic mutation. Ref.23
VAR_036165
Natural variant4541I → T.
Corresponds to variant rs2228046 [ dbSNP | Ensembl ].
VAR_047785
Natural variant4991V → I.
Corresponds to variant rs34417936 [ dbSNP | Ensembl ].
VAR_047786

Experimental info

Mutagenesis7821S → A: Increases cell surface expression. Ref.10

Secondary structure

............................................................................................................ 918
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 6510A4409FFCF08C

FASTA918103,537
        10         20         30         40         50         60 
MLTLQTWLVQ ALFIFLTTES TGELLDPCGY ISPESPVVQL HSNFTAVCVL KEKCMDYFHV 

        70         80         90        100        110        120 
NANYIVWKTN HFTIPKEQYT IINRTASSVT FTDIASLNIQ LTCNILTFGQ LEQNVYGITI 

       130        140        150        160        170        180 
ISGLPPEKPK NLSCIVNEGK KMRCEWDGGR ETHLETNFTL KSEWATHKFA DCKAKRDTPT 

       190        200        210        220        230        240 
SCTVDYSTVY FVNIEVWVEA ENALGKVTSD HINFDPVYKV KPNPPHNLSV INSEELSSIL 

       250        260        270        280        290        300 
KLTWTNPSIK SVIILKYNIQ YRTKDASTWS QIPPEDTAST RSSFTVQDLK PFTEYVFRIR 

       310        320        330        340        350        360 
CMKEDGKGYW SDWSEEASGI TYEDRPSKAP SFWYKIDPSH TQGYRTVQLV WKTLPPFEAN 

       370        380        390        400        410        420 
GKILDYEVTL TRWKSHLQNY TVNATKLTVN LTNDRYLATL TVRNLVGKSD AAVLTIPACD 

       430        440        450        460        470        480 
FQATHPVMDL KAFPKDNMLW VEWTTPRESV KKYILEWCVL SDKAPCITDW QQEDGTVHRT 

       490        500        510        520        530        540 
YLRGNLAESK CYLITVTPVY ADGPGSPESI KAYLKQAPPS KGPTVRTKKV GKNEAVLEWD 

       550        560        570        580        590        600 
QLPVDVQNGF IRNYTIFYRT IIGNETAVNV DSSHTEYTLS SLTSDTLYMV RMAAYTDEGG 

       610        620        630        640        650        660 
KDGPEFTFTT PKFAQGEIEA IVVPVCLAFL LTTLLGVLFC FNKRDLIKKH IWPNVPDPSK 

       670        680        690        700        710        720 
SHIAQWSPHT PPRHNFNSKD QMYSDGNFTD VSVVEIEAND KKPFPEDLKS LDLFKKEKIN 

       730        740        750        760        770        780 
TEGHSSGIGG SSCMSSSRPS ISSSDENESS QNTSSTVQYS TVVHSGYRHQ VPSVQVFSRS 

       790        800        810        820        830        840 
ESTQPLLDSE ERPEDLQLVD HVDGGDGILP RQQYFKQNCS QHESSPDISH FERSKQVSSV 

       850        860        870        880        890        900 
NEEDFVRLKQ QISDHISQSC GSGQMKMFQE VSAADAFGPG TEGQVERFET VGMEAATDEG 

       910 
MPKSYLPQTV RQGGYMPQ 

« Hide

Isoform 2 (GP130-RAPS) [UniParc].

Checksum: D556124C867984E4
Show »

FASTA32937,499
Isoform 3 [UniParc].

Checksum: 726208A5073B5451
Show »

FASTA85796,276

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of an IL-6 signal transducer, gp130."
Hibi M., Murakami M., Saito M., Hirano T., Taga T., Kishimoto T.
Cell 63:1149-1157(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-8.
Tissue: Myeloma and Placenta.
[2]"Cloning of novel soluble gp130 and detection of its neutralizing autoantibodies in rheumatoid arthritis."
Tanaka M., Kishimura M., Ozaki S., Osakada F., Hashimoto H., Okubo M., Murakami M., Nakao K.
J. Clin. Invest. 106:137-144(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-8.
Tissue: Synovium.
[3]"IL6ST mRNA, nirs splice variant 4."
Hayashi A., Sameshima E., Tabata Y., Iida K., Mitsuyama M., Kanai S., Furuya T., Saito T.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]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
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The DNA sequence and comparative analysis of human chromosome 5."
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. expand/collapse author list , 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.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130."
Moritz R.L., Hall N.E., Connolly L.M., Simpson R.J.
J. Biol. Chem. 276:8244-8253(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-43; ASN-83; ASN-131; ASN-157; ASN-227; ASN-379; ASN-383; ASN-553 AND ASN-564.
[8]"Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation."
Mosley B., De Imus C., Friend D., Boiani N., Thoma B., Park L.S., Cosman D.
J. Biol. Chem. 271:32635-32643(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INDUCTION.
[9]"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."
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.
Exp. Hematol. 25:1367-1377(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCK.
[10]"Phosphorylation of human gp130 at Ser-782 adjacent to the di-leucine internalization motif. Effects on expression and signaling."
Gibson R.M., Schiemann W.P., Prichard L.B., Reno J.M., Ericsson L.H., Nathanson N.M.
J. Biol. Chem. 275:22574-22582(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-782, MUTAGENESIS OF SER-782, MASS SPECTROMETRY.
[11]"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."
Li H., Wang H., Nicholas J.
J. Virol. 75:3325-3334(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-8 PROTEIN VIL6.
[12]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-379 AND ASN-383.
Tissue: Plasma.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227 AND ASN-390.
Tissue: Liver.
[17]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
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.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-390.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Crystal structure of a cytokine-binding region of gp130."
Bravo J., Staunton D., Heath J.K., Jones E.Y.
EMBO J. 17:1665-1674(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 122-325.
[20]"Structure of an extracellular gp130 cytokine receptor signaling complex."
Chow D.-C., He X.-L., Snow A.L., Rose-John S., Garcia K.C.
Science 291:2150-2155(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-325 IN COMPLEX WITH HERPES VIRUS IL6, SUBUNIT, GLYCOSYLATION.
[21]"Convergent mechanisms for recognition of divergent cytokines by the shared signaling receptor gp130."
Boulanger M.J., Bankovich A.J., Kortemme T., Baker D., Garcia K.C.
Mol. Cell 12:577-589(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 123-323 IN COMPLEX WITH LIF.
[22]"Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex."
Boulanger M.J., Chow D.-C., Brevnova E.E., Garcia K.C.
Science 300:2101-2104(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS) OF 23-321 IN COMPLEX WITH IL6 AND IL6R, SUBUNIT.
[23]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-415.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57230 mRNA. Translation: AAA59155.1.
AB015706 mRNA. Translation: BAA78112.1.
AB102802 mRNA. Translation: BAD89393.1.
EF064722 Genomic DNA. Translation: ABK41905.1.
AC008914 Genomic DNA. No translation available.
AC016596 Genomic DNA. No translation available.
CH471123 Genomic DNA. Translation: EAW54936.1.
PIRA36337.
RefSeqNP_001177910.1. NM_001190981.1.
NP_002175.2. NM_002184.3.
NP_786943.1. NM_175767.2.
UniGeneHs.532082.
Hs.706627.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJ8NMR-A219-325[»]
1BQUX-ray2.00A/B122-333[»]
1I1RX-ray2.40A23-325[»]
1N2Qmodel-A/B23-324[»]
1P9MX-ray3.65A23-321[»]
1PVHX-ray2.50A/C123-323[»]
3L5HX-ray3.60A24-612[»]
3L5IX-ray1.90A323-612[»]
3L5JX-ray3.04A/B323-610[»]
ProteinModelPortalP40189.
SMRP40189. Positions 24-612.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109786. 23 interactions.
DIPDIP-95N.
IntActP40189. 9 interactions.
MINTMINT-130473.
STRING9606.ENSP00000338799.

PTM databases

PhosphoSiteP40189.

Polymorphism databases

DMDM215273999.

Proteomic databases

PaxDbP40189.
PRIDEP40189.

Protocols and materials databases

DNASU3572.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336909; ENSP00000338799; ENSG00000134352. [P40189-1]
ENST00000381287; ENSP00000370687; ENSG00000134352. [P40189-2]
ENST00000381294; ENSP00000370694; ENSG00000134352. [P40189-3]
ENST00000381298; ENSP00000370698; ENSG00000134352. [P40189-1]
ENST00000502326; ENSP00000462158; ENSG00000134352. [P40189-1]
ENST00000522633; ENSP00000435399; ENSG00000134352. [P40189-2]
ENST00000536319; ENSP00000444456; ENSG00000134352. [P40189-2]
GeneID3572.
KEGGhsa:3572.
UCSCuc003jqq.3. human. [P40189-1]
uc003jqr.3. human. [P40189-2]
uc010iwb.3. human. [P40189-3]

Organism-specific databases

CTD3572.
GeneCardsGC05M055230.
HGNCHGNC:6021. IL6ST.
HPACAB025784.
HPA010558.
MIM600694. gene.
neXtProtNX_P40189.
PharmGKBPA29837.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145009.
HOGENOMHOG000015771.
HOVERGENHBG052119.
InParanoidP40189.
KOK05060.
OMAFKQNCSQ.
OrthoDBEOG7FXZXN.
PhylomeDBP40189.
TreeFamTF338122.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP40189.

Gene expression databases

ArrayExpressP40189.
BgeeP40189.
CleanExHS_IL6ST.
GenevestigatorP40189.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR003961. Fibronectin_type3.
IPR003529. Hematopoietin_rcpt_Gp130_CS.
IPR013783. Ig-like_fold.
IPR010457. IgC2-like_lig-bd.
IPR015321. IL-6_rcpt_alpha-bd.
[Graphical view]
PfamPF00041. fn3. 2 hits.
PF09240. IL6Ra-bind. 1 hit.
PF06328. Lep_receptor_Ig. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 5 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 5 hits.
PROSITEPS50853. FN3. 4 hits.
PS01353. HEMATOPO_REC_L_F2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIL6ST. human.
EvolutionaryTraceP40189.
GeneWikiGlycoprotein_130.
GenomeRNAi3572.
NextBio13960.
PROP40189.
SOURCESearch...

Entry information

Entry nameIL6RB_HUMAN
AccessionPrimary (citable) accession number: P40189
Secondary accession number(s): A0N0L4, Q5FC04, Q9UQ41
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 25, 2008
Last modified: March 19, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries