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P08887 (IL6RA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 169. 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 alpha

Short name=IL-6 receptor subunit alpha
Short name=IL-6R subunit alpha
Short name=IL-6R-alpha
Short name=IL-6RA
Alternative name(s):
IL-6R 1
Membrane glycoprotein 80
Short name=gp80
CD_antigen=CD126
Gene names
Name:IL6R
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation may lead to the regulation of the immune response, acute-phase reactions and hematopoiesis. Ref.13 Ref.14

Low concentration of a soluble form of IL6 receptor acts as an agonist of IL6 activity. Ref.13 Ref.14

Subunit structure

Hexamer of two molecules each of IL6, IL6R and IL6ST.

Subcellular location

Isoform 1: Basolateral cell membrane; Single-pass type I membrane protein Ref.11 Ref.14.

Isoform 2: Secreted Ref.11 Ref.14.

Tissue specificity

Isoform 2 is expressed in peripheral blood mononuclear cells and weakly found in urine and serum.

Domain

The two fibronectin type-III-like domains, contained in the N-terminal part, form together a cytokine-binding domain.

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

Post-translational modification

A short soluble form may also be released from the membrane by proteolysis.

Polymorphism

Genetic variations in IL6R determine soluble IL6R serum levels [MIM:614689].

Genetic variations in IL6R define the IL6 serum level quantitative trait locus [MIM:614752].

Sequence similarities

Belongs to the type I cytokine receptor family. Type 3 subfamily.

Contains 2 fibronectin type-III domains.

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

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Traceable author statement PubMed 12832423. Source: BHF-UCL

ciliary neurotrophic factor-mediated signaling pathway

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

cytokine-mediated signaling pathway

Inferred from direct assay PubMed 2261637. Source: BHF-UCL

defense response to Gram-negative bacterium

Inferred from expression pattern PubMed 16034137. Source: BHF-UCL

defense response to Gram-positive bacterium

Inferred from expression pattern PubMed 16034137. Source: BHF-UCL

endocrine pancreas development

Inferred from mutant phenotype PubMed 18719127. Source: BHF-UCL

extrinsic apoptotic signaling pathway

Traceable author statement PubMed 15100312. Source: BHF-UCL

hepatic immune response

Traceable author statement PubMed 12832423. Source: BHF-UCL

interleukin-6-mediated signaling pathway

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

monocyte chemotaxis

Inferred by curator PubMed 10510402. Source: BHF-UCL

negative regulation of collagen biosynthetic process

Inferred from direct assay PubMed 12419823. Source: BHF-UCL

negative regulation of interleukin-8 production

Inferred from expression pattern PubMed 16034137. Source: BHF-UCL

neutrophil mediated immunity

Inferred by curator PubMed 16034137. Source: BHF-UCL

positive regulation of MAPK cascade

Inferred from direct assay PubMed 12419823. Source: BHF-UCL

positive regulation of activation of Janus kinase activity

Inferred from direct assay PubMed 12419823. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from direct assay PubMed 2261637. Source: BHF-UCL

positive regulation of chemokine production

Inferred from direct assay PubMed 10510402. Source: BHF-UCL

positive regulation of interleukin-6 production

Inferred from direct assay PubMed 10510402. Source: BHF-UCL

positive regulation of leukocyte chemotaxis

Inferred by curator PubMed 16034137. Source: BHF-UCL

positive regulation of osteoblast differentiation

Traceable author statement PubMed 12372336. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 11884403. Source: BHF-UCL

positive regulation of smooth muscle cell proliferation

Inferred from direct assay PubMed 10510402. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of Stat3 protein

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

response to cytokine

Inferred from direct assay PubMed 2261637. Source: BHF-UCL

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 16034137. Source: BHF-UCL

basolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from direct assay PubMed 12748171. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 16034137PubMed 12419823PubMed 15579373. Source: BHF-UCL

interleukin-6 receptor complex

Inferred from direct assay Ref.16PubMed 2261637. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionciliary neurotrophic factor binding

Inferred from physical interaction PubMed 12643274. Source: BHF-UCL

enzyme binding

Inferred from physical interaction PubMed 12748171. Source: UniProtKB

interleukin-6 binding

Inferred from physical interaction Ref.16. Source: BHF-UCL

interleukin-6 receptor activity

Inferred from electronic annotation. Source: Ensembl

protein homodimerization activity

Inferred from physical interaction PubMed 12633863. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IL6P052315EBI-299383,EBI-720533
K2Q2HRC73EBI-299383,EBI-9007403From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08887-1)

Also known as: Long;

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: P08887-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     356-365: VQDSSSVPLP → GSRRRGSCGL
     366-468: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.11
Chain20 – 468449Interleukin-6 receptor subunit alpha
PRO_0000010895

Regions

Topological domain20 – 365346Extracellular Potential
Transmembrane366 – 38621Helical; Potential
Topological domain387 – 46882Cytoplasmic Potential
Domain26 – 11287Ig-like C2-type
Domain113 – 217105Fibronectin type-III 1
Domain218 – 31699Fibronectin type-III 2
Motif303 – 3075WSXWS motif

Sites

Site2451Not glycosylated

Amino acid modifications

Glycosylation551N-linked (GlcNAc...) Ref.10
Glycosylation931N-linked (GlcNAc...) Ref.10
Glycosylation2211N-linked (GlcNAc...) Ref.10
Disulfide bond25 ↔ 193 Ref.10
Disulfide bond47 ↔ 96 Ref.10
Disulfide bond121 ↔ 132 Ref.10
Disulfide bond165 ↔ 176 Ref.10

Natural variations

Alternative sequence356 – 36510VQDSSSVPLP → GSRRRGSCGL in isoform 2.
VSP_001682
Alternative sequence366 – 468103Missing in isoform 2.
VSP_001683
Natural variant3581D → A Significantly associated with circulating levels of IL6 and soluble IL6R. Ref.4 Ref.17
Corresponds to variant rs2228145 [ dbSNP | Ensembl ].
VAR_021995
Natural variant3851V → I.
Corresponds to variant rs28730736 [ dbSNP | Ensembl ].
VAR_049166

Experimental info

Mutagenesis1211C → S: Complete loss of ligand-binding.
Mutagenesis1221F → A: No change of ligand-binding and IL6 signaling.
Mutagenesis1321C → A: Complete loss of ligand-binding.
Mutagenesis1341W → L: Complete loss of ligand-binding.
Mutagenesis1401P → G: No change of ligand-binding and IL6 signaling.
Mutagenesis1531F → L: No change of ligand-binding and IL6 signaling.
Mutagenesis1651C → L: Complete loss of ligand-binding.
Mutagenesis1741F → L: No change of ligand-binding and IL6 signaling.
Mutagenesis1761C → A: Complete loss of ligand-binding.
Mutagenesis1841D → T: 30% decrease of ligand-binding and IL6 signaling.
Mutagenesis1901V → G: 80% decrease of ligand-binding and no IL6 signaling.
Mutagenesis1931C → D: Complete loss of ligand-binding.
Mutagenesis2111C → A: No change of ligand-binding and IL6 signaling.
Mutagenesis2171D → V: Complete loss of ligand-binding.
Mutagenesis2321R → S: 30% decrease of ligand-binding and IL6 signaling.
Mutagenesis2331W → Q: 30% decrease of ligand-binding and increase of IL6 signaling.
Mutagenesis2541E → A: 50% decrease of ligand-binding and IL6 signaling.
Mutagenesis2771C → D: 30% increase of ligand-binding and 100% increase in IL6 signaling.
Mutagenesis2781V → N: 50% Decrease of ligand-binding and 50% increase in IL6 signaling.
Mutagenesis2791I → D: Complete loss of ligand-binding.
Mutagenesis2801H → I: No change of ligand-binding and no IL6 signaling.
Mutagenesis2811D → G: 70% decrease of ligand-binding and no IL6 signaling.
Mutagenesis2851G → D: 80% decrease of ligand-binding and no IL6 signaling.
Mutagenesis2911Q → K: Complete loss of ligand-binding.
Mutagenesis2931R → G: Complete loss of ligand-binding.
Sequence conflict2101G → D in BAD97302. Ref.5

Secondary structure

..................................................... 468
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1988. Version 1.
Checksum: 62AA239FA14F1B8B

FASTA46851,548
        10         20         30         40         50         60 
MLAVGCALLA ALLAAPGAAL APRRCPAQEV ARGVLTSLPG DSVTLTCPGV EPEDNATVHW 

        70         80         90        100        110        120 
VLRKPAAGSH PSRWAGMGRR LLLRSVQLHD SGNYSCYRAG RPAGTVHLLV DVPPEEPQLS 

       130        140        150        160        170        180 
CFRKSPLSNV VCEWGPRSTP SLTTKAVLLV RKFQNSPAED FQEPCQYSQE SQKFSCQLAV 

       190        200        210        220        230        240 
PEGDSSFYIV SMCVASSVGS KFSKTQTFQG CGILQPDPPA NITVTAVARN PRWLSVTWQD 

       250        260        270        280        290        300 
PHSWNSSFYR LRFELRYRAE RSKTFTTWMV KDLQHHCVIH DAWSGLRHVV QLRAQEEFGQ 

       310        320        330        340        350        360 
GEWSEWSPEA MGTPWTESRS PPAENEVSTP MQALTTNKDD DNILFRDSAN ATSLPVQDSS 

       370        380        390        400        410        420 
SVPLPTFLVA GGSLAFGTLL CIAIVLRFKK TWKLRALKEG KTSMHPPYSL GQLVPERPRP 

       430        440        450        460 
TPVLVPLISP PVSPSSLGSD NTSSHNRPDA RDPRSPYDIS NTDYFFPR 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: ECC8FC9E142823F2
Show »

FASTA36540,237

References

« Hide 'large scale' references
[1]"Cloning and expression of the human interleukin-6 (BSF-2/IFN beta 2) receptor."
Yamasaki K., Taga T., Hirata Y., Yawata H., Kawanishi Y., Seed B., Taniguchi T., Hirano T., Kishimoto T.
Science 241:825-828(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular structure of interleukin 6 receptor."
Yamasaki K., Taga T., Hirata Y., Yawata H., Kawanishi Y., Seed B., Taniguchi T., Hirano T., Kishimoto T.
Proc. Jpn. Acad., B, Phys. Biol. Sci. 64:209-211(1988)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Structural and functional studies on the human hepatic interleukin-6 receptor. Molecular cloning and overexpression in HepG2 cells."
Schooltink H., Stoyan T., Lenz D., Schmitz H., Hirano T., Kishimoto T., Heinrich P.C., Rose-John S.
Biochem. J. 277:659-664(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ALA-358.
Tissue: Trachea.
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney.
[6]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Lymph.
[9]"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."
Horiuchi S., Koyanagi Y., Zhou Y., Miyamoto H., Tanaka Y., Waki M., Matsumoto A., Yamamoto M., Yamamoto N.
Eur. J. Immunol. 24:1945-1948(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 313-365 (ISOFORM 2).
[10]"Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor."
Cole A.R., Hall N.E., Treutlein H.R., Eddes J.S., Reid G.E., Moritz R.L., Simpson R.J.
J. Biol. Chem. 274:7207-7215(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-55; ASN-93 AND ASN-221, LACK OF GLYCOSYLATION AT ASN-245, DISULFIDE BONDS.
[11]"Soluble cytokine receptors are present in normal human urine."
Novick D., Engelmann H., Wallach D., Rubinstein M.
J. Exp. Med. 170:1409-1414(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-49, SUBCELLULAR LOCATION.
[12]"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."
Yawata H., Yasukawa K., Natsuka S., Murakami M., Yamasaki K., Hibi M., Taga T., Kishimoto T.
EMBO J. 12:1705-1712(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[13]"The cytoplasmic domain of the interleukin-6 receptor gp80 mediates its basolateral sorting in polarized Madin-Darby canine kidney cells."
Martens A.S., Bode J.G., Heinrich P.C., Graeve L.
J. Cell Sci. 113:3593-3602(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Increased association with detergent-resistant membranes/lipid rafts of apically targeted mutants of the interleukin-6 receptor gp80."
Buk D.M., Renner O., Graeve L.
Eur. J. Cell Biol. 84:819-831(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]"Structure of the extracellular domains of the human interleukin-6 receptor alpha-chain."
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.
Proc. Natl. Acad. Sci. U.S.A. 99:15959-15964(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-344.
[16]"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 115-315.
[17]"Admixture mapping of an allele affecting interleukin 6 soluble receptor and interleukin 6 levels."
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. expand/collapse author list , Cummings S., Kwok P.Y., Harris T., Zmuda J.M., Ziv E.
Am. J. Hum. Genet. 80:716-726(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM, VARIANT ALA-358, ASSOCIATION OF VARIANT ALA-358 WITH IL6 AND SOLUBLE IL6R SERUM LEVELS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12830 mRNA. Translation: CAA31312.1.
X58298 mRNA. Translation: CAA41231.1.
AK293013 mRNA. Translation: BAF85702.1.
AK312730 mRNA. Translation: BAG35601.1.
AK223582 mRNA. Translation: BAD97302.1.
AL162591 Genomic DNA. Translation: CAH72853.1.
CH471121 Genomic DNA. Translation: EAW53200.1.
BC089410 mRNA. Translation: AAH89410.1.
S72848 mRNA. Translation: AAC60635.1.
PIRA41242.
RefSeqNP_000556.1. NM_000565.3.
NP_001193795.1. NM_001206866.1.
NP_852004.1. NM_181359.2.
UniGeneHs.135087.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N26X-ray2.40A20-344[»]
1N2Qmodel-C/D20-344[»]
1P9MX-ray3.65C115-315[»]
2ARWNMR-A212-336[»]
ProteinModelPortalP08887.
SMRP08887. Positions 20-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109784. 4 interactions.
DIPDIP-162N.
DIP-3777N.
IntActP08887. 5 interactions.
MINTMINT-190110.
STRING9606.ENSP00000357470.

Chemistry

ChEMBLCHEMBL2364155.

PTM databases

PhosphoSiteP08887.

Polymorphism databases

DMDM124343.

Proteomic databases

PaxDbP08887.
PRIDEP08887.

Protocols and materials databases

DNASU3570.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344086; ENSP00000340589; ENSG00000160712. [P08887-2]
ENST00000368485; ENSP00000357470; ENSG00000160712. [P08887-1]
GeneID3570.
KEGGhsa:3570.
UCSCuc001fez.2. human. [P08887-1]
uc001ffa.2. human. [P08887-2]

Organism-specific databases

CTD3570.
GeneCardsGC01P154377.
HGNCHGNC:6019. IL6R.
MIM147880. gene.
614689. phenotype.
614752. phenotype.
neXtProtNX_P08887.
PharmGKBPA29835.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47227.
HOVERGENHBG052118.
InParanoidP08887.
KOK05055.
OMACQLAVPE.
OrthoDBEOG71CFM2.
PhylomeDBP08887.
TreeFamTF331210.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP08887.

Gene expression databases

ArrayExpressP08887.
BgeeP08887.
CleanExHS_IL6R.
GenevestigatorP08887.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR003961. Fibronectin_type3.
IPR003530. Hematopoietin_rcpt_L_F3_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR015321. IL-6_rcpt_alpha-bd.
[Graphical view]
PfamPF09240. IL6Ra-bind. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 2 hits.
PS01354. HEMATOPO_REC_L_F3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08887.
GeneWikiInterleukin-6_receptor.
GenomeRNAi3570.
NextBio13954.
PMAP-CutDBP08887.
PROP08887.
SOURCESearch...

Entry information

Entry nameIL6RA_HUMAN
AccessionPrimary (citable) accession number: P08887
Secondary accession number(s): A8KAE8 expand/collapse secondary AC list , B2R6V4, Q16202, Q53EQ7, Q5FWG2, Q5VZ23
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: April 16, 2014
This is version 169 of the entry and version 1 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 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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