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P08887

- IL6RA_HUMAN

UniProt

P08887 - IL6RA_HUMAN

Protein

Interleukin-6 receptor subunit alpha

Gene

IL6R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei245 – 2451Not glycosylated

    GO - Molecular functioni

    1. ciliary neurotrophic factor binding Source: BHF-UCL
    2. enzyme binding Source: UniProtKB
    3. interleukin-6 binding Source: BHF-UCL
    4. interleukin-6 receptor activity Source: Ensembl
    5. protein binding Source: IntAct
    6. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. acute-phase response Source: BHF-UCL
    2. ciliary neurotrophic factor-mediated signaling pathway Source: BHF-UCL
    3. cytokine-mediated signaling pathway Source: BHF-UCL
    4. defense response to Gram-negative bacterium Source: BHF-UCL
    5. defense response to Gram-positive bacterium Source: BHF-UCL
    6. endocrine pancreas development Source: BHF-UCL
    7. extrinsic apoptotic signaling pathway Source: BHF-UCL
    8. hepatic immune response Source: BHF-UCL
    9. interleukin-6-mediated signaling pathway Source: BHF-UCL
    10. monocyte chemotaxis Source: BHF-UCL
    11. negative regulation of collagen biosynthetic process Source: BHF-UCL
    12. negative regulation of interleukin-8 production Source: BHF-UCL
    13. neutrophil mediated immunity Source: BHF-UCL
    14. positive regulation of activation of Janus kinase activity Source: BHF-UCL
    15. positive regulation of cell proliferation Source: BHF-UCL
    16. positive regulation of chemokine production Source: BHF-UCL
    17. positive regulation of interleukin-6 production Source: BHF-UCL
    18. positive regulation of leukocyte chemotaxis Source: BHF-UCL
    19. positive regulation of MAPK cascade Source: BHF-UCL
    20. positive regulation of osteoblast differentiation Source: BHF-UCL
    21. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    22. positive regulation of smooth muscle cell proliferation Source: BHF-UCL
    23. positive regulation of tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
    24. response to cytokine Source: BHF-UCL

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_27307. Interleukin-6 signaling.
    SignaLinkiP08887.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:IL6R
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6019. IL6R.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: BHF-UCL
    2. basolateral plasma membrane Source: UniProtKB-SubCell
    3. cell surface Source: Ensembl
    4. extracellular region Source: UniProtKB
    5. extracellular space Source: BHF-UCL
    6. interleukin-6 receptor complex Source: BHF-UCL
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi121 – 1211C → S: Complete loss of ligand-binding. 1 Publication
    Mutagenesisi122 – 1221F → A: No change of ligand-binding and IL6 signaling. 1 Publication
    Mutagenesisi132 – 1321C → A: Complete loss of ligand-binding. 1 Publication
    Mutagenesisi134 – 1341W → L: Complete loss of ligand-binding. 1 Publication
    Mutagenesisi140 – 1401P → G: No change of ligand-binding and IL6 signaling. 1 Publication
    Mutagenesisi153 – 1531F → L: No change of ligand-binding and IL6 signaling. 1 Publication
    Mutagenesisi165 – 1651C → L: Complete loss of ligand-binding. 1 Publication
    Mutagenesisi174 – 1741F → L: No change of ligand-binding and IL6 signaling. 1 Publication
    Mutagenesisi176 – 1761C → A: Complete loss of ligand-binding. 1 Publication
    Mutagenesisi184 – 1841D → T: 30% decrease of ligand-binding and IL6 signaling. 1 Publication
    Mutagenesisi190 – 1901V → G: 80% decrease of ligand-binding and no IL6 signaling. 1 Publication
    Mutagenesisi193 – 1931C → D: Complete loss of ligand-binding. 1 Publication
    Mutagenesisi211 – 2111C → A: No change of ligand-binding and IL6 signaling. 1 Publication
    Mutagenesisi217 – 2171D → V: Complete loss of ligand-binding. 1 Publication
    Mutagenesisi232 – 2321R → S: 30% decrease of ligand-binding and IL6 signaling. 1 Publication
    Mutagenesisi233 – 2331W → Q: 30% decrease of ligand-binding and increase of IL6 signaling. 1 Publication
    Mutagenesisi254 – 2541E → A: 50% decrease of ligand-binding and IL6 signaling. 1 Publication
    Mutagenesisi277 – 2771C → D: 30% increase of ligand-binding and 100% increase in IL6 signaling. 1 Publication
    Mutagenesisi278 – 2781V → N: 50% Decrease of ligand-binding and 50% increase in IL6 signaling. 1 Publication
    Mutagenesisi279 – 2791I → D: Complete loss of ligand-binding. 1 Publication
    Mutagenesisi280 – 2801H → I: No change of ligand-binding and no IL6 signaling. 1 Publication
    Mutagenesisi281 – 2811D → G: 70% decrease of ligand-binding and no IL6 signaling. 1 Publication
    Mutagenesisi285 – 2851G → D: 80% decrease of ligand-binding and no IL6 signaling. 1 Publication
    Mutagenesisi291 – 2911Q → K: Complete loss of ligand-binding. 1 Publication
    Mutagenesisi293 – 2931R → G: Complete loss of ligand-binding. 1 Publication

    Organism-specific databases

    MIMi614689. phenotype.
    614752. phenotype.
    PharmGKBiPA29835.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 468449Interleukin-6 receptor subunit alphaPRO_0000010895Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi25 ↔ 1931 PublicationPROSITE-ProRule annotation
    Disulfide bondi47 ↔ 961 PublicationPROSITE-ProRule annotation
    Glycosylationi55 – 551N-linked (GlcNAc...)1 Publication
    Glycosylationi93 – 931N-linked (GlcNAc...)1 Publication
    Disulfide bondi121 ↔ 1321 PublicationPROSITE-ProRule annotation
    Disulfide bondi165 ↔ 1761 PublicationPROSITE-ProRule annotation
    Glycosylationi221 – 2211N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP08887.
    PaxDbiP08887.
    PRIDEiP08887.

    PTM databases

    PhosphoSiteiP08887.

    Miscellaneous databases

    PMAP-CutDBP08887.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP08887.
    BgeeiP08887.
    CleanExiHS_IL6R.
    GenevestigatoriP08887.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IL6P052315EBI-299383,EBI-720533
    K2Q2HRC73EBI-299383,EBI-9007403From a different organism.

    Protein-protein interaction databases

    BioGridi109784. 5 interactions.
    DIPiDIP-162N.
    DIP-3777N.
    IntActiP08887. 5 interactions.
    MINTiMINT-190110.
    STRINGi9606.ENSP00000357470.

    Structurei

    Secondary structure

    1
    468
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 374
    Beta strandi43 – 464
    Beta strandi56 – 638
    Beta strandi65 – 684
    Beta strandi72 – 8312
    Helixi88 – 903
    Beta strandi92 – 10110
    Beta strandi105 – 1106
    Beta strandi120 – 1256
    Beta strandi130 – 1345
    Beta strandi145 – 15713
    Beta strandi159 – 16810
    Turni169 – 1724
    Beta strandi173 – 1786
    Beta strandi187 – 19610
    Beta strandi199 – 2024
    Beta strandi206 – 2094
    Turni210 – 2123
    Beta strandi220 – 2267
    Beta strandi234 – 2396
    Beta strandi247 – 2493
    Beta strandi251 – 2599
    Beta strandi266 – 2694
    Helixi271 – 2733
    Beta strandi275 – 2817
    Beta strandi288 – 2969
    Turni297 – 2993
    Beta strandi310 – 3123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N26X-ray2.40A20-344[»]
    1N2Qmodel-C/D20-344[»]
    1P9MX-ray3.65C115-315[»]
    2ARWNMR-A212-336[»]
    ProteinModelPortaliP08887.
    SMRiP08887. Positions 20-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08887.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 365346ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini387 – 46882CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei366 – 38621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 11287Ig-like C2-typeAdd
    BLAST
    Domaini113 – 217105Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini218 – 31699Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi303 – 3075WSXWS motif

    Domaini

    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.

    Sequence similaritiesi

    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG47227.
    HOVERGENiHBG052118.
    InParanoidiP08887.
    KOiK05055.
    OMAiCQLAVPE.
    OrthoDBiEOG71CFM2.
    PhylomeDBiP08887.
    TreeFamiTF331210.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR003961. 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]
    PfamiPF09240. IL6Ra-bind. 1 hit.
    [Graphical view]
    SMARTiSM00060. FN3. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 2 hits.
    PROSITEiPS50853. FN3. 2 hits.
    PS01354. HEMATOPO_REC_L_F3. 1 hit.
    PS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P08887-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLAVGCALLA ALLAAPGAAL APRRCPAQEV ARGVLTSLPG DSVTLTCPGV    50
    EPEDNATVHW VLRKPAAGSH PSRWAGMGRR LLLRSVQLHD SGNYSCYRAG 100
    RPAGTVHLLV DVPPEEPQLS CFRKSPLSNV VCEWGPRSTP SLTTKAVLLV 150
    RKFQNSPAED FQEPCQYSQE SQKFSCQLAV PEGDSSFYIV SMCVASSVGS 200
    KFSKTQTFQG CGILQPDPPA NITVTAVARN PRWLSVTWQD PHSWNSSFYR 250
    LRFELRYRAE RSKTFTTWMV KDLQHHCVIH DAWSGLRHVV QLRAQEEFGQ 300
    GEWSEWSPEA MGTPWTESRS PPAENEVSTP MQALTTNKDD DNILFRDSAN 350
    ATSLPVQDSS SVPLPTFLVA GGSLAFGTLL CIAIVLRFKK TWKLRALKEG 400
    KTSMHPPYSL GQLVPERPRP TPVLVPLISP PVSPSSLGSD NTSSHNRPDA 450
    RDPRSPYDIS NTDYFFPR 468
    Length:468
    Mass (Da):51,548
    Last modified:November 1, 1988 - v1
    Checksum:i62AA239FA14F1B8B
    GO
    Isoform 2 (identifier: P08887-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

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

    Show »
    Length:365
    Mass (Da):40,237
    Checksum:iECC8FC9E142823F2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti210 – 2101G → D in BAD97302. 1 PublicationCurated

    Polymorphismi

    Genetic variations in IL6R determine soluble IL6R serum levels [MIMi:614689].
    Genetic variations in IL6R define the IL6 serum level quantitative trait locus [MIMi:614752].

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti358 – 3581D → A Significantly associated with circulating levels of IL6 and soluble IL6R. 2 Publications
    Corresponds to variant rs2228145 [ dbSNP | Ensembl ].
    VAR_021995
    Natural varianti385 – 3851V → I.
    Corresponds to variant rs28730736 [ dbSNP | Ensembl ].
    VAR_049166

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei356 – 36510VQDSSSVPLP → GSRRRGSCGL in isoform 2. 3 PublicationsVSP_001682
    Alternative sequencei366 – 468103Missing in isoform 2. 3 PublicationsVSP_001683Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1067.1. [P08887-1]
    CCDS1068.1. [P08887-2]
    PIRiA41242.
    RefSeqiNP_000556.1. NM_000565.3. [P08887-1]
    NP_001193795.1. NM_001206866.1.
    NP_852004.1. NM_181359.2. [P08887-2]
    UniGeneiHs.135087.

    Genome annotation databases

    EnsembliENST00000344086; ENSP00000340589; ENSG00000160712. [P08887-2]
    ENST00000368485; ENSP00000357470; ENSG00000160712. [P08887-1]
    GeneIDi3570.
    KEGGihsa:3570.
    UCSCiuc001fez.2. human. [P08887-1]
    uc001ffa.2. human. [P08887-2]

    Polymorphism databases

    DMDMi124343.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1067.1. [P08887-1 ]
    CCDS1068.1. [P08887-2 ]
    PIRi A41242.
    RefSeqi NP_000556.1. NM_000565.3. [P08887-1 ]
    NP_001193795.1. NM_001206866.1.
    NP_852004.1. NM_181359.2. [P08887-2 ]
    UniGenei Hs.135087.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N26 X-ray 2.40 A 20-344 [» ]
    1N2Q model - C/D 20-344 [» ]
    1P9M X-ray 3.65 C 115-315 [» ]
    2ARW NMR - A 212-336 [» ]
    ProteinModelPortali P08887.
    SMRi P08887. Positions 20-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109784. 5 interactions.
    DIPi DIP-162N.
    DIP-3777N.
    IntActi P08887. 5 interactions.
    MINTi MINT-190110.
    STRINGi 9606.ENSP00000357470.

    Chemistry

    ChEMBLi CHEMBL2364155.

    PTM databases

    PhosphoSitei P08887.

    Polymorphism databases

    DMDMi 124343.

    Proteomic databases

    MaxQBi P08887.
    PaxDbi P08887.
    PRIDEi P08887.

    Protocols and materials databases

    DNASUi 3570.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344086 ; ENSP00000340589 ; ENSG00000160712 . [P08887-2 ]
    ENST00000368485 ; ENSP00000357470 ; ENSG00000160712 . [P08887-1 ]
    GeneIDi 3570.
    KEGGi hsa:3570.
    UCSCi uc001fez.2. human. [P08887-1 ]
    uc001ffa.2. human. [P08887-2 ]

    Organism-specific databases

    CTDi 3570.
    GeneCardsi GC01P154377.
    HGNCi HGNC:6019. IL6R.
    MIMi 147880. gene.
    614689. phenotype.
    614752. phenotype.
    neXtProti NX_P08887.
    PharmGKBi PA29835.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47227.
    HOVERGENi HBG052118.
    InParanoidi P08887.
    KOi K05055.
    OMAi CQLAVPE.
    OrthoDBi EOG71CFM2.
    PhylomeDBi P08887.
    TreeFami TF331210.

    Enzyme and pathway databases

    Reactomei REACT_27307. Interleukin-6 signaling.
    SignaLinki P08887.

    Miscellaneous databases

    EvolutionaryTracei P08887.
    GeneWikii Interleukin-6_receptor.
    GenomeRNAii 3570.
    NextBioi 13954.
    PMAP-CutDB P08887.
    PROi P08887.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08887.
    Bgeei P08887.
    CleanExi HS_IL6R.
    Genevestigatori P08887.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR003961. 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 ]
    Pfami PF09240. IL6Ra-bind. 1 hit.
    [Graphical view ]
    SMARTi SM00060. FN3. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    PROSITEi PS50853. FN3. 2 hits.
    PS01354. HEMATOPO_REC_L_F3. 1 hit.
    PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: POLYMORPHISM, VARIANT ALA-358, ASSOCIATION OF VARIANT ALA-358 WITH IL6 AND SOLUBLE IL6R SERUM LEVELS.

    Entry informationi

    Entry nameiIL6RA_HUMAN
    AccessioniPrimary (citable) accession number: P08887
    Secondary accession number(s): A8KAE8
    , B2R6V4, Q16202, Q53EQ7, Q5FWG2, Q5VZ23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 174 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3