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P08887

- IL6RA_HUMAN

UniProt

P08887 - IL6RA_HUMAN

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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

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. cytokine receptor activity Source: InterPro
  3. enzyme binding Source: UniProtKB
  4. interleukin-6 binding Source: BHF-UCL
  5. 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
Complete GO annotation...

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. extracellular region Source: UniProtKB
  3. extracellular space Source: BHF-UCL
  4. interleukin-6 receptor complex Source: BHF-UCL
  5. plasma membrane Source: Reactome
Complete GO annotation...

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

BgeeiP08887.
CleanExiHS_IL6R.
ExpressionAtlasiP08887. baseline and differential.
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.
GeneTreeiENSGT00530000063103.
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

        10         20         30         40         50
MLAVGCALLA ALLAAPGAAL APRRCPAQEV ARGVLTSLPG DSVTLTCPGV
60 70 80 90 100
EPEDNATVHW VLRKPAAGSH PSRWAGMGRR LLLRSVQLHD SGNYSCYRAG
110 120 130 140 150
RPAGTVHLLV DVPPEEPQLS CFRKSPLSNV VCEWGPRSTP SLTTKAVLLV
160 170 180 190 200
RKFQNSPAED FQEPCQYSQE SQKFSCQLAV PEGDSSFYIV SMCVASSVGS
210 220 230 240 250
KFSKTQTFQG CGILQPDPPA NITVTAVARN PRWLSVTWQD PHSWNSSFYR
260 270 280 290 300
LRFELRYRAE RSKTFTTWMV KDLQHHCVIH DAWSGLRHVV QLRAQEEFGQ
310 320 330 340 350
GEWSEWSPEA MGTPWTESRS PPAENEVSTP MQALTTNKDD DNILFRDSAN
360 370 380 390 400
ATSLPVQDSS SVPLPTFLVA GGSLAFGTLL CIAIVLRFKK TWKLRALKEG
410 420 430 440 450
KTSMHPPYSL GQLVPERPRP TPVLVPLISP PVSPSSLGSD NTSSHNRPDA
460
RDPRSPYDIS NTDYFFPR
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 CHEMBL3137266.
DrugBanki DB06273. Tocilizumab.

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.
GeneTreei ENSGT00530000063103.
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

Bgeei P08887.
CleanExi HS_IL6R.
ExpressionAtlasi P08887. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 175 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