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UniProtKB - P40189 (IL6RB_HUMAN)

UniProt

P40189 - IL6RB_HUMAN

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Protein

Interleukin-6 receptor subunit beta

Gene

IL6ST

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Molecular functioni

  • ciliary neurotrophic factor receptor activity Source: BHF-UCL
  • ciliary neurotrophic factor receptor binding Source: BHF-UCL
  • growth factor binding Source: BHF-UCL
  • interleukin-11 receptor activity Source: Ensembl
  • interleukin-27 receptor activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  • ciliary neurotrophic factor-mediated signaling pathway Source: BHF-UCL
  • cytokine-mediated signaling pathway Source: BHF-UCL
  • glycogen metabolic process Source: Ensembl
  • interleukin-27-mediated signaling pathway Source: BHF-UCL
  • interleukin-6-mediated signaling pathway Source: BHF-UCL
  • leukemia inhibitory factor signaling pathway Source: BHF-UCL
  • negative regulation of apoptotic process Source: BHF-UCL
  • negative regulation of interleukin-6-mediated signaling pathway Source: BHF-UCL
  • oncostatin-M-mediated signaling pathway Source: BHF-UCL
  • positive regulation of acute inflammatory response Source: BHF-UCL
  • positive regulation of adaptive immune response Source: BHF-UCL
  • positive regulation of astrocyte differentiation Source: Ensembl
  • positive regulation of cardiac muscle hypertrophy Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of osteoblast differentiation Source: BHF-UCL
  • positive regulation of T cell proliferation Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor production Source: BHF-UCL
  • regulation of Notch signaling pathway Source: Ensembl
  • response to cytokine Source: BHF-UCL
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-1059683. Interleukin-6 signaling.
R-HSA-110056. MAPK3 (ERK1) activation.
R-HSA-112411. MAPK1 (ERK2) activation.
SignaLinkiP40189.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:IL6ST
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:6021. IL6ST.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 619597ExtracellularSequence AnalysisAdd
BLAST
Transmembranei620 – 64122HelicalSequence AnalysisAdd
BLAST
Topological domaini642 – 918277CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • ciliary neurotrophic factor receptor complex Source: BHF-UCL
  • dendrite Source: Ensembl
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • interleukin-6 receptor complex Source: BHF-UCL
  • membrane Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • oncostatin-M receptor complex Source: BHF-UCL
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi782 – 7821S → A: Increases cell surface expression. 1 Publication

Organism-specific databases

PharmGKBiPA29837.

Polymorphism and mutation databases

BioMutaiIL6ST.
DMDMi215273999.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 918896Interleukin-6 receptor subunit betaPRO_0000010899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 541 Publication
Glycosylationi43 – 431N-linked (GlcNAc...)1 Publication
Disulfide bondi48 ↔ 1031 Publication
Glycosylationi83 – 831N-linked (GlcNAc...)1 Publication
Glycosylationi131 – 1311N-linked (GlcNAc...)1 Publication
Disulfide bondi134 ↔ 1441 Publication
Glycosylationi157 – 1571N-linked (GlcNAc...)1 Publication
Disulfide bondi172 ↔ 1821 Publication
Glycosylationi227 – 2271N-linked (GlcNAc...)2 Publications
Glycosylationi379 – 3791N-linked (GlcNAc...)2 Publications
Glycosylationi383 – 3831N-linked (GlcNAc...)2 Publications
Glycosylationi390 – 3901N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi458 ↔ 4661 Publication
Glycosylationi553 – 5531N-linked (GlcNAc...)1 Publication
Glycosylationi564 – 5641N-linked (GlcNAc...)1 Publication
Modified residuei661 – 6611PhosphoserineCombined sources
Modified residuei667 – 6671PhosphoserineCombined sources
Modified residuei782 – 7821Phosphoserine1 Publication
Modified residuei829 – 8291PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation of Ser-782 down-regulates cell surface expression.1 Publication
Heavily N-glycosylated.5 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP40189.
PaxDbiP40189.
PRIDEiP40189.

PTM databases

PhosphoSiteiP40189.

Expressioni

Tissue specificityi

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

Inductioni

LIF and OSM activate the type I OSM receptor while only OSM can activate the type II OSM receptor.1 Publication

Gene expression databases

BgeeiP40189.
CleanExiHS_IL6ST.
ExpressionAtlasiP40189. baseline and differential.
GenevisibleiP40189. HS.

Organism-specific databases

HPAiCAB025784.
HPA010558.

Interactioni

Subunit structurei

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.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
K2Q2HRC72EBI-1030834,EBI-9007403From a different organism.
Stat3P422274EBI-1030834,EBI-602878From a different organism.

Protein-protein interaction databases

BioGridi109786. 28 interactions.
DIPiDIP-95N.
IntActiP40189. 10 interactions.
MINTiMINT-130473.
STRINGi9606.ENSP00000338799.

Structurei

Secondary structure

1
918
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 358Combined sources
Beta strandi37 – 393Combined sources
Beta strandi44 – 507Combined sources
Helixi52 – 587Combined sources
Helixi62 – 643Combined sources
Beta strandi65 – 695Combined sources
Helixi76 – 783Combined sources
Beta strandi80 – 834Combined sources
Beta strandi86 – 916Combined sources
Beta strandi97 – 10711Combined sources
Turni108 – 1103Combined sources
Beta strandi111 – 12313Combined sources
Beta strandi130 – 1378Combined sources
Beta strandi143 – 1475Combined sources
Beta strandi157 – 1648Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi194 – 2029Combined sources
Beta strandi205 – 2084Combined sources
Beta strandi212 – 2143Combined sources
Helixi216 – 2183Combined sources
Beta strandi219 – 2213Combined sources
Beta strandi226 – 2316Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi240 – 2456Combined sources
Helixi248 – 2514Combined sources
Beta strandi255 – 2639Combined sources
Helixi274 – 2774Combined sources
Beta strandi282 – 2865Combined sources
Beta strandi291 – 30313Combined sources
Beta strandi317 – 3215Combined sources
Helixi325 – 3317Combined sources
Beta strandi332 – 3387Combined sources
Beta strandi345 – 3517Combined sources
Helixi356 – 3594Combined sources
Beta strandi363 – 37210Combined sources
Beta strandi378 – 39114Combined sources
Beta strandi396 – 40611Combined sources
Beta strandi412 – 4165Combined sources
Beta strandi428 – 4358Combined sources
Beta strandi438 – 4447Combined sources
Beta strandi452 – 4609Combined sources
Beta strandi462 – 4643Combined sources
Beta strandi469 – 4746Combined sources
Beta strandi478 – 4814Combined sources
Beta strandi491 – 50010Combined sources
Beta strandi508 – 5158Combined sources
Beta strandi525 – 5306Combined sources
Beta strandi535 – 5395Combined sources
Helixi544 – 5474Combined sources
Beta strandi553 – 5608Combined sources
Beta strandi566 – 5716Combined sources
Beta strandi575 – 5795Combined sources
Beta strandi587 – 59610Combined sources
Beta strandi599 – 6024Combined sources
Beta strandi606 – 6094Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP40189.
SMRiP40189. Positions 24-612.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40189.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 12095Ig-like C2-typeAdd
BLAST
Domaini125 – 21692Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini224 – 324101Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini329 – 42496Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini426 – 51792Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini518 – 61396Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi310 – 3145WSXWS motif
Motifi651 – 6599Box 1 motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi725 – 75531Ser-richAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the type I cytokine receptor family. Type 2 subfamily.Curated
Contains 5 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 Ig-like C2-type (immunoglobulin-like) domain.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG145009.
GeneTreeiENSGT00550000074436.
HOGENOMiHOG000015771.
HOVERGENiHBG052119.
InParanoidiP40189.
KOiK05060.
OMAiFKQNCSQ.
OrthoDBiEOG7FXZXN.
PhylomeDBiP40189.
TreeFamiTF338122.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR003961. FN3_dom.
IPR003529. Hematopoietin_rcpt_Gp130_CS.
IPR013783. Ig-like_fold.
IPR010457. IgC2-like_lig-bd.
IPR015321. TypeI_recpt_CBD.
[Graphical view]
PfamiPF00041. fn3. 2 hits.
PF09240. IL6Ra-bind. 1 hit.
PF06328. Lep_receptor_Ig. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 5 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
PROSITEiPS50853. FN3. 4 hits.
PS01353. HEMATOPO_REC_L_F2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P40189-1) [UniParc]FASTAAdd to basket

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
MLTLQTWLVQ ALFIFLTTES TGELLDPCGY ISPESPVVQL HSNFTAVCVL 
        60         70         80         90        100
KEKCMDYFHV NANYIVWKTN HFTIPKEQYT IINRTASSVT FTDIASLNIQ 
       110        120        130        140        150
LTCNILTFGQ LEQNVYGITI ISGLPPEKPK NLSCIVNEGK KMRCEWDGGR 
       160        170        180        190        200
ETHLETNFTL KSEWATHKFA DCKAKRDTPT SCTVDYSTVY FVNIEVWVEA 
       210        220        230        240        250
ENALGKVTSD HINFDPVYKV KPNPPHNLSV INSEELSSIL KLTWTNPSIK 
       260        270        280        290        300
SVIILKYNIQ YRTKDASTWS QIPPEDTAST RSSFTVQDLK PFTEYVFRIR 
       310        320        330        340        350
CMKEDGKGYW SDWSEEASGI TYEDRPSKAP SFWYKIDPSH TQGYRTVQLV 
       360        370        380        390        400
WKTLPPFEAN GKILDYEVTL TRWKSHLQNY TVNATKLTVN LTNDRYLATL 
       410        420        430        440        450
TVRNLVGKSD AAVLTIPACD FQATHPVMDL KAFPKDNMLW VEWTTPRESV 
       460        470        480        490        500
KKYILEWCVL SDKAPCITDW QQEDGTVHRT YLRGNLAESK CYLITVTPVY 
       510        520        530        540        550
ADGPGSPESI KAYLKQAPPS KGPTVRTKKV GKNEAVLEWD QLPVDVQNGF 
       560        570        580        590        600
IRNYTIFYRT IIGNETAVNV DSSHTEYTLS SLTSDTLYMV RMAAYTDEGG 
       610        620        630        640        650
KDGPEFTFTT PKFAQGEIEA IVVPVCLAFL LTTLLGVLFC FNKRDLIKKH 
       660        670        680        690        700
IWPNVPDPSK SHIAQWSPHT PPRHNFNSKD QMYSDGNFTD VSVVEIEAND 
       710        720        730        740        750
KKPFPEDLKS LDLFKKEKIN TEGHSSGIGG SSCMSSSRPS ISSSDENESS 
       760        770        780        790        800
QNTSSTVQYS TVVHSGYRHQ VPSVQVFSRS ESTQPLLDSE ERPEDLQLVD 
       810        820        830        840        850
HVDGGDGILP RQQYFKQNCS QHESSPDISH FERSKQVSSV NEEDFVRLKQ 
       860        870        880        890        900
QISDHISQSC GSGQMKMFQE VSAADAFGPG TEGQVERFET VGMEAATDEG 
       910 
MPKSYLPQTV RQGGYMPQ
Length:918
Mass (Da):103,537
Last modified:November 25, 2008 - v2
Checksum:i6510A4409FFCF08C
GO
Isoform 2 (identifier: P40189-2) [UniParc]FASTAAdd to basket

Also known as: GP130-RAPS

The sequence of this isoform differs from the canonical sequence as follows:
     325-329: RPSKA → NIASF
     330-918: Missing.

Show »
Length:329
Mass (Da):37,499
Checksum:iD556124C867984E4
GO
Isoform 3 (identifier: P40189-3) [UniParc]FASTAAdd to basket

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

Show »
Length:857
Mass (Da):96,276
Checksum:i726208A5073B5451
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81L → V.2 Publications
Corresponds to variant rs1063560 [ dbSNP | Ensembl ].		VAR_047782
Natural varianti148 – 1481G → R.
Corresponds to variant rs2228044 [ dbSNP | Ensembl ].		VAR_047783
Natural varianti397 – 3971L → V.
Corresponds to variant rs2228043 [ dbSNP | Ensembl ].		VAR_047784
Natural varianti415 – 4151T → I in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036165
Natural varianti454 – 4541I → T.
Corresponds to variant rs2228046 [ dbSNP | Ensembl ].		VAR_047785
Natural varianti499 – 4991V → I.
Corresponds to variant rs34417936 [ dbSNP | Ensembl ].		VAR_047786

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei325 – 3295RPSKA → NIASF in isoform 2. 1 PublicationVSP_001684
Alternative sequencei330 – 918589Missing in isoform 2. 1 PublicationVSP_001685Add
BLAST
Alternative sequencei423 – 48361Missing in isoform 3. 1 PublicationVSP_043716Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3971.1. [P40189-1]
CCDS47209.1. [P40189-2]
CCDS54856.1. [P40189-3]
PIRiA36337.
RefSeqiNP_001177910.1. NM_001190981.1. [P40189-3]
NP_002175.2. NM_002184.3. [P40189-1]
NP_786943.1. NM_175767.2. [P40189-2]
UniGeneiHs.532082.
Hs.706627.

Genome annotation databases

EnsembliENST00000336909; 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]
GeneIDi3572.
KEGGihsa:3572.
UCSCiuc003jqq.3. human. [P40189-1]
uc003jqr.3. human. [P40189-2]
uc010iwb.3. human. [P40189-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3971.1. [P40189-1]
CCDS47209.1. [P40189-2]
CCDS54856.1. [P40189-3]
PIRiA36337.
RefSeqiNP_001177910.1. NM_001190981.1. [P40189-3]
NP_002175.2. NM_002184.3. [P40189-1]
NP_786943.1. NM_175767.2. [P40189-2]
UniGeneiHs.532082.
Hs.706627.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP40189.
SMRiP40189. Positions 24-612.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109786. 28 interactions.
DIPiDIP-95N.
IntActiP40189. 10 interactions.
MINTiMINT-130473.
STRINGi9606.ENSP00000338799.

Chemistry

ChEMBLiCHEMBL3137266.

PTM databases

PhosphoSiteiP40189.

Polymorphism and mutation databases

BioMutaiIL6ST.
DMDMi215273999.

Proteomic databases

MaxQBiP40189.
PaxDbiP40189.
PRIDEiP40189.

Protocols and materials databases

DNASUi3572.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336909; 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]
GeneIDi3572.
KEGGihsa:3572.
UCSCiuc003jqq.3. human. [P40189-1]
uc003jqr.3. human. [P40189-2]
uc010iwb.3. human. [P40189-3]

Organism-specific databases

CTDi3572.
GeneCardsiGC05M055935.
HGNCiHGNC:6021. IL6ST.
HPAiCAB025784.
HPA010558.
MIMi600694. gene.
neXtProtiNX_P40189.
PharmGKBiPA29837.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG145009.
GeneTreeiENSGT00550000074436.
HOGENOMiHOG000015771.
HOVERGENiHBG052119.
InParanoidiP40189.
KOiK05060.
OMAiFKQNCSQ.
OrthoDBiEOG7FXZXN.
PhylomeDBiP40189.
TreeFamiTF338122.

Enzyme and pathway databases

ReactomeiR-HSA-1059683. Interleukin-6 signaling.
R-HSA-110056. MAPK3 (ERK1) activation.
R-HSA-112411. MAPK1 (ERK2) activation.
SignaLinkiP40189.

Miscellaneous databases

ChiTaRSiIL6ST. human.
EvolutionaryTraceiP40189.
GeneWikiiGlycoprotein_130.
GenomeRNAii3572.
NextBioi13960.
PROiP40189.
SOURCEiSearch...

Gene expression databases

BgeeiP40189.
CleanExiHS_IL6ST.
ExpressionAtlasiP40189. baseline and differential.
GenevisibleiP40189. HS.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR003961. FN3_dom.
IPR003529. Hematopoietin_rcpt_Gp130_CS.
IPR013783. Ig-like_fold.
IPR010457. IgC2-like_lig-bd.
IPR015321. TypeI_recpt_CBD.
[Graphical view]
PfamiPF00041. fn3. 2 hits.
PF09240. IL6Ra-bind. 1 hit.
PF06328. Lep_receptor_Ig. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 5 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
PROSITEiPS50853. FN3. 4 hits.
PS01353. HEMATOPO_REC_L_F2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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, IDENTIFICATION BY 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  15. 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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661 AND SER-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-415.
+Additional computationally mapped references.

Entry informationi

Entry nameiIL6RB_HUMAN
AccessioniPrimary (citable) accession number: P40189
Secondary accession number(s): A0N0L4, Q5FC04, Q9UQ41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 25, 2008
Last modified: September 16, 2015
This is version 183 of the entry and version 2 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 5
    Human chromosome 5: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.