P40189 (IL6RB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

IL6ST

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	918 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Signal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize gp130 for initiating signal transmission. Binds to IL6/IL6R (alpha chain) complex, resulting in the formation of high-affinity IL6 binding sites, and transduces the signal. Does not bind IL6. May have a role in embryonic development By similarity. The type I OSM receptor is capable of transducing OSM-specific signaling events.
Subunit structure	Interacts with INPP5D/SHIP1 By similarity. Forms heterodimers composed of LIPR and IL6ST (type I OSM receptor). Also forms heterodimers composed of OSMR and IL6ST (type II OSM receptor). Homodimer. The homodimer binds two molecules of herpes virus IL6. Component of a hexamer of two molecules each of IL6, IL6R and IL6ST. Interacts with HCK. Ref.8 Ref.9 Ref.18 Ref.20
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted.
Tissue specificity	Found in all the tissues and cell lines examined. Expression not restricted to IL6 responsive cells.
Induction	LIF and OSM activate the type I OSM receptor while only OSM can activate the type II OSM receptor. Ref.8
Domain	The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. The box 1 motif is required for JAK interaction and/or activation.
Post-translational modification	Phosphorylation of Ser-782 down-regulates cell surface expression. Heavily N-glycosylated. Ref.7 Ref.18
Sequence similarities	Belongs to the type I cytokine receptor family. Type 2 subfamily. Contains 5 fibronectin type-III domains. Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycogen metabolic process Inferred from electronic annotation. Source: Compara interleukin-6-mediated signaling pathway Inferred from direct assay Ref.1. Source: GOC leukemia inhibitory factor signaling pathway Inferred from genetic interaction PubMed 12643274Ref.8. Source: BHF-UCL negative regulation of apoptotic process Traceable author statement PubMed 17530315. Source: BHF-UCL negative regulation of interleukin-6-mediated signaling pathway Inferred from direct assay PubMed 8353278. Source: BHF-UCL oncostatin-M-mediated signaling pathway Inferred from direct assay Ref.8. Source: GOC positive regulation of T cell proliferation Inferred from mutant phenotype PubMed 14764690. Source: BHF-UCL positive regulation of acute inflammatory response Inferred by curator Ref.8. Source: BHF-UCL positive regulation of adaptive immune response Inferred by curator PubMed 14764690. Source: BHF-UCL positive regulation of astrocyte differentiation Inferred from electronic annotation. Source: Compara positive regulation of cardiac muscle hypertrophy Traceable author statement PubMed 10744750. Source: BHF-UCL positive regulation of osteoblast differentiation Inferred from mutant phenotype PubMed 12372336. Source: BHF-UCL positive regulation of tyrosine phosphorylation of Stat1 protein Inferred from mutant phenotype PubMed 14764690. Source: BHF-UCL positive regulation of tyrosine phosphorylation of Stat3 protein Inferred from mutant phenotype PubMed 14764690. Source: BHF-UCL positive regulation vascular endothelial growth factor production Traceable author statement PubMed 10744750. Source: BHF-UCL regulation of Notch signaling pathway Inferred from electronic annotation. Source: Compara
Cellular_component	ciliary neurotrophic factor receptor complex Inferred from direct assay PubMed 12707266. Source: BHF-UCL dendrite Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from electronic annotation. Source: Compara extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from direct assay PubMed 8353278. Source: BHF-UCL interleukin-6 receptor complex Inferred from direct assay Ref.20Ref.1. Source: BHF-UCL neuronal cell body Inferred from electronic annotation. Source: Compara oncostatin-M receptor complex Inferred from direct assay Ref.8. Source: BHF-UCL
Molecular_function	ciliary neurotrophic factor receptor activity Inferred from direct assay PubMed 12643274. Source: BHF-UCL interleukin-11 receptor activity Inferred from electronic annotation. Source: Compara interleukin-27 receptor activity Inferred by curator PubMed 14764690. Source: BHF-UCL protein homodimerization activity Traceable author statement PubMed 8390097. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Stat3	P42227	2	EBI-1030834,EBI-602878	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P40189-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P40189-2)

Also known as: GP130-RAPS;

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

Isoform 3 (identifier: P40189-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Chain

23 – 918

896

Interleukin-6 receptor subunit beta

PRO_0000010899

Regions

Topological domain

23 – 619

597

Extracellular Potential

Transmembrane

620 – 641

22

Helical; Potential

Topological domain

642 – 918

277

Cytoplasmic Potential

Domain

26 – 120

95

Ig-like C2-type

Domain

125 – 216

92

Fibronectin type-III 1

Domain

222 – 321

100

Fibronectin type-III 2

Domain

326 – 418

93

Fibronectin type-III 3

Domain

423 – 514

92

Fibronectin type-III 4

Domain

518 – 610

93

Fibronectin type-III 5

Motif

310 – 314

5

WSXWS motif

Motif

651 – 659

9

Box 1 motif

Compositional bias

725 – 755

31

Ser-rich

Amino acid modifications

Modified residue

667

1

Phosphoserine Ref.13 Ref.16

Modified residue

782

1

Phosphoserine Ref.10

Modified residue

829

1

Phosphoserine Ref.12

Glycosylation

43

1

N-linked (GlcNAc...) Ref.7

Glycosylation

83

1

N-linked (GlcNAc...) Ref.7

Glycosylation

131

1

N-linked (GlcNAc...) Ref.7

Glycosylation

157

1

N-linked (GlcNAc...) Ref.7

Glycosylation

227

1

N-linked (GlcNAc...) Ref.7 Ref.15

Glycosylation

379

1

N-linked (GlcNAc...) Ref.7 Ref.11

Glycosylation

383

1

N-linked (GlcNAc...) Ref.7 Ref.11

Glycosylation

390

1

N-linked (GlcNAc...) Ref.15

Glycosylation

553

1

N-linked (GlcNAc...) Ref.7

Glycosylation

564

1

N-linked (GlcNAc...) Ref.7

Disulfide bond

28 ↔ 54

Ref.7

Disulfide bond

48 ↔ 103

Ref.7

Disulfide bond

134 ↔ 144

Ref.7

Disulfide bond

172 ↔ 182

Ref.7

Disulfide bond

458 ↔ 466

Ref.7

Natural variations

Alternative sequence

325 – 329

5

RPSKA → NIASF in isoform 2.

VSP_001684

Alternative sequence

330 – 918

589

Missing in isoform 2.

VSP_001685

Alternative sequence

423 – 483

61

Missing in isoform 3.

VSP_043716

Natural variant

8

1

L → V. Ref.1 Ref.2
Corresponds to variant rs1063560 [ dbSNP | Ensembl ].

VAR_047782

Natural variant

148

1

G → R.
Corresponds to variant rs2228044 [ dbSNP | Ensembl ].

VAR_047783

Natural variant

397

1

L → V.
Corresponds to variant rs2228043 [ dbSNP | Ensembl ].

VAR_047784

Natural variant

415

1

T → I in a colorectal cancer sample; somatic mutation. Ref.21

VAR_036165

Natural variant

454

1

I → T.
Corresponds to variant rs2228046 [ dbSNP | Ensembl ].

VAR_047785

Natural variant

499

1

V → I.
Corresponds to variant rs34417936 [ dbSNP | Ensembl ].

VAR_047786

Experimental info

Mutagenesis

782

1

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

Secondary structure

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918

Helix Strand Turn

Details...

Beta strand

28 – 35

8

Beta strand

37 – 39

3

Beta strand

44 – 50

7

Helix

52 – 58

7

Helix

62 – 64

3

Beta strand

65 – 69

5

Helix

76 – 78

3

Beta strand

80 – 83

4

Beta strand

86 – 91

6

Beta strand

97 – 107

11

Turn

108 – 110

3

Beta strand

111 – 123

13

Beta strand

130 – 137

8

Beta strand

143 – 147

5

Beta strand

157 – 164

8

Beta strand

176 – 178

3

Beta strand

181 – 183

3

Beta strand

194 – 202

9

Beta strand

205 – 208

4

Beta strand

212 – 214

3

Helix

216 – 218

3

Beta strand

219 – 221

3

Beta strand

226 – 231

6

Beta strand

234 – 238

5

Beta strand

240 – 245

6

Helix

248 – 251

4

Beta strand

255 – 263

9

Helix

274 – 277

4

Beta strand

282 – 286

5

Beta strand

291 – 303

13

Beta strand

317 – 321

5

Helix

325 – 331

7

Beta strand

332 – 338

7

Beta strand

345 – 351

7

Helix

356 – 359

4

Beta strand

363 – 372

10

Beta strand

378 – 391

14

Beta strand

396 – 406

11

Beta strand

412 – 416

5

Beta strand

428 – 435

8

Beta strand

438 – 444

7

Beta strand

452 – 460

9

Beta strand

462 – 464

3

Beta strand

469 – 474

6

Beta strand

478 – 481

4

Beta strand

491 – 500

10

Beta strand

508 – 515

8

Beta strand

525 – 530

6

Beta strand

535 – 539

5

Helix

544 – 547

4

Beta strand

553 – 560

8

Beta strand

566 – 571

6

Beta strand

575 – 579

5

Beta strand

587 – 596

10

Beta strand

599 – 602

4

Beta strand

606 – 609

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 6510A4409FFCF08C	FASTA	918	103,537
	10 20 30 40 50 60 MLTLQTWLVQ ALFIFLTTES TGELLDPCGY ISPESPVVQL HSNFTAVCVL KEKCMDYFHV 70 80 90 100 110 120 NANYIVWKTN HFTIPKEQYT IINRTASSVT FTDIASLNIQ LTCNILTFGQ LEQNVYGITI 130 140 150 160 170 180 ISGLPPEKPK NLSCIVNEGK KMRCEWDGGR ETHLETNFTL KSEWATHKFA DCKAKRDTPT 190 200 210 220 230 240 SCTVDYSTVY FVNIEVWVEA ENALGKVTSD HINFDPVYKV KPNPPHNLSV INSEELSSIL 250 260 270 280 290 300 KLTWTNPSIK SVIILKYNIQ YRTKDASTWS QIPPEDTAST RSSFTVQDLK PFTEYVFRIR 310 320 330 340 350 360 CMKEDGKGYW SDWSEEASGI TYEDRPSKAP SFWYKIDPSH TQGYRTVQLV WKTLPPFEAN 370 380 390 400 410 420 GKILDYEVTL TRWKSHLQNY TVNATKLTVN LTNDRYLATL TVRNLVGKSD AAVLTIPACD 430 440 450 460 470 480 FQATHPVMDL KAFPKDNMLW VEWTTPRESV KKYILEWCVL SDKAPCITDW QQEDGTVHRT 490 500 510 520 530 540 YLRGNLAESK CYLITVTPVY ADGPGSPESI KAYLKQAPPS KGPTVRTKKV GKNEAVLEWD 550 560 570 580 590 600 QLPVDVQNGF IRNYTIFYRT IIGNETAVNV DSSHTEYTLS SLTSDTLYMV RMAAYTDEGG 610 620 630 640 650 660 KDGPEFTFTT PKFAQGEIEA IVVPVCLAFL LTTLLGVLFC FNKRDLIKKH IWPNVPDPSK 670 680 690 700 710 720 SHIAQWSPHT PPRHNFNSKD QMYSDGNFTD VSVVEIEAND KKPFPEDLKS LDLFKKEKIN 730 740 750 760 770 780 TEGHSSGIGG SSCMSSSRPS ISSSDENESS QNTSSTVQYS TVVHSGYRHQ VPSVQVFSRS 790 800 810 820 830 840 ESTQPLLDSE ERPEDLQLVD HVDGGDGILP RQQYFKQNCS QHESSPDISH FERSKQVSSV 850 860 870 880 890 900 NEEDFVRLKQ QISDHISQSC GSGQMKMFQE VSAADAFGPG TEGQVERFET VGMEAATDEG 910 MPKSYLPQTV RQGGYMPQ
	Isoform 2 (GP130-RAPS) [UniParc]. Checksum: D556124C867984E4	FASTA	329	37,499
	10 20 30 40 50 60 MLTLQTWLVQ ALFIFLTTES TGELLDPCGY ISPESPVVQL HSNFTAVCVL KEKCMDYFHV 70 80 90 100 110 120 NANYIVWKTN HFTIPKEQYT IINRTASSVT FTDIASLNIQ LTCNILTFGQ LEQNVYGITI 130 140 150 160 170 180 ISGLPPEKPK NLSCIVNEGK KMRCEWDGGR ETHLETNFTL KSEWATHKFA DCKAKRDTPT 190 200 210 220 230 240 SCTVDYSTVY FVNIEVWVEA ENALGKVTSD HINFDPVYKV KPNPPHNLSV INSEELSSIL 250 260 270 280 290 300 KLTWTNPSIK SVIILKYNIQ YRTKDASTWS QIPPEDTAST RSSFTVQDLK PFTEYVFRIR 310 320 CMKEDGKGYW SDWSEEASGI TYEDNIASF
	Isoform 3 [UniParc]. Checksum: 726208A5073B5451	FASTA	857	96,276
	10 20 30 40 50 60 MLTLQTWLVQ ALFIFLTTES TGELLDPCGY ISPESPVVQL HSNFTAVCVL KEKCMDYFHV 70 80 90 100 110 120 NANYIVWKTN HFTIPKEQYT IINRTASSVT FTDIASLNIQ LTCNILTFGQ LEQNVYGITI 130 140 150 160 170 180 ISGLPPEKPK NLSCIVNEGK KMRCEWDGGR ETHLETNFTL KSEWATHKFA DCKAKRDTPT 190 200 210 220 230 240 SCTVDYSTVY FVNIEVWVEA ENALGKVTSD HINFDPVYKV KPNPPHNLSV INSEELSSIL 250 260 270 280 290 300 KLTWTNPSIK SVIILKYNIQ YRTKDASTWS QIPPEDTAST RSSFTVQDLK PFTEYVFRIR 310 320 330 340 350 360 CMKEDGKGYW SDWSEEASGI TYEDRPSKAP SFWYKIDPSH TQGYRTVQLV WKTLPPFEAN 370 380 390 400 410 420 GKILDYEVTL TRWKSHLQNY TVNATKLTVN LTNDRYLATL TVRNLVGKSD AAVLTIPACD 430 440 450 460 470 480 FQGNLAESKC YLITVTPVYA DGPGSPESIK AYLKQAPPSK GPTVRTKKVG KNEAVLEWDQ 490 500 510 520 530 540 LPVDVQNGFI RNYTIFYRTI IGNETAVNVD SSHTEYTLSS LTSDTLYMVR MAAYTDEGGK 550 560 570 580 590 600 DGPEFTFTTP KFAQGEIEAI VVPVCLAFLL TTLLGVLFCF NKRDLIKKHI WPNVPDPSKS 610 620 630 640 650 660 HIAQWSPHTP PRHNFNSKDQ MYSDGNFTDV SVVEIEANDK KPFPEDLKSL DLFKKEKINT 670 680 690 700 710 720 EGHSSGIGGS SCMSSSRPSI SSSDENESSQ NTSSTVQYST VVHSGYRHQV PSVQVFSRSE 730 740 750 760 770 780 STQPLLDSEE RPEDLQLVDH VDGGDGILPR QQYFKQNCSQ HESSPDISHF ERSKQVSSVN 790 800 810 820 830 840 EEDFVRLKQQ ISDHISQSCG SGQMKMFQEV SAADAFGPGT EGQVERFETV GMEAATDEGM 850 PKSYLPQTVR QGGYMPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of an IL-6 signal transducer, gp130." Hibi M., Murakami M., Saito M., Hirano T., Taga T., Kishimoto T. Cell 63:1149-1157(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-8. Tissue: Myeloma and Placenta.
[2]	"Cloning of novel soluble gp130 and detection of its neutralizing autoantibodies in rheumatoid arthritis." Tanaka M., Kishimura M., Ozaki S., Osakada F., Hashimoto H., Okubo M., Murakami M., Nakao K. J. Clin. Invest. 106:137-144(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-8. Tissue: Synovium.
[3]	"IL6ST mRNA, nirs splice variant 4." Hayashi A., Sameshima E., Tabata Y., Iida K., Mitsuyama M., Kanai S., Furuya T., Saito T. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]	Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., Nickerson D.A. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130." Moritz R.L., Hall N.E., Connolly L.M., Simpson R.J. J. Biol. Chem. 276:8244-8253(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-43; ASN-83; ASN-131; ASN-157; ASN-227; ASN-379; ASN-383; ASN-553 AND ASN-564.
[8]	"Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation." Mosley B., De Imus C., Friend D., Boiani N., Thoma B., Park L.S., Cosman D. J. Biol. Chem. 271:32635-32643(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, INDUCTION.
[9]	"Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines." Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S., von Bubnoff N., de Vos G., Druker B.J., Yasukawa K., Griffin J.D., Emmerich B. Exp. Hematol. 25:1367-1377(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCK.
[10]	"Phosphorylation of human gp130 at Ser-782 adjacent to the di-leucine internalization motif. Effects on expression and signaling." Gibson R.M., Schiemann W.P., Prichard L.B., Reno J.M., Ericsson L.H., Nathanson N.M. J. Biol. Chem. 275:22574-22582(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-782, MUTAGENESIS OF SER-782, MASS SPECTROMETRY.
[11]	"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, MASS SPECTROMETRY. Tissue: Plasma.
[12]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, MASS SPECTROMETRY. Tissue: Platelet.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY. Tissue: Liver.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-415.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M57230 mRNA. Translation: AAA59155.1.
AB015706 mRNA. Translation: BAA78112.1.
AB102802 mRNA. Translation: BAD89393.1.
EF064722 Genomic DNA. Translation: ABK41905.1.
AC008914 Genomic DNA. No translation available.
AC016596 Genomic DNA. No translation available.
CH471123 Genomic DNA. Translation: EAW54936.1.

IPI

IPI00297124.
IPI00554518.
IPI00939624.

PIR

A36337.

RefSeq

NP_001177910.1. NM_001190981.1.
NP_002175.2. NM_002184.3.
NP_786943.1. NM_175767.2.

UniGene

Hs.532082.
Hs.706627.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BJ8	NMR	-	A	219-325	[»]
1BQU	X-ray	2.00	A/B	122-333	[»]
1I1R	X-ray	2.40	A	23-325	[»]
1N2Q	model	-	A/B	23-324	[»]
1P9M	X-ray	3.65	A	23-321	[»]
1PVH	X-ray	2.50	A/C	123-323	[»]
3L5H	X-ray	3.60	A	24-612	[»]
3L5I	X-ray	1.90	A	323-612	[»]
3L5J	X-ray	3.04	A/B	323-610	[»]

ProteinModelPortal

P40189.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-95N.

IntAct

P40189. 6 interactions.

MINT

MINT-130473.

STRING

9606.ENSP00000338799.

PTM databases

PhosphoSite

P40189.

Polymorphism databases

DMDM

215273999.

Proteomic databases

PaxDb

P40189.

PRIDE

P40189.

Protocols and materials databases

DNASU

3572.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000336909; ENSP00000338799; ENSG00000134352.
ENST00000381287; ENSP00000370687; ENSG00000134352.
ENST00000381294; ENSP00000370694; ENSG00000134352.
ENST00000381298; ENSP00000370698; ENSG00000134352.
ENST00000502326; ENSP00000462158; ENSG00000134352.
ENST00000522633; ENSP00000435399; ENSG00000134352.
ENST00000536319; ENSP00000444456; ENSG00000134352.

GeneID

3572.

KEGG

hsa:3572.

UCSC

uc003jqq.3. human.
uc003jqr.3. human.

Organism-specific databases

CTD

3572.

GeneCards

GC05M055230.

HGNC

HGNC:6021. IL6ST.

HPA

CAB025784.
HPA010558.

MIM

600694. gene.

neXtProt

NX_P40189.

PharmGKB

PA29837.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG145009.

HOGENOM

HOG000015771.

HOVERGEN

HBG052119.

InParanoid

P40189.

KO

K05060.

OMA

KDQMYSD.

OrthoDB

EOG42BX7V.

PhylomeDB

P40189.

Enzyme and pathway databases

Pathway_Interaction_DB

il27pathway. IL27-mediated signaling events.
il6_7pathway. IL6-mediated signaling events.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P40189.

Bgee

P40189.

CleanEx

HS_IL6ST.

Genevestigator

P40189.

GermOnline

ENSG00000134352. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 5 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR003529. Hematopoietin_rcpt_Gp130_CS.
IPR013783. Ig-like_fold.
IPR010457. IgC2-like_lig-bd.
IPR015321. IL6_recept-bd.
[Graphical view]

Pfam

PF00041. fn3. 2 hits.
PF09240. IL6Ra-bind. 1 hit.
PF06328. Lep_receptor_Ig. 1 hit.
[Graphical view]

SMART

SM00060. FN3. 5 hits.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 6 hits.

PROSITE

PS50853. FN3. 5 hits.
PS01353. HEMATOPO_REC_L_F2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

IL6ST. human.

EvolutionaryTrace

P40189.

GenomeRNAi

3572.

NextBio

13960.

SOURCE

Search...

Entry information

Entry name

IL6RB_HUMAN

Accession

Primary (citable) accession number: P40189
Secondary accession number(s): A0N0L4, Q5FC04, Q9UQ41

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 157 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.