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Interleukin-6 (IL-6) (B-cell hybridoma growth factor) (Interleukin HP-1)

 IL6_MOUSE               Reviewed;         211 AA.
P08505; Q3UCQ0; Q8BN26;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
02-JUN-2021, entry version 191.
RecName: Full=Interleukin-6 {ECO:0000305};
Short=IL-6;
AltName: Full=B-cell hybridoma growth factor;
AltName: Full=Interleukin HP-1;
Flags: Precursor;
Name=Il6 {ECO:0000312|MGI:MGI:96559}; Synonyms=Il-6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2965020; DOI=10.1002/eji.1830180202;
van Snick J., Cayphas S., Szikora J.-P., Renauld J.-C., van Roost E.,
Boon T., Simpson R.J.;
"cDNA cloning of murine interleukin-HP1: homology with human interleukin
6.";
Eur. J. Immunol. 18:193-197(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3263439;
Tanabe O., Akira S., Kamiya T., Wong G.G., Hirano T., Kishimoto T.;
"Genomic structure of the murine IL-6 gene. High degree conservation of
potential regulatory sequences between mouse and human.";
J. Immunol. 141:3875-3881(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3262872; DOI=10.1073/pnas.85.19.7099;
Chiu C.P., Moulds C., Coffman R.L., Rennick D., Lee F.;
"Multiple biological activities are expressed by a mouse interleukin 6 cDNA
clone isolated from bone marrow stromal cells.";
Proc. Natl. Acad. Sci. U.S.A. 85:7099-7103(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=2243807; DOI=10.1093/nar/18.21.6455;
Grenett H.E., Fuentes N.L., Fuller G.M.;
"Cloning and sequence analysis of the cDNA for murine interleukin-6.";
Nucleic Acids Res. 18:6455-6455(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Macrophage;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
STRAIN=BALB/cJ;
PubMed=2106569; DOI=10.1084/jem.171.3.965;
Blankenstein T., Qin Z., Li W., Diamantstein T.;
"DNA rearrangement and constitutive expression of the interleukin 6 gene in
a mouse plasmacytoma.";
J. Exp. Med. 171:965-970(1990).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-211.
STRAIN=C57BL/6J;
PubMed=2563387;
Mock B.A., Nordan R.P., Justice M.J., Kozak C., Jenkins N.A.,
Copeland N.G., Clark S.C., Wong G.G., Rudikoff S.;
"The murine Il-6 gene maps to the proximal region of chromosome 5.";
J. Immunol. 142:1372-1376(1989).
[8]
PROTEIN SEQUENCE OF 25-45.
PubMed=2948184; DOI=10.1073/pnas.83.24.9679;
van Snick J., Cayphas S., Vink A., Uyttenhove C., Coulie P.G., Rubira M.R.,
Simpson R.J.;
"Purification and NH2-terminal amino acid sequence of a T-cell-derived
lymphokine with growth factor activity for B-cell hybridomas.";
Proc. Natl. Acad. Sci. U.S.A. 83:9679-9683(1986).
[9]
PROTEIN SEQUENCE OF 25-211.
PubMed=3262059; DOI=10.1111/j.1432-1033.1988.tb14267.x;
Simpson R.J., Moritz R.L., Rubira M.R., van Snick J.;
"Murine hybridoma/plasmacytoma growth factor. Complete amino-acid sequence
and relation to human interleukin-6.";
Eur. J. Biochem. 176:187-197(1988).
[10]
PROTEIN SEQUENCE OF 66-75; 78-84 AND 128-148.
PubMed=2302197; DOI=10.1016/0006-291x(90)91922-f;
Jahnen W., Ward L.D., Reid G.E., Moritz R.L., Simpson R.J.;
"Internal amino acid sequencing of proteins by in situ cyanogen bromide
cleavage in polyacrylamide gels.";
Biochem. Biophys. Res. Commun. 166:139-145(1990).
[11]
DISULFIDE BONDS.
PubMed=3264160; DOI=10.1016/s0006-291x(88)80056-1;
Simpson R.J., Moritz R.L., van Roost E., van Snick J.;
"Characterization of a recombinant murine interleukin-6: assignment of
disulphide bonds.";
Biochem. Biophys. Res. Commun. 157:364-372(1988).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8910279; DOI=10.1126/science.274.5291.1379;
Cressman D.E., Greenbaum L.E., DeAngelis R.A., Ciliberto G., Furth E.E.,
Poli V., Taub R.;
"Liver failure and defective hepatocyte regeneration in interleukin-6-
deficient mice.";
Science 274:1379-1383(1996).
[13]
FUNCTION.
PubMed=11113088; DOI=10.1053/gast.2000.20236;
Peters M., Blinn G., Jostock T., Schirmacher P.,
Meyer zum Bueschenfelde K.H., Galle P.R., Rose-John S.;
"Combined interleukin 6 and soluble interleukin 6 receptor accelerates
murine liver regeneration.";
Gastroenterology 119:1663-1671(2000).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11786910; DOI=10.1038/nm0102-75;
Wallenius V., Wallenius K., Ahren B., Rudling M., Carlsten H.,
Dickson S.L., Ohlsson C., Jansson J.O.;
"Interleukin-6-deficient mice develop mature-onset obesity.";
Nat. Med. 8:75-79(2002).
[15]
FUNCTION.
PubMed=15124018; DOI=10.1172/jci200420945;
Nemeth E., Rivera S., Gabayan V., Keller C., Taudorf S., Pedersen B.K.,
Ganz T.;
"IL-6 mediates hypoferremia of inflammation by inducing the synthesis of
the iron regulatory hormone hepcidin.";
J. Clin. Invest. 113:1271-1276(2004).
[16]
FUNCTION.
PubMed=17075861; DOI=10.1002/art.22175;
De Benedetti F., Rucci N., Del Fattore A., Peruzzi B., Paro R., Longo M.,
Vivarelli M., Muratori F., Berni S., Ballanti P., Ferrari S., Teti A.;
"Impaired skeletal development in interleukin-6-transgenic mice: a model
for the impact of chronic inflammation on the growing skeletal system.";
Arthritis Rheum. 54:3551-3563(2006).
[17]
FUNCTION IN TH17 DIFFERENTIATION, AND DISRUPTION PHENOTYPE.
PubMed=16990136; DOI=10.1016/j.cell.2006.07.035;
Ivanov I.I., McKenzie B.S., Zhou L., Tadokoro C.E., Lepelley A.,
Lafaille J.J., Cua D.J., Littman D.R.;
"The orphan nuclear receptor RORgammat directs the differentiation program
of proinflammatory IL-17+ T helper cells.";
Cell 126:1121-1133(2006).
[18]
FUNCTION, AND INDUCTION BY EXERCISE.
PubMed=22037645; DOI=10.1038/nm.2513;
Ellingsgaard H., Hauselmann I., Schuler B., Habib A.M., Baggio L.L.,
Meier D.T., Eppler E., Bouzakri K., Wueest S., Muller Y.D., Hansen A.M.,
Reinecke M., Konrad D., Gassmann M., Reimann F., Halban P.A., Gromada J.,
Drucker D.J., Gribble F.M., Ehses J.A., Donath M.Y.;
"Interleukin-6 enhances insulin secretion by increasing glucagon-like
peptide-1 secretion from L cells and alpha cells.";
Nat. Med. 17:1481-1489(2011).
[19]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY VIRAL
INFECTION.
PubMed=23045607; DOI=10.1084/jem.20111504;
Karnowski A., Chevrier S., Belz G.T., Mount A., Emslie D., D'Costa K.,
Tarlinton D.M., Kallies A., Corcoran L.M.;
"B and T cells collaborate in antiviral responses via IL-6, IL-21, and
transcriptional activator and coactivator, Oct2 and OBF-1.";
J. Exp. Med. 209:2049-2064(2012).
[20]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=28402851; DOI=10.1016/j.celrep.2017.03.043;
Timper K., Denson J.L., Steculorum S.M., Heilinger C., Engstroem-Ruud L.,
Wunderlich C.M., Rose-John S., Wunderlich F.T., Bruening J.C.;
"IL-6 Improves Energy and Glucose Homeostasis in Obesity via Enhanced
Central IL-6 trans-Signaling.";
Cell Rep. 19:267-280(2017).
[21]
INTERACTION WITH SORL1.
PubMed=28265003; DOI=10.1128/mcb.00641-16;
Larsen J.V., Petersen C.M.;
"SorLA in Interleukin-6 Signaling and Turnover.";
Mol. Cell. Biol. 37:0-0(2017).
[22]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=27893700; DOI=10.1038/ni.3632;
Heink S., Yogev N., Garbers C., Herwerth M., Aly L., Gasperi C.,
Husterer V., Croxford A.L., Moeller-Hackbarth K., Bartsch H.S., Sotlar K.,
Krebs S., Regen T., Blum H., Hemmer B., Misgeld T., Wunderlich T.F.,
Hidalgo J., Oukka M., Rose-John S., Schmidt-Supprian M., Waisman A.,
Korn T.;
"Trans-presentation of IL-6 by dendritic cells is required for the priming
of pathogenic TH17 cells.";
Nat. Immunol. 18:74-85(2017).
[23]
REVIEW ON FUNCTION.
PubMed=30995492; DOI=10.1016/j.immuni.2019.03.026;
Kang S., Tanaka T., Narazaki M., Kishimoto T.;
"Targeting Interleukin-6 Signaling in Clinic.";
Immunity 50:1007-1023(2019).
-!- FUNCTION: Cytokine with a wide variety of biological functions in
immunity, tissue regeneration, and metabolism (Probable). Binds to
IL6R, then the complex associates to the signaling subunit IL6ST/gp130
to trigger the intracellular IL6-signaling pathway (PubMed:8910279).
The interaction with the membrane-bound IL6R and IL6ST stimulates
'classic signaling', whereas the binding of IL6 and soluble IL6R to
IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling'
occurs when membrane-bound IL6:IL6R complexes on transmitter cells
activate IL6ST receptors on neighboring receiver cells
(PubMed:27893700). {ECO:0000269|PubMed:27893700,
ECO:0000269|PubMed:8910279, ECO:0000305|PubMed:30995492}.
-!- FUNCTION: IL6 is a potent inducer of the acute phase response. Rapid
production of IL6 contributes to host defense during infection and
tissue injury, but excessive IL6 synthesis is involved in disease
pathology. In the innate immune response, is synthesized by myeloid
cells, such as macrophages and dendritic cells, upon recognition of
pathogens through toll-like receptors (TLRs) at the site of infection
or tissue injury. In the adaptive immune response, is required for the
differentiation of B-cells into immunoglolin-secreting cells
(Probable). Plays a major role in the differentiation of CD4(+) T cell
subsets. Essential factor for the development of T follicular helper
(Tfh) cells that are required for the induction of germinal-center
formation. Together with IL21, controls the early generation of Tfh
cells and are critical for an effective antibody response to acute
viral infection (PubMed:23045607). Required to drive naive CD4(+) T
cells to the Th17 lineage, through 'cluster signaling' by dendritic
cells (PubMed:16990136, PubMed:27893700). Also required for
proliferation of myeloma cells and the survival of plasmablast cells
(Probable). {ECO:0000269|PubMed:16990136, ECO:0000269|PubMed:23045607,
ECO:0000269|PubMed:27893700, ECO:0000305|PubMed:30995492}.
-!- FUNCTION: Acts as an essential factor in bone homeostasis and on
vessels directly or indirectly by induction of VEGF, resulting in
increased angiogenesis activity and vascular permeability. Induces,
through 'trans-signaling' and synergistically with IL1B and TNF, the
production of VEGF (PubMed:17075861). Involved in metabolic controls,
is discharged into the bloodstream after muscle contraction increasing
lipolysis and improving insulin resistance (PubMed:11786910). 'Trans-
signaling' in central nervous system regulates energy and glucose
homeostasis (PubMed:28402851). Mediates, through GLP-1, crosstalk
between insulin-sensitive tissues, intestinal L cells and pancreatic
islets to adapt to changes in insulin demand (PubMed:11113088). Also
acts as a myokine (By similarity). Plays a protective role during liver
injury, being required for maintenance of tissue regeneration
(PubMed:11113088, PubMed:8910279). Also has a pivotal role in iron
metabolism by regulating HAMP/hepcidin expression upon inflammation or
bacterial infection (PubMed:15124018). Through activation of IL6ST-YAP-
NOTCH pathway, induces inflammation-induced epithelial regeneration (By
similarity). {ECO:0000250|UniProtKB:P05231,
ECO:0000269|PubMed:11113088, ECO:0000269|PubMed:11786910,
ECO:0000269|PubMed:15124018, ECO:0000269|PubMed:17075861,
ECO:0000269|PubMed:28402851, ECO:0000269|PubMed:8910279}.
-!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R and
IL6ST; first binds to IL6R to associate with the signaling subunit
IL6ST (PubMed:28265003). Interacts with IL6R (via the N-terminal
ectodomain); this interaction may be affected by IL6R-binding with
SORL1, hence decreasing IL6 cis signaling. Interacts with SORL1 (via
the N-terminal ectodomain); this interaction leads to IL6
internalization and lysosomal degradation. May form a trimeric complex
with the soluble SORL1 ectodomain and soluble IL6R receptor; this
interaction might stabilize circulating IL6, hence promoting IL6 trans
signaling (PubMed:28265003). {ECO:0000269|PubMed:28265003}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27893700}.
-!- TISSUE SPECIFICITY: Expressed by dendritic cells and macrophages
(PubMed:27893700, PubMed:23045607). Expressed by activated follicular B
cells (PubMed:23045607). Abundantly expressed in the central nervous
system (CNS), particularly the hypothalamic region (PubMed:28402851).
{ECO:0000269|PubMed:23045607, ECO:0000269|PubMed:27893700,
ECO:0000269|PubMed:28402851}.
-!- INDUCTION: In activated follicular B cells, expression is induced early
after influenza virus infection (PubMed:23045607). Plasma levels are
highly increased upon exercise, due to enhanced production by
contracting skeletal muscles (PubMed:22037645).
{ECO:0000269|PubMed:22037645, ECO:0000269|PubMed:23045607}.
-!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P05231}.
-!- DISRUPTION PHENOTYPE: Animals have normal T-cell numbers in the lamina
propria but the T(H)17 cells are reduced by about 10-fold
(PubMed:16990136). They develop mature-onset obesity and have disturbed
carbohydrate and lipid metabolism, increased leptin levels and
decreased responsiveness to leptin treatment (PubMed:11786910). Animals
have impaired liver regeneration characterized by liver necrosis and
failure (PubMed:8910279). Mutants infected with influenza virus do not
show a significant difference on germinal center B cells compared to
wild-types (PubMed:23045607). Double knockouts for IL21 and IL6
infected with influenza virus show a significant reduction in germinal
centers in both the draining lymphatic nodes and the spleens to wild-
types. Animals show a significant reduction in virus-specific IgM and
IgG (PubMed:23045607). {ECO:0000269|PubMed:11786910,
ECO:0000269|PubMed:16990136, ECO:0000269|PubMed:23045607,
ECO:0000269|PubMed:8910279}.
-!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; X06203; CAA29560.1; -; mRNA.
EMBL; M20572; AAA39302.1; -; Genomic_DNA.
EMBL; J03783; AAA39301.1; -; mRNA.
EMBL; X54542; CAA38411.1; -; mRNA.
EMBL; AK150440; BAE29562.1; -; mRNA.
EMBL; X51457; CAA35824.1; -; Genomic_DNA.
EMBL; M24221; AAA68814.1; -; Genomic_DNA.
CCDS; CCDS19153.1; -.
PIR; A30531; ICMS6.
RefSeq; NP_001300983.1; NM_001314054.1.
RefSeq; NP_112445.1; NM_031168.2.
PDB; 2L3Y; NMR; -; A=27-211.
PDBsum; 2L3Y; -.
SMR; P08505; -.
BioGRID; 200641; 2.
IntAct; P08505; 1.
STRING; 10090.ENSMUSP00000026845; -.
PhosphoSitePlus; P08505; -.
MaxQB; P08505; -.
PaxDb; P08505; -.
PRIDE; P08505; -.
ProteomicsDB; 267327; -.
Antibodypedia; 12025; 2980 antibodies.
DNASU; 16193; -.
Ensembl; ENSMUST00000026845; ENSMUSP00000026845; ENSMUSG00000025746.
GeneID; 16193; -.
KEGG; mmu:16193; -.
UCSC; uc008wuu.1; mouse.
CTD; 3569; -.
MGI; MGI:96559; Il6.
eggNOG; ENOG502S7Q4; Eukaryota.
GeneTree; ENSGT00390000000878; -.
HOGENOM; CLU_096521_0_0_1; -.
InParanoid; P08505; -.
OrthoDB; 1144279at2759; -.
PhylomeDB; P08505; -.
TreeFam; TF335984; -.
Reactome; R-MMU-1059683; Interleukin-6 signaling.
Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
Reactome; R-MMU-112411; MAPK1 (ERK2) activation.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
BioGRID-ORCS; 16193; 0 hits in 54 CRISPR screens.
EvolutionaryTrace; P08505; -.
PRO; PR:P08505; -.
Proteomes; UP000000589; Chromosome 5.
RNAct; P08505; protein.
Bgee; ENSMUSG00000025746; Expressed in subcutaneous adipose tissue and 67 other tissues.
Genevisible; P08505; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005896; C:interleukin-6 receptor complex; IDA:UniProtKB.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0008083; F:growth factor activity; ISO:MGI.
GO; GO:0005138; F:interleukin-6 receptor binding; IDA:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IDA:MGI.
GO; GO:0045454; P:cell redox homeostasis; ISO:MGI.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
GO; GO:1990646; P:cellular response to prolactin; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0031018; P:endocrine pancreas development; IMP:BHF-UCL.
GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; IDA:MGI.
GO; GO:0010467; P:gene expression; IDA:MGI.
GO; GO:0002314; P:germinal center B cell differentiation; IMP:UniProtKB.
GO; GO:0070091; P:glucagon secretion; IMP:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB.
GO; GO:0002384; P:hepatic immune response; ISO:MGI.
GO; GO:0072574; P:hepatocyte proliferation; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISO:MGI.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0097421; P:liver regeneration; IMP:UniProtKB.
GO; GO:0031294; P:lymphocyte costimulation; IEA:Ensembl.
GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:MGI.
GO; GO:0002262; P:myeloid cell homeostasis; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0045779; P:negative regulation of bone resorption; IMP:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
GO; GO:0032682; P:negative regulation of chemokine production; IDA:MGI.
GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0045721; P:negative regulation of gluconeogenesis; ISO:MGI.
GO; GO:0046888; P:negative regulation of hormone secretion; IDA:MGI.
GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0045837; P:negative regulation of membrane potential; ISO:MGI.
GO; GO:0048635; P:negative regulation of muscle organ development; ISO:MGI.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:2000635; P:negative regulation of primary miRNA processing; ISO:MGI.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
GO; GO:0031175; P:neuron projection development; ISO:MGI.
GO; GO:0001781; P:neutrophil apoptotic process; IDA:MGI.
GO; GO:0002675; P:positive regulation of acute inflammatory response; ISO:MGI.
GO; GO:1902512; P:positive regulation of apoptotic DNA fragmentation; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0050871; P:positive regulation of B cell activation; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IGI:MGI.
GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISO:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:MGI.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
GO; GO:0014015; P:positive regulation of gliogenesis; IMP:ARUK-UCL.
GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:UniProtKB.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:MGI.
GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:MGI.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:ARUK-UCL.
GO; GO:0032745; P:positive regulation of interleukin-21 production; IDA:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; IMP:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IMP:BHF-UCL.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
GO; GO:0051971; P:positive regulation of transmission of nerve impulse; ISO:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
GO; GO:0045188; P:regulation of circadian sleep/wake cycle, non-REM sleep; ISO:MGI.
GO; GO:0070092; P:regulation of glucagon secretion; IDA:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; IDA:UniProtKB.
GO; GO:0010574; P:regulation of vascular endothelial growth factor production; ISO:MGI.
GO; GO:0014823; P:response to activity; IDA:UniProtKB.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
GO; GO:0009408; P:response to heat; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; IDA:MGI.
GO; GO:0001878; P:response to yeast; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; IGI:MGI.
GO; GO:0061470; P:T follicular helper cell differentiation; IMP:UniProtKB.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; IDA:UniProtKB.
GO; GO:0010573; P:vascular endothelial growth factor production; ISS:UniProtKB.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR003574; IL-6.
InterPro; IPR030474; IL-6/GCSF/MGF.
InterPro; IPR030473; IL6/GCSF/MGF_CS.
PANTHER; PTHR10511; PTHR10511; 1.
PANTHER; PTHR10511:SF3; PTHR10511:SF3; 1.
Pfam; PF00489; IL6; 1.
PIRSF; PIRSF001935; IL6_MGF_GCSF; 1.
PRINTS; PR00433; IL6GCSFMGF.
SMART; SM00126; IL6; 1.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00254; INTERLEUKIN_6; 1.
1: Evidence at protein level;
3D-structure; Acute phase; Cytokine; Direct protein sequencing;
Disulfide bond; Growth factor; Reference proteome; Secreted; Signal.
SIGNAL 1..24
/evidence="ECO:0000269|PubMed:2948184,
ECO:0000269|PubMed:3262059"
CHAIN 25..211
/note="Interleukin-6"
/id="PRO_0000015588"
DISULFID 70..76
/evidence="ECO:0000269|PubMed:3264160"
DISULFID 99..109
/evidence="ECO:0000269|PubMed:3264160"
HELIX 48..68
/evidence="ECO:0007829|PDB:2L3Y"
TURN 69..72
/evidence="ECO:0007829|PDB:2L3Y"
HELIX 74..77
/evidence="ECO:0007829|PDB:2L3Y"
TURN 81..83
/evidence="ECO:0007829|PDB:2L3Y"
HELIX 84..86
/evidence="ECO:0007829|PDB:2L3Y"
STRAND 101..103
/evidence="ECO:0007829|PDB:2L3Y"
HELIX 114..129
/evidence="ECO:0007829|PDB:2L3Y"
HELIX 133..160
/evidence="ECO:0007829|PDB:2L3Y"
HELIX 170..176
/evidence="ECO:0007829|PDB:2L3Y"
HELIX 186..209
/evidence="ECO:0007829|PDB:2L3Y"
SEQUENCE 211 AA; 24384 MW; BBB47DDA9E86787A CRC64;
MKFLSARDFH PVAFLGLMLV TTTAFPTSQV RRGDFTEDTT PNRPVYTTSQ VGGLITHVLW
EIVEMRKELC NGNSDCMNND DALAENNLKL PEIQRNDGCY QTGYNQEICL LKISSGLLEY
HSYLEYMKNN LKDNKKDKAR VLQRDTETLI HIFNQEVKDL HKIVLPTPIS NALLTDKLES
QKEWLRTKTI QFILKSLEEF LKVTLRSTRQ T


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Pathways :
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
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WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1840: Interleukin-3, 5 and GM-CSF signaling
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1839: Interleukin-1 signaling
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP2332: Interleukin-11 Signaling Pathway
WP1838: Interleukin-1 processing
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP413: G1 to S cell cycle control
WP1011: T Cell Receptor Signaling Pathway
WP1793: Cell junction organization
WP2328: Allograft rejection
WP2005: Muscle cell TarBase
WP840: G1 to S cell cycle control
WP1308: Endochondral Ossification
WP2023: Cell Differentiation - meta
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Related Genes :
[Il6 Il-6] Interleukin-6 (IL-6) (B-cell hybridoma growth factor) (Interleukin HP-1)
[IL6 IFNB2] Interleukin-6 (IL-6) (B-cell stimulatory factor 2) (BSF-2) (CTL differentiation factor) (CDF) (Hybridoma growth factor) (Interferon beta-2) (IFN-beta-2)
[Il2 Il-2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[Il36a Fil1e Il1e Il1f6 Il1h1] Interleukin-36 alpha (FIL1 epsilon) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 6) (IL-1F6) (Interleukin-1 homolog 1) (IL-1H1)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF) (Aldesleukin)
[IL1R1 IL1R IL1RA IL1RT1] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[IL4] Interleukin-4 (IL-4) (B-cell stimulatory factor 1) (BSF-1) (Binetrakin) (Lymphocyte stimulatory factor 1) (Pitrakinra)
[Il3ra Sut-1] Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (Interleukin-3 receptor class II alpha chain) (CD antigen CD123)
[Il27ra Tccr Wsx1] Interleukin-27 receptor subunit alpha (IL-27 receptor subunit alpha) (IL-27R subunit alpha) (IL-27R-alpha) (IL-27RA) (Type I T-cell cytokine receptor) (TCCR) (WSX-1)
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (EC 3.2.2.6) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (CDw218b) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-1 receptor 7) (IL-1R-7) (IL-1R7) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)
[Il2 Il-2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[ORF1ab ORF1a orf1ab] 3C-like proteinase (EC 3.4.19.12) (EC 3.4.22.69) (Growth factor-like peptide) (Leader protein) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (Papain-like proteinase) (p65 homolog)
[IL6R] Interleukin-6 receptor subunit alpha (IL-6 receptor subunit alpha) (IL-6R subunit alpha) (IL-6R-alpha) (IL-6RA) (IL-6R 1) (Membrane glycoprotein 80) (gp80) (CD antigen CD126) [Cleaved into: Soluble interleukin-6 receptor subunit alpha (sIL6R)]
[Il11ra1 Etl2 Il11ra] Interleukin-11 receptor subunit alpha-1 (IL-11 receptor subunit alpha-1) (IL-11R subunit alpha-1) (IL-11R-alpha-1) (IL-11RA1) (Enhancer trap locus homolog 2) (Etl-2) (Novel cytokine receptor 1) (NR-1) (NR1) [Cleaved into: Soluble interleukin-11 receptor subunit alpha (sIL-11R) (sIL-11RA) (sIL11RA)]
[Il1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[Il1r1 Il-1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[Il4r Il4ra] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[IL36RN Fil1d Il1f5 Il1h3 Il1hy1] Interleukin-36 receptor antagonist protein (IL-36Ra) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 homolog 3) (IL-1H3) (Interleukin-1-like protein 1) (IL-1L1)
[IL6ST] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (CDw130) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[Cebpb Crp2 Nf-il6 Sfb] CCAAT/enhancer-binding protein beta (C/EBP beta) (C/EBP-related protein 2) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched inhibitory protein) (LIP) (Liver-enriched transcriptional activator) (LAP) (Silencer factor B) (SF-B)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[Il36b Fil1e Il1f8] Interleukin-36 beta (Interleukin-1 family member 8) (IL-1F8)
[IL36A FIL1E IL1E IL1F6] Interleukin-36 alpha (FIL1 epsilon) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 6) (IL-1F6)
[IL33 C9orf26 IL1F11 NFHEV] Interleukin-33 (IL-33) (Interleukin-1 family member 11) (IL-1F11) (Nuclear factor from high endothelial venules) (NF-HEV) [Cleaved into: Interleukin-33 (95-270); Interleukin-33 (99-270); Interleukin-33 (109-270)]
[Il33] Interleukin-33 (IL-33) [Cleaved into: Interleukin-33(102-266); Interleukin-33(109-266)]
[IL18R1 IL1RRP] Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (EC 3.2.2.6) (CD218 antigen-like family member A) (CDw218a) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (Interleukin-18 receptor alpha) (IL-18R-alpha) (IL-18Ralpha) (CD antigen CD218a)

Bibliography :
No related Items