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Interleukin-6 (IL-6) (B-cell stimulatory factor 2) (BSF-2) (CTL differentiation factor) (CDF) (Hybridoma growth factor) (Interferon beta-2) (IFN-beta-2)

 IL6_HUMAN               Reviewed;         212 AA.
P05231; Q9UCU2; Q9UCU3; Q9UCU4;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
02-JUN-2021, entry version 236.
RecName: Full=Interleukin-6 {ECO:0000305};
Short=IL-6;
AltName: Full=B-cell stimulatory factor 2;
Short=BSF-2;
AltName: Full=CTL differentiation factor;
Short=CDF;
AltName: Full=Hybridoma growth factor;
AltName: Full=Interferon beta-2;
Short=IFN-beta-2;
Flags: Precursor;
Name=IL6 {ECO:0000312|HGNC:HGNC:6018}; Synonyms=IFNB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3491322; DOI=10.1038/324073a0;
Hirano T., Yasukawa K., Harada H., Taga T., Watanabe Y., Matsuda T.,
Kashiwamura S., Nakajima K., Koyama K., Iwamatsu A., Tsunasawa S.,
Sakiyama F., Matsui H., Takahara Y., Taniguchi T., Kishimoto T.;
"Complementary DNA for a novel human interleukin (BSF-2) that induces B
lymphocytes to produce immunoglobulin.";
Nature 324:73-76(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3500852; DOI=10.1002/j.1460-2075.1987.tb02598.x;
Yasukawa K., Hirano T., Watanabe Y., Muratani K., Matsuda T., Nakai S.,
Kishimoto T.;
"Structure and expression of human B cell stimulatory factor-2 (BSF-2/IL-6)
gene.";
EMBO J. 6:2939-2945(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3538015; DOI=10.1073/pnas.83.23.8957;
May L.T., Helfgott D.C., Sehgal P.B.;
"Anti-beta-interferon antibodies inhibit the increased expression of HLA-B7
mRNA in tumor necrosis factor-treated human fibroblasts: structural studies
of the beta 2 interferon involved.";
Proc. Natl. Acad. Sci. U.S.A. 83:8957-8961(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3023045; DOI=10.1002/j.1460-2075.1986.tb04531.x;
Zilberstein A., Ruggieri R., Korn J.H., Revel M.;
"Structure and expression of cDNA and genes for human interferon-beta-2, a
distinct species inducible by growth-stimulatory cytokines.";
EMBO J. 5:2529-2537(1986).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3320204;
Brakenhoff J.P.J., de Groot E.R., Evers R.F., Pannekoek H., Aarden L.A.;
"Molecular cloning and expression of hybridoma growth factor in Escherichia
coli.";
J. Immunol. 139:4116-4121(1987).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2789513; DOI=10.1016/0006-291x(89)92328-0;
Tonouchi N., Miwa K., Karasuyama H., Matsui H.;
"Deletion of 3' untranslated region of human BSF-2 mRNA causes
stabilization of the mRNA and high-level expression in mouse NIH3T3
cells.";
Biochem. Biophys. Res. Commun. 163:1056-1062(1989).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Fibroblast;
PubMed=3758081; DOI=10.1111/j.1432-1033.1986.tb09931.x;
Haegeman G., Content J., Volckaert G., Derynck R., Tavernier J., Fiers W.;
"Structural analysis of the sequence coding for an inducible 26-kDa protein
in human fibroblasts.";
Eur. J. Biochem. 159:625-632(1986).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3266463;
Wong G., Witek-Giannotti J., Hewick R., Clark S., Ogawa M.;
"Interleukin 6: identification as a hematopoietic colony-stimulating
factor.";
Behring Inst. Mitt. 83:40-47(1988).
[9]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1291290;
Chen Q.Y.;
"Stable and efficient expression of human interleukin-6 cDNA in mammalian
cells after gene transfer.";
Zhonghua Zhong Liu Za Zhi 14:340-344(1992).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-32 AND VAL-162.
SeattleSNPs variation discovery resource;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 30-63.
PubMed=3279116;
van Damme J., van Beeumen J., Decock B., van Snick J., de Ley M.,
Billiau A.;
"Separation and comparison of two monokines with lymphocyte-activating
factor activity: IL-1 beta and hybridoma growth factor (HGF).
Identification of leukocyte-derived HGF as IL-6.";
J. Immunol. 140:1534-1541(1988).
[13]
PROTEIN SEQUENCE OF 30-50.
PubMed=2610854;
Ming J.E., Cernetti C., Steinman R.M., Granelli-Piperno A.;
"Interleukin 6 is the principal cytolytic T lymphocyte differentiation
factor for thymocytes in human leukocyte conditioned medium.";
J. Mol. Cell. Immunol. 4:203-211(1989).
[14]
PROTEIN SEQUENCE OF 30-40, AND GLYCOSYLATION.
PubMed=1883960; DOI=10.1016/1043-4666(91)90018-9;
May L.T., Shaw J.E., Khanna A.K., Zabriskie J.B., Sehgal P.B.;
"Marked cell-type-specific differences in glycosylation of human
interleukin-6.";
Cytokine 3:204-211(1991).
[15]
PROTEIN SEQUENCE OF 50-212.
PubMed=7851440; DOI=10.1111/j.1432-1033.1995.tb20427.x;
Breton J., la Fiura A., Bertolero F., Orsini G., Valsasina B., Ziliotto R.,
de Filippis V., Polverino de Laureto P., Fontana A.;
"Structure, stability and biological properties of a N-terminally truncated
form of recombinant human interleukin-6 containing a single disulfide
bond.";
Eur. J. Biochem. 227:573-581(1995).
[16]
DISULFIDE BONDS.
PubMed=2472117; DOI=10.1016/0003-9861(89)90205-1;
Clogston C.L., Boone T.C., Crandall B.C., Mendiaz E.A., Lu H.S.;
"Disulfide structures of human interleukin-6 are similar to those of human
granulocyte colony stimulating factor.";
Arch. Biochem. Biophys. 272:144-151(1989).
[17]
MUTAGENESIS.
PubMed=2037043; DOI=10.1016/0014-5793(91)80491-k;
Luetticken C., Kruettgen A., Moeller C., Heinrich P.C., Rose-John S.;
"Evidence for the importance of a positive charge and an alpha-helical
structure of the C-terminus for biological activity of human IL-6.";
FEBS Lett. 282:265-267(1991).
[18]
TISSUE SPECIFICITY, INDUCTION BY EXERCISE, AND SUBCELLULAR LOCATION.
PubMed=11080265; DOI=10.1111/j.1469-7793.2000.00237.x;
Steensberg A., van Hall G., Osada T., Sacchetti M., Saltin B.,
Klarlund Pedersen B.;
"Production of interleukin-6 in contracting human skeletal muscles can
account for the exercise-induced increase in plasma interleukin-6.";
J. Physiol. (Lond.) 529:237-242(2000).
[19]
FUNCTION.
PubMed=12794819; DOI=10.1002/art.11143;
Nakahara H., Song J., Sugimoto M., Hagihara K., Kishimoto T., Yoshizaki K.,
Nishimoto N.;
"Anti-interleukin-6 receptor antibody therapy reduces vascular endothelial
growth factor production in rheumatoid arthritis.";
Arthritis Rheum. 48:1521-1529(2003).
[20]
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).
[21]
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).
[22]
FUNCTION.
PubMed=20823453; DOI=10.1152/ajpendo.00328.2010;
Wolsk E., Mygind H., Groendahl T.S., Pedersen B.K., van Hall G.;
"IL-6 selectively stimulates fat metabolism in human skeletal muscle.";
Am. J. Physiol. 299:E832-E840(2010).
[23]
FUNCTION.
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).
[24]
PHOSPHORYLATION AT SER-81.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted phosphoproteome.";
Cell 161:1619-1632(2015).
[25]
FUNCTION.
PubMed=25731159; DOI=10.1038/nature14228;
Taniguchi K., Wu L.W., Grivennikov S.I., de Jong P.R., Lian I., Yu F.X.,
Wang K., Ho S.B., Boland B.S., Chang J.T., Sandborn W.J., Hardiman G.,
Raz E., Maehara Y., Yoshimura A., Zucman-Rossi J., Guan K.L., Karin M.;
"A gp130-Src-YAP module links inflammation to epithelial regeneration.";
Nature 519:57-62(2015).
[26]
INTERACTION WITH IL6R AND 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).
[27]
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).
[28]
STRUCTURE BY NMR.
PubMed=8555185; DOI=10.1021/bi951949e;
Nishimura C., Watanabe A., Gouda H., Shimada I., Arata Y.;
"Folding topologies of human interleukin-6 and its mutants as studied by
NMR spectroscopy.";
Biochemistry 35:273-281(1996).
[29]
STRUCTURE BY NMR.
PubMed=9159484; DOI=10.1006/jmbi.1997.0933;
Xu G.-Y., Yu H.-A., Hong J., Stahl M., McDonagh T., Kay L.E., Cumming D.A.;
"Solution structure of recombinant human interleukin-6.";
J. Mol. Biol. 268:468-481(1997).
[30]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=9118960; DOI=10.1093/emboj/16.5.989;
Somers W., Stahl M., Seehra J.S.;
"1.9-A crystal structure of interleukin 6: implications for a novel mode of
receptor dimerization and signaling.";
EMBO J. 16:989-997(1997).
[31] {ECO:0007744|PDB:1P9M}
X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS) OF 29-212 IN COMPLEX WITH IL6ST AND
IL6R, AND SUBUNIT.
PubMed=12829785; DOI=10.1126/science.1083901;
Boulanger M.J., Chow D.C., Brevnova E.E., Garcia K.C.;
"Hexameric structure and assembly of the interleukin-6/IL-6 alpha-
receptor/gp130 complex.";
Science 300:2101-2104(2003).
[32]
INVOLVEMENT IN RASJ.
PubMed=9769329; DOI=10.1172/jci2629;
Fishman D., Faulds G., Jeffery R., Mohamed-Ali V., Yudkin J.S.,
Humphries S., Woo P.;
"The effect of novel polymorphisms in the interleukin-6 (IL-6) gene on IL-6
transcription and plasma IL-6 levels, and an association with systemic-
onset juvenile chronic arthritis.";
J. Clin. Invest. 102:1369-1376(1998).
[33]
INVOLVEMENT IN SUSCEPTIBILITY TO KAPOSI SARCOMA.
PubMed=11001912;
Foster C.B., Lehrnbecher T., Samuels S., Stein S., Mol F., Metcalf J.A.,
Wyvill K., Steinberg S.M., Kovacs J., Blauvelt A., Yarchoan R.,
Chanock S.J.;
"An IL6 promoter polymorphism is associated with a lifetime risk of
development of Kaposi sarcoma in men infected with human immunodeficiency
virus.";
Blood 96:2562-2567(2000).
[34]
INVOLVEMENT IN BMD.
PubMed=11355017; DOI=10.1007/s100380170077;
Ota N., Nakajima T., Nakazawa I., Suzuki T., Hosoi T., Orimo H., Inoue S.,
Shirai Y., Emi M.;
"A nucleotide variant in the promoter region of the interleukin-6 gene
associated with decreased bone mineral density.";
J. Hum. Genet. 46:267-272(2001).
[35]
INVOLVEMENT IN BMD.
PubMed=12768442; DOI=10.1007/s10038-003-0020-8;
Chung H.W., Seo J.-S., Hur S.E., Kim H.L., Kim J.Y., Jung J.H., Kim L.H.,
Park B.L., Shin H.D.;
"Association of interleukin-6 promoter variant with bone mineral density in
pre-menopausal women.";
J. Hum. Genet. 48:243-248(2003).
-!- FUNCTION: Cytokine with a wide variety of biological functions in
immunity, tissue regeneration, and metabolism. Binds to IL6R, then the
complex associates to the signaling subunit IL6ST/gp130 to trigger the
intracellular IL6-signaling pathway (Probable). 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 (Probable).
{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 (Probable). In the adaptive immune response, is
required for the differentiation of B cells into immunoglobulin-
secreting cells. 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. Required to drive naive CD4(+) T cells to the Th17
lineage. Also required for proliferation of myeloma cells and the
survival of plasmablast cells (By similarity).
{ECO:0000250|UniProtKB:P08505, 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
(PubMed:17075861, PubMed:12794819). Induces, through 'trans-signaling'
and synergistically with IL1B and TNF, the production of VEGF
(PubMed:12794819). Involved in metabolic controls, is discharged into
the bloodstream after muscle contraction increasing lipolysis and
improving insulin resistance (PubMed:20823453). 'Trans-signaling' in
central nervous system also regulates energy and glucose homeostasis
(By similarity). Mediates, through GLP-1, crosstalk between insulin-
sensitive tissues, intestinal L cells and pancreatic islets to adapt to
changes in insulin demand (By similarity). Also acts as a myokine
(Probable). Plays a protective role during liver injury, being required
for maintenance of tissue regeneration (By similarity). 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:P08505,
ECO:0000269|PubMed:12794819, ECO:0000269|PubMed:15124018,
ECO:0000269|PubMed:17075861, ECO:0000269|PubMed:20823453,
ECO:0000305|PubMed:30995492}.
-!- 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:12829785). Interacts with IL6R (via the N-terminal
ectodomain); this interaction may be affected by IL6R-binding with
SORL1, hence decreasing IL6 cis signaling (PubMed:28265003). Interacts
with SORL1 (via the N-terminal ectodomain); this interaction leads to
IL6 internalization and lysosomal degradation (PubMed:28265003). 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:12829785, ECO:0000269|PubMed:28265003}.
-!- INTERACTION:
P05231; P08887: IL6R; NbExp=7; IntAct=EBI-720533, EBI-299383;
P05231; Q92673: SORL1; NbExp=4; IntAct=EBI-720533, EBI-1171329;
P05231; Q99523: SORT1; NbExp=4; IntAct=EBI-720533, EBI-1057058;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11080265}.
-!- TISSUE SPECIFICITY: Produced by skeletal muscle.
{ECO:0000269|PubMed:11080265}.
-!- INDUCTION: Plasma levels are highly increased upon exercise, due to
enhanced production by contracting skeletal muscles.
{ECO:0000269|PubMed:11080265}.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:1883960}.
-!- POLYMORPHISM: Genetic variations in IL6 may be correlated with bone
mineral density (BMD). Low BMD is a risk factor for osteoporotic
fracture. Osteoporosis is characterized by reduced bone mineral
density, disruption of bone microarchitecture, and the alteration of
the amount and variety of non-collagenous proteins in bone.
Osteoporotic bones are more at risk of fracture.
{ECO:0000269|PubMed:11355017, ECO:0000269|PubMed:12768442}.
-!- DISEASE: Rheumatoid arthritis systemic juvenile (RASJ) [MIM:604302]: An
inflammatory articular disorder with systemic onset beginning before
the age of 16. It represents a subgroup of juvenile arthritis
associated with severe extraarticular features and occasionally fatal
complications. During active phases of the disorder, patients display a
typical daily spiking fever, an evanescent macular rash,
lymphadenopathy, hepatosplenomegaly, serositis, myalgia and arthritis.
{ECO:0000269|PubMed:9769329}. Note=Disease susceptibility is associated
with variants affecting the gene represented in this entry.
-!- DISEASE: Note=A IL6 promoter polymorphism is associated with a lifetime
risk of development of Kaposi sarcoma in HIV-infected men.
{ECO:0000269|PubMed:11001912}.
-!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-6 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_6";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il6/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=IL6";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/IL6ID519ch7p15.html";
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EMBL; X04430; CAA28026.1; -; mRNA.
EMBL; M14584; AAA52728.1; -; mRNA.
EMBL; X04602; CAA28268.1; -; mRNA.
EMBL; Y00081; CAA68278.1; -; Genomic_DNA.
EMBL; M18403; AAA52729.1; -; mRNA.
EMBL; M29150; AAA59154.1; -; mRNA.
EMBL; X04402; CAA27990.1; -; Genomic_DNA.
EMBL; X04403; CAA27991.1; -; mRNA.
EMBL; M54894; AAC41704.1; -; mRNA.
EMBL; S56892; AAD13886.1; -; mRNA.
EMBL; AF372214; AAK48987.1; -; Genomic_DNA.
EMBL; BC015511; AAH15511.1; -; mRNA.
CCDS; CCDS5375.1; -.
PIR; A32648; IVHUB2.
RefSeq; NP_000591.1; NM_000600.4.
RefSeq; XP_011513692.1; XM_011515390.2.
PDB; 1ALU; X-ray; 1.90 A; A=28-212.
PDB; 1IL6; NMR; -; A=28-212.
PDB; 1N2Q; Model; -; E/F=30-212.
PDB; 1P9M; X-ray; 3.65 A; B=29-212.
PDB; 2IL6; NMR; -; A=28-212.
PDB; 4CNI; X-ray; 2.20 A; C/D=42-212.
PDB; 4J4L; X-ray; 2.30 A; C/D=47-212.
PDB; 4NI7; X-ray; 2.40 A; A=28-212.
PDB; 4NI9; X-ray; 2.55 A; A/C=28-212.
PDB; 4O9H; X-ray; 2.42 A; A=28-212.
PDB; 4ZS7; X-ray; 2.93 A; A=42-212.
PDB; 5FUC; X-ray; 2.70 A; A/B=49-212.
PDBsum; 1ALU; -.
PDBsum; 1IL6; -.
PDBsum; 1N2Q; -.
PDBsum; 1P9M; -.
PDBsum; 2IL6; -.
PDBsum; 4CNI; -.
PDBsum; 4J4L; -.
PDBsum; 4NI7; -.
PDBsum; 4NI9; -.
PDBsum; 4O9H; -.
PDBsum; 4ZS7; -.
PDBsum; 5FUC; -.
SMR; P05231; -.
BioGRID; 109783; 9.
DIP; DIP-482N; -.
IntAct; P05231; 8.
STRING; 9606.ENSP00000385675; -.
BindingDB; P05231; -.
ChEMBL; CHEMBL1795129; -.
DrugBank; DB05767; Andrographolide.
DrugBank; DB05513; Atiprimod.
DrugBank; DB11967; Binimetinib.
DrugBank; DB05744; CRx-139.
DrugBank; DB12140; Dilmapimod.
DrugBank; DB10770; Foreskin fibroblast (neonatal).
DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DrugBank; DB01404; Ginseng.
DrugBank; DB09221; Polaprezinc.
DrugBank; DB09036; Siltuximab.
DrugBank; DB06083; Tapinarof.
DrugBank; DB05470; VX-702.
DrugBank; DB05017; YSIL6.
DrugCentral; P05231; -.
GlyGen; P05231; 1 site.
iPTMnet; P05231; -.
MetOSite; P05231; -.
PhosphoSitePlus; P05231; -.
BioMuta; IL6; -.
DMDM; 124347; -.
MassIVE; P05231; -.
PaxDb; P05231; -.
PeptideAtlas; P05231; -.
PRIDE; P05231; -.
ProteomicsDB; 51828; -.
ABCD; P05231; 186 sequenced antibodies.
Antibodypedia; 12025; 2980 antibodies.
CPTC; P05231; 3 antibodies.
DNASU; 3569; -.
Ensembl; ENST00000258743; ENSP00000258743; ENSG00000136244.
Ensembl; ENST00000404625; ENSP00000385675; ENSG00000136244.
GeneID; 3569; -.
KEGG; hsa:3569; -.
CTD; 3569; -.
DisGeNET; 3569; -.
GeneCards; IL6; -.
HGNC; HGNC:6018; IL6.
HPA; ENSG00000136244; Tissue enhanced (adipose tissue, lymphoid tissue).
MalaCards; IL6; -.
MIM; 147620; gene.
MIM; 148000; phenotype.
MIM; 604302; phenotype.
neXtProt; NX_P05231; -.
OpenTargets; ENSG00000136244; -.
Orphanet; 206; NON RARE IN EUROPE: Crohn disease.
Orphanet; 85414; Systemic-onset juvenile idiopathic arthritis.
PharmGKB; PA198; -.
VEuPathDB; HostDB:ENSG00000136244.11; -.
eggNOG; ENOG502S7Q4; Eukaryota.
GeneTree; ENSGT00390000000878; -.
InParanoid; P05231; -.
OMA; YDKCENS; -.
PhylomeDB; P05231; -.
TreeFam; TF335984; -.
PathwayCommons; P05231; -.
Reactome; R-HSA-1059683; Interleukin-6 signaling.
Reactome; R-HSA-110056; MAPK3 (ERK1) activation.
Reactome; R-HSA-112411; MAPK1 (ERK2) activation.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
Reactome; R-HSA-9662834; CD163 mediating an anti-inflammatory response.
SignaLink; P05231; -.
SIGNOR; P05231; -.
BioGRID-ORCS; 3569; 5 hits in 995 CRISPR screens.
ChiTaRS; IL6; human.
EvolutionaryTrace; P05231; -.
GeneWiki; Interleukin_6; -.
GenomeRNAi; 3569; -.
Pharos; P05231; Tclin.
PRO; PR:P05231; -.
Proteomes; UP000005640; Chromosome 7.
RNAct; P05231; protein.
Bgee; ENSG00000136244; Expressed in left coronary artery and 160 other tissues.
ExpressionAtlas; P05231; baseline and differential.
Genevisible; P05231; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005896; C:interleukin-6 receptor complex; IDA:BHF-UCL.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
GO; GO:0005138; F:interleukin-6 receptor binding; IPI:BHF-UCL.
GO; GO:0006953; P:acute-phase response; TAS:BHF-UCL.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
GO; GO:0098586; P:cellular response to virus; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0050829; P:defense response to Gram-negative bacterium; TAS:BHF-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; TAS:BHF-UCL.
GO; GO:0051607; P:defense response to virus; IDA:BHF-UCL.
GO; GO:0031018; P:endocrine pancreas development; ISS:BHF-UCL.
GO; GO:0002314; P:germinal center B cell differentiation; ISS:UniProtKB.
GO; GO:0070091; P:glucagon secretion; ISS:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB.
GO; GO:0002384; P:hepatic immune response; IDA:BHF-UCL.
GO; GO:0072574; P:hepatocyte proliferation; ISS:UniProtKB.
GO; GO:0006959; P:humoral immune response; IC:BHF-UCL.
GO; GO:0006954; P:inflammatory response; IDA:BHF-UCL.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0097421; P:liver regeneration; ISS:UniProtKB.
GO; GO:0035633; P:maintenance of blood-brain barrier; TAS:ARUK-UCL.
GO; GO:0002548; P:monocyte chemotaxis; IC:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0045779; P:negative regulation of bone resorption; ISS:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
GO; GO:0032682; P:negative regulation of chemokine production; ISS:UniProtKB.
GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IDA:BHF-UCL.
GO; GO:0045599; P:negative regulation of fat cell differentiation; NAS:BHF-UCL.
GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; TAS:Reactome.
GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; ISS:BHF-UCL.
GO; GO:0010888; P:negative regulation of lipid storage; NAS:BHF-UCL.
GO; GO:0050768; P:negative regulation of neurogenesis; TAS:ARUK-UCL.
GO; GO:2000635; P:negative regulation of primary miRNA processing; IGI:ARUK-UCL.
GO; GO:0070050; P:neuron cellular homeostasis; TAS:ARUK-UCL.
GO; GO:0031175; P:neuron projection development; IMP:BHF-UCL.
GO; GO:0001781; P:neutrophil apoptotic process; IDA:UniProtKB.
GO; GO:0002446; P:neutrophil mediated immunity; TAS:BHF-UCL.
GO; GO:0030168; P:platelet activation; TAS:BHF-UCL.
GO; GO:0002675; P:positive regulation of acute inflammatory response; IDA:BHF-UCL.
GO; GO:1902512; P:positive regulation of apoptotic DNA fragmentation; IMP:ARUK-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0050871; P:positive regulation of B cell activation; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IGI:ARUK-UCL.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:ARUK-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:ARUK-UCL.
GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IMP:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:0060252; P:positive regulation of glial cell proliferation; IDA:ARUK-UCL.
GO; GO:0002639; P:positive regulation of immunoglobulin production; IDA:BHF-UCL.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:ARUK-UCL.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:ARUK-UCL.
GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:ARUK-UCL.
GO; GO:0032745; P:positive regulation of interleukin-21 production; ISS:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:ARUK-UCL.
GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IDA:ARUK-UCL.
GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; TAS:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
GO; GO:0150078; P:positive regulation of neuroinflammatory response; TAS:ARUK-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:ARUK-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IDA:ARUK-UCL.
GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:BHF-UCL.
GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; IGI:ARUK-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; ISS:BHF-UCL.
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:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:ARUK-UCL.
GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; TAS:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:ARUK-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0045765; P:regulation of angiogenesis; IC:BHF-UCL.
GO; GO:0061888; P:regulation of astrocyte activation; TAS:ARUK-UCL.
GO; GO:0070092; P:regulation of glucagon secretion; IDA:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; IDA:UniProtKB.
GO; GO:1903978; P:regulation of microglial cell activation; TAS:ARUK-UCL.
GO; GO:0150077; P:regulation of neuroinflammatory response; TAS:ARUK-UCL.
GO; GO:0060260; P:regulation of transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0010574; P:regulation of vascular endothelial growth factor production; IDA:BHF-UCL.
GO; GO:0014823; P:response to activity; ISS:UniProtKB.
GO; GO:0051384; P:response to glucocorticoid; IDA:BHF-UCL.
GO; GO:0032494; P:response to peptidoglycan; NAS:BHF-UCL.
GO; GO:0061470; P:T follicular helper cell differentiation; ISS:UniProtKB.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB.
GO; GO:0010573; P:vascular endothelial growth factor production; IDA:UniProtKB.
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; Glycoprotein; Growth factor; Phosphoprotein;
Reference proteome; Secreted; Signal.
SIGNAL 1..29
/evidence="ECO:0000269|PubMed:1883960,
ECO:0000269|PubMed:2610854, ECO:0000269|PubMed:3279116"
CHAIN 30..212
/note="Interleukin-6"
/id="PRO_0000015582"
MOD_RES 81
/note="Phosphoserine; by FAM20C"
/evidence="ECO:0000269|PubMed:26091039"
CARBOHYD 73
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:1883960"
DISULFID 72..78
/evidence="ECO:0000269|PubMed:2472117"
DISULFID 101..111
/evidence="ECO:0000269|PubMed:2472117"
VARIANT 32
/note="P -> S (in dbSNP:rs2069830)"
/evidence="ECO:0000269|Ref.10"
/id="VAR_013075"
VARIANT 162
/note="D -> E (in dbSNP:rs13306435)"
/id="VAR_029266"
VARIANT 162
/note="D -> V (in dbSNP:rs2069860)"
/evidence="ECO:0000269|Ref.10"
/id="VAR_013076"
MUTAGEN 173
/note="A->V: Almost no loss of activity."
/evidence="ECO:0000269|PubMed:2037043"
MUTAGEN 185
/note="W->R: No loss of activity."
/evidence="ECO:0000269|PubMed:2037043"
MUTAGEN 204
/note="S->P: 87% loss of activity."
/evidence="ECO:0000269|PubMed:2037043"
MUTAGEN 210
/note="R->K,E,Q,T,A,P: Loss of activity."
/evidence="ECO:0000269|PubMed:2037043"
MUTAGEN 212
/note="M->T,N,S,R: Loss of activity."
/evidence="ECO:0000269|PubMed:2037043"
HELIX 49..75
/evidence="ECO:0007829|PDB:1ALU"
STRAND 76..79
/evidence="ECO:0007829|PDB:2IL6"
TURN 81..83
/evidence="ECO:0007829|PDB:4CNI"
HELIX 84..87
/evidence="ECO:0007829|PDB:4CNI"
HELIX 97..99
/evidence="ECO:0007829|PDB:1ALU"
STRAND 102..105
/evidence="ECO:0007829|PDB:4J4L"
HELIX 108..132
/evidence="ECO:0007829|PDB:1ALU"
STRAND 134..136
/evidence="ECO:0007829|PDB:4J4L"
HELIX 137..157
/evidence="ECO:0007829|PDB:1ALU"
STRAND 159..161
/evidence="ECO:0007829|PDB:1ALU"
HELIX 169..180
/evidence="ECO:0007829|PDB:1ALU"
HELIX 184..209
/evidence="ECO:0007829|PDB:1ALU"
SEQUENCE 212 AA; 23718 MW; 1F1ED1FE1B734079 CRC64;
MNSFSTSAFG PVAFSLGLLL VLPAAFPAPV PPGEDSKDVA APHRQPLTSS ERIDKQIRYI
LDGISALRKE TCNKSNMCES SKEALAENNL NLPKMAEKDG CFQSGFNEET CLVKIITGLL
EFEVYLEYLQ NRFESSEEQA RAVQMSTKVL IQFLQKKAKN LDAITTPDPT TNASLLTKLQ
AQNQWLQDMT THLILRSFKE FLQSSLRALR QM


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Pathways :
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1897: Regulation of beta-cell development
WP272: Blood Clotting Cascade
WP1835: Interferon alpha/beta signaling
WP1983: Splicing factor NOVA regulated synpatic proteins
WP2148: Brain derived neurotrophic factor
WP443: Beta Oxidation Meta MAPP
WP809: TGF-beta Receptor Signaling Pathway
WP113: TGF Beta Signaling Pathway
WP1370: TGF Beta Signaling Pathway
WP1225: estrogen signalling
WP2012: miRs in Muscle Cell Differentiation
WP580: Dauer formation
WP1237: Fatty Acid Beta Oxidation

Related Genes :
[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)
[Il6 Il-6] Interleukin-6 (IL-6) (B-cell hybridoma growth factor) (Interleukin HP-1)
[IL4] Interleukin-4 (IL-4) (B-cell stimulatory factor 1) (BSF-1) (Binetrakin) (Lymphocyte stimulatory factor 1) (Pitrakinra)
[Il2 Il-2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL18 IGIF IL1F4] Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[Il18 Igif] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[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 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)
[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)
[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)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF) (Aldesleukin)
[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)
[IFNLR1 IL28RA LICR2] Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL2-PRO) (Papain-like protease) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Non-structural protein 12) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Non-structural protein 13) (nsp13); Proofreading exoribonuclease (ExoN) (EC 3.1.13.-) (Guanine-N7 methyltransferase) (Non-structural protein 14) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (Non-structural protein 15) (nsp15); 2'-O-methyltransferase (EC 2.1.1.-) (Non-structural protein 16) (nsp16)]
[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)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[Il18 Igif] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Tnf Tnfa Tnfsf2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[Ticam1 Trif] TIR domain-containing adapter molecule 1 (TICAM-1) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (TIR domain-containing adapter protein inducing IFN-beta)
[TRAF6 RNF85] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6)
[Il2 Il-2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL1B IL1F2] Interleukin-1 beta (IL-1 beta) (Catabolin)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL2-PRO) (Papain-like protease) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[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)
[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)
[TICAM1 PRVTIRB TRIF] TIR domain-containing adapter molecule 1 (TICAM-1) (Proline-rich, vinculin and TIR domain-containing protein B) (Putative NF-kappa-B-activating protein 502H) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (MyD88-3) (TIR domain-containing adapter protein inducing IFN-beta)

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