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Synonyms: B-cell stimulatory factor 2 | CTL differentiation factor | hybridoma growth factor | interferon β2 | interleukin-6
Compound class:
Endogenous peptide in human, mouse or rat
Comment: IL-6 is an interleukin that acts as both a pro-inflammatory cytokine and an anti-inflammatory myokine. It is the originating member of a family of related cytokines that include IL-11, oncostatin M (OSM), leukemia inhibitory factor (LIF), ciliary neurotrophic factor (CNTF), cardiotrophin-1 (CT-1), cardiotrophin-like cytokine factor 1/B-cell stimulating factor 3 (NNT-1), neuropoietin (NPN), IL-27, and IL-31 [14]. IL-6 is produced by T and B cells, macrophages, dendritic cells, and non-immune cells such as fibroblasts, endothelial cells, glial cells, keratinocytes, and placental syncytio- and extravillous trophoblasts.
The receptors for these cytokines (except IL-31) share a common signal transducing subunit gp130 (IL6ST). IL-6 is a critical regulator of the immune system and has been widely implicated in autoimmune disease, infection responses and in the regulation of metabolic, regenerative, and neural processes.
Species: Human
Ligand Activity Visualisation ChartsThese are box plot that provide a unique visualisation, summarising all the activity data for a ligand taken from ChEMBL and GtoPdb across multiple targets and species. Click on a plot to see the median, interquartile range, low and high data points. A value of zero indicates that no data are available. A separate chart is created for each target, and where possible the algorithm tries to merge ChEMBL and GtoPdb targets by matching them on name and UniProt accession, for each available species. However, please note that inconsistency in naming of targets may lead to data for the same target being reported across multiple charts. ✖ |
Peptide Sequence  |
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VPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEE TCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDM TTHLILRSFKEFLQSSLRALRQM |
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| Selected 3D Structures | ||
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| Post-translational Modification | |
| N-linked glycosylation of asparagine residue at position 44; disulphide bond formation between cysteine residues at positions 43 and 49, and 72 and 82 | |
