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Literature summary for 3.4.24.86 extracted from

  • Lorenzen, I.; Lokau, J.; Düsterhöft, S.; Trad, A.; Garbers, C.; Scheller, J.; Rose-John, S.; Grötzinger, J.
    The membrane-proximal domain of A disintegrin and metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin-6 receptor and interleukin-1 receptor II (2012), FEBS Lett., 586, 1093-1100.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Mus musculus Q9Z0F8
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
interleukin (IL)-1R-II + H2O exclusively the extracellular domains of ADAM17 are needed for interaction with substrate, whereas the transmembrane- and cytoplasmic-region are dispensable for this process. In the extracellular part solely the membrane-proximal domain of ADAM17 is mandatory for recognition Mus musculus ?
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interleukin (IL)-6R + H2O exclusively the extracellular domains of ADAM17 are needed for interaction with substrate, whereas the transmembrane- and cytoplasmic-region are dispensable for this process. In the extracellular part solely the membrane-proximal domain of ADAM17 is mandatory for recognition Mus musculus ?
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proTGF-alpha + H2O the membrane-proximal domain in the extracellular part of ADAM17 is mandatory for recognition of the type-I transmembrane proteins, but not for the interaction with the type-II transmembrane molecule TNF-alpha Mus musculus soluble TGF-alpha
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