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Literature summary for 2.7.10.2 extracted from

  • Shenoy-Scaria, A.M.; Gauen, L.K.; Kwong, J.; Shaw, A.S.; Lublin, D.M.
    Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins (1993), Mol. Cell. Biol., 13, 6385-6392.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus enzyme is involved in pathway for signaling through glycosyl-phosphatidylinositol (GPI)-anchored membrane proteins ?
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?

Organism

Organism UniProt Comment Textmining
Mus musculus P06240
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification palmitoylation of an amino-terminal cysteine motif of protein tyrosine kinase mediates interaction with glycosyl-phosphatidylinositol-anchored proteins Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme is involved in pathway for signaling through glycosyl-phosphatidylinositol (GPI)-anchored membrane proteins Mus musculus ?
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?

Synonyms

Synonyms Comment Organism
proto-oncogene tyrosine-protein kinase LCK
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Mus musculus