EC 2.7.1.112

1. [Kinases that phosphorylate protein tyrosine residues. These kinases play major roles in mitogenic signalling, and can be divided into two subfamilies: receptor tyrosine kinases, that have an extracellular ligand-binding domain, a single transmembrane domain, and an intracellular tyrosine kinase domain; and nonreceptor tyrosine kinases, which are soluble, cytoplasmic kinases. (Dictionary of Cell and Molecular Biology Online) ( NCI )]
   UMLS (NCI) C0033681
    

   Amino Acid, Peptide, or Protein

   Enzyme
   

   Relation/PAR: EC 2.7.1.37
   
   Relation/CHD: JAK kinase
2. [LCK is a lymphoid-specific SRC family tyrosine kinase critical for T-cell development and activation. LCK is quickly activated after mIg cross-linking on B-cells or after TCR cross-linking on T-cells and is associated with the cytoplasmic domains of CD4, CD8, and the IL-2R beta chain. LCK may be involved in the earliest steps of TCR-mediated T-cell activation. After antigen binding to the TCR, in concert with co-receptors (CD4, MHC II, CD28, B7, CD8, and MHC I) activation of at least three protein-tyrosine kinases occur, including p59(FYN), p56(LCK), and ZAP70. The pre-TCR co-localizes with LCK into glycolipid rafts, resulting in the phosphorylation of CD3-epsilon and ZAP70. STAT5 is phosphorylated upon TCR stimulation. LCK activates the DNA binding of STAT5A and STAT5B to STAT-inducible elements, which regulate gene transcription and T-cell proliferation during immunologic responses. (from OMIM 153390 and NCI) ( NCI )]
   UMLS (NCI) C0065344
    

   Amino Acid, Peptide, or Protein

   Enzyme