Transferase(Phosphotransferase); domain 1
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
insulin receptor protein-tyrosine kinase
The trk proto-oncogene encodes a receptor for nerve growth factor.
High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor.
A Trk nerve growth factor (NGF) receptor point mutation affecting interaction with phospholipase C-gamma 1 abolishes NGF-promoted peripherin induction but not neurite outgrowth.
Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses.
Structure and ligand recognition of the phosphotyrosine binding domain of Shc.
Trk receptors function as rapid retrograde signal carriers in the adult nervous system.
Cleavage of the TrkA neurotrophin receptor by multiple metalloproteases generates signalling-competent truncated forms.
The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation.
A novel point mutation affecting the tyrosine kinase domain of the TRKA gene in a family with congenital insensitivity to pain with anhidrosis.
Activity-dependent interaction of the intracellular domain of rat trkA with intermediate filament proteins, the beta-6 proteasomal subunit, Ras-GRF1, and the p162 subunit of eIF3.
Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor.
Direct binding of the signaling adapter protein Grb2 to the activation loop tyrosines on the nerve growth factor receptor tyrosine kinase, TrkA.
Identification of novel trkA variants with deletions in leucine-rich motifs of the extracellular domain.
Identification and structure of the nerve growth factor binding site on TrkA.
Congenital insensitivity to pain with anhidrosis (CIPA): effect of TRKA (NTRK1) missense mutations on autophosphorylation of the receptor tyrosine kinase for nerve growth factor.
IRS-1 and IRS-2 are recruited by TrkA receptor and oncogenic TRK-T1.
SH2-B and APS are multimeric adapters that augment TrkA signaling.
A novel mutation within the extracellular domain of TrkA causes constitutive receptor activation.
Grit, a GTPase-activating protein for the Rho family, regulates neurite extension through association with the TrkA receptor and N-Shc and CrkL/Crk adapter molecules.
The E.C. was transferred from 2.7.1.112 to 2.7.10.1. This receptor enzyme has N-terminal extracellular region, transmembrane region, and C-terminal cytoplasmic region. The extracellular region is composed of two Ig-like C2-type domains, whilst the cytoplasmic region contains protein kinase domain, which is homologous to other tyrosine protein kinase domains (M00129 in EzCatDB). The structure of the catalytic domain has not been obtained, though. This receptor belongs to the Insulin receptor superfamily. The PDB structures correspond to the second Ig-like C2-type domain.