This protein belongs to a subfamily of tyrosine kinase receptors with a homology region to the Dictyostelium discoideum protein discoidin I in their extracellular domain. Its autophosphorylation is achieved by all collagens so far tested (type I to type VI).

2024年12月24日 · DDR1 (Discoidin Domain Receptor Tyrosine Kinase 1) is a Protein Coding gene. Diseases associated with DDR1 include Adenocarcinoma and Melanoma. Among its related pathways are GPCR Pathway and ERK Signaling.

2023年10月13日 · Here, we demonstrate that the discoidin domain receptor 1 (DDR1) tyrosine kinase is a direct mechanosensor and is essential for connecting the force imposed by shear to the endothelial responses....

2025年2月8日 · Discoidin domain receptor 1 (DDR1) promote intestinal barrier disruption in Ulcerative Colitis through tight junction proteins degradation and epithelium apoptosis. Discoidin domain receptor 1 is a potential target correlated with …

The tyrosine kinase family receptor of discoidin domain receptors (DDR1 and DDR2) is known to be activated by extracellular matrix collagen catalytic binding protein receptors. They play a remarkable role in cell proliferation, differentiation, ...

For instance, the T cell receptor can induce DDR1 expression in human T cells through Ras/Raf/ERK and protein kinase C-dependent pathways (Chetoui et al., 2011). Moreover, in primary lung fibroblasts, DDR1 expression can be induced by collagen I, through DDR2 activation, in an ERK1/2-dependent manner ( Ruiz and Jarai, 2011 ).

Know comprehensive DDR1 protein information including protein sequence, molecular weight, theoretical pI, structure, function and protein interaction.

Expression of this protein is restricted to epithelial cells, particularly in the kidney, lung, gastrointestinal tract, and brain. In addition, it has been shown to be significantly overexpressed in several human tumors.

2013年10月18日 · DDR1-IN-1 binds to DDR1 in the 'DFG-out' conformation and inhibits DDR1 autophosphorylation in cells at submicromolar concentrations with good selectivity as assessed against a panel of 451 kinases measured using the KinomeScan technology.

The protein structure of DDR1 contains 914 amino acids with a molecular mass of 105 k D as predicted through cDNA [58]. There is a profound proline/glycine rich region is present near the N-terminus of DDR1. Another proline-glycine rich region is found amidst the transmembrane and C-terminal tyrosine kinase domain.