DDR2 Recombinant Protein

Receptor tyrosine kinases (RTKs) play a key role in the communication of cells with their microenvironment. These molecules are involved in the regulation of cell growth, differentiation, and metabolism. In several cases the biochemical mechanism by which RTKs transduce signals across the membrane has been shown to be ligand induced receptor oligomerization and subsequent intracellular phosphorylation. This autophosphorylation leads to phosphorylation of cytosolic targets as well as association with other molecules, which are involved in pleiotropic effects of signal transduction. RTKs have a tripartite structure with extracellular, transmembrane, and cytoplasmic regions. This gene encodes a member of a novel subclass of RTKs and contains a distinct extracellular region encompassing a factor VIII-like domain. Alternative splicing in the 5' UTR results in multiple transcript variants encoding the same protein. [provided by RefSeq, Jul 2008]

DDR2: This tyrosine kinase receptor for fibrillar collagen mediates fibroblast migration and proliferation. Contributes to cutaneous wound healing. Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.

Protein type: Protein kinase, TK; EC 2.7.10.1; Kinase, protein; Protein kinase, tyrosine (receptor); Membrane protein, integral; TK group; DDR family

Chromosomal Location of Human Ortholog: 1q23.3

Cellular Component: focal adhesion; integral to plasma membrane; apical plasma membrane; plasma membrane

Molecular Function: collagen binding; protein binding; transmembrane receptor protein tyrosine kinase activity; ATP binding

Biological Process: positive regulation of osteoblast differentiation; extracellular matrix organization and biogenesis; positive regulation of fibroblast proliferation; ossification; peptidyl-tyrosine phosphorylation; collagen fibril organization; biomineral formation; protein amino acid autophosphorylation; positive regulation of protein kinase activity; positive regulation of transcription factor activity; signal transduction; cell adhesion; regulation of bone mineralization

Disease: Spondylometaepiphyseal Dysplasia, Short Limb-hand Type