Discoidin domain receptor 2 (DDR2), a collagen receptor tyrosine kinase, initiates signal transduction upon collagen binding, but little is known as to how DDR2 signaling is negatively regulated. Herein we demonstrate that Cbl family member Cbl‐b predominantly promotes the ubiquitination of DDR2 upon collagen II stimulation. Cbl‐b‐mediated ubiquitination accelerates the degradation of activated DDR2. Finally, the production of MMP‐13, a downstream target of DDR2, is enhanced in Cbl‐b‐knocked down MC3T3‐E1 cells and Cbl‐b‐deficient mouse primary synovial fibroblasts. Thus, Cbl‐b, by promoting the ubiquitination and degradation of DDR2, functions as a negative regulator in the DDR2 signaling pathway.