Figure 3From: Proteomic database mining opens up avenues utilizing extracellular protein phosphorylation for novel therapeutic applicationsMultiple sequence alignment of the trimerization domain. A.: Top view of C-propeptide domain of procollagen α1(III) [74]. The discontinuous chain recognition sequence (CRS) is highlighted in orange and green and the experimentally verified phosphorylated sites in red. B.: Multiple sequence alignment of the C-propeptide domain of procollagen I-III. The chain recognition sequence is highlighted in an orange and green box and the experimentally verified phosphorylated sites are shown in red. The boxed residue corresponds to a known mutation leading to Osteogenesis Imperfecta [72]. Motifs recognized by FAM20C are highlighted in bold black.Back to article page