| Objective To analyze the structure and function of human dentin matrix protein 1 (DMP1), in order to provide reference for further study on the mechanism of DMP1. Methods The physicochemical properties, subcellular structural localization, transmembrane region and signal peptide, secondary structure, tertiary structure, potential phosphorylation and glycosylation sites, protein interaction networks, the potential transcricption factor binding sites in the 5’ UTR, and the evolutionary conservation of the DMP1 protein were analyzed using bioinformatics methods. Results Human DMP1 is an acidic hydrophilic protein. The signal peptide cleavage site is between 16 and 17 amino acid residues, and there is no transmembrane region. The main secondary structural element is random coil. There are 123 phosphorylation sites,118 O-glycosylation site and 8 N-glycosylation sites. DMP1 has structural features that facilitate protein-protein interactions, and there are multiple transcription factor possible binding sites in the 5’ UTR. Meanwhile, it is expressed in all tissues of human body, and it has the localization characteristics of subcellular structures. Conclusion The loose structure, extensive expression, abundant modification sites, and many transcription factor binding sites suggest that DMP1 has more complex biological functions. |