Phosphosite Mapping of HIP-55 Protein in Mammalian Cells
AbstractIn the present study, hematopoietic progenitor kinase 1 (HPK1)-interacting protein of 55 kDa (HIP-55) protein was over-expressed in HEK293 cells, which was genetically attached with 6x His tag. The protein was purified by nickel-charged resin and was then subjected to tryptic digestion. The phosphorylated peptides within the HIP-55 protein were enriched by TiO2 affinity chromatography, followed by mass spectrometry analysis. Fourteen phosphorylation sites along the primary structure of HIP-55 protein were identified, most of which had not been previously reported. Our results indicate that bio-mass spectrometry coupled with manual interpretation can be used to successfully identify the phosphorylation modification in HIP-55 protein in HEK293 cells.
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Liu, N.; Sun, N.; Gao, X.; Li, Z. Phosphosite Mapping of HIP-55 Protein in Mammalian Cells. Int. J. Mol. Sci. 2014, 15, 4903-4914.
Liu N, Sun N, Gao X, Li Z. Phosphosite Mapping of HIP-55 Protein in Mammalian Cells. International Journal of Molecular Sciences. 2014; 15(3):4903-4914.Chicago/Turabian Style
Liu, Ning; Sun, Ningning; Gao, Xiang; Li, Zijian. 2014. "Phosphosite Mapping of HIP-55 Protein in Mammalian Cells." Int. J. Mol. Sci. 15, no. 3: 4903-4914.