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Int. J. Mol. Sci. 2014, 15(3), 4903-4914; doi:10.3390/ijms15034903

Phosphosite Mapping of HIP-55 Protein in Mammalian Cells

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 and 1,*
Received: 19 January 2014 / Revised: 20 February 2014 / Accepted: 7 March 2014 / Published: 19 March 2014
(This article belongs to the Special Issue Mass Spectrometry Application in Biology)
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Abstract: In 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.
Keywords: mass spectrometry; HIP-55; phosphorylation mass spectrometry; HIP-55; phosphorylation
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

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.

AMA Style

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.

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