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. 2019 Oct 15;9:14822. doi: 10.1038/s41598-019-51428-x

Table 2.

The 10 most abundant, validated human glycosylation sites and their relative abundances in the enriched HeLa cell lysate.

Glycoprotein Peptide backbone Glycosylation site Relative abundance High-mannose % Hybrid % Complex % Degree of sialylation % Degree of fucosylation %
TFR1_HUMAN QNNGAFN * ETLFR 727 8.9 100.0 0.0 0.0
CBPM_HUMAN NFPDAFEYNN * VSR 164 8.5 92.1 0.0 7.9 0.0 100.0
LAMP1_HUMAN GHTLTLN * FTR 103 7.6 69.6 9.6 20.7 53.8 77.8
FOLR1_HUMAN NAccSTN * TSQEAHK 69 4.3 0.0 4.6 95.4 59.3 100.0
DAF_HUMAN GSQWSDIEEFcN * R 95 4.0 0.0 0.0 100.0 91.7 8.4
LAMP1_HUMAN LLNINPN * K 261 4.0 23.6 35.2 41.2 3.5 84.0
PLOD1_HUMAN YIHQN * YTK 538 3.9 42.6 57.4 0.0 0.0 0.0
FOLR1_HUMAN GWN * WTSGFNK 161 3.7 0.0 0.0 100.0 50.0 72.8
LAMP2_HUMAN VQPFN * VTQGK 356 3.2 81.0 8.6 10,4 0.0 0.0
NICA_HUMAN IYIPLN * K 45 2.5 13.3 52.0 34.7 44.5 100.0
Distribution among all validated human glycoforms 64.9 5.1 30.0 46.8 68.7

Glycosylation site is the position of the glycosylated asparagine in the glycoprotein’s amino acid sequence. Sum of the abundance of all glycoforms corresponding to the given site and the percentage of different N-glycan structure types are also given, together with the degree of sialylation (ratio of sialic acid and galactose residues) and degree of fucosylation (ratio of fucosylated glycoforms compared to the sum of complex and hybrid glycoforms).