FIGURE 2:

The yeast secretome does not contain cysteine-rich glycoproteins. (A) Yeast glycosylation sites were identified in the following mass spectrometry studies: data set 1, Class 1 sites, Supplemental Table S2 from Zielinska et al. (2012); data set 2, Supplemental Table S1 from Chen et al. (2014b); data set 3, Supplemental Table S2 from Chen et al. (2014b); data set 4, Supplemental Table S3 from Chen et al. (2014a). Data sets were trimmed by excluding sites that did not match a consensus glycosylation site (NXT/S/C) or were derived from nonsecretome proteins. The data sets were merged to obtain 830 glycosylation sites that were present in one to four of the initial data sets, as indicated in the overlap column. The 830 glycosylation sites were derived from 251 yeast secretome proteins. (B) The distribution of cysteine content in 251 yeast glycoproteins. The cysteine content of several glycoproteins is indicated by labeled arrows. (C) The distribution of cysteine content in a collection of 892 human glycoproteins (Cherepanova et al., 2019). The cysteine content of an STT3B-dependent (SHBG) and two STT3A-dependent (SAP and GRAN) substrates is indicated by labeled arrows.