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Human COG defects lead to severe multisystemic diseases known as COG\u2010congenital disorders of glycosylation (COG\u2010CDG).<\/jats:p><jats:p>To gain better understanding of COG\u2010CDGs, we compared COG knockout cells with cells deficient to 2 key enzymes, Alpha\u20101,3\u2010mannosyl\u2010glycoprotein 2\u2010beta\u2010<jats:italic>N<\/jats:italic>\u2010acetylglucosaminyltransferase and uridine diphosphate\u2010glucose 4\u2010epimerase (GALE), which contribute to proper N\u2010 and O\u2010glycosylation. While all knockout cells share similar defects in glycosylation, these defects only account for a small fraction of observed COG knockout phenotypes. Glycosylation deficiencies were not associated with the fragmented Golgi, abnormal endolysosomes, defective sorting and secretion or delayed retrograde trafficking, indicating that these phenotypes are probably not due to hypoglycosylation, but to other specific interactions or roles of the COG complex.<\/jats:p><jats:p>Importantly, these COG deficiency specific phenotypes were also apparent in COG7\u2010CDG patient fibroblasts, proving the human disease relevance of our CRISPR knockout findings. 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