In this study, we demonstrated the presence and the activity of the P2Y14 receptor in glioma C6 cells. We found that P2Y14 could exist in two forms, highly predominating glycosylated and non-glycosylated. Binding of UDP-glucose evoked two responses: calcium signal and adenylate cyclase inhibition, both pertussis toxin-sensitive. Separate glycosylation pattern and functional profile of these two receptor forms were observed in non-starved and serum-starved cells. During long-term serum deprivation (96 h), the level of glycosylated form strongly decreased, while non-glycosylated increased, what was correlated with the decrease of calcium signaling activity and stronger adenylate cyclase inhibition, suggesting that receptor N-glycosylation may modulate its functional activity.