doc_id	sent_index	relation_id	relation	trigger	trigger_offset	arg_num	arg_base_np	arg_protein	arg_domain	arg_site	arg_sugar	PSource	SiteSource	NProtein	NID	SiteName	sent_text
31958346	11	42	part_of	GluA1	1782:1786	arg1	the N401-glycosite	GluA1		the N401-glycosite		PUBTATOR	SpecificSite	GluA1	2890	N401	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	2	38	gly	N-glycosylation	381:395	arg1	the major subunits	the major subunits				OGER		subunits	14799		In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	38	gly	N-glycosylation	381:395	arg1	mouse GluA1	mouse GluA1				PUBTATOR		GluA1	14799		In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	11	71	gly	N401-glycosite	1764:1777	arg1	GluA1	GluA1				PUBTATOR		GluA1	2890		Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.