16474139	5	45	gly	glycosylation	937:949	arg1	the coronavirus M proteins	the coronavirus M proteins				Fterm		proteins			The conserved glycosylation of the coronavirus M proteins and the resemblance of the 3a protein to them led us to investigate the glycosylation of these two SARS-CoV membrane proteins.
16474139	5	90	gly	glycosylation	1053:1065	arg1	these two SARS-CoV membrane proteins	these two SARS-CoV membrane proteins				Fterm		proteins			The conserved glycosylation of the coronavirus M proteins and the resemblance of the 3a protein to them led us to investigate the glycosylation of these two SARS-CoV membrane proteins.
16474139	11	54	part_of	protein	1894:1900	arg1	the ectodomain	protein		the ectodomain		Fterm	Site	protein		ectodomain	In addition, we showed that substitution of serine and threonine residues in the ectodomain of the 3a protein abolished the addition of the O-linked sugars.
16474139	9	43	gly	contain	1588:1594	arg1	The SARS-CoV 3a protein AND sialic acids	The SARS-CoV 3a protein			sialic acids	Fterm		protein			The SARS-CoV 3a protein, however, was demonstrated to contain sialic acids, indicating the presence of oligosaccharides.
16474139	12	31	gly	glycosylated	2100:2111	arg1	the SARS-CoV M protein	the SARS-CoV M protein				OGER		M protein	P54296		Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
16474139	12	78	gly	O-glycosylated	1985:1998	arg1	the SARS-CoV 3a protein	the SARS-CoV 3a protein				Fterm		protein			Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
16474139	12	78	gly	O-glycosylated	1985:1998	arg1	an O-glycosylated glycoprotein	an O-glycosylated glycoprotein				Fterm		glycoprotein			Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
16474139	12	83	gly	glycoprotein	2000:2011	arg1	the SARS-CoV 3a protein	the SARS-CoV 3a protein				Fterm		protein			Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
16474139	12	83	gly	glycoprotein	2000:2011	arg1	an O-glycosylated glycoprotein	an O-glycosylated glycoprotein				Fterm		glycoprotein			Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
19202066	3	38	gly	modified	530:537	arg3	IKKbeta AND O-linked beta-N-acetyl glucosamine	IKKbeta			O-linked beta-N-acetyl glucosamine	PUBTATOR		IKKbeta	12675		Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	38	gly	modified	530:537	arg3	IKKbeta AND O-GlcNAc	IKKbeta			O-GlcNAc	PUBTATOR		IKKbeta	12675		Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
16474139	4	87	gly	glycosylated	836:847	arg1	The M protein	The M protein				OGER		M protein	P54296		The M protein plays a crucial role in coronavirus assembly and is glycosylated in all coronaviruses, either by N-linked or by O-linked oligosaccharides.
21389326	4	50	part_of	Flt3	915:918	arg1	extracellular domain 3	Flt3		extracellular domain 3		PUBTATOR	Site	Flt3	2322	domain	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
16474139	10	96	gly	O-glycosylation	1655:1669	arg1	the 3a protein	the 3a protein				Fterm		protein			O-glycosylation of the 3a protein was indeed confirmed using an in situ O-glycosylation assay of endoplasmic reticulum-retained mutants.