PMID: 11226831

 

    Legend: Gene, Sites

Title : Glycosylation of the murine estrogen receptor-alpha

Abstract :

1. O-linked N-acetylglucosamine (O-GlcNAc) is a highly dynamic and abundant modification found on nuclear and cytoplasmic proteins of nearly all eukaryotes
2. O-GlcNAc addition is required for life at the single cell level and is analogous to protein phosphorylation in most respects
3. In a previous study (M.S. Jiang, G.W. Hart , A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine
4. J. Biol
5. Chem
6. 270 (1997) 2421-2428), we demonstrated that a subpopulation of the murine estrogen receptor-alpha ( mER-alpha) is modified by O-GlcNAc at Thr(575)
7. Here we mutated mER-alpha to convert Thr(575) and Ser(576) to Val and Ala , respectively
8. Surprisingly, this glycosylation-site mutant is still extensively modified by O-GlcNAc
9. Analyses of glycopeptides identified two additional sites of modification on mER-alpha, at Ser(10) and Thr(50) near the N-terminus
10. The major glycosylation sites are within or near PEST regions , suggesting that O-GlcNAc may regulate mER-alpha turnover

Output (sent_index, trigger, protein, sugar, site):

• 0. Glycosylation, , estrogen receptor, -, -
• 1. found, , proteins, O-linked N-acetylglucosamine, -
• 10. glycosylation, , -, -, sites
• 9. glycopeptides, , -, -, glycopeptides

Output(Part-Of) (sent_index, protein, site):

• 9. mER, sites

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX