Title : Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.

Pub. Date : 2002 Jul

PMID : 12065289






5 Functional Relationships(s)
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1 We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314). e138 solute carrier family 19 member 2 Homo sapiens
2 Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake. Thiamine solute carrier family 19 member 2 Homo sapiens
3 Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein. Nitrogen solute carrier family 19 member 2 Homo sapiens
4 Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein. n63q solute carrier family 19 member 2 Homo sapiens
5 Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein. n314q solute carrier family 19 member 2 Homo sapiens