ABCC8 p.Gly1400Asp
| Predicted by SNAP2: | A: D (71%), C: D (75%), D: D (85%), E: D (75%), F: D (85%), H: D (85%), I: D (85%), K: D (91%), L: D (85%), M: D (80%), N: D (80%), P: D (91%), Q: D (75%), R: D (91%), S: D (71%), T: D (71%), V: D (80%), W: D (91%), Y: D (85%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, H: D, I: D, K: D, L: D, M: D, N: D, P: D, Q: D, R: D, S: D, T: D, V: D, W: D, Y: D, |
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[hide] The structure and function of the ATP-sensitive K+... J Mol Endocrinol. 1999 Apr;22(2):113-23. Miki T, Nagashima K, Seino S
The structure and function of the ATP-sensitive K+ channel in insulin-secreting pancreatic beta-cells.
J Mol Endocrinol. 1999 Apr;22(2):113-23., [PMID:10194514]
Abstract [show]
ATP-sensitive K+ channels (KATP channels) play important roles in many cellular functions by coupling cell metabolism to electrical activity. The KATP channels in pancreatic beta-cells are thought to be critical in the regulation of glucose-induced and sulfonylurea-induced insulin secretion. Until recently, however, the molecular structure of the KATP channel was not known. Cloning members of the novel inwardly rectifying K+ channel subfamily Kir6.0 (Kir6.1 and Kir6.2) and the sulfonylurea receptors (SUR1 and SUR2) has clarified the molecular structure of KATP channels. The pancreatic beta-cell KATP channel comprises two subunits: a Kir6.2 subunit and an SUR1 subunit. Molecular biological and molecular genetic studies have provided insights into the physiological and pathophysiological roles of the pancreatic beta-cell KATP channel in insulin secretion.
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No. Sentence Comment
128 This results in the substitution of glycine with aspartic acid at codon 1400 followed by the additional 23 extraneous amino acids.
X
ABCC8 p.Gly1400Asp 10194514:128:36
status: NEW