KChannelDB: Extraction of mutation data from the literature

2005, KChannelDB.

This data was extracted from Medline abstracts and full texts (when available) in an automated manner.

The table below describes the selected point mutation and provides links to other documents. The sentence(s) where the point mutation G144S was found are listed after the table.

The mutated residues are also indicated in the family sequence alignments and hyperlinked to the corresponding mutation pages.

Point mutation G144S in IRK2_HUMAN

Point mutation:	G144S
Domain:	Loop 1-2
General numbering (KChannelDB):	-
Protein:	IRK2_HUMAN (KCNJ2,HIRK)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 144 in IRK2_HUMAN
Other point mutations / same protein	List of mutations in IRK2_HUMAN
Family alignments	Inward rectifiers (Kir) Potassium channels 2 TMs
Other point mutations / same position	Position 126 in Inward rectifiers (Kir) family Position 126 in Potassium channels 2 TMs family
Reference:	PIP2 binding residues of Kir2.1 are common targets of mutations causing Andersen syndrome. Donaldson MR, Jensen JL, Tristani-Firouzi M, Tawil R, Bendahhou S, Suarez WA, Cobo AM, Poza JJ, Behr E, Wagstaff J, Szepetowski P, Pereira S, Mozaffar T, Escolar DM, Fu YH, Ptacek LJ Neurology 2003 Jun 10;60(11):1811-6.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

G144S

This GYG (amino acids 144 to 146) sequence is vital for potassium selectivity in inward-rectifying and other potassium channels.18 A mutation changing the first glycine of this motif (G144S) in another kindred was shown to have a severe dominant negative effect on Kir2.1 current.6 T75R and D71N change residues in the N terminus with unknown contributions to channel function

F.Horn (kchanneldbcmbi.ru.nl), 17-Aug-2005