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 S103E 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 S103E in IRK11_HUMAN

Point mutation:	S103E
Domain:	Loop 1-2
General numbering (KChannelDB):	-
Protein:	IRK11_HUMAN (KCNJ1)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein	List of mutations in IRK11_HUMAN
Family alignments	Inward rectifiers (Kir) Potassium channels 2 TMs
Other point mutations / same position	Position 97 in Inward rectifiers (Kir) family
Reference:	Interaction between the RGS domain of RGS4 with G protein alpha subunits mediates the voltage-dependent relaxation of the G protein-gated potassium channel. Inanobe A, Fujita S, Makino Y, Matsushita K, Ishii M, Chachin M, Kurachi Y J Physiol 2001 Aug 15;535(Pt 1):133-43.	Medline
Other point mutations / same article	List
Text source	PDF full text
Validation status	Not yet checked

Relevant sentences:

S103E

Otherwise the results obtained with mutations of RGS4 were divided into two groups , those with wild-type characteristics , E87A , N88A , S103E and P144A , and those where the effects of RGS4 on the off-rate and the relaxation of ACh currents were abolished , N128A , N128H , L159F , R167A and F168A
Of the former group the effects of S103E and P144A were perhaps not surprising since these locations are not thought to be involved in the interaction between A

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