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 R312K 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 R312K in IRK2_HUMAN

Point mutation:	R312K
Domain:	C-term
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 312 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 294 in Inward rectifiers (Kir) family Position 294 in Potassium channels 2 TMs family
Reference:	Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies. Lopes CM, Zhang H, Rohacs T, Jin T, Yang J, Logothetis DE Neuron 2002 Jun 13;34(6):933-44.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

R312K

In order to assess whether this was due to either the inaccessibility of these residues to MTSEA or to the requirement of a particular residue at that position , we mutated these sites to other positive charged residues (R67K , R312K , H271K , H271R)
In the cases of R67K and R312K , the alternative positively charged residues increased PIP2-channel interaction , but the interaction was weaker than for the wild-type channel
T50 for poly-Lys inhibition was 25 ą 5 s (R67K , n = 4) and 53 ą 11 s (R312K , n = 5) when compared to 4.7 ą 0.9 s (R67C , n = 4) and 20 ą 3 s (R312C , n = 11) for neutral amino acids mutations and 209 ą 49 s for wild-type channels
Yet , all mutations that destroy the phosphorylation motif (R217 / R218K / Q and R311 / R312K / Q) weakened chanel-PIP2 interactions , suggesting complex interactions at these sites

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