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 G102A 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 G102A in KCNK5_HUMAN

Point mutation:	G102A
Domain:	Loop 1-2
General numbering (KChannelDB):	-
Protein:	KCNK5_HUMAN (KCNK5,TASK)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein	List of mutations in KCNK5_HUMAN
Family alignments	Two-pore channels (K2p) Potassium channels 4 TMs 2P
Other point mutations / same position
Reference:	Na(+)-induced inward rectification in the two-pore domain K(+) channel, TASK-2. Morton MJ, Chipperfield S, Abohamed A, Sivaprasadarao A, Hunter M Am J Physiol Renal Physiol 2005 Jan;288(1):F162-9. Epub 2004 Aug 24.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

G102A

A G102A / G207A double mutant of mouse TASK-2 was generated in two steps by the QuikChange site-directed mutagenesis technique (Stratagene) and confirmed by automated fluorescence DNA sequencing (Lark)
We have introduced mutations of the second glycine in both pore regions of TASK-2 (the double mutant G102A / G207A)
Mutant G102A / G207A shows no rectification
I-V plots are shown from cells transfected with the G102A / G207A double mutant with 50 mM Na + in the pipette in the presence of Na + , NMDG , or K + Ringer solution (n = 4 in each case)
We mutated the second (outermost) glycine residue of both TASK-2 pore domains (G102A / G207A double mutant)

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