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 T256E 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 T256E in KAT1_ARATH

Point mutation:	T256E
Domain:	Loop 5-6
General numbering (KChannelDB):	-
Protein:	KAT1_ARATH (KAT1,At5g46240,MPL12.)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 256 in KAT1_ARATH
Other point mutations / same protein	List of mutations in KAT1_ARATH
Family alignments	AKT-like Inward rectifiers 6TMs Plant potassium channels
Other point mutations / same position	Position 258 in AKT-like Inward rectifiers 6TMs family Position 258 in Plant potassium channels family
Reference:	Sodium blocking induced by a point mutation at the C-terminal end of the pore helix of the KAT1 channel. Uozumi N, Yamada K, Goshima S, Ona T, Oiki S J Membr Biol 2001 Jun 1;181(3):163-70.	Medline
Other point mutations / same article	List
Text source	abstract
Validation status	True positive

Relevant sentences:

T256E

However , the activity of both mutant channels was significantly depressed by Na+ with apparent dissociation constants of 6.7 mm and 11.3 mm for T256Q and T256E , respectively
On the other hand , the blocking for the T256E mutant was voltage-independent at low Na+ concentrations and became voltage-dependent at higher concentrations

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