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 T469S 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 T469S in KCNH2_HUMAN

Point mutation:	T469S
Domain:	TRANSMEM II
General numbering (KChannelDB):	244
Protein:	KCNH2_HUMAN (KCNH2,ERG, ERG1, HERG, HERG)	Swiss-Prot Cross-reference table Family page
Protein isoforms	4
Other point mutations / same protein / same position	Point mutations at position 469 in KCNH2_HUMAN
Other point mutations / same protein	List of mutations in KCNH2_HUMAN
Family alignments	eag related KCNH (Kv10-12) K+ voltage-gated channels (Kv1-12,Kca2-5) Potassium channels 6 TMs
Other point mutations / same position	Position 469 in eag related KCNH (Kv10-12) family Position 453 in K+ voltage-gated channels (Kv1-12,Kca2-5) family Position 239 in Potassium channels 6 TMs family
Reference:	Molecular determinant of high-affinity dofetilide binding to HERG1 expressed in Xenopus oocytes: involvement of S6 sites. Lees-Miller JP, Duan Y, Teng GQ, Duff HJ Mol Pharmacol 2000 Feb;57(2):367-74.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

T469S

In Shaker , the T469S mutation reduced the affinity for internal TEA by ~2-fold but substitution with a hydrophobic residue , T469V , produced little effect (Choi et al. , 1993(image) )

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