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 F137S 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 F137S in IRK3_RAT

Point mutation:	F137S
Cited point mutation:	Phe137Ser,Phe-137
Domain:	Loop 1-2
General numbering (KChannelDB):	-
Protein:	IRK3_RAT (Kcnj3,Girk1, Kg)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 137 in IRK3_RAT
Other point mutations / same protein	List of mutations in IRK3_RAT
Family alignments	Inward rectifiers (Kir) Potassium channels 2 TMs
Other point mutations / same position	Position 118 in Inward rectifiers (Kir) family Position 118 in Potassium channels 2 TMs family
Reference:	Molecular determinants for activation of G-protein-coupled inward rectifier K+ (GIRK) channels by extracellular acidosis. Mao J, Li L, McManus M, Wu J, Cui N, Jiang C J Biol Chem 2002 Nov 29;277(48):46166-71.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

Phe-137

Therefore , we constructed the GIRK1 with Phe-137 mutated to serine (GIRK1-F137S) and GIRK4 with Ser-143 mutated to threonine (GIRK4-S143T) as shown previously by Vivaudou et al. (35 )

F137S

We found that homomeric GIRK1-F137S and GIRK4-S143T channels were activated at pH o 6.2 by ~20 and ~70% , respectively
Therefore , we constructed the GIRK1 with Phe-137 mutated to serine (GIRK1-F137S) and GIRK4 with Ser-143 mutated to threonine (GIRK4-S143T) as shown previously by Vivaudou et al. (35 )
Homomeric expressions of GIRK1 and GIRK4 channels were achieved by F137S mutation in GIRK1 and S143T mutation in GIRK4
The GIRK1-F137S was moderately stimulated at pH o 6.2 (A) , whereas the GIRK4-S143T currents were strongly augmented (B)
We found that the histidine mutation totally abolished the pH o sensitivity in both homomeric GIRK1-F137S and GIRK4-S143T channels (Figs
Because the homomeric GIRK4-S143T is more sensitive to pH o than the GIRK1-F137S , it is possible that the His-120 in GIRK4 plays a more important role in the pH o sensitivity of the heteromeric GIRK1 / GIRK4 channels

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