KChannelDB: Extraction of mutation data from the literature

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This data was extracted from Medline abstracts and full texts (when available) in an automated manner.

The table below describes different point mutations at a given position and provides links to other documents. The sentence(s) where the point mutations in IRK2_HUMAN at position 82 were found are listed after the table.

Point mutations at position R82 in IRK2_HUMAN

ProteinIRK2_HUMAN (P63252)    Gene: KCNJ2,HIRK    (other point mutations)Swiss-Prot
Cross-reference table
Family page
PositionR82
General numbering (KChannelDB) -
DomainN-term
Family alignments Inward rectifiers (Kir)
Potassium channels 2 TMs
Other point mutations at the same position Position 61 in Inward rectifiers (Kir) family
Position 61 in Potassium channels 2 TMs family
Reference #1Lopes CM, Zhang H, Rohacs T, Jin T, Yang J, Logothetis DE
Neuron 2002 Jun 13;34(6):933-44.		Medline
Text sourceHTML full text
Point mutationR82C (Not yet checked)
Cited point mutationR82C,R82
Point mutationR82Q (Not yet checked)

Relevant sentences

Reference #1 (Lopes CM et al.): R82
  • Seven of the mutants (R67Q , R82Q , K187Q , K188Q , R189Q , R218Q , and H271Q) produced very little whole-cell current , indicating a crucial importance of those residues for the functional integrity of the channel but preventing T50 measurement in five of them (Figure 1B , marked with ?)

  • Two residues (R82 and R189) still could not be assessed because the Cys mutants did not show detectable membrane current

  • View larger version: [In this window] [In new window] Tandem Tetramers with One Single Mutation Allow Investigation of Dead Mutants In order to titrate the functionally lethal effect of the two mutations (R82 and R189) , a strategy of concatenating four subunits into a tandem tetramer was used (Lu et al. , 1999a(image) )

  • For R189 , the mutation in the tetramer made the inhibition significantly faster than control , but the R82 mutation did not have an effect in channel-PIP2 interactions , suggesting a PIP2-independent control on channel activity by this mutation

Reference #1 (Lopes CM et al.): R82Q
  • Seven of the mutants (R67Q , R82Q , K187Q , K188Q , R189Q , R218Q , and H271Q) produced very little whole-cell current , indicating a crucial importance of those residues for the functional integrity of the channel but preventing T50 measurement in five of them (Figure 1B , marked with ?)

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