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 KAT1_ARATH at position 176 were found are listed after the table.

Point mutations at position R176 in KAT1_ARATH

ProteinKAT1_ARATH (Q39128)    Gene: KAT1,At5g46240,MPL12.    (other point mutations)Swiss-Prot
Cross-reference table
Family page
PositionR176
General numbering (KChannelDB) 455
DomainTRANSMEM IV
Family alignments AKT-like Inward rectifiers 6TMs
Plant potassium channels
Other point mutations at the same position Position 178 in AKT-like Inward rectifiers 6TMs family
Position 178 in Plant potassium channels family
Reference #1Sato Y, Sakaguchi M, Goshima S, Nakamura T, Uozumi N
J Biol Chem 2003 Apr 11;278(15):13227-34. Epub 2003 Jan 29.		Medline
Text sourceHTML full text
Point mutationR176D (Not yet checked)
Point mutationR176V (Not yet checked)
Cited point mutationArg176Val,Arg176

Relevant sentences

Reference #1 (Sato Y et al.): Arg176
  • To produce PL fusion proteins , DNA encoding Met1-Arg165 , Met1-Arg171 , Met1-Trp173 , Met1-Arg174 , Met1-Arg176 , Met1-Arg177 , or Met1-Arg184 from KAT1 was fused to DNA coding for PL gly using a two-step PCR approach (18 )

  • A series of S1-4-PL / PLgly fusion proteins in which Arg165 , Arg171 , Arg174 , Arg176 , or Arg177 in S4 was replaced by valine was constructed to eliminate single positive charges (Fig. 4 , A and B)

  • Single mutation of the negatively charged residues , Asp95 , Asp105 , and Asp141 , had a clear effect on KAT1 topology , whereas single mutation of the positively charged residues , Arg165 , Arg171 , Arg174 , Arg176 , and Arg177 , did not

  • Arg176 , Arg177 , and / or Arg184 also contribute in stabilizing S4 in the membrane

  • Arg174 , Arg176 , Arg177 , and / or Arg184 helped stabilize S4 in the membrane at the end of the S4 insertion event (Fig. 5 )

Reference #1 (Sato Y et al.): R176D
  • D , membrane topology of double mutants containing D105R plus R165D , R171D , R174D , R176D , or R177D

  • As shown in Fig. 4 D , the four D105R mutants containing R165D , R174D , R176D , or R177D gave a mixture of mono- and di-glycosylated bands , whereas that containing R171D gave only the mono-glycosylated band

Reference #1 (Sato Y et al.): R176V
  • We therefore measured K + currents of full-length KAT1 containing these same mutations to evaluate the effect of the mutations on K + channel function and found that R174V , R176V , and R177V had the channel activity , although the voltage dependence of current amplitude of R176V and R177V differed from that of the wild-type (Fig. 4 C)

  • B , membrane topology of the R165V , R171V , R174V , R176V , or R177V mutants

  • K + current was detected (+) in the R174V- , R176V- , or R177V-expressing oocytes but not detected (ND) in the D95V- , D105V- , D141V- , R165V- or R171V-expressing oocytes

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