Variant position: 64 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 390 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human VAHKNIREQGRFLQDVFTTL VDLKWPHTLLIFTMSFLCSWL
Mouse VAHKNIREQGRFLQDVFTTL VDLKWPHTLLIFTMSFLCSWL
Rat VAHKNIREQGRFLQDVFTTL VDLKWPHTLLIFTMSFLCSWL
Rabbit VAHKNIREQGRFLQDVFTTL VDLKWTHTLLIFTMSFLCSWL
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 390 ATP-sensitive inward rectifier potassium channel 11
1 – 68 Cytoplasmic
1 – 87 Missing. In isoform 2.
64 – 64 V -> M. Displays gain of function; increased open state stability, reduced ATP sensitivity and increased channel activity; almost completely abolishes high affinity sensitivity to glibenclamide, an inhibitor of ATP-sensitive potassium channels.
Interaction between mutations in the slide helix of Kir6.2 associated with neonatal diabetes and neurological symptoms.
Maennikkoe R.; Jefferies C.; Flanagan S.E.; Hattersley A.; Ellard S.; Ashcroft F.M.;
Hum. Mol. Genet. 19:963-972(2010)
Cited for: INVOLVEMENT IN PNDM2; VARIANTS PNDM2 TYR-60 AND LEU-64; CHARACTERIZATION OF VARIANTS PNDM2 TYR-60 AND LEU-64;
Conserved functional consequences of disease-associated mutations in the slide-helix of Kir6.1 and Kir6.2 subunits of the ATP-sensitive potassium channel.
Cooper P.E.; McClenaghan C.; Chen X.; Stary-Weinzinger A.; Nichols C.G.;
J. Biol. Chem. 292:17387-17398(2017)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANT PNDM2 LEU-64; MUTAGENESIS OF VAL-64;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.