Variant position: 320 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 676 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 ADALWWGVVTVTTIGYGDKV PQTWVGKTIASCFSVFAISFF
Mouse ADALWWGVVTVTTIGYGDKV PQTWVGKTIASCFSVFAISFF
Rat ADALWWGVVTVTTIGYGDKV PQTWVGKTIASCFSVFAISFF
Rabbit ADALWWGVVTVTTIGYGDKV PQTWVGKTIASCFSVFAISFF
Xenopus laevis ADALWWGVVTVTTIGYGDKV PQTWIGKTIASCFSVFAISFF
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 – 676 Potassium voltage-gated channel subfamily KQT member 1
300 – 320 Pore-forming; Name=Segment H5
324 – 324 V -> L. Has a voltage-gated potassium channel activity. Inhibition of voltage-gated potassium channel activity by KCNE4.
326 – 326 K -> R. Has a voltage-gated potassium channel activity. Disrupts KCNE4-mediated voltage-gated potassium channel activity inhibition.
327 – 327 T -> V. Has a voltage-gated potassium channel activity. Disrupts KCNE4-mediated voltage-gated potassium channel activity inhibition.
328 – 328 I -> L. Has a voltage-gated potassium channel activity. Inhibition of voltage-gated potassium channel activity by KCNE4.
338 – 338 S -> C. Inhibits voltage-gated potassium channel activity.
340 – 340 F -> C. Inhibits voltage-gated potassium channel activity.
Biophysical characterization of KCNQ1 P320 mutations linked to long QT syndrome 1.
Thomas D.; Khalil M.; Alter M.; Schweizer P.A.; Karle C.A.; Wimmer A.B.; Licka M.; Katus H.A.; Koenen M.; Ulmer H.E.; Zehelein J.;
J. Mol. Cell. Cardiol. 48:230-237(2010)
Cited for: VARIANT LQT1 HIS-320; CHARACTERIZATION OF VARIANTS LQT1 ALA-320 AND HIS-320;
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.