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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P56696: Variant p.Gly285Cys

Potassium voltage-gated channel subfamily KQT member 4
Gene: KCNQ4
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Variant information Variant position: help 285 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Glycine (G) to Cysteine (C) at position 285 (G285C, p.Gly285Cys). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from glycine (G) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In DFNA2A; loss of potassium selectivity of the pore. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 285 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 695 The length of the canonical sequence.
Location on the sequence: help SDFSSYADSLWWGTITLTTI G YGDKTPHTWLGRVLAAGFAL 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         SDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFAL

Mouse                         SDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFAL
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 1 – 695 Potassium voltage-gated channel subfamily KQT member 4
Intramembrane 271 – 292 Pore-forming; Name=Segment H5
Motif 283 – 288 Selectivity filter
Mutagenesis 266 – 266 D -> G. Resistant to inhibition by potassium channel toxin SsTX. Normal voltage activation.
Mutagenesis 268 – 268 S -> G. No effect on inhibition by potassium channel toxin SsTX.
Mutagenesis 272 – 272 D -> G. No effect on inhibition by potassium channel toxin SsTX.
Mutagenesis 288 – 288 D -> G. Resistant to inhibition by potassium channel toxin SsTX. Normal voltage activation.
Mutagenesis 290 – 290 T -> V. No effect on inhibition by potassium channel toxin SsTX.
Mutagenesis 292 – 292 H -> G. No effect on inhibition by potassium channel toxin SsTX.
Mutagenesis 295 – 295 L -> V. No effect on inhibition by potassium channel toxin SsTX.
Mutagenesis 298 – 298 V -> T. No effect on inhibition by potassium channel toxin SsTX.



Literature citations
Mutations in the KCNQ4 gene are responsible for autosomal dominant deafness in four DFNA2 families.
Coucke P.J.; Van Hauwe P.; Kelley P.M.; Kunst H.; Schatteman I.; Van Velzen D.; Meyers J.; Ensink R.J.; Verstreken M.; Declau F.; Marres H.; Kastury K.; Bhasin S.; McGuirt W.T.; Smith R.J.H.; Cremers C.W.R.J.; Van de Heyning P.; Willems P.J.; Smith S.D.; Van Camp G.;
Hum. Mol. Genet. 8:1321-1328(1999)
Cited for: VARIANTS DFNA2A SER-276; CYS-285 AND SER-321;
Disclaimer: 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.