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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q09470: Variant p.Val408Ala

Potassium voltage-gated channel subfamily A member 1
Gene: KCNA1
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Variant information Variant position: help 408 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 Valine (V) to Alanine (A) at position 408 (V408A, p.Val408Ala). 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 medium size and hydrophobic (V) to small size and hydrophobic (A) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 EA1; channels have voltage dependence similar to that of wild-type channels but with faster kinetics and increased C-type inactivation; accelerates recovery from N-type inactivation due to interaction with KCNAB1; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 408 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 495 The length of the canonical sequence.
Location on the sequence: help VGSLCAIAGVLTIALPVPVI V SNFNYFYHRETEGEEQAQLL 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                         VGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQLL

Mouse                         VGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQLL

Rat                           VGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQLL

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 – 495 Potassium voltage-gated channel subfamily A member 1
Transmembrane 387 – 415 Helical; Name=Segment S6



Literature citations
Episodic ataxia/myokymia syndrome is associated with point mutations in the human potassium channel gene, KCNA1.
Browne D.L.; Gancher S.T.; Nutt J.G.; Brunt E.R.P.; Smith E.A.; Kramer P.; Litt M.;
Nat. Genet. 8:136-140(1994)
Cited for: VARIANTS EA1 PHE-174; SER-239; ILE-249 AND ALA-408; Episodic ataxia results from voltage-dependent potassium channels with altered functions.
Adelman J.P.; Bond C.T.; Pessia M.; Maylie J.;
Neuron 15:1449-1454(1995)
Cited for: CHARACTERIZATION OF VARIANTS EA1 CYS-184; ASP-325 AND ALA-408; FUNCTION; TRANSPORTER ACTIVITY; Episodic ataxia type 1 mutations in the human Kv1.1 potassium channel alter hKvbeta 1-induced N-type inactivation.
Maylie B.; Bissonnette E.; Virk M.; Adelman J.P.; Maylie J.G.;
J. Neurosci. 22:4786-4793(2002)
Cited for: CHARACTERIZATION OF VARIANTS EA1 ASP-325 AND ALA-408; FUNCTION; SUBCELLULAR LOCATION; SUBUNIT; INTERACTION WITH KCNAB1; Episodic ataxia type 1 mutations in the KCNA1 gene impair the fast inactivation properties of the human potassium channels Kv1.4-1.1/Kvbeta1.1 and Kv1.4-1.1/Kvbeta1.2.
Imbrici P.; D'Adamo M.C.; Kullmann D.M.; Pessia M.;
Eur. J. Neurosci. 24:3073-3083(2006)
Cited for: CHARACTERIZATION OF VARIANTS EA1 ASP-325; ILE-404 AND ALA-408; MUTAGENESIS OF ILE-177; FUNCTION; SUBCELLULAR LOCATION;
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.