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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P51787: Variant p.Asn586Asp

Potassium voltage-gated channel subfamily KQT member 1
Gene: KCNQ1
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Variant information Variant position: help 586 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 Asparagine (N) to Aspartate (D) at position 586 (N586D, p.Asn586Asp). 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 polar (N) to medium size and acidic (D) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 LQT1; decreases outward potassium current; decreases plasma membrane localization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 586 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 676 The length of the canonical sequence.
Location on the sequence: help SIGKPSLFISVSEKSKDRGS N TIGARLNRVEDKVTQLDQRL 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                         SIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVTQLDQRL

Mouse                         SIGKPSLFIPISEKSKDRGSNTIGARLNRVEDKVTQLDQRL

Rat                           SIGKPSLFIPISEKSKDRGSNTIGARLNRVEDKVTQLDQRL

Pig                           SIGRPALFISSSEKVKDRGSNTIGARLNRVEDKVTQLDQRL

Rabbit                        SIGKPSLFVPISEKSKDRGSNSIGARLNRVEDKVTQLDQRL

Xenopus laevis                SLGKPSLFLSVSDKVKDKGINTIGSRLNRVEDKVTQMDHKL
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 – 676 Potassium voltage-gated channel subfamily KQT member 1
Topological domain 349 – 676 Cytoplasmic
Coiled coil 585 – 621
Mutagenesis 589 – 589 G -> M. No effect.
Mutagenesis 590 – 590 A -> W. Reduced cell surface expression and strongly reduced potassium current.
Mutagenesis 593 – 593 N -> G. Reduced cell surface expression and moderately reduced potassium current.
Mutagenesis 602 – 602 L -> A. Does not interact with AKAP9 and the targeting protein kinase A (PKA) catalytic subunit and protein phosphatase 1 (PP1); when associated with I-609.



Literature citations
Genetic testing in the long QT syndrome: development and validation of an efficient approach to genotyping in clinical practice.
Napolitano C.; Priori S.G.; Schwartz P.J.; Bloise R.; Ronchetti E.; Nastoli J.; Bottelli G.; Cerrone M.; Leonardi S.;
JAMA 294:2975-2980(2005)
Cited for: VARIANTS LQT1 THR-46; PHE-137; LYS-146; ASP-173; PRO-174; TRP-190; PRO-192; HIS-202; MET-204; PHE-209; MET-215; HIS-231; PRO-239; LEU-254; ARG-258; ASN-258; VAL-262; ASP-272; TRP-277; GLU-280; GLU-287; THR-302; ASP-308; GLU-316; MET-322; ARG-343; LEU-343; PRO-349; ARG-350; SER-351; THR-360; ASP-372; MET-393; GLY-518; PRO-518; ASP-548; ALA-554; THR-567; LEU-573; HIS-583 AND ASP-586; Cellular mechanisms of mutations in Kv7.1: auditory functions in Jervell and Lange-Nielsen syndrome vs. Romano-Ward syndrome.
Mousavi Nik A.; Gharaie S.; Jeong Kim H.;
Front. Cell. Neurosci. 9:32-32(2015)
Cited for: CHARACTERIZATION OF VARIANTS LQT1 ASN-242; PRO-243; HIS-250; VAL-306; ASN-317; ASP-586 AND MET-619; CHARACTERIZATION OF VARIANTS JLNS1 PHE-248; ILE-311; MET-322 AND ASP-589;
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.