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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P13637: Variant p.Glu815Lys

Sodium/potassium-transporting ATPase subunit alpha-3
Gene: ATP1A3
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Variant information Variant position: help 815 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 Glutamate (E) to Lysine (K) at position 815 (E815K, p.Glu815Lys). 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 acidic (E) to large size and basic (K) 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 AHC2; strong decrease in ATPase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 815 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1013 The length of the canonical sequence.
Location on the sequence: help ITILCIDLGTDMVPAISLAY E AAESDIMKRQPRNPRTDKLV 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                         ITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLV

Mouse                         ITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLV

Rat                           ITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLV

Chicken                       ITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRSDKLV
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 – 1013 Sodium/potassium-transporting ATPase subunit alpha-3
Topological domain 814 – 833 Cytoplasmic



Literature citations
Heterozygous de-novo mutations in ATP1A3 in patients with alternating hemiplegia of childhood: a whole-exome sequencing gene-identification study.
Rosewich H.; Thiele H.; Ohlenbusch A.; Maschke U.; Altmuller J.; Frommolt P.; Zirn B.; Ebinger F.; Siemes H.; Nurnberg P.; Brockmann K.; Gartner J.;
Lancet Neurol. 11:764-773(2012)
Cited for: VARIANTS AHC2 ASN-274; ASP-322; PRO-371; CYS-755; ARG-772; ILE-773; ASN-801; LYS-815 AND TYR-923; De novo mutations in ATP1A3 cause alternating hemiplegia of childhood.
Heinzen E.L.; Swoboda K.J.; Hitomi Y.; Gurrieri F.; Nicole S.; de Vries B.; Tiziano F.D.; Fontaine B.; Walley N.M.; Heavin S.; Panagiotakaki E.; Neri G.; Koelewijn S.; Kamphorst J.; Geilenkirchen M.; Pelzer N.; Laan L.; Haan J.; Ferrari M.; van den Maagdenberg A.M.; Zucca C.; Bassi M.T.; Franchini F.; Vavassori R.; Giannotta M.; Gobbi G.; Granata T.; Nardocci N.; De Grandis E.; Veneselli E.; Stagnaro M.; Vigevano F.; Oechsler C.; Arzimanoglou A.; Ninan M.; Neville B.; Ebinger F.; Fons C.; Campistol J.; Kemlink D.; Nevsimalova S.; Peeters-Scholte C.; Casaer P.; Casari G.; Sange G.; Spiel G.; Martinelli Boneschi F.; Schyns T.; Crawley F.; Poncelin D.; Fiori S.; Abiusi E.; Di Pietro L.; Sweney M.T.; Newcomb T.M.; Viollet L.; Huff C.; Jorde L.B.; Reyna S.P.; Murphy K.J.; Shianna K.V.; Gumbs C.E.; Little L.; Silver K.; Ptacek L.J.; Ferrari M.D.; Bye A.M.; Herkes G.K.; Whitelaw C.M.; Webb D.; Lynch B.J.; Uldall P.; King M.D.; Scheffer I.E.; Sisodiya S.M.; Mikati M.A.; Goldstein D.B.;
Nat. Genet. 44:1030-1034(2012)
Cited for: VARIANTS AHC2 TYR-137; PHE-137; LEU-140; ASN-220; ASN-274; PHE-333; SER-755; SER-773; ASN-801; ARG-806; SER-810; PRO-811; LYS-815; VAL-919 DEL; ARG-947; ASP-955 AND TYR-992; CHARACTERIZATION OF VARIANTS AHC2 PHE-137; PHE-333; ASN-801; PRO-811 AND LYS-815; Identification of ATP1A3 mutations by exome sequencing as the cause of alternating hemiplegia of childhood in Japanese patients.
Ishii A.; Saito Y.; Mitsui J.; Ishiura H.; Yoshimura J.; Arai H.; Yamashita S.; Kimura S.; Oguni H.; Morishita S.; Tsuji S.; Sasaki M.; Hirose S.;
PLoS ONE 8:E56120-E56120(2013)
Cited for: VARIANTS AHC2 CYS-755; ASN-801; LYS-815 AND TYR-927; Alternating Hemiplegia of Childhood mutations have a differential effect on Na(+),K(+)-ATPase activity and ouabain binding.
Weigand K.M.; Messchaert M.; Swarts H.G.; Russel F.G.; Koenderink J.B.;
Biochim. Biophys. Acta 1842:1010-1016(2014)
Cited for: CHARACTERIZATION OF VARIANTS AHC2 TYR-137; ASN-220; ASN-127; ASN-801; LYS-815 AND ARG-947;
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.