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UniProtKB/Swiss-Prot P05023: Variant p.Gly303Arg

Sodium/potassium-transporting ATPase subunit alpha-1
Gene: ATP1A1
Variant information

Variant position:  303
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Glycine (G) to Arginine (R) at position 303 (G303R, p.Gly303Arg).
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:  Change from glycine (G) to large size and basic (R)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
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:  In HOMGSMR2; results in altered sodium and potassium transport as shown by in vitro functional expression of the homologous rat variant.
Any additional useful information about the variant.



Sequence information

Variant position:  303
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  1023
The length of the canonical sequence.

Location on the sequence:   PIAAEIEHFIHIITGVAVFL  G VSFFILSLILEYTWLEAVIF
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                         PIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIF

                              PIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIF

Mouse                         PIAEEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEAVIF

Rat                           PIAEEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEAVIF

Pig                           PIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIF

Bovine                        PIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIF

Rabbit                        PIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIF

Sheep                         PIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIF

Horse                         PIAAEIEHFIHIITGVAVFLGVTFFILSLILEYTWLEAVIF

Chicken                       PIAMEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEAVIF

Xenopus laevis                PIAIEIEHFIHIITGVAVFLGVSFFILSLILQYTWLEAVIF

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.

TypePositionsDescription
Chain 6 – 1023 Sodium/potassium-transporting ATPase subunit alpha-1
Transmembrane 289 – 308 Helical


Literature citations

Germline de novo mutations in ATP1A1 cause renal hypomagnesemia, refractory seizures, and intellectual disability.
Schlingmann K.P.; Bandulik S.; Mammen C.; Tarailo-Graovac M.; Holm R.; Baumann M.; Koenig J.; Lee J.J.Y.; Droegemoeller B.; Imminger K.; Beck B.B.; Altmueller J.; Thiele H.; Waldegger S.; Van't Hoff W.; Kleta R.; Warth R.; van Karnebeek C.D.M.; Vilsen B.; Bockenhauer D.; Konrad M.;
Am. J. Hum. Genet. 103:808-816(2018)
Cited for: INVOLVEMENT IN HOMGSMR2; VARIANTS HOMGSMR2 ARG-302; ARG-303 AND ARG-859; CHARACTERIZATION OF VARIANTS HOMGSMR2 ARG-302; ARG-303 AND ARG-859; FUNCTION;

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.