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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O43681: Variant p.Val163Ala

ATPase GET3
Gene: GET3
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Variant information Variant position: help 163 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 163 (V163A, p.Val163Ala). 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 CMD2H; contrary to the wild type, the mutant is unable to rescue cardiac failure in zebrafish lacking GET3; results in decreased function in tail-anchored membrane protein insertion into ER membrane; has no effect on thermal stability. Any additional useful information about the variant.


Sequence information Variant position: help 163 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 348 The length of the canonical sequence.
Location on the sequence: help DEAMSYAEVMRLVKGMNFSV V VFDTAPTGHTLRLLNFPTIV 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                         DEAMSYAEVMRLVK------GMNFSVVVFDTAPTGHTLRLLNFPTIV

Mouse                         DEAMSYAEVMRLVK------GMNFSVVVFDTAPTGHTLRLL

Rat                           DEAMSYAEVMRLVK------GMNFSVVVFDTAPTGHTLRLL

Bovine                        DEAMSYAEVMRLVK------GMNFSVVVFDTAPTGHTLRLL

Xenopus laevis                DEAMSYAEVMRLVK------GMNFSVVVFDTAPTGHTLRLL

Xenopus tropicalis            DEAMSYAEVMRLVK------GMNFSVVVFDTAPTGHTLRLL

Zebrafish                     DEAMSYAEVMRLVK------GMNFSVVVFDTAPTGHTLRLL

Baker's yeast                 DEALSFMEVMKHIKRQEQGEGETFDTVIFDTAPTGHTLRFL

Fission yeast                 DEALAFAEILKQIK------SMEFDCVIFDTAPTGHTLRFL
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 2 – 348 ATPase GET3
Beta strand 161 – 166



Literature citations
Biallelic variants in ASNA1, encoding a cytosolic targeting factor of tail-anchored proteins, cause rapidly progressive pediatric cardiomyopathy.
Verhagen J.M.A.; van den Born M.; van der Linde H.C.; Nikkels P.G.J.; Verdijk R.M.; Kivlen M.H.; van Unen L.M.A.; Baas A.F.; Ter Heide H.; van Osch-Gevers L.; Hoogeveen-Westerveld M.; Herkert J.C.; Bertoli-Avella A.M.; van Slegtenhorst M.A.; Wessels M.W.; Verheijen F.W.; Hassel D.; Hofstra R.M.W.; Hegde R.S.; van Hasselt P.M.; van Ham T.J.; van de Laar I.M.B.H.;
Circ. Genom. Precis. Med. 12:397-406(2019)
Cited for: INVOLVEMENT IN CMD2H; VARIANTS CMD2H ALA-163; TRP-289 AND 305-GLN--GLN-348 DEL; SUBCELLULAR LOCATION; 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.