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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q7Z2E3: Variant p.Val277Gly

Aprataxin
Gene: APTX
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Variant information Variant position: help 277 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 Glycine (G) at position 277 (V277G, p.Val277Gly). 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 glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 AOA; abolishes DNA-binding and enzymatic activity towards Ap(4)A. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 277 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 356 The length of the canonical sequence.
Location on the sequence: help KLRFRLGYHAIPSMSHVHLH V ISQDFDSPCLKNKKHWNSFN 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                         KLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFN

                              KLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFN

Mouse                         KLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFN

Rat                           KLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFN

Pig                           KLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFN

Bovine                        KFRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFN

Xenopus laevis                CAPFRFGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFT

Xenopus tropicalis            CAPFQLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFT

Zebrafish                     KLSFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFT

Drosophila                    SRNFLIGFKVNTFWNRLNLHVISNDFYSMAMKRISHWNSFN

Baker's yeast                 ------GIHSVPSMANLHIHVISKDFHSVRLKNKKHYNSFN

Fission yeast                 CNYIKVGFHAGPSMNNLHLHIMTLDHVSPSLKNSAHYISFT

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 – 356 Aprataxin
Domain 182 – 287 HIT
Active site 274 – 274 Tele-AMP-histidine intermediate
Site 265 – 265 Interaction with DNA substrate
Site 276 – 276 Interaction with DNA substrate
Site 291 – 291 Interaction with DNA substrate
Alternative sequence 64 – 356 Missing. In isoform 12.
Alternative sequence 196 – 356 VYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFNTEYFLESQAVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ -> PCTSSCDQPGF. In isoform 13.
Mutagenesis 274 – 274 H -> A. Abolishes enzyme activity.
Beta strand 275 – 279



Literature citations
Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is caused by mutations in a new HIT superfamily gene.
Date H.; Onodera O.; Tanaka H.; Iwabuchi K.; Uekawa K.; Igarashi S.; Koike R.; Hiroi T.; Yuasa T.; Awaya Y.; Sakai T.; Takahashi T.; Nagatomo H.; Sekijima Y.; Kawachi I.; Takiyama Y.; Nishizawa M.; Fukuhara N.; Saito K.; Sugano S.; Tsuji S.;
Nat. Genet. 29:184-188(2001)
Cited for: TISSUE SPECIFICITY; VARIANTS AOA LEU-220 AND GLY-277; Aprataxin forms a discrete branch in the HIT (histidine triad) superfamily of proteins with both DNA/RNA binding and nucleotide hydrolase activities.
Kijas A.W.; Harris J.L.; Harris J.M.; Lavin M.F.;
J. Biol. Chem. 281:13939-13948(2006)
Cited for: FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; DNA-BINDING; CHARACTERIZATION OF VARIANT GLY-277; Cerebellar ataxia with oculomotor apRAxia type 1: clinical and genetic studies.
Le Ber I.; Moreira M.-C.; Rivaud-Pechoux S.; Chamayou C.; Ochsner F.; Kuntzer T.; Tardieu M.; Saied G.; Habert M.-O.; Demarquay G.; Tannier C.; Beis J.-M.; Brice A.; Koenig M.; Duerr A.;
Brain 126:2761-2772(2003)
Cited for: VARIANTS AOA VAL-212; GLY-277 AND ARG-293;
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.