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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q7Z2E3: Variant p.His215Arg

Aprataxin
Gene: APTX
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Variant information Variant position: help 215 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 Histidine (H) to Arginine (R) at position 215 (H215R, p.His215Arg). 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 (H) to large size and basic (R) 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 AOA. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 215 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 QVYKDEQVVVIKDKYPKARY H WLVLPWTSISSLKAVAREHL 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                         QVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHL

                              QVYKDEQVVVIKDKYPKARYHWLVLPWASVSSLKAVTGEHL

Mouse                         QVYKDDQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHL

Rat                           QVYKDDQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHL

Pig                           QVYKDDQVVVIKDKYPKARYHWLVLPWASISSLKAVTREHL

Bovine                        QVYKDEQVVVIKDKYPKARFHWLVLPWASISSLKAVTREHL

Xenopus laevis                QVFKDDKIVVIKDKYPKARYHWLVLPWQSIASLKVLRAEHL

Xenopus tropicalis            QVFKDDKVVVIKDKYPKARYHWLVLPWQSIANLKVLRAEHL

Zebrafish                     QVYKDDSVVVIKDKYPKARYHWLVLPWQSISSLKALRSEHV

Drosophila                    FLIESDRAVVMKADYPKSQYHFRVVAKEEFRDITQLTEAQL

Baker's yeast                 DPCWDD---ILKDK---------------------------

Fission yeast                 LIFDEAR----------------------------------
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
Alternative sequence 64 – 356 Missing. In isoform 12.
Alternative sequence 196 – 356 VYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFNTEYFLESQAVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ -> PCTSSCDQPGF. In isoform 13.
Beta strand 215 – 222



Literature citations
Early-onset ataxia with ocular motor apraxia and hypoalbuminemia: the aprataxin gene mutations.
Shimazaki H.; Takiyama Y.; Sakoe K.; Ikeguchi K.; Niijima K.; Kaneko J.; Namekawa M.; Ogawa T.; Date H.; Tsuji S.; Nakano I.; Nishizawa M.;
Neurology 59:590-595(2002)
Cited for: VARIANT AOA ARG-215;
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.