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UniProtKB/Swiss-Prot Q7Z2E3: Variant p.Pro220Leu

Aprataxin
Gene: APTX
Variant information

Variant position:  220
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 Proline (P) to Leucine (L) at position 220 (P220L, p.Pro220Leu).
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:  Similar physico-chemical property. Both residues are medium size and hydrophobic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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

Involvement in disease:  Ataxia-oculomotor apraxia syndrome (AOA) [MIM:208920]: An autosomal recessive syndrome characterized by early-onset cerebellar ataxia, oculomotor apraxia, early areflexia and late peripheral neuropathy. {ECO:0000269|PubMed:11586299, ECO:0000269|PubMed:11586300, ECO:0000269|PubMed:12196655, ECO:0000269|PubMed:12629250, ECO:0000269|PubMed:14506070, ECO:0000269|PubMed:15699391, ECO:0000269|PubMed:15852392, ECO:0000269|PubMed:24362567}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In AOA.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  220
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  356
The length of the canonical sequence.

Location on the sequence:   EQVVVIKDKYPKARYHWLVL  P WTSISSLKAVAREHLELLKH
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                         EQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKH

                              EQVVVIKDKYPKARYHWLVLPWASVSSLKAVTGEHLELLKH

Mouse                         DQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHLELLKH

Rat                           DQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHLELLKH

Pig                           DQVVVIKDKYPKARYHWLVLPWASISSLKAVTREHLELLRH

Bovine                        EQVVVIKDKYPKARFHWLVLPWASISSLKAVTREHLELLRH

Xenopus laevis                DKIVVIKDKYPKARYHWLVLPWQSIASLKVLRAEHLELVQH

Xenopus tropicalis            DKVVVIKDKYPKARYHWLVLPWQSIANLKVLRAEHLELVQH

Zebrafish                     DSVVVIKDKYPKARYHWLVLPWQSISSLKALRSEHVELLKH

Drosophila                    DRAVVMKADYPKSQYHFRVVAKEEFRDITQLTEAQLPLLDH

Baker's yeast                 ----AIDHIFRHFQEKFRIKKSDDDKDP-------------

Fission yeast                 DDVVLVRDMFPKSKMHLLLMT----RDPHLTHVHPLEIMMK

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 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 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;

The gene mutated in ataxia-ocular apraxia 1 encodes the new HIT/Zn-finger protein aprataxin.
Moreira M.-C.; Barbot C.; Tachi N.; Kozuka N.; Uchida E.; Gibson T.; Mendonca P.; Costa M.; Barros J.; Yanagisawa T.; Watanabe M.; Ikeda Y.; Aoki M.; Nagata T.; Coutinho P.; Sequeiros J.; Koenig M.;
Nat. Genet. 29:189-193(2001)
Cited for: ALTERNATIVE SPLICING; TISSUE SPECIFICITY; VARIANTS AOA HIS-213 AND LEU-220;

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.