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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60313: Variant p.Arg290Gln

Dynamin-like GTPase OPA1, mitochondrial
Gene: OPA1
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Variant information Variant position: help 290 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 Arginine (R) to Glutamine (Q) at position 290 (R290Q, p.Arg290Gln). 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 large size and basic (R) to medium size and polar (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 OPA1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 290 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 960 The length of the canonical sequence.
Location on the sequence: help EVLDVLSDYDASYNTQDHLP R VVVVGDQSAGKTSVLEMIAQ 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                         EVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQ

Mouse                         EVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQ

Rat                           EVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQ

Chicken                       EVLDILSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQ

Zebrafish                     EVLDILSDYDSNYNTQDHLPRVVVVGDQSAGKTSVLEMIAQ
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 88 – 960 Dynamin-like GTPase OPA1, long form
Chain 195 – 960 Dynamin-like GTPase OPA1, short form
Topological domain 114 – 770 Mitochondrial intermembrane
Domain 285 – 561 Dynamin-type G
Binding site 298 – 298
Binding site 300 – 300
Binding site 301 – 301
Binding site 302 – 302
Binding site 302 – 302
Binding site 303 – 303
Mutagenesis 297 – 297 Q -> E. Abolished GTPase activity without affecting the ability to bind membranes.
Mutagenesis 298 – 298 S -> A. Abolished GTPase activity without affecting the ability to bind membranes.
Mutagenesis 300 – 300 G -> E. Abolished GTPase activity without affecting the ability to bind membranes.
Mutagenesis 301 – 301 K -> A. Abolished GTPase activity.
Mutagenesis 302 – 302 T -> A. Abolished GTPase activity.
Mutagenesis 302 – 302 T -> N. Abolished GTPase activity without affecting the ability to bind membranes.



Literature citations
Mutation spectrum and splicing variants in the OPA1 gene.
Delettre C.; Griffoin J.-M.; Kaplan J.; Dollfus H.; Lorenz B.; Faivre L.; Lenaers G.; Belenguer P.; Hamel C.P.;
Hum. Genet. 109:584-591(2001)
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2); ALTERNATIVE SPLICING; TISSUE SPECIFICITY; VARIANTS OPA1 GLN-290; ARG-785 AND PRO-939; OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28.
Alexander C.; Votruba M.; Pesch U.E.A.; Thiselton D.L.; Mayer S.; Moore A.; Rodriguez M.; Kellner U.; Leo-Kottler B.; Auburger G.; Bhattacharya S.S.; Wissinger B.;
Nat. Genet. 26:211-215(2000)
Cited for: TISSUE SPECIFICITY; VARIANTS OPA1 GLN-290 AND ILE-432 DEL; OPA1 mutations in patients with autosomal dominant optic atrophy and evidence for semi-dominant inheritance.
Pesch U.E.A.; Leo-Kottler B.; Mayer S.; Jurklies B.; Kellner U.; Apfelstedt-Sylla E.; Zrenner E.; Alexander C.; Wissinger B.;
Hum. Mol. Genet. 10:1359-1368(2001)
Cited for: VARIANTS OPA1 LYS-270; ALA-273; GLN-290; TRP-290; VAL-438; GLU-468; CYS-551 DEL AND ARG-785; VARIANTS ASN-158; VAL-192 AND ASN-550; Spectrum, frequency and penetrance of OPA1 mutations in dominant optic atrophy.
Toomes C.; Marchbank N.J.; Mackey D.A.; Craig J.E.; Newbury-Ecob R.A.; Bennett C.P.; Vize C.J.; Desai S.P.; Black G.C.M.; Patel N.; Teimory M.; Markham A.F.; Inglehearn C.F.; Churchill A.J.;
Hum. Mol. Genet. 10:1369-1378(2001)
Cited for: VARIANTS OPA1 GLN-290; GLU-300; PHE-384; LYS-503 AND ASN-505; VARIANTS ASN-158 AND GLY-907;
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.