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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q16518: Variant p.Arg91Trp

Retinoid isomerohydrolase
Gene: RPE65
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Variant information Variant position: help 91 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 Tryptophan (W) at position 91 (R91W, p.Arg91Trp). 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 large size and aromatic (W) 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 RP20 and LCA2; reduced protein levels; decreased function in the retinoid cycle. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 91 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 533 The length of the canonical sequence.
Location on the sequence: help DFKEGHVTYHRRFIRTDAYV R AMTEKRIVITEFGTCAFPDP 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                         DFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDP

                              DFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDP

Mouse                         DFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDP

Rat                           DFKEGHVTYYRRFIRTDAYVRAMTEKRIVITEFGTCAFPDP

Bovine                        DFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDP

Chicken                       DFKEGHVTYHRRFVRTDAYVRAMTEKRIVITEFGTYAYPDP

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 – 533 Retinoid isomerohydrolase
Modified residue 101 – 101 Phosphothreonine
Modified residue 105 – 105 Phosphothreonine
Mutagenesis 106 – 106 C -> A. No loss of enzymatic activity. No effect on palmitoylation. No loss of membrane association.
Mutagenesis 106 – 106 C -> Y. Does not affect isomerohydrolase activity.



Literature citations
Mutations in the RPE65 gene in patients with autosomal recessive retinitis pigmentosa or Leber congenital amaurosis.
Morimura H.; Fishman G.A.; Grover S.A.; Fulton A.B.; Berson E.L.; Dryja T.P.;
Proc. Natl. Acad. Sci. U.S.A. 95:3088-3093(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS RP20 TRP-91; LYS-102; THR-132; SER-341; GLY-452 AND ASP-473; Genetics and phenotypes of RPE65 mutations in inherited retinal degeneration.
Thompson D.A.; Gyuerues P.; Fleischer L.L.; Bingham E.L.; McHenry C.L.; Apfelstedt-Sylla E.; Zrenner E.; Lorenz B.; Richards J.E.; Jacobson S.G.; Sieving P.A.; Gal A.;
Invest. Ophthalmol. Vis. Sci. 41:4293-4299(2000)
Cited for: VARIANTS RP20 HIS-79; HIS-85; TRP-91; GLN-95; THR-132; TYR-167; THR-294; VAL-436 AND VAL-528; Evaluation of genotype-phenotype associations in Leber congenital amaurosis.
Galvin J.A.; Fishman G.A.; Stone E.M.; Koenekoop R.K.;
Retina 25:919-929(2005)
Cited for: VARIANTS LCA2 SER-40; TRP-91; TYR-182; ASP-239; GLU-393 AND ASP-473; Molecular characterization of Leber congenital amaurosis in Koreans.
Seong M.W.; Kim S.Y.; Yu Y.S.; Hwang J.M.; Kim J.Y.; Park S.S.;
Mol. Vis. 14:1429-1436(2008)
Cited for: VARIANT LCA2 TRP-91; Predicting the pathogenicity of RPE65 mutations.
Philp A.R.; Jin M.; Li S.; Schindler E.I.; Iannaccone A.; Lam B.L.; Weleber R.G.; Fishman G.A.; Jacobson S.G.; Mullins R.F.; Travis G.H.; Stone E.M.;
Hum. Mutat. 30:1183-1188(2009)
Cited for: CHARACTERIZATION OF VARIANTS LCA2 SER-40; GLN-44; GLN-91; TRP-91; ILE-101; ASP-239; ASN-318; PRO-408 AND VAL-434; CHARACTERIZATION OF VARIANT LYS-321; CHARACTERIZATION OF VARIANT RP20 THR-294; Next-generation genetic testing for retinitis pigmentosa.
Neveling K.; Collin R.W.; Gilissen C.; van Huet R.A.; Visser L.; Kwint M.P.; Gijsen S.J.; Zonneveld M.N.; Wieskamp N.; de Ligt J.; Siemiatkowska A.M.; Hoefsloot L.H.; Buckley M.F.; Kellner U.; Branham K.E.; den Hollander A.I.; Hoischen A.; Hoyng C.; Klevering B.J.; van den Born L.I.; Veltman J.A.; Cremers F.P.; Scheffer H.;
Hum. Mutat. 33:963-972(2012)
Cited for: VARIANTS RP20 VAL-70; TRP-91; ASP-239 AND HIS-368;
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.