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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O14832: Variant p.Arg275Trp

Phytanoyl-CoA dioxygenase, peroxisomal
Gene: PHYH
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Variant information Variant position: help 275 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 275 (R275W, p.Arg275Trp). 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 RD; total loss of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 275 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 338 The length of the canonical sequence.
Location on the sequence: help TVFFHPLLIHGSGQNKTQGF R KAISCHFASADCHYIDVKGT 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                         TVFFHPLLIHGSGQNKTQGFRKAISCHFASAD-CHYIDVKGT

Mouse                         TVFFHPLLIHGSGRNKTQGFRKAISCHFGSSD-CQCIDVSG

Rat                           TVFFHPLLIHGSGRNRTQGFRKAISCHYGSSD-CKYISVKG

Bovine                        TVFFHPLLIHGSGRNKSQGFRKAISCHFADAN-CHYIDVEG

Caenorhabditis elegans        TVFFHPILIHGSGANRTEGFRKAISCHYANDDLCRYVNVEG

Slime mold                    IVVWNQQMPHGSMSNKSFNPRMAQFIKIFPTS-----TVNS
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 31 – 338 Phytanoyl-CoA dioxygenase, peroxisomal
Binding site 264 – 264
Binding site 266 – 266
Binding site 275 – 275
Beta strand 275 – 284



Literature citations
Identification of PAHX, a Refsum disease gene.
Mihalik S.J.; Morrell J.C.; Kim D.; Sachsteder K.A.; Watkins P.A.; Gould S.J.;
Nat. Genet. 17:185-189(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANT RD TRP-275; CHARACTERIZATION OF VARIANT RD TRP-275; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; COFACTOR; Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease.
Jansen G.A.; Hogenhout E.M.; Ferdinandusse S.; Waterham H.R.; Ofman R.; Jakobs C.; Skjeldal O.H.; Wanders R.J.A.;
Hum. Mol. Genet. 9:1195-1200(2000)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS RD SER-173; LYS-176; GLY-177; ALA-192 INS; ARG-193; GLN-197; PHE-199; SER-204; TYR-220; SER-257; HIS-269; GLN-275 AND TRP-275; VARIANTS SER-29 AND GLN-245; CHARACTERIZATION OF VARIANTS RD GLY-177; SER-204; GLN-275 AND TRP-275; CATALYTIC ACTIVITY;
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.