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UniProtKB/Swiss-Prot Q6ZQW0: Variant p.Arg248Trp

Indoleamine 2,3-dioxygenase 2
Gene: IDO2
Variant information

Variant position:  248
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
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 Arginine (R) to Tryptophan (W) at position 248 (R248W, p.Arg248Trp).
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:  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:  -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

Polymorphism:  The variant Trp-248 (p.R248W) drastically reduces the enzymatic activity (PubMed:17671174, PubMed:18418598). The Del359-420 variant (p.Y359X) generates a truncated, enzymatically inactive protein (PubMed:17671174). The high prevalence of these polymorphic alleles results in a non-functional IDO2 enzyme in up to 50% of Caucasians (PubMed:18418598).
Additional information on the polymorphism described.

Variant description:  Decreased indoleamine 2,3-dioxygenase activity.
Any additional useful information about the variant.

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



Sequence information

Variant position:  248
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  420
The length of the canonical sequence.

Location on the sequence:   TKTLGQMHDYVDPDIFYAGI  R IFLSGWKDNPAMPAGLMYEG
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                         TKTLGQMHDYVDPDIFYAGIRIFLSGWKDNPAMPAGLMYEG

Mouse                         TRALAQMHDYVDPDIFYSVIRIFLSGWKDNPAMPVGLVYEG

Rat                           TRALAQMHDYVDPEIFYLVIRIFLSGWKDNPVMPVGLVYEG

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 – 420 Indoleamine 2,3-dioxygenase 2
Alternative sequence 173 – 420 Missing. In isoform 2.


Literature citations

Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan.
Metz R.; Duhadaway J.B.; Kamasani U.; Laury-Kleintop L.; Muller A.J.; Prendergast G.C.;
Cancer Res. 67:7082-7087(2007)
Cited for: FUNCTION; CATALYTIC ACTIVITY; ALTERNATIVE SPLICING; ACTIVITY REGULATION; TISSUE SPECIFICITY; VARIANTS TRP-248 AND 359-TYR--GLY-420 DEL;

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.