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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P09417: Variant p.Gly23Asp

Dihydropteridine reductase
Gene: QDPR
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Variant information Variant position: help 23 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 Glycine (G) to Aspartate (D) at position 23 (G23D, p.Gly23Asp). 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 glycine (G) to medium size and acidic (D) 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 HPABH4C; severe. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 23 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 244 The length of the canonical sequence.
Location on the sequence: help AAAAAGEARRVLVYGGRGAL G SRCVQAFRARNWWVASVDVV 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                         AAAAAGEARRVLVYGGRGALGSRCVQAFRARNWWVASVDVV

Mouse                         -MAASGEARRVLVYGGRGALGSRCVQAFRARNWWVASIDVV

Rat                           -MAASGEARRVLVYGGRGALGSRCVQAFRARNWWVASIDVV

Pig                           AAAAAGEARRVLVYGGRGALGSRCVQAFRARNWWVASIDVV

Bovine                        MAAAAGEARRVLVYGGRGALGSRCVQAFRARNWWVASIDVQ

Slime mold                    ------MSKNILVLGGSGALGAEVVKFFKSKSWNTISIDFR
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 – 244 Dihydropteridine reductase
Binding site 14 – 38
Helix 21 – 32



Literature citations
Dihydropteridine reductase deficiency: physical structure of the QDPR gene, identification of two new mutations and genotype-phenotype correlations.
Dianzani I.; de Sanctis L.; Smooker P.M.; Gough T.J.; Alliaudi C.; Brusco A.; Spada M.; Blau N.; Dobos M.; Zhang H.-P.; Yang N.; Ponzone A.; Armarego W.L.F.; Cotton R.G.H.;
Hum. Mutat. 12:267-273(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT THR-51; VARIANTS HPABH4C ASP-23; CYS-150; TYR-158 AND ILE-THR-GLY-218 INS; Two new mutations in the dihydropteridine reductase gene in patients with tetrahydrobiopterin deficiency.
Dianzani I.; Howells D.W.; Ponzone A.; Saleeba J.A.; Smooker P.M.; Cotton R.G.H.;
J. Med. Genet. 30:465-469(1993)
Cited for: VARIANTS HPABH4C ASP-23 AND GLY-108; Molecular analysis of 16 Turkish families with DHPR deficiency using denaturing gradient gel electrophoresis (DGGE).
Romstad A.; Kalkanoglu H.S.; Coskun T.; Demirkol M.; Tokatli A.; Dursun A.; Baykal T.; Oezalp I.; Guldberg P.; Guettler F.;
Hum. Genet. 107:546-553(2000)
Cited for: VARIANTS HPABH4C ARG-17; ASP-18; ASP-23; ARG-66; ARG-149 AND CYS-150;
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.