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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q93099: Variant p.Gly161Arg

Homogentisate 1,2-dioxygenase
Gene: HGD
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Variant information Variant position: help 161 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 Arginine (R) at position 161 (G161R, p.Gly161Arg). 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 large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 AKU; loss of activity; most prevalent mutation in Slovak and Czech patients. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 161 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 445 The length of the canonical sequence.
Location on the sequence: help SMENRCFYNSDGDFLIVPQK G NLLIYTEFGKMLVQPNEICV 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                         SMENRCFYNSDGDFLIVPQKGNLLIYTEFGKMLVQPNEICV

Mouse                         SMENRCFYNSDGDFLIVPQKGKLLIYTEFGKMSLQPNEICV

Caenorhabditis elegans        SMEHTAMYNSDGDFLIVPQQGALEITTEFGRLLVNPQEIAV

Drosophila                    SMDNSAFYNSDGDFLIVPQQGVLDITTEFGRMSVAPNEICV

Slime mold                    SMENKSFYNSDGDFLIVPQQGTLDIQTEFGFMKVKSGEICV
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 1 – 445 Homogentisate 1,2-dioxygenase
Beta strand 144 – 161



Literature citations
Molecular defects in alkaptonuria.
Gehrig A.; Schmidt S.R.; Mueller C.R.; Srsen S.; Srsnova K.; Kress W.;
Cytogenet. Cell Genet. 76:14-16(1997)
Cited for: VARIANT AKU ARG-161; Allelic heterogeneity of alkaptonuria in Central Europe.
Mueller C.R.; Fregin A.; Srsen S.; Srsnova K.; Halliger-Keller B.; Felbor U.; Seemanova E.; Kress W.;
Eur. J. Hum. Genet. 7:645-651(1999)
Cited for: VARIANTS AKU PRO-25; ARG-161; SER-230; ARG-270; GLY-300 AND VAL-368; Mutation spectrum of homogentisic acid oxidase (HGD) in alkaptonuria.
Vilboux T.; Kayser M.; Introne W.; Suwannarat P.; Bernardini I.; Fischer R.; O'Brien K.; Kleta R.; Huizing M.; Gahl W.A.;
Hum. Mutat. 30:1611-1619(2009)
Cited for: VARIANTS AKU ALA-3; ALA-42; GLY-60; PRO-61; CYS-62; LEU-73; THR-92; ARG-97; PHE-120; TRP-120; VAL-122; ARG-123; PRO-137; LEU-158; ARG-161; ASP-168; LYS-168; ARG-183; GLY-187; TRP-217; LEU-225; SER-230; PRO-258; ARG-269; ARG-270; GLY-300; PRO-321; LEU-359; ARG-360; GLU-362; VAL-368; LEU-373 AND GLN-401; Analysis of HGD gene mutations in patients with alkaptonuria from the United Kingdom: identification of novel mutations.
Usher J.L.; Ascher D.B.; Pires D.E.; Milan A.M.; Blundell T.L.; Ranganath L.R.;
JIMD Rep. 24:3-11(2015)
Cited for: VARIANTS AKU LYS-13; ASN-18; ALA-42; GLN-53; ARG-115; PHE-120; ARG-123; ARG-161; LEU-169; ASN-171; GLY-197; SER-219; HIS-225; PRO-225; SER-230; PHE-245; ARG-270; ASN-276; GLY-300; ASP-337; LEU-359; ARG-360; ARG-361; VAL-368 AND HIS-374; VARIANT THR-172;
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.