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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q93099: Variant p.Pro230Ser

Homogentisate 1,2-dioxygenase
Gene: HGD
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Variant information Variant position: help 230 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 Proline (P) to Serine (S) at position 230 (P230S, p.Pro230Ser). 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 medium size and hydrophobic (P) to small size and polar (S) 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 AKU; complete 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 230 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 LPDLGPIGANGLANPRDFLI P IAWYEDRQVPGGYTVINKYQ 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                         LPDLGPIGANGLANPRDFLIPIAWYEDRQVPGGYTVINKYQ

Mouse                         LPDLGPIGANGLANPRDFLIPVAWYEDRRVPGGYTVINKFQ

Caenorhabditis elegans        LPDLGPIGANGLANPRDFEAPVAWFEDLDV--EFTIINKYQ

Drosophila                    LPDLGPIGANGLANPRDFETPVAWFDDRDVK-DFQVISKFQ

Slime mold                    LPDLGPIGANGLANPRDFLSPVAAYEKKEGI-EHTKINKFL
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 227 – 230



Literature citations
The molecular basis of alkaptonuria.
Fernandez-Canon J.M.; Granadino B.; Beltran-Valero de Bernabe D.; Renedo M.; Fernandez-Ruiz E.; Penalva M.A.; Rodriguez de Cordoba S.;
Nat. Genet. 14:19-24(1996)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANTS AKU SER-230 AND GLY-300; VARIANT HIS-80; CHARACTERIZATION OF VARIANT AKU SER-230; FUNCTION; CATALYTIC ACTIVITY; 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.