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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P30793: Variant p.Lys224Arg

GTP cyclohydrolase 1
Gene: GCH1
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Variant information Variant position: help 224 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 Lysine (K) to Arginine (R) at position 224 (K224R, p.Lys224Arg). 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 Similar physico-chemical property. Both residues are large size and basic. 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 HPABH4B and DRD; phenotype presenting with dystonia and myoclonus. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 224 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 250 The length of the canonical sequence.
Location on the sequence: help VVVEATHMCMVMRGVQKMNS K TVTSTMLGVFREDPKTREEF 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                         VVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEF

Mouse                         VVIEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEF

Rat                           VVIEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEF

Chicken                       VVIEATHMCMVMRGVQKMNSKTATSTMLGVFREDPKTREEF

Caenorhabditis elegans        VVIEASHMCMVMRGVQKINASTTTSCMLGVFRDDPKTREEF

Drosophila                    VVVEGVHMCMVMRGVQKINSKTVTSTMLGVFRDDPKTREEF

Slime mold                    VVIEASHMCMVMRGVQKPGASTVTSSVCGIFEKDSRTRAEF

Baker's yeast                 VVMEASHMCMVSRGIQKTGSSTVTSCMLGGFR-AHKTREEF

Fission yeast                 VVMEATHMCMVMRGVEKPGSSTVTSSLTGIFQRSHKTREEF

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 – 250 GTP cyclohydrolase 1
Binding site 212 – 212
Alternative sequence 210 – 250 Missing. In isoform GCH-3.
Alternative sequence 210 – 233 HMCMVMRGVQKMNSKTVTSTMLGV -> KSNKYNKGLSPLLSSCHLFVAILK. In isoform GCH-4.
Alternative sequence 214 – 250 Missing. In isoform GCH-2.
Beta strand 224 – 232



Literature citations
Dopa-responsive dystonia in British patients: new mutations of the GTP-cyclohydrolase I gene and evidence for genetic heterogeneity.
Bandmann O.; Nygaard T.G.; Surtess R.; Mardsen C.D.; Wood N.W.; Harding A.E.;
Hum. Mol. Genet. 5:403-406(1996)
Cited for: VARIANTS DRD PRO-88; PRO-153; ARG-203; ARG-224 AND SER-234; Dystonia with motor delay in compound heterozygotes for GTP-cyclohydrolase I gene mutations.
Furukawa Y.; Kish S.J.; Bebin E.M.; Jacobson R.D.; Fryburg J.S.; Wilson W.G.; Shimadzu M.; Hyland K.; Trugman J.M.;
Ann. Neurol. 44:10-16(1998)
Cited for: VARIANTS HPABH4B ASP-108; THR-221 AND ARG-224; Autosomal dominant GTP-CH deficiency presenting as a dopa-responsive myoclonus-dystonia syndrome.
Leuzzi V.; Carducci C.; Carducci C.; Cardona F.; Artiola C.; Antonozzi I.;
Neurology 59:1241-1243(2002)
Cited for: VARIANT DRD ARG-224;
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.