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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P07101: Variant p.Gln412Lys

Tyrosine 3-monooxygenase
Gene: TH
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Variant information Variant position: help 412 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 Glutamine (Q) to Lysine (K) at position 412 (Q412K, p.Gln412Lys). 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 polar (Q) to large size and basic (K) 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 ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; reduced affinity for L-tyrosine. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 412 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 528 The length of the canonical sequence.
Location on the sequence: help EEIEKLSTLYWFTVEFGLCK Q NGEVKAYGAGLLSSYGELLH 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                         EEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLH

                              EEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLH

Mouse                         EEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLH

Rat                           EEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLH

Bovine                        EEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLH

Caenorhabditis elegans        EHIEKLSTVYWFIVEFGLCKEDGKLKAIGAGLLSAYGELMH

Drosophila                    EEIEKLSTVYWFTVEFGLCKEHGQIKAYGAGLLSSYGELLH
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 – 528 Tyrosine 3-monooxygenase
Binding site 406 – 406
Beta strand 409 – 412



Literature citations
A point mutation in the tyrosine hydroxylase gene associated with Segawa's syndrome.
Luedecke B.; Dworniczak B.; Bartholome K.;
Hum. Genet. 95:123-125(1995)
Cited for: INVOLVEMENT IN ARSEGS; VARIANT ARSEGS LYS-412; Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene.
Knappskog P.M.; Flatmark T.; Mallet J.; Luedecke B.; Bartholome K.;
Hum. Mol. Genet. 4:1209-1212(1995)
Cited for: FUNCTION; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANT ARSEGS LYS-412; Functional studies of tyrosine hydroxylase missense variants reveal distinct patterns of molecular defects in Dopa-responsive dystonia.
Fossbakk A.; Kleppe R.; Knappskog P.M.; Martinez A.; Haavik J.;
Hum. Mutat. 35:880-890(2014)
Cited for: FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANTS ARSEGS TYR-207; GLY-227; HIS-233; PRO-236; THR-241; TYR-246; SER-247; GLY-259; PRO-276; ALA-301; SER-309; MET-314; PRO-319; TRP-328; HIS-337; PHE-359; LEU-375; VAL-376; MET-387; THR-394; MET-399; LYS-412; ARG-414; PRO-441; GLY-467; LEU-492; MET-494; GLY-498 AND GLN-510;
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.