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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P07101: Variant p.Phe309Ser

Tyrosine 3-monooxygenase
Gene: TH
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Variant information Variant position: help 309 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 Phenylalanine (F) to Serine (S) at position 309 (F309S, p.Phe309Ser). 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 large size and aromatic (F) to small size and polar (S) 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 ARSEGS; complete loss of tyrosine 3-monooxygenase activity. Any additional useful information about the variant.


Sequence information Variant position: help 309 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 LERFSGYREDNIPQLEDVSR F LKERTGFQLRPVAGLLSARD 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                         LERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARD

                              LERFSGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARD

Mouse                         LERYCGYREDSIPQLEDVSHFLKERTGFQLRPVAGLLSARD

Rat                           LERYCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARD

Bovine                        LERFCGYREDRIPQLEDVSRFLKERTGFQLRPAAGLLSARD

Caenorhabditis elegans        LQEEKVLTADRIPQIRDVNKFLQKKTGFELRPCSGLLSARD

Drosophila                    LQDEQIFVETRLPQLQEMSDFLRKNTGFSLRPAAGLLTARD
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
Alternative sequence 264 – 357 Missing. In isoform 5 and isoform 6.
Helix 303 – 314



Literature citations
Tyrosine hydroxylase deficiency unresponsive to L-dopa treatment with unusual clinical and biochemical presentation.
De Lonlay P.; Nassogne M.C.; van Gennip A.H.; van Cruchten A.C.; Billatte de Villemeur T.; Cretz M.; Stoll C.; Launay J.M.; Steenberger-Spante G.C.; van den Heuvel L.P.; Wevers R.A.; Saudubray J.M.; Abeling N.G.;
J. Inherit. Metab. Dis. 23:819-825(2000)
Cited for: VARIANT ARSEGS SER-309; 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.