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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00439: Variant p.Val190Ala

Phenylalanine-4-hydroxylase
Gene: PAH
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Variant information Variant position: help 190 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 Valine (V) to Alanine (A) at position 190 (V190A, p.Val190Ala). 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 (V) to small size and hydrophobic (A) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 PKU; haplotype 3. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 190 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 452 The length of the canonical sequence.
Location on the sequence: help HGQPIPRVEYMEEEKKTWGT V FKTLKSLYKTHACYEYNHIF 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                         HGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIF

Mouse                         HGQPIPRVEYTEEERKTWGTVFRTLKALYKTHACYEHNHIF

Rat                           HGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIF

Bovine                        HGQPIPRVEYTEEEKKTWGTVFRTLKSLYKTHACYEHNHIF

Caenorhabditis elegans        HGDKIPTITYTDEEIATWRTVYNELTVMYPKNACQEFNYIF

Drosophila                    HGEPLPHVDYTKEEIETWGIIFRNLTKLYKTHACREYNHVF

Slime mold                    HGDEIPRIDYTEEEIKTWGVVYNRLKELFPTNACHQHAYIF

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 – 452 Phenylalanine-4-hydroxylase
Helix 181 – 201



Literature citations
Identification of seven new mutations in the phenylalanine hydroxylase gene, associated with hyperphenylalaninemia in the Belgian population.
Michiels L.; Francois B.; Raus J.; Vandevyver C.;
Hum. Mutat. Suppl. 1:S123-S124(1998)
Cited for: VARIANTS PKU PHE-39 DEL; THR-65; GLN-158; ILE-167; ALA-190; CYS-241 AND TRP-408; Phenylketonuria and hyperphenylalaninemia in eastern Germany: a characteristic molecular profile and 15 novel mutations.
Hennermann J.B.; Vetter B.; Wolf C.; Windt E.; Buehrdel P.; Seidel J.; Moench E.; Kulozik A.E.;
Hum. Mutat. 15:254-260(2000)
Cited for: VARIANTS PKU LEU-39; PRO-41; SER-48; LEU-55; THR-65; SER-68; TYR-84; ASP-104; PRO-155; GLN-158; GLN-183; ALA-190; THR-211; ILE-230; PHE-231; GLN-243; ALA-245; TRP-252; GLN-261; LEU-281; CYS-299; SER-300; VAL-306; VAL-309; CYS-325; ASP-330; ARG-344; VAL-344; VAL-348; PRO-349; CYS-386; GLY-390; PRO-395; VAL-403; TRP-408; SER-410 AND CYS-414; VARIANTS HPA LEU-20 AND CYS-110; Five novel mutations and two large deletions in a population analysis of the phenylalanine hydroxylase gene.
Groselj U.; Tansek M.Z.; Kovac J.; Hovnik T.; Podkrajsek K.T.; Battelino T.;
Mol. Genet. Metab. 106:142-148(2012)
Cited for: VARIANTS PKU ALA-45; SER-48; PRO-62; SER-157; GLN-158; LEU-177; GLY-178; ALA-190; HIS-226; ALA-245; TRP-252; GLN-261; LYS-280; LEU-281; SER-300; PRO-349; GLY-390; VAL-403; TRP-408 AND ASN-415;
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.