Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00439: Variant p.Ser231Pro

Phenylalanine-4-hydroxylase
Gene: PAH
Feedback?
Variant information Variant position: help 231 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 Serine (S) to Proline (P) at position 231 (S231P, p.Ser231Pro). 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 small size and polar (S) to medium size and hydrophobic (P) 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 PKU. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 231 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 PLLEKYCGFHEDNIPQLEDV S QFLQTCTGFRLRPVAGLLSS 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                         PLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSS

Mouse                         PLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSS

Rat                           PLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSS

Bovine                        PLLEKYCGFREDNIPQLEEVSQFLQSCTGFRLRPVAGLLSS

Caenorhabditis elegans        PLLQQNCGFGPDRIPQLQDVSDFLKDCTGYTIRPVAGLLSS

Drosophila                    PLLVDNCGFREDNIPQLEDVSNFLRDCTGFTLRPVAGLLSS

Slime mold                    PLLEQNCGYSPDNIPQLQDISNFLQECTGWRIRPVQGLLSA

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 227 – 238



Literature citations
A European multicenter study of phenylalanine hydroxylase deficiency: classification of 105 mutations and a general system for genotype-based prediction of metabolic phenotype.
Guldberg P.; Rey F.; Zschocke J.; Romano V.; Francois B.; Michiels L.; Ullrich K.; Hoffmann G.F.; Burgard P.; Schmidt H.; Meli C.; Riva E.; Dianzani I.; Ponzone A.; Rey J.; Guettler F.;
Am. J. Hum. Genet. 63:71-79(1998)
Cited for: VARIANTS PKU PHE-41; 63-THR-HIS-64 DELINS PRO-ASN; PRO-67; ILE-92; THR-174; PRO-194; VAL-218; PRO-231; SER-239; GLU-245; GLY-252; VAL-259; ASN-282; PHE-283; PRO-303; HIS-314; LEU-331; PHE-333; THR-342; THR-350; HIS-366; ALA-394; GLY-395 AND PRO-395; In vitro expression analysis of mutations in phenylalanine hydroxylase: linking genotype to phenotype and structure to function.
Waters P.J.; Parniak M.A.; Nowacki P.; Scriver C.R.;
Hum. Mutat. 11:4-17(1998)
Cited for: CHARACTERIZATION OF VARIANTS; VARIANTS PKU PRO-231 AND THR-259;
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.