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UniProtKB/Swiss-Prot P05093: Variant p.Phe114Val

Steroid 17-alpha-hydroxylase/17,20 lyase
Gene: CYP17A1
Variant information

Variant position:  114
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Phenylalanine (F) to Valine (V) at position 114 (F114V, p.Phe114Val).
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:  Change from large size and aromatic (F) to medium size and hydrophobic (V)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In AH5.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  114
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  508
The length of the canonical sequence.

Location on the sequence:   SGRPQMATLDIASNNRKGIA  F ADSGAHWQLHRRLAMATFAL
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         SGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMATFAL

Rhesus macaque                SGRPQVTTLDILSNNRKGIAFADYGAHWQLHRRLAMATFAL

Chimpanzee                    SGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMATFAL

Mouse                         SGRPQMVTLGLLSDQGKGVAFADSSSSWQLHRKLVFSTFSL

Rat                           SGRPQMVTQSLLSDQGKGVAFADAGSSWHLHRKLVFSTFSL

Pig                           SGRPRVMTLDILSDNQKGIAFADHGTSWQLHRKLALSTFSL

Bovine                        SGRPKVATLDILSDNQKGIAFADHGAHWQLHRKLALNAFAL

Goat                          SGRPKVATLDILSDNQKGIAFADHGAHWQLHRKLVLNAFAL

Sheep                         SGRPKVATLDILSDNQKGIAFADHGAHWQLHRKLVLNAFAL

Cat                           SGRPHVVTLDILSDNQKGIAFADHGASWQMHRKLALATFAL

Horse                         SGRPQVATLNILSDNQKGVAFADHGAPWQLHRKLVRAAFAL

Chicken                       AGRPRTVTTDLLSRGGKDIAFASYGPLWKFQRKLVHAALSM

Sequence annotation in neighborhood:  
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 – 508 Steroid 17-alpha-hydroxylase/17,20 lyase
Mutagenesis 105 – 105 A -> L. Increases the affinity for progesterone, resulting in preferential hydroxylation of progesterone at C17 over C16; increases the catalytic efficiency in the 17,20 lyase reaction.
Beta strand 111 – 114


Literature citations

Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency.
Van Den Akker E.L.T.; Koper J.W.; Boehmer A.L.M.; Themmen A.P.N.; Verhoef-Post M.; Timmerman M.A.; Otten B.J.; Drop S.L.S.; De Jong F.H.;
J. Clin. Endocrinol. Metab. 87:5714-5721(2002)
Cited for: VARIANTS AH5 VAL-114; VAL-116; CYS-347 AND HIS-347;

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.