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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P05093: Variant p.Arg96Trp

Steroid 17-alpha-hydroxylase/17,20 lyase
Gene: CYP17A1
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Variant information Variant position: help 96 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 Arginine (R) to Tryptophan (W) at position 96 (R96W, p.Arg96Trp). 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 basic (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 AH5; 25% of both 17alpha-hydroxylase and 17,20-lyase activities. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 96 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 508 The length of the canonical sequence.
Location on the sequence: help VGHHQLAKEVLIKKGKDFSG R PQMATLDIASNNRKGIAFAD 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                         VGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFAD

Rhesus macaque                VGHHQLAKEVLIKKGKDFSGRPQVTTLDILSNNRKGIAFAD

Chimpanzee                    VGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFAD

Mouse                         VGHYQLAREVLVKKGKEFSGRPQMVTLGLLSDQGKGVAFAD

Rat                           IGHYQLAREVLIKKGKEFSGRPQMVTQSLLSDQGKGVAFAD

Pig                           IGDHQLAKEVLLKKGKEFSGRPRVMTLDILSDNQKGIAFAD

Bovine                        IGHHQLAREVLLKKGKEFSGRPKVATLDILSDNQKGIAFAD

Goat                          IGHHQLAREVLLKKGKEFSGRPKVATLDILSDNQKGIAFAD

Sheep                         IGHHQLAREVLLKKGKEFSGRPKVATLDILSDNQKGIAFAD

Cat                           VGDHQLAKEVLVKKGKEFSGRPHVVTLDILSDNQKGIAFAD

Horse                         VGHYQLAKEVLIKKGKEFSGRPQVATLNILSDNQKGVAFAD

Chicken                       VNSYQHAREVLLKKGKAFAGRPRTVTTDLLSRGGKDIAFAS
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 – 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.



Literature citations
Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients.
Laflamme N.; Leblanc J.-F.; Mailloux J.; Faure N.; Labrie F.; Simard J.;
J. Clin. Endocrinol. Metab. 81:264-268(1996)
Cited for: VARIANT AH5 TRP-96; 17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation.
Biason-Lauber A.; Kempken B.; Werder E.; Forest M.G.; Einaudi S.; Ranke M.B.; Matsuo N.; Brunelli V.; Schoenle E.J.; Zachmann M.;
J. Clin. Endocrinol. Metab. 85:1226-1231(2000)
Cited for: VARIANTS AH5 LEU-35; PHE-53 DEL; TRP-96; ASP-177; GLU-330 DEL; CYS-417 AND HIS-496; PHOSPHORYLATION; P450c17 deficiency in Brazilian patients: biochemical diagnosis through progesterone levels confirmed by CYP17 genotyping.
Martin R.M.; Lin C.J.; Costa E.M.F.; de Oliveira M.L.; Carrilho A.; Villar H.; Longui C.A.; Mendonca B.B.;
J. Clin. Endocrinol. Metab. 88:5739-5746(2003)
Cited for: VARIANTS AH5 TRP-96; ASP-329; CYS-362; ARG-406 AND LEU-428;
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.