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UniProtKB/Swiss-Prot P05093: Variant p.Phe417Cys

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

Variant position:  417
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 Cysteine (C) at position 417 (F417C, p.Phe417Cys).
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 polar (C)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In AH5; ablates both 17,20-lyase activity and 17alpha-hydroxylase activity; loss of heme-binding and loss of phosphorylation.
Any additional useful information about the variant.

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



Sequence information

Variant position:  417
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:   WALHHNEKEWHQPDQFMPER  F LNPAGTQLISPSVSYLPFGA
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                         WALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYLPFGA

Rhesus macaque                WALHHNEKEWHQPDQFMPERFLNPAGTQLISPSLSYLPFGA

Chimpanzee                    WALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYLPFGA

Mouse                         WALHHDKNEWDQPDRFMPERFLDPTGSHLITPTPSYLPFGA

Rat                           WALHHDENEWDQPDQFMPERFLDPTGSHLITPTQSYLPFGA

Pig                           WALHHNEKEWHRPDLFMPERFLDPTGTQLISPSLSYLPFGA

Bovine                        WALHHSEKEWQHPDLFMPERFLDPTGTQLISPSLSYLPFGA

Goat                          WALHHNEKEWQQPDLFMPERFLDPTGTQLISPSLSYLPFGA

Sheep                         WALHHNEKEWQQPDLFMPERFLDPTGTQLISPSLSYLPFGA

Cat                           WALHHNEKEWYRPDQFMPERFLDPTRSQLISPSLSYLPFGA

Horse                         WALHHNEKEWHQPDRFMPERFLDPTGSQLISPSLSYLPFGA

Chicken                       WSVHHDEKEWDKPEEFNPGRFLDEQGQHIHSPSPSYLPFGA

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
Helix 414 – 417


Literature citations

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;

Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency.
Gupta M.K.; Geller D.H.; Auchus R.J.;
J. Clin. Endocrinol. Metab. 86:4416-4423(2001)
Cited for: VARIANTS AH5 HIS-347; GLN-358 AND CYS-417;

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.