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UniProtKB/Swiss-Prot P05093: Variant p.Trp121Arg

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

Variant position:  121
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 Tryptophan (W) to Arginine (R) at position 121 (W121R, p.Trp121Arg).
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 (W) to large size and basic (R)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In AH5; partial loss of activity.
Any additional useful information about the variant.



Sequence information

Variant position:  121
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:   TLDIASNNRKGIAFADSGAH  W QLHRRLAMATFALFKDGDQK
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                         TLDIASNNRKGIAFADSGAHWQLHRRLAMATFALFKDGDQK

Rhesus macaque                TLDILSNNRKGIAFADYGAHWQLHRRLAMATFALFKDGDQK

Chimpanzee                    TLDIASNNRKGIAFADSGAHWQLHRRLAMATFALFKDGDQK

Mouse                         TLGLLSDQGKGVAFADSSSSWQLHRKLVFSTFSLFRDD-QK

Rat                           TQSLLSDQGKGVAFADAGSSWHLHRKLVFSTFSLFKDG-QK

Pig                           TLDILSDNQKGIAFADHGTSWQLHRKLALSTFSLFKGGNLK

Bovine                        TLDILSDNQKGIAFADHGAHWQLHRKLALNAFALFKDGNLK

Goat                          TLDILSDNQKGIAFADHGAHWQLHRKLVLNAFALFKDGNLK

Sheep                         TLDILSDNQKGIAFADHGAHWQLHRKLVLNAFALFKDGNLK

Cat                           TLDILSDNQKGIAFADHGASWQMHRKLALATFALFKDGDQR

Horse                         TLNILSDNQKGVAFADHGAPWQLHRKLVRAAFALFKDGNQK

Chicken                       TTDLLSRGGKDIAFASYGPLWKFQRKLVHAALSMFGEGSVA

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.
Helix 119 – 131


Literature citations

Partial deficiency of 17alpha-hydroxylase/17,20-lyase caused by a novel missense mutation in the canonical cytochrome heme-interacting motif.
Rubtsov P.; Nizhnik A.; Dedov I.I.; Kalinchenko N.; Petrov V.; Orekhova A.; Spirin P.; Prassolov V.; Tiulpakov A.;
Eur. J. Endocrinol. 172:K19-25(2015)
Cited for: VARIANT AH5 ARG-121; CHARACTERIZATION OF VARIANT AH5 ARG-121;

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.