Variant position: 116 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:
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 RPQMATLDIASNNRKGIAFA DSGAHWQLHRRLAMATFALFK
Rhesus macaque RPQVTTLDILSNNRKGIAFA DYGAHWQLHRRLAMATFALFK
Chimpanzee RPQMATLDIASNNRKGIAFA DSGAHWQLHRRLAMATFALFK
Mouse RPQMVTLGLLSDQGKGVAFA DSSSSWQLHRKLVFSTFSLFR
Rat RPQMVTQSLLSDQGKGVAFA DAGSSWHLHRKLVFSTFSLFK
Pig RPRVMTLDILSDNQKGIAFA DHGTSWQLHRKLALSTFSLFK
Bovine RPKVATLDILSDNQKGIAFA DHGAHWQLHRKLALNAFALFK
Goat RPKVATLDILSDNQKGIAFA DHGAHWQLHRKLVLNAFALFK
Sheep RPKVATLDILSDNQKGIAFA DHGAHWQLHRKLVLNAFALFK
Cat RPHVVTLDILSDNQKGIAFA DHGASWQMHRKLALATFALFK
Horse RPQVATLNILSDNQKGVAFA DHGAPWQLHRKLVRAAFALFK
Chicken RPRTVTTDLLSRGGKDIAFA SYGPLWKFQRKLVHAALSMFG
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.
Type Positions Description
1 – 508 Steroid 17-alpha-hydroxylase/17,20 lyase
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.
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;
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