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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P05093: Variant p.Arg347His

Steroid 17-alpha-hydroxylase/17,20 lyase
Gene: CYP17A1
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Variant information Variant position: help 347 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 Histidine (H) at position 347 (R347H, p.Arg347His). 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 medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 347 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 KLYEEIDQNVGFSRTPTISD R NRLLLLEATIREVLRLRPVA 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                         KLYEEIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVA

Rhesus macaque                KLYEEIDQNVGFSRTPTISDRNRLLLLEATIREVLRIRPVA

Chimpanzee                    KLYEEIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVA

Mouse                         KIQKEIDQYVGFSRTPSFNDRTHLLMLEATIREVLRIRPVA

Rat                           KIQKEIDQYVGFSRTPTFNDRSHLLMLEATIREVLRIRPVA

Pig                           KIQDAIDQNIGFNRAPSISDRNQLVLLEATIREVLRFRPVS

Bovine                        RIQDDIDQIIGFNRTPTISDRNRLVLLEATIREVLRIRPVA

Goat                          RIQDSIDQNIGFNRTPTISDRNCLVLLEATIREVLRIRPVA

Sheep                         RIQDSIDQNIGFNRTPTISDRNRLVLLEATIREVLRIRPVA

Cat                           KLQEEIDQNIGFSRTPTMSDRNQLILLEATIREVLRIRPVA

Horse                         KIQEEIDQNVGFSRTPTLSDRNRLLLLEATIREVLRIRPVA

Chicken                       KIQEEMDQKIGLARHPHLSDRPLLPYLEATISEGLRIRPVS
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
Helix 344 – 348



Literature citations
The molecular basis of isolated 17,20 lyase deficiency.
Geller D.H.; Mendonca B.B.; Miller W.L.;
Cited for: VARIANTS AH5 HIS-347 AND GLN-358; 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; 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.