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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P19099: Variant p.Val386Ala

Cytochrome P450 11B2, mitochondrial
Gene: CYP11B2
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Variant information Variant position: help 386 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 Valine (V) to Alanine (A) at position 386 (V386A, p.Val386Ala). 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 medium size and hydrophobic (V) to small size and hydrophobic (A) 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 CMO-2 deficiency; associated in cis with D-198; small but consistent reduction in the production of 18-hydroxycorticosterone; slightly reduced 11-beta-hydroxylase activity, greatly decreased 18-hydroxylase activity and absent 18-oxidase activity when associated with D-198. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 386 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 503 The length of the canonical sequence.
Location on the sequence: help RAALKETLRLYPVGLFLERV V SSDLVLQNYHIPAGTLVQVF 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                         RAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVF

Mouse                         RAALKETLRLYPVGGFLERILSSDLVLQNYHVPAGTLVLLY

Rat                           RAALKETLRLYPVGGFLERILNSDLVLQNYHVPAGTLVLLY
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 25 – 503 Cytochrome P450 11B2, mitochondrial
Binding site 381 – 381



Literature citations
Mutations in the human CYP11B2 (aldosterone synthase) gene causing corticosterone methyloxidase II deficiency.
Pascoe L.; Curnow K.M.; Slutsker L.; Roesler A.; White P.C.;
Proc. Natl. Acad. Sci. U.S.A. 89:4996-5000(1992)
Cited for: VARIANTS CMO-2 DEFICIENCY TRP-181 AND ALA-386; CATALYTIC ACTIVITY; FUNCTION; PATHWAY; Congenitally defective aldosterone biosynthesis in humans: the involvement of point mutations of the P-450C18 gene (CYP11B2) in CMO II deficient patients.
Mitsuuchi Y.; Kawamoto T.; Naiki Y.; Miyahara K.; Toda K.; Kuribayashi I.; Orii T.; Yasuda K.; Miura K.; Nakao K.; Imura H.; Ulick S.; Shizuta Y.;
Biochem. Biophys. Res. Commun. 182:974-979(1992)
Cited for: VARIANTS CMO-2 DEFICIENCY TRP-181 AND ALA-386; Isolated aldosterone synthase deficiency caused by simultaneous E198D and V386A mutations in the CYP11B2 gene.
Portrat-Doyen S.; Tourniaire J.; Richard O.; Mulatero P.; Aupetit-Faisant B.; Curnow K.M.; Pascoe L.; Morel Y.;
J. Clin. Endocrinol. Metab. 83:4156-4161(1998)
Cited for: VARIANTS CMO-2 DEFICIENCY ASP-198 AND ALA-386; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; Characterization of single-nucleotide polymorphisms in coding regions of human genes.
Cargill M.; Altshuler D.; Ireland J.; Sklar P.; Ardlie K.; Patil N.; Shaw N.; Lane C.R.; Lim E.P.; Kalyanaraman N.; Nemesh J.; Ziaugra L.; Friedland L.; Rolfe A.; Warrington J.; Lipshutz R.; Daley G.Q.; Lander E.S.;
Nat. Genet. 22:231-238(1999)
Cited for: VARIANTS THR-29; GLN-30; ARG-173; THR-248; SER-281; THR-339; ALA-386 AND SER-435; Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis.
Halushka M.K.; Fan J.-B.; Bentley K.; Hsie L.; Shen N.; Weder A.; Cooper R.; Lipshutz R.; Chakravarti A.;
Nat. Genet. 22:239-247(1999)
Cited for: VARIANTS ARG-173; THR-248; SER-281; THR-339; ALA-386 AND SER-435;
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.