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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O15528: Variant p.Arg389His

25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
Gene: CYP27B1
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Variant information Variant position: help 389 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 389 (R389H, p.Arg389His). 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 VDDR1A; complete loss of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 389 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 LLKAVVKEVLRLYPVVPGNS R VPDKDIHVGDYIIPKNTLVT 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                         LLKAVVKEVLRLYPVVPGNSRVPDKDIHVGDYIIPKNTLVT

Mouse                         LLKAVIKEVLRLYPVVPGNSRVPDRDIRVGNYVIPQDTLVS

Rat                           LLKAVIKEVLRLYPVVPGNSRVPDRDICVGNYVIPQDTLVS


Literature citations
Genetics of vitamin D 1-alpha-hydroxylase deficiency in 17 families.
Wang J.T.; Lin C.-J.; Burridge S.M.; Fu G.K.; Labuda M.; Portale A.A.; Miller W.L.;
Am. J. Hum. Genet. 63:1694-1702(1998)
Cited for: VARIANTS VDDR1A HIS-65; LYS-189; HIS-389; ILE-409; PRO-429; CYS-453 AND ARG-497; Novel gene mutations in patients with 1alpha-hydroxylase deficiency that confer partial enzyme activity in vitro.
Wang X.; Zhang M.Y.; Miller W.L.; Portale A.A.;
J. Clin. Endocrinol. Metab. 87:2424-2430(2002)
Cited for: VARIANTS VDDR1A GLY-189; PHE-343; GLY-389; HIS-389 AND ILE-409; FUNCTION; CATALYTIC ACTIVITY;
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.