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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P15538: Variant p.Arg448His

Cytochrome P450 11B1, mitochondrial
Gene: CYP11B1
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Variant information Variant position: help 448 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 448 (R448H, p.Arg448His). 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 AH4; abolishes steroid 11-beta-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 448 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 WLDIRGSGRNFYHVPFGFGM R QCLGRRLAEAEMLLLLHHVL 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                         WLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVL

Rat                           WLERKRS---FQHLAFGFGVRQCLGRRLAEVEMLLLLHHML

Pig                           WLDNQGSGTRFPHLAFGFGMRQCLGRRLAQVEMLLLLHHVL

Bovine                        WLDRQGSGSRFPHLAFGFGVRQCLGRRVAEVEMLLLLHHVL

Sheep                         WLDRQGSGSRFPHLAFGFGMRQCLGRRVAEVEMLLLLHHVL
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 11B1, mitochondrial
Binding site 450 – 450 axial binding residue
Alternative sequence 401 – 466 Missing. In isoform 2.
Helix 446 – 448



Literature citations
A mutation in CYP11B1 (Arg-448-->His) associated with steroid 11 beta-hydroxylase deficiency in Jews of Moroccan origin.
White P.C.; Dupont J.; New M.I.; Leiberman E.; Hochberg Z.; Roesler A.;
J. Clin. Invest. 87:1664-1667(1991)
Cited for: VARIANT AH4 HIS-448; 21-Hydroxylase and 11beta-hydroxylase mutations in Romanian patients with classic congenital adrenal hyperplasia.
Grigorescu Sido A.; Weber M.M.; Grigorescu Sido P.; Clausmeyer S.; Heinrich U.; Schulze E.;
J. Clin. Endocrinol. Metab. 90:5769-5773(2005)
Cited for: VARIANTS AH4 LEU-94; ARG-318 AND HIS-448; Functional consequences of seven novel mutations in the CYP11B1 gene: four mutations associated with nonclassic and three mutations causing classic 11{beta}-hydroxylase deficiency.
Parajes S.; Loidi L.; Reisch N.; Dhir V.; Rose I.T.; Hampel R.; Quinkler M.; Conway G.S.; Castro-Feijoo L.; Araujo-Vilar D.; Pombo M.; Dominguez F.; Williams E.L.; Cole T.R.; Kirk J.M.; Kaminsky E.; Rumsby G.; Arlt W.; Krone N.;
J. Clin. Endocrinol. Metab. 95:779-788(2010)
Cited for: VARIANTS AH4 SER-42; SER-83; ILE-88; LEU-94; CYS-116; GLY-116; ARG-125; MET-129; HIS-133; SER-135; LEU-139; PRO-158; LEU-159; VAL-161 DEL; ASP-165; ALA-196; 254-LYS--ALA-259 DEL; ASP-267; PRO-299; VAL-306; ARG-314; ARG-318; MET-318; PRO-318; MET-319; VAL-321; VAL-331; SER-341; CYS-366; ASP-368; GLY-371; GLN-374; GLN-384; GLY-384; VAL-386; ALA-401; HIS-427; PHE-438 DEL; GLY-441; ASP-444; CYS-448; HIS-448; GLN-453 AND SER-489; VARIANT GLN-43; CHARACTERIZATION OF VARIANTS AH4 SER-42; SER-83; ILE-88; LEU-94; CYS-116; GLY-116; ARG-125; MET-129; HIS-133; SER-135; LEU-139; PRO-158; LEU-159; ASP-165; ALA-196; 254-LYS--ALA-259 DEL; PRO-299; ARG-314; MET-318; MET-319; VAL-331; CYS-366; ASP-368; GLY-371; GLN-374; GLN-384; ALA-401; PHE-438 DEL; GLY-441; CYS-448; HIS-448 AND GLN-453; CHARACTERIZATION OF VARIANT GLN-43; Two novel CYP11B1 gene mutations in patients from two Croatian families with 11 beta-hydroxylase deficiency.
Dumic K.; Yuen T.; Grubic Z.; Kusec V.; Barisic I.; New M.I.;
Int. J. Endocrinol. 2014:185974-185979(2014)
Cited for: VARIANTS AH4 GLN-141; ARG-318 AND HIS-448; Phenotypic, metabolic, and molecular genetic characterization of six patients with congenital adrenal hyperplasia caused by novel mutations in the CYP11B1 gene.
Nguyen H.H.; Eiden-Plach A.; Hannemann F.; Malunowicz E.M.; Hartmann M.F.; Wudy S.A.; Bernhardt R.;
J. Steroid Biochem. Mol. Biol. 155:126-134(2016)
Cited for: VARIANTS AH4 ARG-318; GLY-332 AND HIS-448; CHARACTERIZATION OF VARIANT GLY-332;
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.