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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08686: Variant p.Gly292Ser

Steroid 21-hydroxylase
Gene: CYP21A2
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Variant information Variant position: help 292 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 Glycine (G) to Serine (S) at position 292 (G292S, p.Gly292Ser). 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 glycine (G) to small size and polar (S) 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 AH3; salt wasting form; less then 1% activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 292 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 495 The length of the canonical sequence.
Location on the sequence: help EGSGQLLEGHVHMAAVDLLI G GTETTANTLSWAVVFLLHHP 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                         EGSGQLLEGHVHMAAVDLLIGGTETTANTLSWAVVFLLHHP

                              EGCGQLLEGHVHMSVVDLFIGGTETTATTLSWAVAFLLHHP

Mouse                         KDEERLHEGHVHMSVVDLFIGGTETTATTLSWAVAFLLHHP

Rat                           RDPGQLHERHVHMSVVDLFVGGTETTAATLSWAVAFLLHHP

Pig                           EGQGQLLEGHVHMSVVDLFIGGTETTANTLSWAVVYLLHHP

Bovine                        EGPGQLLEGHVHMSVVDLFIGGTETTASTLSWAVAFLLHHP

Cat                           KGHGRLLEGHVHMSVVDLFIGGTETTATTLSWAVAFLLHHP
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 – 495 Steroid 21-hydroxylase
Mutagenesis 282 – 282 V -> I. Decreased 21-hydroxylase activity. Normal KM but 50% reduced Vmax.
Mutagenesis 282 – 282 V -> T. Decreased 21-hydroxylase activity. Normal KM but 10% reduced Vmax.
Helix 279 – 310



Literature citations
Steroid 21-hydroxylase deficiency: three additional mutated alleles and establishment of phenotype-genotype relationships of common mutations.
Wedell A.; Ritzen E.M.; Haglund-Stengler B.; Luthman H.;
Proc. Natl. Acad. Sci. U.S.A. 89:7232-7236(1992)
Cited for: VARIANTS AH3 LEU-106; SER-292 AND SER-454; Naturally occurring mutants of human steroid 21-hydroxylase (P450c21) pinpoint residues important for enzyme activity and stability.
Nikoshkov A.; Lajic S.; Vlamis-Gardikas A.; Tranebjaerg L.; Holst M.; Wedell A.; Luthman H.;
J. Biol. Chem. 273:6163-6165(1998)
Cited for: VARIANTS AH3 GLU-197 DEL; SER-292 AND PRO-484; Steroid 21-hydroxylase deficiency: mutational spectrum in Denmark, three novel mutations, and in vitro expression analysis.
Ohlsson G.; Mueller J.; Skakkebaek N.E.; Schwartz M.;
Hum. Mutat. 13:482-486(1999)
Cited for: VARIANTS AH3 LEU-31; GLU-65; ASN-173; ASN-237; LEU-282; SER-292; TRP-357 AND VAL-363; Mutational spectrum of the steroid 21-hydroxylase gene in Austria: identification of a novel missense mutation.
Baumgartner-Parzer S.M.; Schulze E.; Waldhaeusl W.; Pauschenwein S.; Rondot S.; Nowotny P.; Meyer K.; Frisch H.; Waldhauser F.; Vierhapper H.;
J. Clin. Endocrinol. Metab. 86:4771-4775(2001)
Cited for: VARIANTS AH3 LEU-31; ASN-173; LEU-282; SER-292; TRP-357; SER-425; HIS-427; SER-454 AND PRO-484; CHARACTERIZATION OF VARIANT AH3 HIS-427; Detection and assignment of CYP21 mutations using peptide mass signature genotyping.
Zeng X.; Witchel S.F.; Dobrowolski S.F.; Moulder P.V.; Jarvik J.W.; Telmer C.A.;
Mol. Genet. Metab. 82:38-47(2004)
Cited for: VARIANTS AH3 LEU-31; ASN-173; ASN-237; GLU-238; LYS-240; LEU-282; SER-292; GLN-357; TRP-357; TYR-366; SER-454; LEU-480 AND PRO-484; Phenotype-genotype correlations of 13 rare CYP21A2 mutations detected in 46 patients affected with 21-hydroxylase deficiency and in one carrier.
Tardy V.; Menassa R.; Sulmont V.; Lienhardt-Roussie A.; Lecointre C.; Brauner R.; David M.; Morel Y.;
J. Clin. Endocrinol. Metab. 95:1288-1300(2010)
Cited for: VARIANTS AH3 THR-78; PRO-168; ASN-173; THR-231; LYS-234; LEU-282; SER-292; ASP-293; LYS-321; PRO-342; HIS-355; TRP-357; TRP-370; CYS-409; SER-425; HIS-427 AND SER-454; CHARACTERIZATION OF VARIANTS AH3 PRO-168; ASN-173; LEU-282; ASP-293; LYS-321; TRP-370 AND SER-425;
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.