Sequence information
Variant position: 291 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 494 The length of the canonical sequence.
Location on the sequence:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human EGSGQLLEGHVHMAAVDLLIG GTETTANTLSWAVVFLLHHP
Mouse KDEERLHEGHVHMSVVDLFIG GTETTATTLSWAVAFLLHHP
Rat RDPGQLHERHVHMSVVDLFVG GTETTAATLSWAVAFLLHHP
Pig EGQGQLLEGHVHMSVVDLFIG GTETTANTLSWAVVYLLHHP
Bovine EGPGQLLEGHVHMSVVDLFIG GTETTASTLSWAVAFLLHHP
Cat KGHGRLLEGHVHMSVVDLFIG GTETTATTLSWAVAFLLHHP
Sequence annotation in neighborhood: 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.
Type Positions Description
Chain
1 – 494
Steroid 21-hydroxylase
Mutagenesis
281 – 281
V -> I. Normal KM but 50% reduced Vmax.
Mutagenesis
281 – 281
V -> T. Normal KM but 10% reduced Vmax.
Helix
278 – 309
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-105; SER-291 AND SER-453;
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-196 DEL; SER-291 AND PRO-483;
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-30; GLU-64; ASN-172; ASN-236; LEU-281; SER-291; TRP-356 AND VAL-362;
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-30; ASN-172; LEU-281; SER-291; TRP-356; SER-424; HIS-426; SER-453 AND PRO-483; CHARACTERIZATION OF VARIANT AH3 HIS-426;
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-30; ASN-172; ASN-236; GLU-237; LYS-239; LEU-281; SER-291; GLN-356; TRP-356; TYR-365; SER-453; LEU-479 AND PRO-483; VARIANT ARG-102;
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-77; PRO-167; ASN-172; THR-230; LYS-233; LEU-281; SER-291; ASP-292; LYS-320; PRO-341; HIS-354; TRP-356; TRP-369; CYS-408; SER-424; HIS-426 AND SER-453; CHARACTERIZATION OF VARIANTS AH3 PRO-167; ASN-172; LEU-281; ASP-292; LYS-320; TRP-369 AND SER-424;
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.