Sequence information
Variant position: 424 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:
FWPDRFLEPGKNSRALAFGC
G ARVCLGEPLARLELFVVLTR
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 FWPDRFLEPGKNSRALAFGCG ARVCLGEPLARLELFVVLTR
Mouse FWPDRFLEPGKNPRTPSFGCG ARVCLGEPLARLELFVVLAR
Rat FWPDRFLESGKSPRIPTFGCG ARVCLGEPLARLEFFVVLAR
Pig FRPDRFLAPGANPSALAFGCG ARVCLGEPLARLELFVVLVQ
Bovine FRPDRFLEPGANPSALAFGCG ARVCLGESLARLELFVVLLR
Cat FRPDRFLVPGASPRVLAFGCG ARVCLGEPLARLELFVVLAR
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
Binding site
426 – 426
Binding site
428 – 428
axial binding residue
Mutagenesis
428 – 428
C -> MST. Loss of activity and loss of P450 absorption.
Literature citations
A novel missense mutation, GLY424SER, in Brazilian patients with 21-hydroxylase deficiency.
Billerbeck A.E.C.; Bachega T.A.S.S.; Frazatto E.T.; Nishi M.Y.; Goldberg A.C.; Marin M.L.C.; Madureira G.; Monte O.; Arnhold I.J.P.; Mendonca B.B.;
J. Clin. Endocrinol. Metab. 84:2870-2872(1999)
Cited for: VARIANTS AH3 LEU-281; TRP-356 AND SER-424;
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;
Three novel mutations in CYP21 gene in Brazilian patients with the classical form of 21-hydroxylase deficiency due to a founder effect.
Billerbeck A.E.C.; Mendonca B.B.; Pinto E.M.; Madureira G.; Arnhold I.J.P.; Bachega T.A.S.S.;
J. Clin. Endocrinol. Metab. 87:4314-4317(2002)
Cited for: VARIANTS AH3 CYS-408 AND SER-424;
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.