Variant position: 253 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 372 The length of the canonical sequence.
Location on the sequence:
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 ILALRALRDPKKAPSVRGQF YYISDDTPHQSYDNLNYILSK
Mouse ILAARGLRDPKKSPNIQGEF YYISDDTPHQSFDDISYTLSK
Rat ILAARGLRDPKKSQNIQGQF YYISDDTPHQSYDDLNCTLSK
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
1 – 372 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
223 – 372 Missing. In isoform 2.
Molecular basis of congenital adrenal hyperplasia due to 3 beta-hydroxysteroid dehydrogenase deficiency.
Simard J.; Rheaume E.; Sanchez R.; Laflamme N.; de Launoit Y.; Luu-The V.; van Seters A.P.; Gordon R.D.; Bettendorf M.; Heinrich U.; Moshang T.; New M.I.; Labrie F.;
Mol. Endocrinol. 7:716-728(1993)
Cited for: VARIANTS AH2 LYS-142; PRO-245 AND ASN-253;
New insight into the molecular basis of 3beta-hydroxysteroid dehydrogenase deficiency: identification of eight mutations in the HSD3B2 gene in eleven patients from seven new families and comparison of the functional properties of twenty-five mutant enzymes.
Moisan A.M.; Ricketts M.L.; Tardy V.; Desrochers M.; Mebarki F.; Chaussain J.-L.; Cabrol S.; Raux-Demay M.C.; Forest M.G.; Sippell W.G.; Peter M.; Morel Y.; Simard J.;
J. Clin. Endocrinol. Metab. 84:4410-4425(1999)
Cited for: VARIANTS AH2 GLU-10; VAL-10; ASP-15; THR-82; SER-100; TRP-108; ARG-129; LYS-142; LEU-155; VAL-167; ARG-173; LEU-186; PRO-205; GLY-213; GLU-216; GLN-222; HIS-222; SER-236; PRO-245; ASN-253; ASP-254; ARG-259; MET-259 AND VAL-294;
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.