UniProtKB/SwissProt variant VAR

Variant information

Variant position:

236

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:

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:

From Isoleucine (I) to Asparagine (N) at position 236 (I236N, p.Ile236Asn).

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:

Change from medium size and hydrophobic (I) to medium size and polar (N)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

-3

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:

In AH3; salt wasting form.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs111647200 [ dbSNP | Ensembl ]

Sequence information

Variant position:

236

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:

RFFPNPGLRRLKQAIEKRDH I VEMQLRQHKESLVAGQWRDM

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                         RFFPNPGLRRLKQAIEKRDHIVEMQLRQHKESLVAGQWRDM

Mouse                         RFLPNPGLQKLKQIQESRDHIVKQQLKQHKDSLVAGQWKDM

Rat                           RFFPNPGLWKLKQFQESRDHIVMQELKRHKDSLVAGQWKDM

Pig                           RFFPSPGLRRLKQAIENRDHLVEKQLRRHKESMVAGQWRDM

Bovine                        RFFPNPGLWRLKQAIENRDHMVEKQLTRHKESMVAGQWRDM

Cat                           RFFPNPGLRRLKQALENRDRIVEKQLRQHKDSMVAGQWRDM

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	233 – 233
Binding site	233 – 233
Helix	223 – 245

Literature citations

Disease expression and molecular genotype in congenital adrenal hyperplasia due to 21-hydroxylase deficiency.
Speiser P.W.; Dupont J.; Zhu D.; Serrat J.; Buegeleisen M.; Tusie-Luna M.-T.; Lesser M.; New M.I.; White P.C.;
J. Clin. Invest. 90:584-595(1992)
Cited for: VARIANTS AH3 LEU-30; ASN-172; ASN-236; GLU-237; LYS-239; LEU-281 AND TRP-356;

Screening of CYP21 gene mutations in 129 French patients affected by steroid 21-hydroxylase deficiency.
Barbat B.; Bogyo A.; Raux-Demay M.-C.; Kuttenn F.; Boue J.; Simon-Bouy B.; Serre J.-L.; Boue A.; Mornet E.;
Hum. Mutat. 5:126-130(1995)
Cited for: VARIANTS AH3 ASN-172; ASN-236; LEU-281 AND PRO-483; VARIANT SER-493;

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;

A rapid screening for steroid 21-hydroxylase mutations in patients with congenital adrenal hyperplasia.
Kapelari K.; Ghanaati Z.; Wollmann H.; Ventz M.; Ranke M.B.; Kofler R.; Peters H.;
Hum. Mutat. 13:505-505(1999)
Cited for: VARIANTS AH3 LEU-30; ASN-172; ASN-236; GLU-237; LYS-239; LEU-281 AND TRP-356;

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;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08686: Variant p.Ile236Asn