UniProtKB/SwissProt variant VAR

Variant information

Variant position:

482

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 Proline (P) to Serine (S) at position 482 (P482S, p.Pro482Ser).

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 (P) to small size and polar (S)

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

BLOSUM score:

-1

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; reduced enzyme activity to 70% of normal.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs776989258 [ dbSNP | Ensembl ]

Sequence information

Variant position:

482

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:

QPLPHCSVILKMQPFQVRLQ P RGMGAHSPGQNQ

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                         QPLPHCSVILKMQPFQVRLQPRGMGAHSPGQNQ---

Mouse                         QPQPYAGINLPIPPFQVRLQPRNLAPQDQGERP

Rat                           QPLPYTGINLLIPPFQVRLQPRNLAPQDQGQKS

Pig                           QPHPHSGINLKVQPFQVRLQPRGGRGEGPGPR-

Bovine                        QPDPYCGVNLKVQPFQVRLQPRGVEA-GAWESA

Cat                           RPRSHCGINLTMQPFQVRLQPRGAVAPGPSQHQ

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
Beta strand	478 – 482

Literature citations

Functional analysis of two recurrent amino acid substitutions in the CYP21 gene from Italian patients with congenital adrenal hyperplasia.
Barbaro M.; Lajic S.; Baldazzi L.; Balsamo A.; Pirazzoli P.; Cicognani A.; Wedell A.; Cacciari E.;
J. Clin. Endocrinol. Metab. 89:2402-2407(2004)
Cited for: VARIANTS AH3 THR-15; LEU-30; LEU-281 AND SER-482; CHARACTERIZATION OF VARIANTS AH3 THR-15 AND SER-482;

Functional and structural consequences of nine CYP21A2 mutations ranging from very mild to severe effects.
de Paula Michelatto D.; Karlsson L.; Lusa A.L.; Silva C.D.; Oestberg L.J.; Persson B.; Guerra-Junior G.; de Lemos-Marini S.H.; Barbaro M.; de Mello M.P.; Lajic S.;
Int. J. Endocrinol. 2016:4209670-4209670(2016)
Cited for: VARIANTS AH3 MET-12; PHE-113; 389-GLN--ALA-391 DEL AND PRO-450; VARIANTS CYS-16; GLY-202; LEU-267 AND MET-450; CHARACTERIZATION OF VARIANTS AH3 MET-12; PHE-113; 389-GLN--ALA-391 DEL; PRO-450 AND SER-482; CHARACTERIZATION OF VARIANTS CYS-16; GLY-202; LEU-267 AND MET-450; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08686: Variant p.Pro482Ser