UniProtKB/SwissProt variant VAR

Variant information

Variant position:

208

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 Arginine (R) to Cysteine (C) at position 208 (R208C, p.Arg208Cys).

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 large size and basic (R) to medium size and polar (C)

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 AME; reduces enzyme activity by at least 95%.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs121917780 [ dbSNP | Ensembl ]

Sequence information

Variant position:

208

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

Protein sequence length:

405

The length of the canonical sequence.

Location on the sequence:

CMEVNFFGALELTKGLLPLL R SSRGRIVTVGSPAGDMPYPC

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                         CMEVNFFGALELTKGLLPLLRSSRGRIVTVGSPAGDMPYPC

Mouse                         CMEVNFFGALELTKGLLPLLRHSRGRIVTVGSPAGDMPYPC

Rat                           CMEVNFFGALELTKGLLPLLRHSRGRIVTVGSPAGDMPYPC

Bovine                        CMEVNFFGALEMTKGLLPLLRRSSGRIVTVSSPAGDMPFPC

Rabbit                        CMEVNFFGALELTKGLLPLLHHSRGRIVTLGSPAGEMPYPC

Sheep                         CMEVNFFGALEMTKGLLPLLRRSSGRIVTVSSPAGDMPFPC

Zebrafish                     CMEVNFFGTVTVTRTFLPLLRQSKGRIVTISSPSGEHPFPC

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 – 405	11-beta-hydroxysteroid dehydrogenase type 2
Binding site	219 – 219

Literature citations

Several homozygous mutations in the gene for 11 beta-hydroxysteroid dehydrogenase type 2 in patients with apparent mineralocorticoid excess.
Wilson R.C.; Harbison M.D.; Krozowski Z.S.; Funder J.W.; Shackleton C.H.L.; Hanauske-Abel H.M.; Wei J.-Q.; Hertecant J.; Moran A.; Neiberger R.E.; Balfe J.W.; Fattah A.; Daneman D.; Licholai T.; New M.I.;
J. Clin. Endocrinol. Metab. 80:3145-3150(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-211; 235-264 AND 325-354; VARIANTS AME CYS-186; CYS-208; 250-PRO-SER-251 AND 337-ARG-TYR-338 DELINS HIS;

Human hypertension caused by mutations in the kidney isozyme of 11 beta-hydroxysteroid dehydrogenase.
Mune T.; Rogerson F.M.; Nikkilae H.; Agarwal A.K.; White P.C.;
Nat. Genet. 10:394-399(1995)
Cited for: CHARACTERIZATION OF VARIANTS AME CYS-208; CYS-213; 250-PRO-SER-251 AND 337-ARG-TYR-338 DELINS HIS;

Examination of genotype and phenotype relationships in 14 patients with apparent mineralocorticoid excess.
Dave-Sharma S.; Wilson R.C.; Harbison M.D.; Newfield R.; Azar M.R.; Krozowski Z.S.; Funder J.W.; Shackleton C.H.L.; Bradlow H.L.; Wei J.-Q.; Hertecant J.; Moran A.; Neiberger R.E.; Balfe J.W.; Fattah A.; Daneman D.; Akkurt H.I.; De Santis C.; New M.I.;
J. Clin. Endocrinol. Metab. 83:2244-2254(1998)
Cited for: VARIANTS AME CYS-186; CYS-208; ASN-244; ARG-250; 250-PRO-SER-251; CYS-337 AND 337-ARG-TYR-338 DELINS HIS;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P80365: Variant p.Arg208Cys