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UniProtKB/Swiss-Prot P80365: Variant p.Ala328Val

11-beta-hydroxysteroid dehydrogenase type 2
Gene: HSD11B2
Variant information

Variant position:  328
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 Alanine (A) to Valine (V) at position 328 (A328V, p.Ala328Val).
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 small size and hydrophobic (A) to medium size and hydrophobic (V)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  0
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; abolishes enzyme activity.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  328
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:   LHSLRLAMSDLTPVVDAITD  A LLAARPRRRYYPGQGLGLMY
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                         LHSLRLAMSDLTPVVDAITDALLAARPRRRYYPGQGLGLMY

Mouse                         LNSLRMALPDLSPVVDAIIDALLAAQPRSRYYPGRGLGLMY

Rat                           LNSLRMALPDLSPVVDAIIDALLAAQPRSRYYTGRGLGLMY

Bovine                        LHSLSQALPDLSPVVDAITDALLAAQPLRRYYPGHGLGLIY

Rabbit                        LHSLRLALPDLSPVVDAITDALLAARPRPRYYPGRGLGLMY

Sheep                         LHSLSQALPDLSPVVDAITDALLAAQPRRRYYPGHGLGLIY

Zebrafish                     QNYAKTANEDLSPVIDTIVEALLSPQPQVRYYAGPGLILMY

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.

TypePositionsDescription
Chain 1 – 405 11-beta-hydroxysteroid dehydrogenase type 2
Mutagenesis 335 – 335 R -> AQ. Reduced enzyme activity.
Mutagenesis 335 – 335 R -> K. No effect on enzyme activity.
Mutagenesis 336 – 336 R -> AQ. Almost complete loss of enzyme activity.
Mutagenesis 336 – 336 R -> K. Reduced enzyme activity.
Mutagenesis 337 – 337 R -> AQ. Almost complete loss of enzyme activity.
Mutagenesis 337 – 337 R -> K. Reduced enzyme activity.
Mutagenesis 338 – 338 Y -> FA. Complete loss of enzyme activity.
Mutagenesis 339 – 339 Y -> AFH. Reduced enzyme activity.


Literature citations

Genetic, biochemical, and clinical studies of patients with A328V or R213C mutations in 11betaHSD2 causing apparent mineralocorticoid excess.
Morineau G.; Marc J.-M.; Boudi A.; Galons H.; Gourmelen M.; Corvol P.; Pascoe L.; Fiet J.;
Hypertension 34:435-441(1999)
Cited for: CHARACTERIZATION OF VARIANTS AME CYS-213 AND VAL-328;

Mutants of 11beta-hydroxysteroid dehydrogenase (11-HSD2) with partial activity: improved correlations between genotype and biochemical phenotype in apparent mineralocorticoid excess.
Nunez B.S.; Rogerson F.M.; Mune T.; Igarashi Y.; Nakagawa Y.; Phillipov G.; Moudgil A.; Travis L.B.; Palermo M.; Shackleton C.H.L.; White P.C.;
Hypertension 34:638-642(1999)
Cited for: CHARACTERIZATION OF VARIANTS AME ARG-179; PHE-180; HIS-208; VAL-237 AND VAL-328;

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.