UniProtKB/SwissProt variant VAR

Variant information

Variant position:

142

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

Type of variant:

Disease [Disclaimer]

The variants are classified into three categories: Disease, Polymorphism and Unclassified.

Disease: Variants implicated in disease according to literature reports.
Polymorphism: Variants not reported to be implicated in disease.
Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:

From Glutamate (E) to Lysine (K) at position 142 (E142K, p.Glu142Lys).

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 acidic (E) to large size and basic (K)

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 AH2; activity abolished.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs80358219 [ dbSNP | Ensembl ]

Sequence information

Variant position:

142

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:

TSSIEVAGPNSYKEIIQNGH E EEPLENTWPTPYPYSKKLAE

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                         TSSIEVAGPNSYKEIIQNGHEEEPLENTWPTPYPYSKKLAE

Mouse                         SSSVDVAGPNSYKEIVLNGHEEECHESTWSDPYPYSKKMAE

Rat                           CSTVDVAGPNSYKKTILNGREEEHHESTWSNPYPYSKKMAE

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 – 372	3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
Active site	154 – 154	Proton acceptor
Binding site	158 – 158	NAD
Alternative sequence	103 – 222	GTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPTPYPYSKKLAEKAVLAANGWNLKNGDTLYTCALRPTYIYGEGGPFLSASINEALNNNGILSSVGKFSTVNP -> ELQNKIKLTVLEGDILDEPFLKRACQDVSVVIHTACIIDVFGVTHRQSIMNVNVKGRVAWGGDKARWGNEDQKEGQEGKRSLSIEHLLCSGPSDFADHYQLGELKAAIFSFIDEKTRTEQ. In isoform 2.

Literature citations

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;

A novel nonstop mutation in the stop codon and a novel missense mutation in the type II 3-beta-hydroxysteroid dehydrogenase (3-beta-HSD) gene causing, respectively, nonclassic and classic 3-beta-HSD deficiency congenital adrenal hyperplasia.
Pang S.; Wang W.; Rich B.; David R.; Chang Y.T.; Carbunaru G.; Myers S.E.; Howie A.F.; Smillie K.J.; Mason J.I.;
J. Clin. Endocrinol. Metab. 87:2556-2563(2002)
Cited for: VARIANTS AH2 LYS-142 AND THR-222;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P26439: Variant p.Glu142Lys