UniProtKB/Swiss-Prot P17516: Variant p.Gln250Arg

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 250 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: LB/B 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 Glutamine (Q) to Arginine (R) at position 250 (Q250R, p.Gln250Arg). 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 polar (Q) to large size and basic (R) 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
Polymorphism: The allele with Cys-145/Val-311 shows a three- to five-fold decrease in catalytic efficiency for xenobiotic and steroidal substrates compared to the Ser-145/Leu-311 allele. Additional information on the polymorphism described.
Other resources: Links to websites of interest for the variant.

• Variant rs4880718 [ dbSNP | Ensembl ]

Sequence information

Variant position: 250 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 323 The length of the canonical sequence.
Location on the sequence: PNSPVLLEDPVLCALAKKHK Q TPALIALRYQLQRGVVVLAK 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.
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 – 323	Aldo-keto reductase family 1 member C4

Literature citations

Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase.
Qin K.-N.; New M.I.; Cheng K.-C.;
J. Steroid Biochem. Mol. Biol. 46:673-679(1993)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT ARG-250; Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases.
Khanna M.; Qin K.-N.; Wang R.W.; Cheng K.-C.;
J. Biol. Chem. 270:20162-20168(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; TISSUE SPECIFICITY; VARIANT ARG-250; CATALYTIC ACTIVITY; FUNCTION; Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans.
Khanna M.; Qin K.-N.; Cheng K.-C.;
J. Steroid Biochem. Mol. Biol. 53:41-46(1995)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT ARG-250; Characterization of a novel variant (S145C/L311V) of 3alpha-hydroxysteroid/dihydrodiol dehydrogenase in human liver.
Kume T.; Iwasa H.; Shiraishi H.; Yokoi T.; Nagashima K.; Otsuka M.; Terada T.; Takagi T.; Hara A.; Kamataki T.;
Pharmacogenetics 9:763-771(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANTS CYS-145; ARG-250 AND VAL-311; CATALYTIC ACTIVITY; FUNCTION; Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes.
Nishizawa M.; Nakajima T.; Yasuda K.; Kanzaki H.; Sasaguri Y.; Watanabe K.; Ito S.;
Genes Cells 5:111-125(2000)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]; VARIANT ARG-250; Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution.
Dufort I.; Labrie F.; Luu-The V.;
J. Clin. Endocrinol. Metab. 86:841-846(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; CATALYTIC ACTIVITY; TISSUE SPECIFICITY; VARIANT ARG-250; BIOPHYSICOCHEMICAL PROPERTIES; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANTS TYR-170 AND ARG-250; Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase.
Winters C.J.; Molowa D.T.; Guzelian P.S.;
Biochemistry 29:1080-1087(1990)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-323; VARIANT ARG-250; Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder.
Deyashiki Y.; Ogasawara A.; Nakayama T.; Nakanishi M.; Miyabe Y.; Sato K.; Hara A.;
Biochem. J. 299:545-552(1994)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-323; PROTEIN SEQUENCE OF 5-29; 76-131; 184-201 AND 271-294; VARIANT ARG-250;