UniProtKB/Swiss-Prot P42330: Variant p.His5Gln

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 5 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 Histidine (H) to Glutamine (Q) at position 5 (H5Q, p.His5Gln). 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: Similar physico-chemical property. Both residues are medium size and polar. 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
Other resources: Links to websites of interest for the variant.

• Variant rs12529 [ dbSNP | Ensembl ]

Sequence information

Variant position: 5 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: MDSK H QCVKLNDGHFMPVLGFGTYA 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 C3
Alternative sequence	1 – 119	Missing. In isoform 2.
Helix	3 – 5

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] (ISOFORM 1); VARIANTS GLN-5 AND ILE-175; 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]; CATALYTIC ACTIVITY; FUNCTION; TISSUE SPECIFICITY; VARIANTS GLN-5 AND ILE-175; 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] (ISOFORM 1); VARIANT GLN-5; Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution.
Lin H.-K.; Jez J.M.; Schlegel B.P.; Peehl D.M.; Pachter J.A.; Penning T.M.;
Mol. Endocrinol. 11:1971-1984(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); FUNCTION; CATALYTIC ACTIVITY; SUBSTRATE SPECIFICITY; BIOPHYSICOCHEMICAL PROPERTIES; TISSUE SPECIFICITY; VARIANT GLN-5; cDNA cloning, expression and characterization of human prostaglandin F synthase.
Suzuki-Yamamoto T.; Nishizawa M.; Fukui M.; Okuda-Ashitaka E.; Nakajima T.; Ito S.; Watanabe K.;
FEBS Lett. 462:335-340(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 124-190; FUNCTION; CATALYTIC ACTIVITY; TISSUE SPECIFICITY; VARIANT GLN-5; SUBCELLULAR LOCATION; Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes.
Griffin L.D.; Mellon S.H.;
Proc. Natl. Acad. Sci. U.S.A. 96:13512-13517(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); BIOPHYSICOCHEMICAL PROPERTIES; TISSUE SPECIFICITY; VARIANT GLN-5; CATALYTIC ACTIVITY; FUNCTION; Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1.
Nagase T.; Miyajima N.; Tanaka A.; Sazuka T.; Seki N.; Sato S.; Tabata S.; Ishikawa K.; Kawarabayasi Y.; Kotani H.; Nomura N.;
DNA Res. 2:37-43(1995)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1); VARIANT GLN-5;