UniProtKB/Swiss-Prot Q06136: Variant p.Gly182Ser

3-ketodihydrosphingosine reductase
Gene: KDSR
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Variant information Variant position:

182 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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 Glycine (G) to Serine (S) at position 182 (G182S, p.Gly182Ser). 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 glycine (G) to small size and polar (S) 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:

Found in patients with a spectrum of keratinization disorders; uncertain significance; no effect on 3-dehydrosphinganine reductase activity. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs751571336 [ dbSNP | Ensembl ]

Sequence information Variant position:

182 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

332 The length of the canonical sequence.
Location on the sequence:

ERRVGRIVFVSSQAGQLGLF G FTAYSASKFAIRGLAEALQM 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                         ER--RVGRIVFVSSQAGQLGLFGFTAYSASKFAIRGLAEALQM

Mouse                         ER--RVGRIVFVSSQAGQLGLFGFTAYSSSKFAIRGLAEAL

Bovine                        ER--RMGRVVFVSSQAGQLGLFGYTAYSSSKFALRGLAEAL

Zebrafish                     ER--RMGRIMFVSSQAGQIGLFGYTAYSPSKFALRGLAEAL

Slime mold                    ENGGQGGHIVFVSSTCGLVGVPGYSTYCPSKFALRGLAETL

Baker's yeast                 QT--KEHHLIIFSSATALYPFVGYSQYAPAKAAIKSLVAIL

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	26 – 332	3-ketodihydrosphingosine reductase
Topological domain	26 – 270	Cytoplasmic
Active site	172 – 172	Proton donor
Active site	186 – 186	Proton acceptor
Active site	190 – 190	Lowers pKa of active site Tyr
Binding site	186 – 186
Binding site	190 – 190
Alternative sequence	139 – 202	Missing. In isoform 2.
Mutagenesis	173 – 173	S -> A. Impairs activity.
Mutagenesis	175 – 175	A -> TV. Impairs activity.
Mutagenesis	186 – 186	Y -> Q. Impairs activity.
Mutagenesis	190 – 190	K -> RI. Impairs activity.

Literature citations
Biallelic Mutations in KDSR Disrupt Ceramide Synthesis and Result in a Spectrum of Keratinization Disorders Associated with Thrombocytopenia.
Takeichi T.; Torrelo A.; Lee J.Y.W.; Ohno Y.; Lozano M.L.; Kihara A.; Liu L.; Yasuda Y.; Ishikawa J.; Murase T.; Rodrigo A.B.; Fernandez-Crehuet P.; Toi Y.; Mellerio J.; Rivera J.; Vicente V.; Kelsell D.P.; Nishimura Y.; Okuno Y.; Kojima D.; Ogawa Y.; Sugiura K.; Simpson M.A.; McLean W.H.I.; Akiyama M.; McGrath J.A.;
J. Invest. Dermatol. 137:2344-2353(2017)
Cited for: CHARACTERIZATION OF VARIANTS CYS-138; SER-182 AND GLU-271; FUNCTION; CATALYTIC ACTIVITY; INVOLVEMENT IN A SPECTRUM OF KERATINIZATION DISORDERS;

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.