UniProtKB/Swiss-Prot O60701: Variant p.Gly271Arg

UDP-glucose 6-dehydrogenase
Gene: UGDH
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Variant information Variant position:

271 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 Arginine (R) at position 271 (G271R, p.Gly271Arg). 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 large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-2 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 DEE84; uncertain significance. Any additional useful information about the variant.

Sequence information Variant position:

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

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

VATAIGMDQRIGNKFLKASV G FGGSCFQKDVLNLVYLCEAL 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                         VATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEAL

Mouse                         VATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEAL

Rat                           VATAIGMDQRIGNKFLKASVGFGGGCFQKDVLNLVYLCEAL

Bovine                        VATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEAL

Chicken                       VARAIGTDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEAL

Caenorhabditis elegans        VAHAVGYDTRIGSKFLQASVGFGGSCFQKDVLSLVYLCESL

Drosophila                    VARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENL

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 – 494	UDP-glucose 6-dehydrogenase
Active site	276 – 276	Nucleophile
Binding site	260 – 260
Binding site	267 – 273
Mutagenesis	276 – 276	C -> AS. Loss of enzyme activity.
Mutagenesis	280 – 280	D -> A. Loss of enzyme activity.

Literature citations
Loss-of-function mutations in UDP-Glucose 6-Dehydrogenase cause recessive developmental epileptic encephalopathy.
Hengel H.; Bosso-Lefevre C.; Grady G.; Szenker-Ravi E.; Li H.; Pierce S.; Lebigot E.; Tan T.T.; Eio M.Y.; Narayanan G.; Utami K.H.; Yau M.; Handal N.; Deigendesch W.; Keimer R.; Marzouqa H.M.; Gunay-Aygun M.; Muriello M.J.; Verhelst H.; Weckhuysen S.; Mahida S.; Naidu S.; Thomas T.G.; Lim J.Y.; Tan E.S.; Haye D.; Willemsen M.A.A.P.; Oegema R.; Mitchell W.G.; Pierson T.M.; Andrews M.V.; Willing M.C.; Rodan L.H.; Barakat T.S.; van Slegtenhorst M.; Gavrilova R.H.; Martinelli D.; Gilboa T.; Tamim A.M.; Hashem M.O.; Al-Sayed M.D.; Abdulrahim M.M.; Al-Owain M.; Awaji A.; Mahmoud A.A.H.; Faqeih E.A.; Asmari A.A.; Algain S.M.; Jad L.A.; Aldhalaan H.M.; Helbig I.; Koolen D.A.; Riess A.; Kraegeloh-Mann I.; Bauer P.; Gulsuner S.; Stamberger H.; Ng A.Y.J.; Tang S.; Tohari S.; Keren B.; Schultz-Rogers L.E.; Klee E.W.; Barresi S.; Tartaglia M.; Mor-Shaked H.; Maddirevula S.; Begtrup A.; Telegrafi A.; Pfundt R.; Schuele R.; Ciruna B.; Bonnard C.; Pouladi M.A.; Stewart J.C.; Claridge-Chang A.; Lefeber D.J.; Alkuraya F.S.; Mathuru A.S.; Venkatesh B.; Barycki J.J.; Simpson M.A.; Jamuar S.S.; Schoels L.; Reversade B.;
Nat. Commun. 11:595-595(2020)
Cited for: VARIANTS DEE84 CYS-14; THR-24; THR-42; VAL-44; 65-ARG--VAL-494 DEL; ALA-72; THR-82; THR-116; 155-GLN--VAL-494 DEL; ALA-175; ASP-217; THR-255; ARG-271; ILE-303; VAL-306; GLN-317; 356-TYR--VAL-494 DEL; CYS-367; TRP-393; SER-410; TRP-442; HIS-443 AND ARG-449; CHARACTERIZATION OF VARIANTS DEE84 VAL-44 AND THR-82; INVOLVEMENT IN DEE84; FUNCTION; CATALYTIC ACTIVITY; SUBUNIT;

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.