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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60701: Variant p.Ala82Thr

UDP-glucose 6-dehydrogenase
Gene: UGDH
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Variant information Variant position: help 82 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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: help From Alanine (A) to Threonine (T) at position 82 (A82T, p.Ala82Thr). 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: help Change from small size and hydrophobic (A) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In DEE84; decreased function in glycosaminoglycan biosynthetic process in patient cells; severely decreased protein stability; decreased hexamer formation; severe decrease of UDP-glucose 6-dehydrogenase activity. Any additional useful information about the variant.


Sequence information Variant position: help 82 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 494 The length of the canonical sequence.
Location on the sequence: help ESCRGKNLFFSTNIDDAIKE A DLVFISVNTPTKTYGMGKGR 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         ESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGR

Mouse                         ESCRGKNLFFSTNIDDAIREADLVFISVNTPTKTYGMGKGR

Rat                           ESCRGKNLFFSTNIDDAIREADLVFISVNTPTKTYGMGKGR

Bovine                        ESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGR

Chicken                       ESCRGRNLFFSTSIDDAIREADLVFISVNTPTKTYGMGKGR

Caenorhabditis elegans        FAARGRNLFFSSDIPKAIAEADLIFISVNTPTKMYGRGKGM

Drosophila                    KKCRNVNLFFSTDIETAIKEADLIFISVNTPTKTCGNGKGR

Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 1 – 494 UDP-glucose 6-dehydrogenase
Alternative sequence 1 – 97 Missing. In isoform 3.
Mutagenesis 94 – 94 K -> E. Loss of hexamer formation. Causes formation of stable dimers. Strongly reduced affinity for NAD and UDP-glucose, and strongly decreased catalytic efficiency at pH 8.6.



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.