UniProtKB/Swiss-Prot Q16851: Variant p.Met12Val

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 12 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: LP/P [Disclaimer: Variants classification is intended for research purposes only, not for clinical and diagnostic use. The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant.] 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 Methionine (M) to Valine (V) at position 12 (M12V, p.Met12Val). 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 hydrophobic. 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
Variant description: In DEE83; the nucleotide substitution also alters the translation of other alternatively spliced products of the gene globally reducing functional enzyme levels and causing reduced synthesis of UDP-glucose and decreased glycogen biosynthetic process; no effect on protein localization; no effect on UTP:glucose-1-phosphate uridylyltransferase activity. Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.

• Variant rs768305634 [ dbSNP | Ensembl ]

Sequence information

Variant position: 12 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 508 The length of the canonical sequence.
Location on the sequence: MSRFVQDLSKA M SQDGASQFQEVIRQELELSV 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 – 508	UTP--glucose-1-phosphate uridylyltransferase
Modified residue	13 – 13	Phosphoserine

Literature citations

Loss of UGP2 in brain leads to a severe epileptic encephalopathy, emphasizing that bi-allelic isoform-specific start-loss mutations of essential genes can cause genetic diseases.
Perenthaler E.; Nikoncuk A.; Yousefi S.; Berdowski W.M.; Alsagob M.; Capo I.; van der Linde H.C.; van den Berg P.; Jacobs E.H.; Putar D.; Ghazvini M.; Aronica E.; van Ijcken W.F.J.; de Valk W.G.; Medici-van den Herik E.; van Slegtenhorst M.; Brick L.; Kozenko M.; Kohler J.N.; Bernstein J.A.; Monaghan K.G.; Begtrup A.; Torene R.; Al Futaisi A.; Al Murshedi F.; Mani R.; Al Azri F.; Kamsteeg E.J.; Mojarrad M.; Eslahi A.; Khazaei Z.; Darmiyan F.M.; Doosti M.; Karimiani E.G.; Vandrovcova J.; Zafar F.; Rana N.; Kandaswamy K.K.; Hertecant J.; Bauer P.; Almuhaizea M.A.; Salih M.A.; Aldosary M.; Almass R.; Al-Quait L.; Qubbaj W.; Coskun S.; Alahmadi K.O.; Hamad M.H.A.; Alwadaee S.; Awartani K.; Dababo A.M.; Almohanna F.; Colak D.; Dehghani M.; Mehrjardi M.Y.V.; Gunel M.; Ercan-Sencicek A.G.; Passi G.R.; Cheema H.A.; Efthymiou S.; Houlden H.; Bertoli-Avella A.M.; Brooks A.S.; Retterer K.; Maroofian R.; Kaya N.; van Ham T.J.; Barakat T.S.;
Acta Neuropathol. 139:415-442(2020)
Cited for: INVOLVEMENT IN DEE83; VARIANT DEE83 VAL-12; CHARACTERIZATION OF VARIANT DEE83 VAL-12; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; DEVELOPMENTAL STAGE (ISOFORM 2);