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UniProtKB/Swiss-Prot P11166 : Variant p.Arg223Gln
Solute carrier family 2, facilitated glucose transporter member 1
Gene: SLC2A1
Variant information
Variant position: 223 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: USThe 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 Arginine (R) to Glutamine (Q) at position 223 (R223Q, p.Arg223Gln).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 large size and basic (R) to medium size and polar (Q)The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: 1The 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 EIG12; unknown pathological significance; no effect on glucose transport; impaired phosphorylation by PKC.Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.
Sequence information
Variant position: 223 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 492 The length of the canonical sequence.
Location on the sequence:
VLPFCPESPRFLLINRNEEN
R AKSVLKKLRGTADVTHDLQE
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 VLPFCPESPRFLLINRNEENR AKSVLKKLRGTADVTHDLQE
Mouse LLPFCPESPRFLLINRNEENR AKSVLKKLRGTADVTRDLQE
Rat LLPFCPESPRFLLINRNEENR AKSVLKKLRGTADVTRDLQE
Pig LLPFCPESPRFLLINRNEENR AKSVLKKLRGTADVTRDLQE
Bovine LLPFCPESPRFLLINRNEENR AKSVLKKLRGTADVTRDLQE
Rabbit VLPLCPESPRFLLINRNEENR AKSVLKKLRGNADVTRDLQE
Sheep LLPFCPESPRFLLINRNEENR AKSVLKKLRGTADVTRDLQE
Chicken ILPFAPESPRFLLINRNEENK AKSVLKKLRGTTDVSSDLQE
Drosophila LLPVCPESPRYLLITKQWEEE ARKALRRLRASGSVEEDIEE
Baker's yeast KYS--PDAKIFVLLHK----- -----------------MDL
Fission yeast ANS--PQARVFCLIHK----- -----------------MDL
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 – 492
Solute carrier family 2, facilitated glucose transporter member 1
Topological domain
207 – 271
Cytoplasmic
Modified residue
226 – 226
Phosphoserine; by PKC/PRKCB
Mutagenesis
204 – 204
L -> C. Abolishes glucose transport.
Mutagenesis
205 – 205
P -> C. Abolishes glucose transport.
Mutagenesis
226 – 226
S -> A. Abolishes phosphorylation by PKA, leading to impaired response to TPA.
Helix
221 – 231
Literature citations
A protein kinase C phosphorylation motif in GLUT1 affects glucose transport and is mutated in GLUT1 deficiency syndrome.
Lee E.E.; Ma J.; Sacharidou A.; Mi W.; Salato V.K.; Nguyen N.; Jiang Y.; Pascual J.M.; North P.E.; Shaul P.W.; Mettlen M.; Wang R.C.;
Mol. Cell 58:845-853(2015)
Cited for: FUNCTION; TRANSPORTER ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; SUBCELLULAR LOCATION; PHOSPHORYLATION AT SER-226; MUTAGENESIS OF SER-226; CHARACTERIZATION OF VARIANTS EIG12 PRO-223 AND GLN-223; CHARACTERIZATION OF VARIANT GLUT1DS1 TRP-223;
Glucose transporter 1 deficiency in the idiopathic generalized epilepsies.
Arsov T.; Mullen S.A.; Rogers S.; Phillips A.M.; Lawrence K.M.; Damiano J.A.; Goldberg-Stern H.; Afawi Z.; Kivity S.; Trager C.; Petrou S.; Berkovic S.F.; Scheffer I.E.;
Ann. Neurol. 72:807-815(2012)
Cited for: VARIANTS EIG12 HIS-51; MET-60; THR-77; ALA-149; SER-218; GLN-223; VAL-243; SER-411 AND TRP-458; CHARACTERIZATION OF VARIANTS EIG12 MET-60; THR-77; SER-218; GLN-223; VAL-243; SER-411 AND TRP-458;
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.