UniProtKB/SwissProt variant VAR

Variant information

Variant position:

223

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 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:

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 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.

Variant rs397514564 [ dbSNP | Ensembl ]

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                         VLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHDLQE

Mouse                         LLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTRDLQE

Rat                           LLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTRDLQE

Pig                           LLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTRDLQE

Bovine                        LLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTRDLQE

Rabbit                        VLPLCPESPRFLLINRNEENRAKSVLKKLRGNADVTRDLQE

Sheep                         LLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTRDLQE

Chicken                       ILPFAPESPRFLLINRNEENKAKSVLKKLRGTTDVSSDLQE

Drosophila                    LLPVCPESPRYLLITKQWEEEARKALRRLRASGSVEEDIEE

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;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P11166: Variant p.Arg223Gln