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UniProtKB/Swiss-Prot P11166: Variant p.Glu329Gln

Solute carrier family 2, facilitated glucose transporter member 1
Gene: SLC2A1
Variant information

Variant position:  329
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Glutamate (E) to Glutamine (Q) at position 329 (E329Q, p.Glu329Gln).
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 medium size and acidic (E) to medium size and polar (Q)
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

Involvement in disease:  GLUT1 deficiency syndrome 1 (GLUT1DS1) [MIM:606777]: A neurologic disorder showing wide phenotypic variability. The most severe 'classic' phenotype comprises infantile-onset epileptic encephalopathy associated with delayed development, acquired microcephaly, motor incoordination, and spasticity. Onset of seizures, usually characterized by apneic episodes, staring spells, and episodic eye movements, occurs within the first 4 months of life. Other paroxysmal findings include intermittent ataxia, confusion, lethargy, sleep disturbance, and headache. Varying degrees of cognitive impairment can occur, ranging from learning disabilities to severe mental retardation. {ECO:0000269|PubMed:10227690, ECO:0000269|PubMed:10980529, ECO:0000269|PubMed:11136715, ECO:0000269|PubMed:11603379, ECO:0000269|PubMed:12325075, ECO:0000269|PubMed:15622525, ECO:0000269|PubMed:19901175, ECO:0000269|PubMed:20129935, ECO:0000269|PubMed:20221955, ECO:0000269|PubMed:20574033, ECO:0000269|PubMed:24847886, ECO:0000269|PubMed:25982116, ECO:0000269|PubMed:30197081}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In GLUT1DS1; stabilizes the inward-open conformation.
Any additional useful information about the variant.



Sequence information

Variant position:  329
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:   ATIGSGIVNTAFTVVSLFVV  E RAGRRTLHLIGLAGMAGCAI
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                         ATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAI

Mouse                         ATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAV

Rat                           ATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAV

Pig                           ATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAV

Bovine                        ATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAV

Rabbit                        ATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAACAV

Sheep                         ATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAV

Chicken                       ATIGSGVVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAI

Drosophila                    ATIGIGAIMVVMTLVSIPLMDRTGRRTLHLYGLGGMFIFSI

Baker's yeast                 -------LYKAWSQIVCSLIPNMSNHQSNLKKFK-----EI

Fission yeast                 -------LFKAWSAIVYTLIPNTPTLESHLREFA-----KA

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.

TypePositionsDescription
Chain 1 – 492 Solute carrier family 2, facilitated glucose transporter member 1
Topological domain 329 – 334 Cytoplasmic
Binding site 317 – 317 Monosaccharide
Mutagenesis 340 – 340 G -> C. Strongly decreases glucose transport.


Literature citations

Crystal structure of the human glucose transporter GLUT1.
Deng D.; Xu C.; Sun P.; Wu J.; Yan C.; Hu M.; Yan N.;
Nature 510:121-125(2014)
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF VARIANT GLUT1DS1 GLN-329 IN COMPLEX WITH NONYL-BETA-D-GLUCOSIDE; SUBCELLULAR LOCATION; TOPOLOGY; MUTAGENESIS OF ASN-45;

Glucose transporter-1 deficiency syndrome: the expanding clinical and genetic spectrum of a treatable disorder.
Leen W.G.; Klepper J.; Verbeek M.M.; Leferink M.; Hofste T.; van Engelen B.G.; Wevers R.A.; Arthur T.; Bahi-Buisson N.; Ballhausen D.; Bekhof J.; van Bogaert P.; Carrilho I.; Chabrol B.; Champion M.P.; Coldwell J.; Clayton P.; Donner E.; Evangeliou A.; Ebinger F.; Farrell K.; Forsyth R.J.; de Goede C.G.; Gross S.; Grunewald S.; Holthausen H.; Jayawant S.; Lachlan K.; Laugel V.; Leppig K.; Lim M.J.; Mancini G.; Marina A.D.; Martorell L.; McMenamin J.; Meuwissen M.E.; Mundy H.; Nilsson N.O.; Panzer A.; Poll-The B.T.; Rauscher C.; Rouselle C.M.; Sandvig I.; Scheffner T.; Sheridan E.; Simpson N.; Sykora P.; Tomlinson R.; Trounce J.; Webb D.; Weschke B.; Scheffer H.; Willemsen M.A.;
Brain 133:655-670(2010)
Cited for: VARIANTS GLUT1DS1 TYR-34; VAL-96; SER-130; VAL-155; CYS-212; HIS-212; TRP-223; MET-295; GLN-329; GLN-333; ASP-382; ASP-405 AND LEU-485; VARIANTS GLUT1DS2 TRP-93 AND HIS-153; VARIANT LEU-303;

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.