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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:  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:  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

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.
Helix 328 – 330


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.