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Entry version 231 (16 Oct 2019)
Sequence version 2 (03 Oct 2006)
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Protein

Solute carrier family 2, facilitated glucose transporter member 1

Gene

SLC2A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Facilitative glucose transporter, which is responsible for constitutive or basal glucose uptake (PubMed:18245775, PubMed:19449892, PubMed:25982116, PubMed:27078104, PubMed:10227690). Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses (PubMed:18245775, PubMed:19449892). Most important energy carrier of the brain: present at the blood-brain barrier and assures the energy-independent, facilitative transport of glucose into the brain (PubMed:10227690).5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The uptake of glucose is inhibited by cytochalasin B and Phe-amide core-scaffold inhibitors GLUT-i1 and GLUT-i2 (PubMed:27078104). These inhibitors bind in the central cavity of the inward-open state and overlap the glucose-binding site (PubMed:27078104). Glucose uptake is increased in response to phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) treatment: TPA-induced glucose uptake requires phosphorylation at Ser-226 (PubMed:25982116).2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=25.6 mM for glucose1 Publication
  2. KM=50.1 mM for glucose (in presence of TPA)1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Carbohydrate degradation

    This protein is involved in Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei137Cytochalasin b inhibitorCombined sources1 Publication1
    Binding sitei282Cytochalasin b inhibitorCombined sources1 Publication1
    Binding sitei317Monosaccharide1 Publication1
    Binding sitei388Cytochalasin b inhibitorCombined sources1 Publication1
    Binding sitei388Monosaccharide1 Publication1
    Binding sitei411Cytochalasin b inhibitorCombined sources1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Biological processSugar transport, Transport

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-189200 Cellular hexose transport
    R-HSA-196836 Vitamin C (ascorbate) metabolism
    R-HSA-422356 Regulation of insulin secretion
    R-HSA-5619043 Defective SLC2A1 causes GLUT1 deficiency syndrome 1 (GLUT1DS1)
    R-HSA-5653890 Lactose synthesis

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P11166

    Protein family/group databases

    Transport Classification Database

    More...
    TCDBi
    2.A.1.1.28 the major facilitator superfamily (mfs)

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Solute carrier family 2, facilitated glucose transporter member 1Curated
    Alternative name(s):
    Glucose transporter type 1, erythrocyte/brain1 Publication
    Short name:
    GLUT-11 Publication
    HepG2 glucose transporter2 Publications
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:SLC2A1Imported
    Synonyms:GLUT11 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:11005 SLC2A1

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    138140 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P11166

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 11Cytoplasmic1 PublicationAdd BLAST11
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei12 – 33Helical; Name=1Add BLAST22
    Topological domaini34 – 66Extracellular1 PublicationAdd BLAST33
    Transmembranei67 – 87Helical; Name=2Add BLAST21
    Topological domaini88 – 90Cytoplasmic1 Publication3
    Transmembranei91 – 112Helical; Name=3Add BLAST22
    Topological domaini113 – 120Extracellular1 Publication8
    Transmembranei121 – 144Helical; Name=4Add BLAST24
    Topological domaini145 – 155Cytoplasmic1 PublicationAdd BLAST11
    Transmembranei156 – 176Helical; Name=5Add BLAST21
    Topological domaini177 – 185Extracellular1 Publication9
    Transmembranei186 – 206Helical; Name=6Add BLAST21
    Topological domaini207 – 271Cytoplasmic1 PublicationAdd BLAST65
    Transmembranei272 – 293Helical; Name=7Add BLAST22
    Topological domaini294 – 306Extracellular1 PublicationAdd BLAST13
    Transmembranei307 – 328Helical; Name=8Add BLAST22
    Topological domaini329 – 334Cytoplasmic1 Publication6
    Transmembranei335 – 355Helical; Name=9Add BLAST21
    Topological domaini356 – 365Extracellular1 Publication10
    Transmembranei366 – 388Helical; Name=10Add BLAST23
    Topological domaini389 – 401Cytoplasmic1 PublicationAdd BLAST13
    Transmembranei402 – 422Helical; Name=11Add BLAST21
    Topological domaini423 – 429Extracellular1 Publication7
    Transmembranei430 – 450Helical; Name=12Add BLAST21
    Topological domaini451 – 492Cytoplasmic1 PublicationAdd BLAST42

    Keywords - Cellular componenti

    Cell membrane, Membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    GLUT1 deficiency syndrome 1 (GLUT1DS1)13 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA 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.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05475634N → S in GLUT1DS1; 55% of wild-type glucose uptake activity. 1 Publication1
    Natural variantiVAR_06520634N → Y in GLUT1DS1. 1 Publication1
    Natural variantiVAR_01328366S → F in GLUT1DS1. 1 PublicationCorresponds to variant dbSNP:rs80359813Ensembl.1
    Natural variantiVAR_01318291G → D in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose. 2 PublicationsCorresponds to variant dbSNP:rs80359814EnsemblClinVar.1
    Natural variantiVAR_06520996M → V in GLUT1DS1. 1 PublicationCorresponds to variant dbSNP:rs753161833EnsemblClinVar.1
    Natural variantiVAR_054757126R → C in GLUT1DS1, GLUT1DS2 and DYT9; reduced transporter activity. 3 PublicationsCorresponds to variant dbSNP:rs80359818EnsemblClinVar.1
    Natural variantiVAR_013183126R → H in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose and dehydroascorbic acid; 57% of wild-type glucose uptake activity. 4 PublicationsCorresponds to variant dbSNP:rs80359816EnsemblClinVar.1
    Natural variantiVAR_013184126R → L in GLUT1DS1; compound heterozygote with V-256. 1 PublicationCorresponds to variant dbSNP:rs80359816EnsemblClinVar.1
    Natural variantiVAR_054758130G → S in GLUT1DS1; 75% of wild-type glucose uptake activity. 2 PublicationsCorresponds to variant dbSNP:rs80359819EnsemblClinVar.1
    Natural variantiVAR_013284146E → K in GLUT1DS1. 2 PublicationsCorresponds to variant dbSNP:rs80359820Ensembl.1
    Natural variantiVAR_054759153R → C in GLUT1DS1; 44% of wild-type glucose uptake activity. 2 Publications1
    Natural variantiVAR_065211155A → V in GLUT1DS1. 1 Publication1
    Natural variantiVAR_054760169Missing in GLUT1DS1; 48% of wild-type glucose uptake activity. 1 Publication1
    Natural variantiVAR_065213212R → C in GLUT1DS1 and DYT9. 2 PublicationsCorresponds to variant dbSNP:rs387907312EnsemblClinVar.1
    Natural variantiVAR_065214212R → H in GLUT1DS1. 1 PublicationCorresponds to variant dbSNP:rs886039517EnsemblClinVar.1
    Natural variantiVAR_065216223R → W in GLUT1DS1; impaired phosphorylation by PKC. 2 PublicationsCorresponds to variant dbSNP:rs796053248EnsemblClinVar.1
    Natural variantiVAR_013185256K → E in GLUT1DS1; compound heterozygote with L-126. 1 PublicationCorresponds to variant dbSNP:rs121909738Ensembl.1
    Natural variantiVAR_069079292Y → YY in GLUT1DS1. 1 Publication1
    Natural variantiVAR_054763295T → M in GLUT1DS1; 75% of wild-type glucose uptake activity. 2 PublicationsCorresponds to variant dbSNP:rs80359823EnsemblClinVar.1
    Natural variantiVAR_013285310T → I in GLUT1DS1. 1 PublicationCorresponds to variant dbSNP:rs80359824Ensembl.1
    Natural variantiVAR_065220329E → Q in GLUT1DS1; stabilizes the inward-open conformation. 1 Publication1
    Natural variantiVAR_065221333R → Q in GLUT1DS1 and GLUT1DS2. 2 PublicationsCorresponds to variant dbSNP:rs1553155986EnsemblClinVar.1
    Natural variantiVAR_013286333R → W in GLUT1DS1; 43% of wild-type glucose uptake activity. 3 PublicationsCorresponds to variant dbSNP:rs80359825EnsemblClinVar.1
    Natural variantiVAR_065222382G → D in GLUT1DS1. 1 Publication1
    Natural variantiVAR_065223405A → D in GLUT1DS1. 1 Publication1
    Natural variantiVAR_069080468R → W in GLUT1DS1. 1 PublicationCorresponds to variant dbSNP:rs267607059EnsemblClinVar.1
    Natural variantiVAR_065224485P → L in GLUT1DS1; creates a dileucine internalization motif that promotes recruitment of clathrin and mislocalization of the protein to endocytic compartments. 2 Publications1
    GLUT1 deficiency syndrome 2 (GLUT1DS2)9 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA clinically variable disorder characterized primarily by onset in childhood of paroxysmal exercise-induced dyskinesia. The dyskinesia involves transient abnormal involuntary movements, such as dystonia and choreoathetosis, induced by exercise or exertion, and affecting the exercised limbs. Some patients may also have epilepsy, most commonly childhood absence epilepsy. Mild mental retardation may also occur. In some patients involuntary exertion-induced dystonic, choreoathetotic, and ballistic movements may be associated with macrocytic hemolytic anemia.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_05475534N → I in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs80359812EnsemblClinVar.1
    Natural variantiVAR_06907792R → W in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs202060209EnsemblClinVar.1
    Natural variantiVAR_06520793R → W in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs267607061EnsemblClinVar.1
    Natural variantiVAR_06520895S → I in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs267607060EnsemblClinVar.1
    Natural variantiVAR_065210153R → H in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs794727642EnsemblClinVar.1
    Natural variantiVAR_065212165V → I in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs1057520545EnsemblClinVar.1
    Natural variantiVAR_054761275A → T in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability. 1 PublicationCorresponds to variant dbSNP:rs121909740EnsemblClinVar.1
    Natural variantiVAR_054762282 – 285Missing in GLUT1DS2; accompanied by hemolytic anemia and altered erythrocyte ion concentrations; the mutation decreases glucose transport and causes a cation leak that alteres intracellular concentrations of sodium potassium and calcium. 1 Publication4
    Natural variantiVAR_065784294S → P in GLUT1DS2. 1 Publication1
    Natural variantiVAR_054764314G → S in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability. 2 PublicationsCorresponds to variant dbSNP:rs121909739EnsemblClinVar.1
    Natural variantiVAR_065218317N → T in GLUT1DS2. 1 Publication1
    Natural variantiVAR_065219324S → L in GLUT1DS2; mild phenotype; reduced transporter activity. 2 PublicationsCorresponds to variant dbSNP:rs796053253EnsemblClinVar.1
    Natural variantiVAR_065221333R → Q in GLUT1DS1 and GLUT1DS2. 2 PublicationsCorresponds to variant dbSNP:rs1553155986EnsemblClinVar.1
    Epilepsy, idiopathic generalized 12 (EIG12)4 Publications
    Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Disease descriptionA disorder characterized by recurring generalized seizures in the absence of detectable brain lesions and/or metabolic abnormalities. Generalized seizures arise diffusely and simultaneously from both hemispheres of the brain. Seizure types include juvenile myoclonic seizures, absence seizures, and generalized tonic-clonic seizures. In some EIG12 patients seizures may remit with age.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07622651R → H in EIG12; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs201815571Ensembl.1
    Natural variantiVAR_07622760T → M in EIG12; unknown pathological significance; decreased glucose transport. 1 PublicationCorresponds to variant dbSNP:rs142986731EnsemblClinVar.1
    Natural variantiVAR_07622877M → T in EIG12; decreased glucose transport. 1 PublicationCorresponds to variant dbSNP:rs1187210267Ensembl.1
    Natural variantiVAR_076229149P → A in EIG12; unknown pathological significance. 1 Publication1
    Natural variantiVAR_076230218R → S in EIG12; decreased glucose transport. 1 Publication1
    Natural variantiVAR_065215223R → P in EIG12; mild phenotype; reduced transporter activity; impaired phosphorylation by PKC. 3 PublicationsCorresponds to variant dbSNP:rs397514564EnsemblClinVar.1
    Natural variantiVAR_076231223R → Q in EIG12; unknown pathological significance; no effect on glucose transport; impaired phosphorylation by PKC. 2 PublicationsCorresponds to variant dbSNP:rs397514564EnsemblClinVar.1
    Natural variantiVAR_069078232R → C in EIG12; the mutant protein is expressed at the cell surface but has mildly decreased glucose uptake (70%) compared to wild-type. 1 PublicationCorresponds to variant dbSNP:rs387907313EnsemblClinVar.1
    Natural variantiVAR_076232243E → V in EIG12; decreased glucose transport. 1 Publication1
    Natural variantiVAR_076234411N → S in EIG12; decreased glucose transport. 1 PublicationCorresponds to variant dbSNP:rs398123069EnsemblClinVar.1
    Natural variantiVAR_076236458R → W in EIG12; decreased glucose transport. 1 PublicationCorresponds to variant dbSNP:rs13306758EnsemblClinVar.1
    Dystonia 9 (DYT9)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal dominant neurologic disorder characterized by childhood onset of paroxysmal choreoathetosis and progressive spastic paraplegia. Most patients show some degree of cognitive impairment. Other variable features may include seizures, migraine headaches, and ataxia.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_054757126R → C in GLUT1DS1, GLUT1DS2 and DYT9; reduced transporter activity. 3 PublicationsCorresponds to variant dbSNP:rs80359818EnsemblClinVar.1
    Natural variantiVAR_065213212R → C in GLUT1DS1 and DYT9. 2 PublicationsCorresponds to variant dbSNP:rs387907312EnsemblClinVar.1
    Stomatin-deficient cryohydrocytosis with neurologic defects (SDCHCN)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA rare form of stomatocytosis characterized by episodic hemolytic anemia, cold-induced red cells cation leak, erratic hyperkalemia, neonatal hyperbilirubinemia, hepatosplenomegaly, cataracts, seizures, mental retardation, and movement disorder.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_076233286G → D in SDCHCN; no effect on protein abundance; no effect on localization to the plasma membrane; loss of D-glucose transporter activity; increased cation leakage. 2 PublicationsCorresponds to variant dbSNP:rs864309514EnsemblClinVar.1
    Natural variantiVAR_076235435Missing in SDCHCN; no effect on protein abundance; no effect on localization to the plasma membrane; loss of D-glucose transporter activity; increased cation leakage. 2 Publications1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi45N → T: Loss of glycosylation site. 1 Publication1
    Mutagenesisi192I → C: Strongly decreases glucose transport. 1 Publication1
    Mutagenesisi204L → C: Abolishes glucose transport. 1 Publication1
    Mutagenesisi205P → C: Abolishes glucose transport. 1 Publication1
    Mutagenesisi226S → A: Abolishes phosphorylation by PKA, leading to impaired response to TPA. 1 Publication1
    Mutagenesisi340G → C: Strongly decreases glucose transport. 1 Publication1

    Keywords - Diseasei

    Cataract, Disease mutation, Dystonia, Epilepsy, Hereditary hemolytic anemia, Mental retardation

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    6513

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...
    GeneReviewsi
    SLC2A1

    MalaCards human disease database

    More...
    MalaCardsi
    SLC2A1
    MIMi601042 phenotype
    606777 phenotype
    608885 phenotype
    612126 phenotype
    614847 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000117394

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    64280 Childhood absence epilepsy
    71277 Classic glucose transporter type 1 deficiency syndrome
    168577 Hereditary cryohydrocytosis with reduced stomatin
    53583 Paroxysmal dystonic choreathetosis with episodic ataxia and spasticity
    98811 Paroxysmal exertion-induced dyskinesia

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA35875

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    P11166

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2535

    Drug and drug target database

    More...
    DrugBanki
    DB08831 2-deoxyglucose
    DB11059 Carboxymethylcellulose
    DB01914 D-glucose
    DB08830 Dehydroascorbic acid
    DB09341 Dextrose, unspecified form
    DB00292 Etomidate
    DB09502 Fludeoxyglucose F-18
    DB02709 Resveratrol

    DrugCentral

    More...
    DrugCentrali
    P11166

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    875

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    SLC2A1

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    115502394

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000503381 – 492Solute carrier family 2, facilitated glucose transporter member 1Add BLAST492

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi45N-linked (GlcNAc...) asparagine2 Publications1
    Modified residuei226Phosphoserine; by PKC/PRKCB1 Publication1
    Modified residuei465PhosphoserineCombined sources1
    Modified residuei478PhosphothreonineCombined sources1
    Modified residuei490PhosphoserineCombined sources1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Phosphorylation at Ser-226 by PKC promotes glucose uptake by increasing cell membrane localization.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei411Not glycosylated1 Publication1

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    The CPTAC Assay portal

    More...
    CPTACi
    CPTAC-274
    CPTAC-275

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P11166

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P11166

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P11166

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P11166

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P11166

    PeptideAtlas

    More...
    PeptideAtlasi
    P11166

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P11166

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    52703

    PTM databases

    GlyConnect protein glycosylation platform

    More...
    GlyConnecti
    573

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P11166

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P11166

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P11166

    UniCarbKB; an annotated and curated database of glycan structures

    More...
    UniCarbKBi
    P11166

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Detected in erythrocytes (at protein level). Expressed at variable levels in many human tissues.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000117394 Expressed in 193 organ(s), highest expression level in pigmented layer of retina

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P11166 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P11166 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB002759
    HPA031345
    HPA058494

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with GIPC (via PDZ domain) (By similarity).

    Found in a complex with ADD2, DMTN and SLC2A1.

    Interacts (via C-terminus cytoplasmic region) with DMTN isoform 2 (PubMed:18347014).

    Interacts with SNX27; the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane (PubMed:23563491).

    Interacts with STOM (PubMed:23219802).

    Interacts with SGTA (via Gln-rich region) (By similarity).

    By similarity3 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    112404, 42 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-3111 Glucose transporter complex 1

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    P11166

    Database of interacting proteins

    More...
    DIPi
    DIP-23N

    Protein interaction database and analysis system

    More...
    IntActi
    P11166, 49 interactors

    Molecular INTeraction database

    More...
    MINTi
    P11166

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000416293

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P11166

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1492
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P11166

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni282 – 288Monosaccharide binding1 Publication7
    Regioni468 – 492Disordered regionSequence analysis1 PublicationAdd BLAST25

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0569 Eukaryota
    COG0477 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000156792

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P11166

    KEGG Orthology (KO)

    More...
    KOi
    K07299

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    RFIIGLY

    Database of Orthologous Groups

    More...
    OrthoDBi
    1016546at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P11166

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF313762

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002439 Glu_transpt_1
    IPR020846 MFS_dom
    IPR005828 MFS_sugar_transport-like
    IPR036259 MFS_trans_sf
    IPR003663 Sugar/inositol_transpt
    IPR005829 Sugar_transporter_CS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00083 Sugar_tr, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01190 GLUCTRSPORT1
    PR00171 SUGRTRNSPORT

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF103473 SSF103473, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00879 SP, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50850 MFS, 1 hit
    PS00216 SUGAR_TRANSPORT_1, 1 hit
    PS00217 SUGAR_TRANSPORT_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

    P11166-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEPSSKKLTG RLMLAVGGAV LGSLQFGYNT GVINAPQKVI EEFYNQTWVH
    60 70 80 90 100
    RYGESILPTT LTTLWSLSVA IFSVGGMIGS FSVGLFVNRF GRRNSMLMMN
    110 120 130 140 150
    LLAFVSAVLM GFSKLGKSFE MLILGRFIIG VYCGLTTGFV PMYVGEVSPT
    160 170 180 190 200
    ALRGALGTLH QLGIVVGILI AQVFGLDSIM GNKDLWPLLL SIIFIPALLQ
    210 220 230 240 250
    CIVLPFCPES PRFLLINRNE ENRAKSVLKK LRGTADVTHD LQEMKEESRQ
    260 270 280 290 300
    MMREKKVTIL ELFRSPAYRQ PILIAVVLQL SQQLSGINAV FYYSTSIFEK
    310 320 330 340 350
    AGVQQPVYAT IGSGIVNTAF TVVSLFVVER AGRRTLHLIG LAGMAGCAIL
    360 370 380 390 400
    MTIALALLEQ LPWMSYLSIV AIFGFVAFFE VGPGPIPWFI VAELFSQGPR
    410 420 430 440 450
    PAAIAVAGFS NWTSNFIVGM CFQYVEQLCG PYVFIIFTVL LVLFFIFTYF
    460 470 480 490
    KVPETKGRTF DEIASGFRQG GASQSDKTPE ELFHPLGADS QV
    Length:492
    Mass (Da):54,084
    Last modified:October 3, 2006 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE71E1C6BD1B00B1E
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    A0A0D9SFK9A0A0D9SFK9_HUMAN
    Solute carrier family 2, facilitate...
    SLC2A1
    173Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    A6NL68A6NL68_HUMAN
    Solute carrier family 2, facilitate...
    SLC2A1
    116Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    A0A0D9SG74A0A0D9SG74_HUMAN
    Solute carrier family 2, facilitate...
    SLC2A1
    142Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    A0A1W2PQ59A0A1W2PQ59_HUMAN
    Solute carrier family 2, facilitate...
    SLC2A1
    43Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti25 – 26Missing in BAF85480 (PubMed:14702039).Curated2
    Sequence conflicti95S → L in BAF85480 (PubMed:14702039).Curated1
    Sequence conflicti152L → F in AAA52571 (PubMed:3839598).Curated1
    Sequence conflicti363W → R in AAI21805 (PubMed:15489334).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_05475534N → I in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs80359812EnsemblClinVar.1
    Natural variantiVAR_05475634N → S in GLUT1DS1; 55% of wild-type glucose uptake activity. 1 Publication1
    Natural variantiVAR_06520634N → Y in GLUT1DS1. 1 Publication1
    Natural variantiVAR_07622651R → H in EIG12; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs201815571Ensembl.1
    Natural variantiVAR_07622760T → M in EIG12; unknown pathological significance; decreased glucose transport. 1 PublicationCorresponds to variant dbSNP:rs142986731EnsemblClinVar.1
    Natural variantiVAR_01328366S → F in GLUT1DS1. 1 PublicationCorresponds to variant dbSNP:rs80359813Ensembl.1
    Natural variantiVAR_07622877M → T in EIG12; decreased glucose transport. 1 PublicationCorresponds to variant dbSNP:rs1187210267Ensembl.1
    Natural variantiVAR_01318291G → D in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose. 2 PublicationsCorresponds to variant dbSNP:rs80359814EnsemblClinVar.1
    Natural variantiVAR_06907792R → W in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs202060209EnsemblClinVar.1
    Natural variantiVAR_06520793R → W in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs267607061EnsemblClinVar.1
    Natural variantiVAR_06520895S → I in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs267607060EnsemblClinVar.1
    Natural variantiVAR_06520996M → V in GLUT1DS1. 1 PublicationCorresponds to variant dbSNP:rs753161833EnsemblClinVar.1
    Natural variantiVAR_054757126R → C in GLUT1DS1, GLUT1DS2 and DYT9; reduced transporter activity. 3 PublicationsCorresponds to variant dbSNP:rs80359818EnsemblClinVar.1
    Natural variantiVAR_013183126R → H in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose and dehydroascorbic acid; 57% of wild-type glucose uptake activity. 4 PublicationsCorresponds to variant dbSNP:rs80359816EnsemblClinVar.1
    Natural variantiVAR_013184126R → L in GLUT1DS1; compound heterozygote with V-256. 1 PublicationCorresponds to variant dbSNP:rs80359816EnsemblClinVar.1
    Natural variantiVAR_054758130G → S in GLUT1DS1; 75% of wild-type glucose uptake activity. 2 PublicationsCorresponds to variant dbSNP:rs80359819EnsemblClinVar.1
    Natural variantiVAR_013284146E → K in GLUT1DS1. 2 PublicationsCorresponds to variant dbSNP:rs80359820Ensembl.1
    Natural variantiVAR_076229149P → A in EIG12; unknown pathological significance. 1 Publication1
    Natural variantiVAR_054759153R → C in GLUT1DS1; 44% of wild-type glucose uptake activity. 2 Publications1
    Natural variantiVAR_065210153R → H in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs794727642EnsemblClinVar.1
    Natural variantiVAR_065211155A → V in GLUT1DS1. 1 Publication1
    Natural variantiVAR_065212165V → I in GLUT1DS2. 1 PublicationCorresponds to variant dbSNP:rs1057520545EnsemblClinVar.1
    Natural variantiVAR_054760169Missing in GLUT1DS1; 48% of wild-type glucose uptake activity. 1 Publication1
    Natural variantiVAR_065213212R → C in GLUT1DS1 and DYT9. 2 PublicationsCorresponds to variant dbSNP:rs387907312EnsemblClinVar.1
    Natural variantiVAR_065214212R → H in GLUT1DS1. 1 PublicationCorresponds to variant dbSNP:rs886039517EnsemblClinVar.1
    Natural variantiVAR_076230218R → S in EIG12; decreased glucose transport. 1 Publication1
    Natural variantiVAR_065215223R → P in EIG12; mild phenotype; reduced transporter activity; impaired phosphorylation by PKC. 3 PublicationsCorresponds to variant dbSNP:rs397514564EnsemblClinVar.1
    Natural variantiVAR_076231223R → Q in EIG12; unknown pathological significance; no effect on glucose transport; impaired phosphorylation by PKC. 2 PublicationsCorresponds to variant dbSNP:rs397514564EnsemblClinVar.1
    Natural variantiVAR_065216223R → W in GLUT1DS1; impaired phosphorylation by PKC. 2 PublicationsCorresponds to variant dbSNP:rs796053248EnsemblClinVar.1
    Natural variantiVAR_069078232R → C in EIG12; the mutant protein is expressed at the cell surface but has mildly decreased glucose uptake (70%) compared to wild-type. 1 PublicationCorresponds to variant dbSNP:rs387907313EnsemblClinVar.1
    Natural variantiVAR_076232243E → V in EIG12; decreased glucose transport. 1 Publication1
    Natural variantiVAR_013185256K → E in GLUT1DS1; compound heterozygote with L-126. 1 PublicationCorresponds to variant dbSNP:rs121909738Ensembl.1
    Natural variantiVAR_054761275A → T in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability. 1 PublicationCorresponds to variant dbSNP:rs121909740EnsemblClinVar.1
    Natural variantiVAR_054762282 – 285Missing in GLUT1DS2; accompanied by hemolytic anemia and altered erythrocyte ion concentrations; the mutation decreases glucose transport and causes a cation leak that alteres intracellular concentrations of sodium potassium and calcium. 1 Publication4
    Natural variantiVAR_076233286G → D in SDCHCN; no effect on protein abundance; no effect on localization to the plasma membrane; loss of D-glucose transporter activity; increased cation leakage. 2 PublicationsCorresponds to variant dbSNP:rs864309514EnsemblClinVar.1
    Natural variantiVAR_069079292Y → YY in GLUT1DS1. 1 Publication1
    Natural variantiVAR_065784294S → P in GLUT1DS2. 1 Publication1
    Natural variantiVAR_054763295T → M in GLUT1DS1; 75% of wild-type glucose uptake activity. 2 PublicationsCorresponds to variant dbSNP:rs80359823EnsemblClinVar.1
    Natural variantiVAR_065217303V → L Found in a patient with GLUT1 deficiency syndrome. 1 PublicationCorresponds to variant dbSNP:rs1205631854EnsemblClinVar.1
    Natural variantiVAR_013285310T → I in GLUT1DS1. 1 Publication