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P11166 (GTR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Solute carrier family 2, facilitated glucose transporter member 1
Alternative name(s):
Glucose transporter type 1, erythrocyte/brain
Short name=GLUT-1
HepG2 glucose transporter
Gene names
Name:SLC2A1
Synonyms:GLUT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Facilitative glucose transporter. This isoform maybe responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses.

Subunit structure

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 Interacts with SNX27; the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane. Ref.9 Ref.16

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Melanosome. Note: Localizes primarily at the cell surface By similarity. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.8

Tissue specificity

Expressed at variable levels in many human tissues.

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.24 Ref.27 Ref.29 Ref.30 Ref.33

GLUT1 deficiency syndrome 2 (GLUT1DS2) [MIM:612126]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Ref.25 Ref.26 Ref.28 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34

Epilepsy, idiopathic generalized 12 (EIG12) [MIM:614847]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26 Ref.36

Dystonia 9 (DYT9) [MIM:601042]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.35

Sequence similarities

Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily. [View classification]

Ontologies

Keywords
   Biological processSugar transport
Transport
   Cellular componentCell membrane
Membrane
   DiseaseDisease mutation
Dystonia
Epilepsy
   DomainTransmembrane
Transmembrane helix
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processL-ascorbic acid metabolic process

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular response to glucose starvation

Inferred from electronic annotation. Source: Ensembl

energy reserve metabolic process

Traceable author statement. Source: Reactome

glucose transport

Traceable author statement. Source: Reactome

hexose transport

Traceable author statement. Source: Reactome

protein complex assembly

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of insulin secretion

Traceable author statement. Source: Reactome

response to osmotic stress

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

vitamin metabolic process

Traceable author statement. Source: Reactome

water-soluble vitamin metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentbasolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

caveola

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

cortical actin cytoskeleton

Inferred from direct assay Ref.9. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

female pronucleus

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Traceable author statement PubMed 3028891PubMed 9462754. Source: ProtInc

midbody

Inferred from direct assay PubMed 15166316. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionD-glucose transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

dehydroascorbic acid transporter activity

Inferred from electronic annotation. Source: Ensembl

glucose transmembrane transporter activity

Traceable author statement PubMed 9462754. Source: ProtInc

identical protein binding

Inferred from physical interaction PubMed 1429721. Source: IntAct

protein self-association

Inferred from direct assay Ref.9. Source: UniProtKB

xenobiotic transporter activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-717153,EBI-717153

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Solute carrier family 2, facilitated glucose transporter member 1
PRO_0000050338

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3321Helical; Name=1; Potential
Topological domain34 – 6633Extracellular Potential
Transmembrane67 – 8721Helical; Name=2; Potential
Topological domain88 – 958Cytoplasmic Potential
Transmembrane96 – 11621Helical; Name=3; Potential
Topological domain117 – 12610Extracellular Potential
Transmembrane127 – 14721Helical; Name=4; Potential
Topological domain148 – 1558Cytoplasmic Potential
Transmembrane156 – 17621Helical; Name=5; Potential
Topological domain177 – 1859Extracellular Potential
Transmembrane186 – 20621Helical; Name=6; Potential
Topological domain207 – 27165Cytoplasmic Potential
Transmembrane272 – 29221Helical; Name=7; Potential
Topological domain293 – 30715Extracellular Potential
Transmembrane308 – 32821Helical; Name=8; Potential
Topological domain329 – 3379Cytoplasmic Potential
Transmembrane338 – 35821Helical; Name=9; Potential
Topological domain359 – 37113Extracellular Potential
Transmembrane372 – 39221Helical; Name=10; Potential
Topological domain393 – 4019Cytoplasmic Potential
Transmembrane402 – 42221Helical; Name=11; Potential
Topological domain423 – 4297Extracellular Potential
Transmembrane430 – 45021Helical; Name=12; Potential
Topological domain451 – 49242Cytoplasmic Potential
Region279 – 2813Defines substrate specificity By similarity

Sites

Site4111Not glycosylated

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15
Modified residue4781Phosphothreonine Ref.12
Modified residue4901Phosphoserine Ref.14
Glycosylation451N-linked (GlcNAc...) Ref.1 Ref.11

Natural variations

Natural variant341N → I in GLUT1DS2. Ref.23
VAR_054755
Natural variant341N → S in GLUT1DS1; 55% of wild-type glucose uptake activity. Ref.24
VAR_054756
Natural variant341N → Y in GLUT1DS1. Ref.30
VAR_065206
Natural variant661S → F in GLUT1DS1. Ref.18
VAR_013283
Natural variant911G → D in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose. Ref.21 Ref.33
VAR_013182
Natural variant921R → W in GLUT1DS2. Ref.28
VAR_069077
Natural variant931R → W in GLUT1DS2. Ref.30
VAR_065207
Natural variant951S → I in GLUT1DS2. Ref.33
VAR_065208
Natural variant961M → V in GLUT1DS1. Ref.30
VAR_065209
Natural variant1261R → C in GLUT1DS1, GLUT1DS2 and DYT9; reduced transporter activity. Ref.22 Ref.26 Ref.35
VAR_054757
Natural variant1261R → H in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose and dehydroascorbic acid; 57% of wild-type glucose uptake activity. Ref.20 Ref.22 Ref.24 Ref.33
VAR_013183
Natural variant1261R → L in GLUT1DS1; compound heterozygote with V-256. Ref.18
VAR_013184
Natural variant1301G → S in GLUT1DS1; 75% of wild-type glucose uptake activity. Ref.24 Ref.30
VAR_054758
Natural variant1461E → K in GLUT1DS1. Ref.18 Ref.22
VAR_013284
Natural variant1531R → C in GLUT1DS1; 44% of wild-type glucose uptake activity. Ref.22 Ref.24
VAR_054759
Natural variant1531R → H in GLUT1DS2. Ref.30
VAR_065210
Natural variant1551A → V in GLUT1DS1. Ref.30
VAR_065211
Natural variant1651V → I in GLUT1DS2. Ref.32
VAR_065212
Natural variant1691Missing in GLUT1DS1; 48% of wild-type glucose uptake activity. Ref.24
VAR_054760
Natural variant2121R → C in GLUT1DS1 and DYT9. Ref.30 Ref.35
VAR_065213
Natural variant2121R → H in GLUT1DS1. Ref.30
VAR_065214
Natural variant2231R → P in EIG12; mild phenotype; reduced transporter activity. Ref.26 Ref.33
VAR_065215
Natural variant2231R → W in GLUT1DS1. Ref.30
VAR_065216
Natural variant2321R → C in EIG12; the mutant protein is expressed at the cell surface but has mildly decreased glucose uptake (70%) compared to wild-type. Ref.36
VAR_069078
Natural variant2561K → E in GLUT1DS1; compound heterozygote with L-126. Ref.18
VAR_013185
Natural variant2751A → T in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability. Ref.25
VAR_054761
Natural variant282 – 2854Missing 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.
VAR_054762
Natural variant2921Y → YY in GLUT1DS1. Ref.27
VAR_069079
Natural variant2941S → P in GLUT1DS2. Ref.34
VAR_065784
Natural variant2951T → M in GLUT1DS1; 75% of wild-type glucose uptake activity. Ref.24 Ref.30
VAR_054763
Natural variant3031V → L Found in a patient with GLUT1 deficiency syndrome. Ref.30
VAR_065217
Natural variant3101T → I in GLUT1DS1. Ref.17
VAR_013285
Natural variant3141G → S in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability. Ref.25 Ref.33
VAR_054764
Natural variant3171N → T in GLUT1DS2. Ref.31
VAR_065218
Natural variant3241S → L in GLUT1DS2; mild phenotype; reduced transporter activity. Ref.26 Ref.33
VAR_065219
Natural variant3291E → Q in GLUT1DS1. Ref.30
VAR_065220
Natural variant3331R → Q in GLUT1DS1 and GLUT1DS2. Ref.28 Ref.30
VAR_065221
Natural variant3331R → W in GLUT1DS1; 43% of wild-type glucose uptake activity. Ref.18 Ref.22 Ref.24
VAR_013286
Natural variant3821G → D in GLUT1DS1. Ref.30
VAR_065222
Natural variant4051A → D in GLUT1DS1. Ref.30
VAR_065223
Natural variant4681R → W in GLUT1DS1. Ref.29
VAR_069080
Natural variant4851P → L in GLUT1DS1. Ref.30
VAR_065224

Experimental info

Sequence conflict25 – 262Missing in BAF85480. Ref.2
Sequence conflict951S → L in BAF85480. Ref.2
Sequence conflict1521L → F in AAA52571. Ref.1

Secondary structure

............................................................ 492
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11166 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: E71E1C6BD1B00B1E

FASTA49254,084
        10         20         30         40         50         60 
MEPSSKKLTG RLMLAVGGAV LGSLQFGYNT GVINAPQKVI EEFYNQTWVH RYGESILPTT 

        70         80         90        100        110        120 
LTTLWSLSVA IFSVGGMIGS FSVGLFVNRF GRRNSMLMMN LLAFVSAVLM GFSKLGKSFE 

       130        140        150        160        170        180 
MLILGRFIIG VYCGLTTGFV PMYVGEVSPT ALRGALGTLH QLGIVVGILI AQVFGLDSIM 

       190        200        210        220        230        240 
GNKDLWPLLL SIIFIPALLQ CIVLPFCPES PRFLLINRNE ENRAKSVLKK LRGTADVTHD 

       250        260        270        280        290        300 
LQEMKEESRQ MMREKKVTIL ELFRSPAYRQ PILIAVVLQL SQQLSGINAV FYYSTSIFEK 

       310        320        330        340        350        360 
AGVQQPVYAT IGSGIVNTAF TVVSLFVVER AGRRTLHLIG LAGMAGCAIL MTIALALLEQ 

       370        380        390        400        410        420 
LPWMSYLSIV AIFGFVAFFE VGPGPIPWFI VAELFSQGPR PAAIAVAGFS NWTSNFIVGM 

       430        440        450        460        470        480 
CFQYVEQLCG PYVFIIFTVL LVLFFIFTYF KVPETKGRTF DEIASGFRQG GASQSDKTPE 

       490 
ELFHPLGADS QV 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and structure of a human glucose transporter."
Mueckler M., Caruso C., Baldwin S.A., Panico M., Blench I., Morris H.R., Allard W.J., Lienhard G.E., Lodish H.F.
Science 229:941-945(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-45, LACK OF GLYCOSYLATION AT ASN-411, IDENTIFICATION BY MASS SPECTROMETRY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Trachea.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Characterization and expression of human HepG2/erythrocyte glucose-transporter gene."
Fukumoto H., Seino S., Imura H., Seino Y., Bell G.I.
Diabetes 37:657-661(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[6]Yu W., Gibbs R.A.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-492.
Tissue: Brain.
[7]"Molecular characterization and cloning of glucose transporters in human articular chondrocytes."
Neama G., Richardson S., Bell S., Carter S., Mobasheri A.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 294-423.
Tissue: Articular cartilage.
[8]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[9]"Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1."
Khan A.A., Hanada T., Mohseni M., Jeong J.J., Zeng L., Gaetani M., Li D., Reed B.C., Speicher D.W., Chishti A.H.
J. Biol. Chem. 283:14600-14609(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH ADD2 AND DMTN, INTERACTION WITH DMTN, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45.
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport."
Steinberg F., Gallon M., Winfield M., Thomas E.C., Bell A.J., Heesom K.J., Tavare J.M., Cullen P.J.
Nat. Cell Biol. 15:461-471(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX27.
[17]"Defective glucose transport across brain tissue barriers: a newly recognized neurological syndrome."
Klepper J., Wang D., Fischbarg J., Vera J.C., Jarjour I.T., O'Driscoll K.R., De Vivo D.C.
Neurochem. Res. 24:587-594(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLUT1DS1 ILE-310.
[18]"Mutational analysis of GLUT1 (SLC2A1) in Glut-1 deficiency syndrome."
Wang D., Kranz-Eble P., De Vivo D.C.
Hum. Mutat. 16:224-231(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLUT1DS1 PHE-66; LEU-126; LYS-146; GLU-256 AND TRP-333.
[19]Erratum
Wang D., Kranz-Eble P., De Vivo D.C.
Hum. Mutat. 16:527-527(2000)
[20]"Autosomal dominant Glut-1 deficiency syndrome and familial epilepsy."
Brockmann K., Wang D., Korenke C.G., von Moers A., Ho Y.-Y., Pascual J.M., Kuang K., Yang H., Ma L., Kranz-Eble P., Fischbarg J., Hanefeld F., De Vivo D.C.
Ann. Neurol. 50:476-485(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLUT1DS1 HIS-126.
[21]"Autosomal dominant transmission of GLUT1 deficiency."
Klepper J., Willemsen M., Verrips A., Guertsen E., Herrmann R., Kutzick C., Floercken A., Voit T.
Hum. Mol. Genet. 10:63-68(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLUT1DS1 ASP-91.
[22]"Imaging the metabolic footprint of Glut1 deficiency on the brain."
Pascual J.M., van Heertum R.L., Wang D., Engelstad K., De Vivo D.C.
Ann. Neurol. 52:458-464(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLUT1DS1 CYS-126; HIS-126; LYS-146; CYS-153 AND TRP-333.
[23]"GLUT-1 deficiency without epilepsy -- an exceptional case."
Overweg-Plandsoen W.C.G., Groener J.E.M., Wang D., Onkenhout W., Brouwer O.F., Bakker H.D., De Vivo D.C.
J. Inherit. Metab. Dis. 26:559-563(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLUT1DS2 ILE-34.
[24]"Glut-1 deficiency syndrome: clinical, genetic, and therapeutic aspects."
Wang D., Pascual J.M., Yang H., Engelstad K., Jhung S., Sun R.P., De Vivo D.C.
Ann. Neurol. 57:111-118(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLUT1DS1 SER-34; HIS-126; SER-130; CYS-153; LEU-169 DEL; MET-295 AND TRP-333, CHARACTERIZATION OF VARIANTS GLUT1 DEFICIENCY SER-34; HIS-126; SER-130; CYS-153; LEU-169 DEL; MET-295 AND TRP-333.
[25]"GLUT1 mutations are a cause of paroxysmal exertion-induced dyskinesias and induce hemolytic anemia by a cation leak."
Weber Y.G., Storch A., Wuttke T.V., Brockmann K., Kempfle J., Maljevic S., Margari L., Kamm C., Schneider S.A., Huber S.M., Pekrun A., Roebling R., Seebohm G., Koka S., Lang C., Kraft E., Blazevic D., Salvo-Vargas A. expand/collapse author list , Fauler M., Mottaghy F.M., Muenchau A., Edwards M.J., Presicci A., Margari F., Gasser T., Lang F., Bhatia K.P., Lehmann-Horn F., Lerche H.
J. Clin. Invest. 118:2157-2168(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLUT1DS2 THR-275; 282-GLN--SER-285 DEL AND SER-314.
[26]"Early-onset absence epilepsy caused by mutations in the glucose transporter GLUT1."
Suls A., Mullen S.A., Weber Y.G., Verhaert K., Ceulemans B., Guerrini R., Wuttke T.V., Salvo-Vargas A., Deprez L., Claes L.R., Jordanova A., Berkovic S.F., Lerche H., De Jonghe P., Scheffer I.E.
Ann. Neurol. 66:415-419(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EIG12 PRO-223, VARIANTS GLUT1DS2 CYS-126 AND LEU-324, CHARACTERIZATION OF VARIANT EIG12 PRO-223, CHARACTERIZATION OF VARIANTS GLUT1DS2 CYS-126 AND LEU-324.
[27]"Childhood chorea with cerebral hypotrophy: a treatable GLUT1 energy failure syndrome."
Perez-Duenas B., Prior C., Ma Q., Fernandez-Alvarez E., Setoain X., Artuch R., Pascual J.M.
Arch. Neurol. 66:1410-1414(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLUT1DS1 TYR-292 INS.
[28]"GLUT1 gene mutations cause sporadic paroxysmal exercise-induced dyskinesias."
Schneider S.A., Paisan-Ruiz C., Garcia-Gorostiaga I., Quinn N.P., Weber Y.G., Lerche H., Hardy J., Bhatia K.P.
Mov. Disord. 24:1684-1688(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLUT1DS2 TRP-92 AND GLN-333.
[29]"Autosomal recessive inheritance of GLUT1 deficiency syndrome."
Klepper J., Scheffer H., Elsaid M.F., Kamsteeg E.J., Leferink M., Ben-Omran T.
Neuropediatrics 40:207-210(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLUT1DS1 TRP-468.
[30]"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. expand/collapse author list , 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) [PubMed] [Europe PMC] [Abstract]
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.
[31]"Mild adolescent/adult onset epilepsy and paroxysmal exercise-induced dyskinesia due to GLUT1 deficiency."
Afawi Z., Suls A., Ekstein D., Kivity S., Neufeld M.Y., Oliver K., De Jonghe P., Korczyn A.D., Berkovic S.F.
Epilepsia 51:2466-2469(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLUT1DS2 THR-317.
[32]"Paroxysmal exercise-induced dyskinesia, writer's cramp, migraine with aura and absence epilepsy in twin brothers with a novel SLC2A1 missense mutation."
Urbizu A., Cuenca-Leon E., Raspall-Chaure M., Gratacos M., Conill J., Redecillas S., Roig-Quilis M., Macaya A.
J. Neurol. Sci. 295:110-113(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLUT1DS2 ILE-165.
[33]"Absence epilepsies with widely variable onset are a key feature of familial GLUT1 deficiency."
Mullen S.A., Suls A., De Jonghe P., Berkovic S.F., Scheffer I.E.
Neurology 75:432-440(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLUT1DS2 ILE-95; PRO-223; SER-314 AND LEU-324, VARIANTS GLUT1DS1 ASP-91 AND HIS-126.
[34]"Excellent response to acetazolamide in a case of paroxysmal dyskinesias due to GLUT1-deficiency."
Anheim M., Maillart E., Vuillaumier-Barrot S., Flamand-Rouviere C., Pineau F., Ewenczyk C., Riant F., Apartis E., Roze E.
J. Neurol. 258:316-317(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLUT1DS2 PRO-294.
[35]"Paroxysmal choreoathetosis/spasticity (DYT9) is caused by a GLUT1 defect."
Weber Y.G., Kamm C., Suls A., Kempfle J., Kotschet K., Schule R., Wuttke T.V., Maljevic S., Liebrich J., Gasser T., Ludolph A.C., Van Paesschen W., Schols L., De Jonghe P., Auburger G., Lerche H.
Neurology 77:959-964(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DYT9 CYS-126 AND CYS-212.
[36]"GLUT1 mutations are a rare cause of familial idiopathic generalized epilepsy."
Striano P., Weber Y.G., Toliat M.R., Schubert J., Leu C., Chaimana R., Baulac S., Guerrero R., LeGuern E., Lehesjoki A.E., Polvi A., Robbiano A., Serratosa J.M., Guerrini R., Nurnberg P., Sander T., Zara F., Lerche H., Marini C.
Neurology 78:557-562(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EIG12 CYS-232, CHARACTERIZATION OF VARIANT EIG12 CYS-232.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K03195 mRNA. Translation: AAA52571.1.
AK292791 mRNA. Translation: BAF85480.1.
AK312403 mRNA. Translation: BAG35317.1.
CH471059 Genomic DNA. Translation: EAX07124.1.
BC118590 mRNA. Translation: AAI18591.1.
M20653 Genomic DNA. Translation: AAB61084.1.
AF070544 mRNA. Translation: AAC28635.1.
AY034633 mRNA. Translation: AAK56795.1.
PIRA27217.
RefSeqNP_006507.2. NM_006516.2.
UniGeneHs.473721.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SUKmodel-A1-492[»]
ProteinModelPortalP11166.
SMRP11166. Positions 19-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112404. 15 interactions.
DIPDIP-23N.
IntActP11166. 5 interactions.
MINTMINT-1386229.
STRING9606.ENSP00000416293.

Chemistry

BindingDBP11166.
ChEMBLCHEMBL2535.
DrugBankDB00292. Etomidate.
GuidetoPHARMACOLOGY875.

Protein family/group databases

TCDB2.A.1.1.28. the major facilitator superfamily (mfs).

PTM databases

PhosphoSiteP11166.
UniCarbKBP11166.

Polymorphism databases

DMDM115502394.

Proteomic databases

PaxDbP11166.
PeptideAtlasP11166.
PRIDEP11166.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000426263; ENSP00000416293; ENSG00000117394.
GeneID6513.
KEGGhsa:6513.
UCSCuc001cik.2. human.

Organism-specific databases

CTD6513.
GeneCardsGC01M043391.
HGNCHGNC:11005. SLC2A1.
HPACAB002759.
MIM138140. gene.
601042. phenotype.
606777. phenotype.
612126. phenotype.
614847. phenotype.
neXtProtNX_P11166.
Orphanet64280. Childhood absence epilepsy.
71277. Encephalopathy due to GLUT1 deficiency.
1942. Epilepsy with myoclonic-astatic seizures.
168577. Hereditary cryohydrocytosis with reduced stomatin.
53583. Paroxysmal dystonic choreathetosis with episodic ataxia and spasticity.
98811. Paroxysmal exertion-induced dyskinesia.
PharmGKBPA35875.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0477.
HOVERGENHBG014816.
KOK07299.
OMALQCIVLP.
PhylomeDBP11166.
TreeFamTF313762.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP11166.
BgeeP11166.
CleanExHS_SLC2A1.
GenevestigatorP11166.

Family and domain databases

InterProIPR002439. Glu_transpt_1.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR005828. Sub_transporter.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PANTHERPTHR24063:SF17. PTHR24063:SF17. 1 hit.
PfamPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSPR01190. GLUCTRSPORT1.
PR00171. SUGRTRNSPORT.
SUPFAMSSF103473. SSF103473. 2 hits.
TIGRFAMsTIGR00879. SP. 1 hit.
PROSITEPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC2A1. human.
GeneWikiGLUT1.
GenomeRNAi6513.
NextBio25327.
PROP11166.
SOURCESearch...

Entry information

Entry nameGTR1_HUMAN
AccessionPrimary (citable) accession number: P11166
Secondary accession number(s): A8K9S6 expand/collapse secondary AC list , B2R620, D3DPX0, O75535, Q147X2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM