P11166 (GTR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Facilitative glucose transporter. This isoform may be 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.
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.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.24 Ref.26 Ref.27 Ref.30 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.20 Ref.22 Ref.23 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 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.23 Ref.33 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.32
Sequence similarities	Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily. [View classification]

Ontologies

Keywords
Biological process	Sugar transport Transport
Cellular component	Cell membrane Membrane
Disease	Disease mutation Dystonia Epilepsy
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-ascorbic acid metabolic process Traceable author statement. Source: Reactome cellular response to glucose starvation Inferred from electronic annotation. Source: Compara energy reserve metabolic process Traceable author statement. Source: Reactome regulation of insulin secretion Traceable author statement. Source: Reactome response to osmotic stress Inferred from electronic annotation. Source: Compara
Cellular_component	basolateral plasma membrane Inferred from electronic annotation. Source: Compara caveola Inferred from electronic annotation. Source: Compara cell-cell junction Inferred from electronic annotation. Source: Compara female pronucleus Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from direct assay PubMed 15166316. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome
Molecular_function	D-glucose transmembrane transporter activity Inferred from electronic annotation. Source: Compara dehydroascorbic acid transporter activity Inferred from electronic annotation. Source: Compara glucose transmembrane transporter activity Traceable author statement PubMed 9462754. Source: ProtInc xenobiotic transporter activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-717153,EBI-717153

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 492

492

Solute carrier family 2, facilitated glucose transporter member 1

PRO_0000050338

Regions

Topological domain

1 – 12

12

Cytoplasmic Potential

Transmembrane

13 – 33

21

Helical; Name=1; Potential

Topological domain

34 – 66

33

Extracellular Potential

Transmembrane

67 – 87

21

Helical; Name=2; Potential

Topological domain

88 – 95

8

Cytoplasmic Potential

Transmembrane

96 – 116

21

Helical; Name=3; Potential

Topological domain

117 – 126

10

Extracellular Potential

Transmembrane

127 – 147

21

Helical; Name=4; Potential

Topological domain

148 – 155

8

Cytoplasmic Potential

Transmembrane

156 – 176

21

Helical; Name=5; Potential

Topological domain

177 – 185

9

Extracellular Potential

Transmembrane

186 – 206

21

Helical; Name=6; Potential

Topological domain

207 – 271

65

Cytoplasmic Potential

Transmembrane

272 – 292

21

Helical; Name=7; Potential

Topological domain

293 – 307

15

Extracellular Potential

Transmembrane

308 – 328

21

Helical; Name=8; Potential

Topological domain

329 – 337

9

Cytoplasmic Potential

Transmembrane

338 – 358

21

Helical; Name=9; Potential

Topological domain

359 – 371

13

Extracellular Potential

Transmembrane

372 – 392

21

Helical; Name=10; Potential

Topological domain

393 – 401

9

Cytoplasmic Potential

Transmembrane

402 – 422

21

Helical; Name=11; Potential

Topological domain

423 – 429

7

Extracellular Potential

Transmembrane

430 – 450

21

Helical; Name=12; Potential

Topological domain

451 – 492

42

Cytoplasmic Potential

Region

279 – 281

3

Defines substrate specificity By similarity

Sites

Site

411

1

Not glycosylated

Amino acid modifications

Modified residue

234

1

Phosphothreonine By similarity

Modified residue

478

1

Phosphothreonine Ref.11

Modified residue

490

1

Phosphoserine Ref.13

Glycosylation

45

1

N-linked (GlcNAc...) Ref.1 Ref.10

Natural variations

Natural variant

34

1

N → I in GLUT1DS2. Ref.20

VAR_054755

Natural variant

34

1

N → S in GLUT1DS1; 55% of wild-type glucose uptake activity. Ref.21

VAR_054756

Natural variant

34

1

N → Y in GLUT1DS1. Ref.27

VAR_065206

Natural variant

66

1

S → F in GLUT1DS1. Ref.15

VAR_013283

Natural variant

91

1

G → D in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose. Ref.18 Ref.30

VAR_013182

Natural variant

92

1

R → W in GLUT1DS2. Ref.25

VAR_069077

Natural variant

93

1

R → W in GLUT1DS2. Ref.27

VAR_065207

Natural variant

95

1

S → I in GLUT1DS2. Ref.30

VAR_065208

Natural variant

96

1

M → V in GLUT1DS1. Ref.27

VAR_065209

Natural variant

126

1

R → C in GLUT1DS1, GLUT1DS2 and DYT9; reduced transporter activity. Ref.19 Ref.23 Ref.32

VAR_054757

Natural variant

126

1

R → H in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose and dehydroascorbic acid; 57% of wild-type glucose uptake activity. Ref.17 Ref.19 Ref.21 Ref.30

VAR_013183

Natural variant

126

1

R → L in GLUT1DS1; compound heterozygote with V-256. Ref.15

VAR_013184

Natural variant

130

1

G → S in GLUT1DS1; 75% of wild-type glucose uptake activity. Ref.21 Ref.27

VAR_054758

Natural variant

146

1

E → K in GLUT1DS1. Ref.15 Ref.19

VAR_013284

Natural variant

153

1

R → C in GLUT1DS1; 44% of wild-type glucose uptake activity. Ref.19 Ref.21

VAR_054759

Natural variant

153

1

R → H in GLUT1DS2. Ref.27

VAR_065210

Natural variant

155

1

A → V in GLUT1DS1. Ref.27

VAR_065211

Natural variant

165

1

V → I in GLUT1DS2. Ref.29

VAR_065212

Natural variant

169

1

Missing in GLUT1DS1; 48% of wild-type glucose uptake activity. Ref.21

VAR_054760

Natural variant

212

1

R → C in GLUT1DS1 and DYT9. Ref.27 Ref.32

VAR_065213

Natural variant

212

1

R → H in GLUT1DS1. Ref.27

VAR_065214

Natural variant

223

1

R → P in EIG12; mild phenotype; reduced transporter activity. Ref.23 Ref.30

VAR_065215

Natural variant

223

1

R → W in GLUT1DS1. Ref.27

VAR_065216

Natural variant

232

1

R → C in EIG12; the mutant protein is expressed at the cell surface but has mildly decreased glucose uptake (70%) compared to wild-type. Ref.33

VAR_069078

Natural variant

256

1

K → E in GLUT1DS1; compound heterozygote with L-126. Ref.15

VAR_013185

Natural variant

275

1

A → T in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability. Ref.22

VAR_054761

Natural variant

282 – 285

4

Missing 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 variant

292

1

Y → YY in GLUT1DS1. Ref.24

VAR_069079

Natural variant

294

1

S → P in GLUT1DS2. Ref.31

VAR_065784

Natural variant

295

1

T → M in GLUT1DS1; 75% of wild-type glucose uptake activity. Ref.21 Ref.27

VAR_054763

Natural variant

303

1

V → L Found in a patient with GLUT1 deficiency syndrome. Ref.27

VAR_065217

Natural variant

310

1

T → I in GLUT1DS1. Ref.14

VAR_013285

Natural variant

314

1

G → S in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability. Ref.22 Ref.30

VAR_054764

Natural variant

317

1

N → T in GLUT1DS2. Ref.28

VAR_065218

Natural variant

324

1

S → L in GLUT1DS2; mild phenotype; reduced transporter activity. Ref.23 Ref.30

VAR_065219

Natural variant

329

1

E → Q in GLUT1DS1. Ref.27

VAR_065220

Natural variant

333

1

R → Q in GLUT1DS1 and GLUT1DS2. Ref.25 Ref.27

VAR_065221

Natural variant

333

1

R → W in GLUT1DS1; 43% of wild-type glucose uptake activity. Ref.15 Ref.19 Ref.21

VAR_013286

Natural variant

382

1

G → D in GLUT1DS1. Ref.27

VAR_065222

Natural variant

405

1

A → D in GLUT1DS1. Ref.27

VAR_065223

Natural variant

468

1

R → W in GLUT1DS1. Ref.26

VAR_069080

Natural variant

485

1

P → L in GLUT1DS1. Ref.27

VAR_065224

Experimental info

Sequence conflict

25 – 26

2

Missing in BAF85480. Ref.2

Sequence conflict

95

1

S → L in BAF85480. Ref.2

Sequence conflict

152

1

L → F in AAA52571. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

492

Helix Strand Turn

Details...

Helix

6 – 30

25

Helix

31 – 33

3

Helix

34 – 39

6

Helix

48 – 50

3

Beta strand

51 – 53

3

Beta strand

56 – 58

3

Helix

61 – 89

29

Helix

92 – 112

21

Turn

119 – 121

3

Helix

122 – 147

26

Beta strand

149 – 151

3

Helix

152 – 168

17

Helix

170 – 181

12

Helix

186 – 188

3

Helix

189 – 206

18

Turn

212 – 214

3

Beta strand

220 – 223

4

Turn

227 – 229

3

Turn

231 – 233

3

Helix

254 – 260

7

Helix

265 – 291

27

Turn

292 – 294

3

Helix

305 – 329

25

Helix

336 – 356

21

Beta strand

358 – 360

3

Helix

361 – 374

14

Helix

376 – 378

3

Turn

380 – 384

5

Helix

385 – 391

7

Helix

395 – 397

3

Helix

399 – 421

23

Helix

431 – 470

40

Beta strand

478 – 481

4

Helix

485 – 489

5

Sequences

	Sequence		Length	Mass (Da)
	P11166 [UniParc]. Last modified October 3, 2006. Version 2. Checksum: E71E1C6BD1B00B1E	FASTA	492	54,084
	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

References

	« Hide 'large scale' referencesShow '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, 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. , 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. , 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], MASS SPECTROMETRY. Tissue: Melanoma.
[9]	"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.
[10]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"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, MASS SPECTROMETRY.
[14]	"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.
[15]	"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.
[16]	Erratum Wang D., Kranz-Eble P., De Vivo D.C. Hum. Mutat. 16:527-527(2000)
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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. , 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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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) [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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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

GeneReviews

Wikipedia

GLUT1 entry

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.

IPI

IPI00220194.

PIR

A27217.

RefSeq

NP_006507.2. NM_006516.2.

UniGene

Hs.473721.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SUK	model	-	A	1-492	[»]

ProteinModelPortal

P11166.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-23N.

IntAct

P11166. 4 interactions.

MINT

MINT-1386229.

STRING

9606.ENSP00000416293.

Protein family/group databases

TCDB

2.A.1.1.28. major facilitator superfamily (MFS).

PTM databases

GlycoSuiteDB

P11166.

PhosphoSite

P11166.

Polymorphism databases

DMDM

115502394.

Proteomic databases

PaxDb

P11166.

PeptideAtlas

P11166.

PRIDE

P11166.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000426263; ENSP00000416293; ENSG00000117394.

GeneID

6513.

KEGG

hsa:6513.

UCSC

uc001cik.2. human.

Organism-specific databases

CTD

6513.

GeneCards

GC01M043391.

HGNC

HGNC:11005. SLC2A1.

HPA

CAB002759.

MIM

138140. gene.
601042. phenotype.
606777. phenotype.
612126. phenotype.
614847. phenotype.

neXtProt

NX_P11166.

Orphanet

64280. Childhood absence epilepsy.
1942. Epilepsy with myoclonic-astatic seizures.
53583. Episodic choreoathetosis/spasticity.
71277. Glucose transporter type 1 deficiency syndrome.
168577. Hereditary cryohydrocytosis with reduced stomatin.
98811. Paroxysmal exertion-induced dyskinesia.

PharmGKB

PA35875.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0477.

HOVERGEN

HBG014816.

KO

K07299.

OMA

HRYGERI.

OrthoDB

EOG4QNMW2.

PhylomeDB

P11166.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

P11166.

Bgee

P11166.

CleanEx

HS_SLC2A1.

Genevestigator

P11166.

GermOnline

ENSG00000117394. Homo sapiens.

Family and domain databases

InterPro

IPR002439. 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]

Pfam

PF00083. Sugar_tr. 1 hit.
[Graphical view]

PRINTS

PR01190. GLUCTRSPORT1.
PR00171. SUGRTRNSPORT.

SUPFAM

SSF103473. MFS_gen_substrate_transporter. 1 hit.

TIGRFAMs

TIGR00879. SP. 1 hit.

PROSITE

PS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P11166.

ChEMBL

CHEMBL2535.

ChiTaRS

SLC2A1. human.

DrugBank

DB00292. Etomidate.

GenomeRNAi

6513.

NextBio

25327.

SOURCE

Search...

Entry information

Entry name

GTR1_HUMAN

Accession

Primary (citable) accession number: P11166
Secondary accession number(s): A8K9S6 , B2R620, D3DPX0, O75535, Q147X2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 3, 2006
Last modified:	May 1, 2013
This is version 163 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.