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4PYP

Crystal structure of the human glucose transporter GLUT1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0001666biological_processresponse to hypoxia
A0001674cellular_componentfemale germ cell nucleus
A0001917cellular_componentphotoreceptor inner segment
A0001939cellular_componentfemale pronucleus
A0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005901cellular_componentcaveola
A0005911cellular_componentcell-cell junction
A0007417biological_processcentral nervous system development
A0007565biological_processfemale pregnancy
A0014704cellular_componentintercalated disc
A0015150molecular_functionfucose transmembrane transporter activity
A0015756biological_processfucose transmembrane transport
A0015911biological_processlong-chain fatty acid import across plasma membrane
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0019852biological_processL-ascorbic acid metabolic process
A0019900molecular_functionkinase binding
A0021987biological_processcerebral cortex development
A0022857molecular_functiontransmembrane transporter activity
A0030018cellular_componentZ disc
A0030496cellular_componentmidbody
A0030864cellular_componentcortical actin cytoskeleton
A0031982cellular_componentvesicle
A0032868biological_processresponse to insulin
A0033300molecular_functiondehydroascorbic acid transmembrane transporter activity
A0042149biological_processcellular response to glucose starvation
A0042352biological_processGDP-L-fucose salvage
A0042383cellular_componentsarcolemma
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042908biological_processxenobiotic transport
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0045121cellular_componentmembrane raft
A0045202cellular_componentsynapse
A0045494biological_processphotoreceptor cell maintenance
A0046323biological_processD-glucose import
A0055056molecular_functionD-glucose transmembrane transporter activity
A0055085biological_processtransmembrane transport
A0065003biological_processprotein-containing complex assembly
A0070062cellular_componentextracellular exosome
A0070837biological_processdehydroascorbic acid transport
A0071260biological_processcellular response to mechanical stimulus
A0071474biological_processcellular hyperosmotic response
A0072562cellular_componentblood microparticle
A0098708biological_processD-glucose import across plasma membrane
A0098793cellular_componentpresynapse
A0150104biological_processtransport across blood-brain barrier
A1904016biological_processresponse to Thyroglobulin triiodothyronine
A1904659biological_processD-glucose transmembrane transport
A1990350cellular_componentglucose transporter complex
Functional Information from PROSITE/UniProt
site_idPS00217
Number of Residues26
DetailsSUGAR_TRANSPORT_2 Sugar transport proteins signature 2. IiGVYcGLttgfvpmYvgEvsptalR
ChainResidueDetails
AILE128-ARG153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues74
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"24847886","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues93
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24847886","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=8"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=9"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=10"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=11"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=12"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27078104","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EQI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24847886","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24847886","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4PYP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27078104","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsSite: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"3839598","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKC/PRKCB","evidences":[{"source":"PubMed","id":"25982116","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3839598","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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