4PYP
Crystal structure of the human glucose transporter GLUT1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000139 | cellular_component | Golgi membrane |
A | 0001666 | biological_process | response to hypoxia |
A | 0001674 | cellular_component | female germ cell nucleus |
A | 0001917 | cellular_component | photoreceptor inner segment |
A | 0001939 | cellular_component | female pronucleus |
A | 0005324 | molecular_function | long-chain fatty acid transmembrane transporter activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0005901 | cellular_component | caveola |
A | 0005911 | cellular_component | cell-cell junction |
A | 0007417 | biological_process | central nervous system development |
A | 0007565 | biological_process | female pregnancy |
A | 0014704 | cellular_component | intercalated disc |
A | 0015150 | molecular_function | fucose transmembrane transporter activity |
A | 0015756 | biological_process | fucose transmembrane transport |
A | 0015911 | biological_process | long-chain fatty acid import across plasma membrane |
A | 0016020 | cellular_component | membrane |
A | 0016323 | cellular_component | basolateral plasma membrane |
A | 0016324 | cellular_component | apical plasma membrane |
A | 0019852 | biological_process | L-ascorbic acid metabolic process |
A | 0019900 | molecular_function | kinase binding |
A | 0021987 | biological_process | cerebral cortex development |
A | 0022857 | molecular_function | transmembrane transporter activity |
A | 0030018 | cellular_component | Z disc |
A | 0030496 | cellular_component | midbody |
A | 0030864 | cellular_component | cortical actin cytoskeleton |
A | 0031982 | cellular_component | vesicle |
A | 0032868 | biological_process | response to insulin |
A | 0033300 | molecular_function | dehydroascorbic acid transmembrane transporter activity |
A | 0042149 | biological_process | cellular response to glucose starvation |
A | 0042352 | biological_process | GDP-L-fucose salvage |
A | 0042383 | cellular_component | sarcolemma |
A | 0042470 | cellular_component | melanosome |
A | 0042802 | molecular_function | identical protein binding |
A | 0042908 | biological_process | xenobiotic transport |
A | 0042910 | molecular_function | xenobiotic transmembrane transporter activity |
A | 0045121 | cellular_component | membrane raft |
A | 0045202 | cellular_component | synapse |
A | 0045494 | biological_process | photoreceptor cell maintenance |
A | 0046323 | biological_process | D-glucose import |
A | 0055056 | molecular_function | D-glucose transmembrane transporter activity |
A | 0055085 | biological_process | transmembrane transport |
A | 0065003 | biological_process | protein-containing complex assembly |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070837 | biological_process | dehydroascorbic acid transport |
A | 0071260 | biological_process | cellular response to mechanical stimulus |
A | 0071474 | biological_process | cellular hyperosmotic response |
A | 0072562 | cellular_component | blood microparticle |
A | 0098708 | biological_process | D-glucose import across plasma membrane |
A | 0098793 | cellular_component | presynapse |
A | 0150104 | biological_process | transport across blood-brain barrier |
A | 1904016 | biological_process | response to Thyroglobulin triiodothyronine |
A | 1904659 | biological_process | D-glucose transmembrane transport |
A | 1990350 | cellular_component | glucose transporter complex |
Functional Information from PROSITE/UniProt
site_id | PS00217 |
Number of Residues | 26 |
Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. IiGVYcGLttgfvpmYvgEvsptalR |
Chain | Residue | Details |
A | ILE128-ARG153 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=1"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 74 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"24847886","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=2"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 93 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24847886","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=3"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 23 |
Details | Transmembrane: {"description":"Helical; Name=4"} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=5"} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=6"} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=7"} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=8"} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=9"} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=10"} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=11"} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=12"} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"27078104","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EQI","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"24847886","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"24847886","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4PYP","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"27078104","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"3839598","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by PKC/PRKCB","evidences":[{"source":"PubMed","id":"25982116","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI21 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3839598","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |