7WSM
Cryo-EM structure of human glucose transporter GLUT4 bound to cytochalasin B in lipid nanodiscs
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005768 | cellular_component | endosome |
| A | 0005771 | cellular_component | multivesicular body |
| A | 0005802 | cellular_component | trans-Golgi network |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005905 | cellular_component | clathrin-coated pit |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0007611 | biological_process | learning or memory |
| A | 0007614 | biological_process | short-term memory |
| A | 0007616 | biological_process | long-term memory |
| A | 0009897 | cellular_component | external side of plasma membrane |
| A | 0009986 | cellular_component | cell surface |
| A | 0012505 | cellular_component | endomembrane system |
| A | 0012506 | cellular_component | vesicle membrane |
| A | 0015304 | molecular_function | D-glucose uniporter activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016529 | cellular_component | sarcoplasmic reticulum |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0030136 | cellular_component | clathrin-coated vesicle |
| A | 0030140 | cellular_component | trans-Golgi network transport vesicle |
| A | 0030315 | cellular_component | T-tubule |
| A | 0030659 | cellular_component | cytoplasmic vesicle membrane |
| A | 0031550 | biological_process | positive regulation of brain-derived neurotrophic factor receptor signaling pathway |
| A | 0031982 | cellular_component | vesicle |
| A | 0032593 | cellular_component | insulin-responsive compartment |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0042383 | cellular_component | sarcolemma |
| A | 0042593 | biological_process | glucose homeostasis |
| A | 0044381 | biological_process | glucose import in response to insulin stimulus |
| A | 0045121 | cellular_component | membrane raft |
| A | 0045471 | biological_process | response to ethanol |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0055056 | molecular_function | D-glucose transmembrane transporter activity |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070343 | biological_process | white fat cell proliferation |
| A | 0070837 | biological_process | dehydroascorbic acid transport |
| A | 0071456 | biological_process | cellular response to hypoxia |
| A | 0098694 | biological_process | regulation of synaptic vesicle budding from presynaptic endocytic zone membrane |
| 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 | 1904659 | biological_process | D-glucose transmembrane transport |
Functional Information from PROSITE/UniProt
| site_id | PS00216 |
| Number of Residues | 17 |
| Details | SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. SVLLVERAGRRtlhll.G |
| Chain | Residue | Details |
| A | SER340-GLY356 |
| site_id | PS00217 |
| Number of Residues | 26 |
| Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. LiGAYsGLtsglvpmYvgEiapthlR |
| Chain | Residue | Details |
| A | LEU144-ARG169 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 81 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 98 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P11169","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by SGK1","evidences":[{"source":"PubMed","id":"17382906","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"28057756","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
