9CAX
Structure of human SLC2A9 transporter
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005351 | molecular_function | carbohydrate:proton symporter activity |
A | 0005353 | molecular_function | fructose transmembrane transporter activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0008645 | biological_process | hexose transmembrane transport |
A | 0009055 | molecular_function | electron transfer activity |
A | 0015143 | molecular_function | urate transmembrane transporter activity |
A | 0015747 | biological_process | urate transport |
A | 0015755 | biological_process | fructose transmembrane transport |
A | 0016020 | cellular_component | membrane |
A | 0016323 | cellular_component | basolateral plasma membrane |
A | 0016324 | cellular_component | apical plasma membrane |
A | 0020037 | molecular_function | heme binding |
A | 0022857 | molecular_function | transmembrane transporter activity |
A | 0022900 | biological_process | electron transport chain |
A | 0042597 | cellular_component | periplasmic space |
A | 0046323 | biological_process | D-glucose import |
A | 0046415 | biological_process | urate metabolic process |
A | 0055056 | molecular_function | D-glucose transmembrane transporter activity |
A | 0055085 | biological_process | transmembrane transport |
A | 0070837 | biological_process | dehydroascorbic acid transport |
A | 1902600 | biological_process | proton transmembrane transport |
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. SGLVIEHLGRRpllig.G |
Chain | Residue | Details |
A | SER371-GLY387 |
site_id | PS00217 |
Number of Residues | 26 |
Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. ImGIDgGValsvlpmYlsEispkeiR |
Chain | Residue | Details |
A | ILE173-ARG198 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 85 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 100 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |