8EJ1
Dephosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005254 | molecular_function | chloride channel activity |
A | 0005260 | molecular_function | intracellularly ATP-gated chloride channel activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005765 | cellular_component | lysosomal membrane |
A | 0005768 | cellular_component | endosome |
A | 0005769 | cellular_component | early endosome |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006695 | biological_process | cholesterol biosynthetic process |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006821 | biological_process | chloride transport |
A | 0006833 | biological_process | water transport |
A | 0006904 | biological_process | vesicle docking involved in exocytosis |
A | 0009986 | cellular_component | cell surface |
A | 0010008 | cellular_component | endosome membrane |
A | 0015106 | molecular_function | bicarbonate transmembrane transporter activity |
A | 0015108 | molecular_function | chloride transmembrane transporter activity |
A | 0015701 | biological_process | bicarbonate transport |
A | 0016020 | cellular_component | membrane |
A | 0016323 | cellular_component | basolateral plasma membrane |
A | 0016324 | cellular_component | apical plasma membrane |
A | 0016853 | molecular_function | isomerase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0017081 | molecular_function | chloride channel regulator activity |
A | 0019869 | molecular_function | chloride channel inhibitor activity |
A | 0019899 | molecular_function | enzyme binding |
A | 0030165 | molecular_function | PDZ domain binding |
A | 0030301 | biological_process | cholesterol transport |
A | 0030660 | cellular_component | Golgi-associated vesicle membrane |
A | 0030669 | cellular_component | clathrin-coated endocytic vesicle membrane |
A | 0031901 | cellular_component | early endosome membrane |
A | 0032991 | cellular_component | protein-containing complex |
A | 0034220 | biological_process | monoatomic ion transmembrane transport |
A | 0034707 | cellular_component | chloride channel complex |
A | 0034976 | biological_process | response to endoplasmic reticulum stress |
A | 0035377 | biological_process | transepithelial water transport |
A | 0035774 | biological_process | positive regulation of insulin secretion involved in cellular response to glucose stimulus |
A | 0043225 | molecular_function | ATPase-coupled inorganic anion transmembrane transporter activity |
A | 0045921 | biological_process | positive regulation of exocytosis |
A | 0048240 | biological_process | sperm capacitation |
A | 0050891 | biological_process | multicellular organismal-level water homeostasis |
A | 0051087 | molecular_function | protein-folding chaperone binding |
A | 0051454 | biological_process | intracellular pH elevation |
A | 0051649 | biological_process | establishment of localization in cell |
A | 0055037 | cellular_component | recycling endosome |
A | 0055038 | cellular_component | recycling endosome membrane |
A | 0055085 | biological_process | transmembrane transport |
A | 0060081 | biological_process | membrane hyperpolarization |
A | 0065008 | biological_process | regulation of biological quality |
A | 0070175 | biological_process | positive regulation of enamel mineralization |
A | 0071320 | biological_process | cellular response to cAMP |
A | 0071889 | molecular_function | 14-3-3 protein binding |
A | 0097186 | biological_process | amelogenesis |
A | 0098660 | biological_process | inorganic ion transmembrane transport |
A | 0106138 | molecular_function | Sec61 translocon complex binding |
A | 0140359 | molecular_function | ABC-type transporter activity |
A | 1902476 | biological_process | chloride transmembrane transport |
A | 1902943 | biological_process | positive regulation of voltage-gated chloride channel activity |
A | 1904322 | biological_process | cellular response to forskolin |
Functional Information from PROSITE/UniProt
site_id | PS00211 |
Number of Residues | 15 |
Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV |
Chain | Residue | Details |
A | LEU548-VAL562 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 23 |
Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 212 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 25 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 18 |
Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Discontinuously helical; Name=8","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15528182","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20150177","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XMJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PZE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PZF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PZG","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15528182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XMJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBT","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15528182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBS","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"3GD7","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3GD7","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"22119790","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |