8ZGT
Structure of the ige-fc bound to its high affinity receptor fc(epsilon)ri state3
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0005768 | cellular_component | endosome |
B | 0005886 | cellular_component | plasma membrane |
B | 0006955 | biological_process | immune response |
B | 0007165 | biological_process | signal transduction |
B | 0007166 | biological_process | cell surface receptor signaling pathway |
B | 0009897 | cellular_component | external side of plasma membrane |
B | 0016020 | cellular_component | membrane |
B | 0019863 | molecular_function | IgE binding |
B | 0019901 | molecular_function | protein kinase binding |
B | 0032998 | cellular_component | Fc-epsilon receptor I complex |
B | 0042169 | molecular_function | SH2 domain binding |
B | 0043306 | biological_process | positive regulation of mast cell degranulation |
B | 0051219 | molecular_function | phosphoprotein binding |
B | 0051279 | biological_process | regulation of release of sequestered calcium ion into cytosol |
C | 0004888 | molecular_function | transmembrane signaling receptor activity |
C | 0007166 | biological_process | cell surface receptor signaling pathway |
C | 0016020 | cellular_component | membrane |
C | 0019767 | molecular_function | IgE receptor activity |
C | 0032998 | cellular_component | Fc-epsilon receptor I complex |
G | 0004888 | molecular_function | transmembrane signaling receptor activity |
G | 0007166 | biological_process | cell surface receptor signaling pathway |
G | 0016020 | cellular_component | membrane |
G | 0019767 | molecular_function | IgE receptor activity |
G | 0032998 | cellular_component | Fc-epsilon receptor I complex |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YQCRVDH |
Chain | Residue | Details |
E | TYR287-HIS293 | |
E | PHE394-HIS400 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 134 |
Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 75 |
Details | Domain: {"description":"Ig-like 1"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 68 |
Details | Domain: {"description":"Ig-like 2"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 45 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 12 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 196 |
Details | Domain: {"description":"Ig-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 200 |
Details | Domain: {"description":"Ig-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 200 |
Details | Domain: {"description":"Ig-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |