8J8I
Membrane-bound structure of CD3z cytoplasmic domain
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0002250 | biological_process | adaptive immune response |
A | 0004888 | molecular_function | transmembrane signaling receptor activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005886 | cellular_component | plasma membrane |
A | 0007166 | biological_process | cell surface receptor signaling pathway |
A | 0033001 | cellular_component | Fc-gamma receptor III complex |
A | 0038094 | biological_process | Fc-gamma receptor signaling pathway |
A | 0042101 | cellular_component | T cell receptor complex |
A | 0042105 | cellular_component | alpha-beta T cell receptor complex |
A | 0042106 | cellular_component | gamma-delta T cell receptor complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046629 | biological_process | gamma-delta T cell activation |
A | 0046631 | biological_process | alpha-beta T cell activation |
A | 0046982 | molecular_function | protein heterodimerization activity |
A | 0050852 | biological_process | T cell receptor signaling pathway |
A | 0051259 | biological_process | protein complex oligomerization |
A | 0065003 | biological_process | protein-containing complex assembly |
A | 0098797 | cellular_component | plasma membrane protein complex |
A | 1990782 | molecular_function | protein tyrosine kinase binding |
A | 2000010 | biological_process | positive regulation of protein localization to cell surface |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | LEU7-LEU27 |
site_id | SWS_FT_FI2 |
Number of Residues | 112 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | ARG28-ARG140 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:15144186 |
Chain | Residue | Details |
A | SER34 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15144186, ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | TYR40 | |
A | TYR48 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:12522270 |
Chain | Residue | Details |
A | TYR59 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:12522270, ECO:0007744|PubMed:15144186, ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | TYR87 | |
A | TYR118 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | TYR99 | |
A | TYR129 |