Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004713 | molecular_function | protein tyrosine kinase activity |
A | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
A | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 8LN A 2284 |
Chain | Residue |
A | PHE981 |
A | SER982 |
A | LEU1005 |
A | VAL1013 |
A | ALA1031 |
A | GLU1080 |
A | MET1082 |
A | GLY1085 |
A | HOH2061 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 29 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGvakgvvkdepetr.....VAIK |
Chain | Residue | Details |
A | LEU1005-LYS1033 | |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV |
Chain | Residue | Details |
A | PHE1131-VAL1143 | |
site_id | PS00239 |
Number of Residues | 9 |
Details | RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR |
Chain | Residue | Details |
A | ASP1159-ARG1167 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP1135 | |
Chain | Residue | Details |
A | LEU1005 | |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS1033 | |
Chain | Residue | Details |
A | TYR980 | |
Chain | Residue | Details |
A | TYR1161 | |
A | TYR1165 | |
A | TYR1166 | |
Chain | Residue | Details |
A | SER1278 | |
Chain | Residue | Details |
A | SER1282 | |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:21994939 |
Chain | Residue | Details |
A | LYS1168 | |
A | LYS1171 | |