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 | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue 25Q A 1001 |
Chain | Residue |
A | ALA651 |
A | SER763 |
A | LYS653 |
A | GLU670 |
A | ILE697 |
A | THR699 |
A | GLU700 |
A | TYR701 |
A | MET702 |
A | LEU753 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 27 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGAGEFGEVCsGrlklpskkeis.......VAIK |
Chain | Residue | Details |
A | VAL627-LYS653 | |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNILI |
Chain | Residue | Details |
A | TYR742-ILE754 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | Binding site: {} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"18547520","evidenceCode":"ECO:0000269"}]} |