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 PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGQYGEVYeGvwkkyslt..........VAVK |
Chain | Residue | Details |
A | LEU267-LYS290 | |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV |
Chain | Residue | Details |
A | PHE378-VAL390 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP382 | |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU267 | |
A | LYS290 | |
A | GLU335 | |
Chain | Residue | Details |
A | SER248 | |
Chain | Residue | Details |
A | TYR272 | |
A | TYR276 | |
A | TYR432 | |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036 |
Chain | Residue | Details |
A | TYR412 | |
Chain | Residue | Details |
A | SER465 | |