Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004712 | molecular_function | protein serine/threonine/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 | 14 |
Details | binding site for residue CC9 A 501 |
Chain | Residue |
A | LYS153 |
A | LEU230 |
A | LEU231 |
A | LEU282 |
A | ASP295 |
A | PHE296 |
A | ILE155 |
A | PHE160 |
A | ALA176 |
A | LYS178 |
A | GLU193 |
A | ILE212 |
A | PHE228 |
A | GLU229 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue DTD A 502 |
Chain | Residue |
A | ILE155 |
A | ASN234 |
A | GLU279 |
A | HOH606 |
A | HOH619 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue PO4 A 503 |
Chain | Residue |
A | HIS56 |
A | HIS57 |
A | HIS174 |
A | HOH631 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for Ligand residues SEP A 59 through GLY A 60 bound to SER A 58 |
Chain | Residue |
A | HIS57 |
A | SER58 |
A | VAL61 |
A | TYR167 |
A | HIS172 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGQVVkAydhkvhqh..........VALK |
Chain | Residue | Details |
A | ILE155-LYS178 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHcDLKpeNILL |
Chain | Residue | Details |
A | ILE271-LEU283 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Motif: {"description":"Nuclear localization signal","evidences":[{"source":"PubMed","id":"19965871","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by MAP3K10","evidences":[{"source":"PubMed","id":"18455992","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"22998443","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by ATM","evidences":[{"source":"PubMed","id":"19965871","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by MAP3K10","evidences":[{"source":"PubMed","id":"18455992","evidenceCode":"ECO:0000269"}]} |