Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006338 | biological_process | chromatin remodeling |
A | 0006468 | biological_process | protein phosphorylation |
A | 0006970 | biological_process | response to osmotic stress |
A | 0009414 | biological_process | response to water deprivation |
A | 0009536 | cellular_component | plastid |
A | 0009651 | biological_process | response to salt stress |
A | 0009737 | biological_process | response to abscisic acid |
A | 0009738 | biological_process | abscisic acid-activated signaling pathway |
A | 0009739 | biological_process | response to gibberellin |
A | 0010029 | biological_process | regulation of seed germination |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0044024 | molecular_function | histone H2AS1 kinase activity |
A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CO A 362 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CO A 363 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CO A 364 |
Chain | Residue |
A | GLN136 |
A | ILE137 |
A | CYS138 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGNFGVARlMrdkltkel..........VAVK |
Chain | Residue | Details |
A | ILE28-LYS51 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IcHrDLKleNTLL |
Chain | Residue | Details |
A | ILE137-LEU149 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP141 | |
Chain | Residue | Details |
A | ILE28 | |
A | LYS51 | |