Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
E | 0000166 | molecular_function | nucleotide binding |
E | 0004672 | molecular_function | protein kinase activity |
E | 0004679 | molecular_function | AMP-activated protein kinase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005634 | cellular_component | nucleus |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0006629 | biological_process | lipid metabolic process |
E | 0006631 | biological_process | fatty acid metabolic process |
E | 0006633 | biological_process | fatty acid biosynthetic process |
E | 0010628 | biological_process | positive regulation of gene expression |
E | 0016208 | molecular_function | AMP binding |
E | 0019887 | molecular_function | protein kinase regulator activity |
E | 0019901 | molecular_function | protein kinase binding |
E | 0031588 | cellular_component | nucleotide-activated protein kinase complex |
E | 0031669 | biological_process | cellular response to nutrient levels |
E | 0032991 | cellular_component | protein-containing complex |
E | 0043531 | molecular_function | ADP binding |
E | 0044877 | molecular_function | protein-containing complex binding |
E | 0051170 | biological_process | import into nucleus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AMP E 1325 |
Chain | Residue |
E | ARG69 |
E | VAL296 |
E | HIS297 |
E | ARG298 |
E | LYS169 |
E | ILE239 |
E | SER241 |
E | PHE243 |
E | ASP244 |
E | ARG268 |
E | VAL275 |
E | LEU276 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AMP E 1326 |
Chain | Residue |
E | HIS150 |
E | THR199 |
E | ILE203 |
E | ALA204 |
E | VAL224 |
E | SER225 |
E | ALA226 |
E | HIS297 |
E | ILE311 |
E | SER313 |
E | SER315 |
E | ASP316 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE STU A 1550 |
Chain | Residue |
A | LEU22 |
A | GLY23 |
A | VAL24 |
A | GLY25 |
A | ALA43 |
A | LYS45 |
A | MET93 |
A | GLU94 |
A | TYR95 |
A | VAL96 |
A | GLY99 |
A | GLU100 |
A | GLU143 |
A | ASN144 |
A | LEU146 |
A | ASP157 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK |
Chain | Residue | Details |
A | LEU22-LYS45 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL |
Chain | Residue | Details |
A | VAL135-LEU147 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 |
Chain | Residue | Details |
E | ARG69 | |
E | MET84 | |
E | VAL129 | |
E | ARG151 | |
E | LYS169 | |
E | SER241 | |
E | ARG268 | |
E | LEU276 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L |
Chain | Residue | Details |
E | HIS150 | |
E | THR199 | |
E | ALA204 | |
E | SER225 | |
E | HIS297 | |
E | SER313 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 |
Chain | Residue | Details |
E | SER260 | |
A | THR344 | |
A | THR371 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634 |
Chain | Residue | Details |
E | THR262 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:21460634 |
Chain | Residue | Details |
E | SER269 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q13131 |
Chain | Residue | Details |
A | SER345 | |
A | SER456 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 |
Chain | Residue | Details |
A | SER349 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634 |
Chain | Residue | Details |
A | THR357 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:21460634 |
Chain | Residue | Details |
A | SER386 |