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 | 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 | 0006110 | biological_process | regulation of glycolytic process |
| E | 0006629 | biological_process | lipid metabolic process |
| E | 0006631 | biological_process | fatty acid metabolic process |
| E | 0006633 | biological_process | fatty acid biosynthetic process |
| 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 | 0042149 | biological_process | cellular response to glucose starvation |
| E | 0043531 | molecular_function | ADP binding |
| E | 0044877 | molecular_function | protein-containing complex binding |
| E | 0045722 | biological_process | positive regulation of gluconeogenesis |
| E | 0050790 | biological_process | regulation of catalytic activity |
| 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 | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q13131","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by LKB1 and CaMKK2","evidences":[{"source":"PubMed","id":"14511394","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14614828","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16054095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16054096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8910387","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"12764152","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q13131","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 60 |
| Details | Domain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 62 |
| Details | Domain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 62 |
| Details | Domain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 21 |
| Details | Motif: {"description":"AMPK pseudosubstrate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V92","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21399626","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V8Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y8L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






