8EWY
Structure of Janus Kinase (JAK) dimer complexed with cytokine receptor intracellular domain
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 | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0016020 | cellular_component | membrane |
| A | 0035556 | biological_process | intracellular signal transduction |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0016020 | cellular_component | membrane |
| B | 0035556 | biological_process | intracellular signal transduction |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 28 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGHFGKVElCrydpegdntgeq......VAVK |
| Chain | Residue | Details |
| A | LEU880-LYS907 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNVLV |
| Chain | Residue | Details |
| A | TYR998-VAL1010 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 556 |
| Details | Domain: {"description":"Protein kinase 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P23458","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"P23458","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
