6ES6
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003713 | molecular_function | transcription coactivator activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0016922 | molecular_function | nuclear receptor binding |
| B | 0000123 | cellular_component | histone acetyltransferase complex |
| B | 0003713 | molecular_function | transcription coactivator activity |
| B | 0004402 | molecular_function | histone acetyltransferase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
