7F4U
Cryo-EM structure of TELO2-TTI1-TTI2 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0000781 | cellular_component | chromosome, telomeric region | 
| A | 0005515 | molecular_function | protein binding | 
| A | 0005634 | cellular_component | nucleus | 
| A | 0005737 | cellular_component | cytoplasm | 
| A | 0005829 | cellular_component | cytosol | 
| A | 0016020 | cellular_component | membrane | 
| A | 0016604 | cellular_component | nuclear body | 
| A | 0019900 | molecular_function | kinase binding | 
| A | 0019901 | molecular_function | protein kinase binding | 
| A | 0042162 | molecular_function | telomeric DNA binding | 
| A | 0044877 | molecular_function | protein-containing complex binding | 
| A | 0050821 | biological_process | protein stabilization | 
| A | 0051083 | biological_process | 'de novo' cotranslational protein folding | 
| A | 0051879 | molecular_function | Hsp90 protein binding | 
| A | 0060090 | molecular_function | molecular adaptor activity | 
| A | 0110078 | cellular_component | TTT Hsp90 cochaperone complex | 
| A | 0140777 | molecular_function | protein-containing complex stabilizing activity | 
| A | 2000003 | biological_process | positive regulation of DNA damage checkpoint | 
| B | 0005515 | molecular_function | protein binding | 
| B | 0005634 | cellular_component | nucleus | 
| B | 0005737 | cellular_component | cytoplasm | 
| B | 0019900 | molecular_function | kinase binding | 
| B | 0031931 | cellular_component | TORC1 complex | 
| B | 0031932 | cellular_component | TORC2 complex | 
| B | 0032006 | biological_process | regulation of TOR signaling | 
| B | 0050821 | biological_process | protein stabilization | 
| B | 0110078 | cellular_component | TTT Hsp90 cochaperone complex | 
| B | 0140777 | molecular_function | protein-containing complex stabilizing activity | 
| B | 2000003 | biological_process | positive regulation of DNA damage checkpoint | 
| C | 0110078 | cellular_component | TTT Hsp90 cochaperone complex | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 3 | 
| Details | Modified residue: {"description":"Hydroxyproline","evidences":[{"source":"PubMed","id":"22797300","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 26 | 
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 10 | 
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 1 | 
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI5 | 
| Number of Residues | 1 | 
| Details | Modified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"PubMed","id":"23263282","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 











