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 | 0005694 | cellular_component | chromosome |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016020 | cellular_component | membrane |
| A | 0016604 | cellular_component | nuclear body |
| 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 | 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 | 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 | 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 | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| B | SER464 | |
| A | SER491 | |
| A | ASP492 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:23263282, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| B | SER828 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | MOD_RES: Hydroxyproline => ECO:0000269|PubMed:22797300 |
| Chain | Residue | Details |
| A | PRO374 | |
| A | PRO419 | |
| A | PRO422 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9DC40 |
| Chain | Residue | Details |
| A | SER456 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:23263282 |
| Chain | Residue | Details |
| A | SER485 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:23263282 |
| Chain | Residue | Details |
| A | SER487 | |
| A | SER491 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| A | SER688 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER836 |
