3KTT
Atomic model of bovine TRiC CCT2(beta) subunit derived from a 4.0 Angstrom cryo-EM map
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0002199 | cellular_component | zona pellucida receptor complex |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005832 | cellular_component | chaperonin-containing T-complex |
| B | 0005874 | cellular_component | microtubule |
| B | 0006457 | biological_process | protein folding |
| B | 0007339 | biological_process | binding of sperm to zona pellucida |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0031625 | molecular_function | ubiquitin protein ligase binding |
| B | 0032212 | biological_process | positive regulation of telomere maintenance via telomerase |
| B | 0044183 | molecular_function | protein folding chaperone |
| B | 0044297 | cellular_component | cell body |
| B | 0050821 | biological_process | protein stabilization |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| B | 0051131 | biological_process | chaperone-mediated protein complex assembly |
| B | 0061077 | biological_process | chaperone-mediated protein folding |
| B | 0090666 | biological_process | scaRNA localization to Cajal body |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 1904874 | biological_process | positive regulation of telomerase RNA localization to Cajal body |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 26 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGDGTTSVTVlAaellreaesl........IAKK |
| Chain | Residue | Details |
| B | VAL82-LYS107 |
| site_id | PS00750 |
| Number of Residues | 13 |
| Details | TCP1_1 Chaperonins TCP-1 signature 1. KStLGPkGmdKIL |
| Chain | Residue | Details |
| B | LYS27-LEU39 |
| site_id | PS00751 |
| Number of Residues | 17 |
| Details | TCP1_2 Chaperonins TCP-1 signature 2. VTNDGATILknIgVdNP |
| Chain | Residue | Details |
| B | VAL50-PRO66 |
| site_id | PS00995 |
| Number of Residues | 9 |
| Details | TCP1_3 Chaperonins TCP-1 signature 3. QDdeVGDGT |
| Chain | Residue | Details |
| B | GLN78-THR86 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P78371 |
| Chain | Residue | Details |
| B | SER47 | |
| B | SER247 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P78371 |
| Chain | Residue | Details |
| B | LYS141 | |
| B | LYS168 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P78371 |
| Chain | Residue | Details |
| B | THR248 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P78371 |
| Chain | Residue | Details |
| B | LYS235 |
