4B2T
The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| a | 0005524 | molecular_function | ATP binding |
| a | 0005813 | cellular_component | centrosome |
| a | 0005829 | cellular_component | cytosol |
| a | 0005832 | cellular_component | chaperonin-containing T-complex |
| a | 0006457 | biological_process | protein folding |
| a | 0016887 | molecular_function | ATP hydrolysis activity |
| a | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005813 | cellular_component | centrosome |
| A | 0005829 | cellular_component | cytosol |
| A | 0005832 | cellular_component | chaperonin-containing T-complex |
| A | 0006457 | biological_process | protein folding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| 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 | 0016887 | molecular_function | ATP hydrolysis activity |
| b | 0031625 | molecular_function | ubiquitin protein ligase binding |
| b | 0044183 | molecular_function | protein folding chaperone |
| b | 0050821 | biological_process | protein stabilization |
| b | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| b | 1904874 | biological_process | positive regulation of telomerase RNA localization to Cajal body |
| 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 | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0031625 | molecular_function | ubiquitin protein ligase binding |
| B | 0044183 | molecular_function | protein folding chaperone |
| B | 0050821 | biological_process | protein stabilization |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 1904874 | biological_process | positive regulation of telomerase RNA localization to Cajal body |
| d | 0005524 | molecular_function | ATP binding |
| d | 0005737 | cellular_component | cytoplasm |
| d | 0005813 | cellular_component | centrosome |
| d | 0005832 | cellular_component | chaperonin-containing T-complex |
| d | 0006457 | biological_process | protein folding |
| d | 0016887 | molecular_function | ATP hydrolysis activity |
| d | 0042470 | cellular_component | melanosome |
| d | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005813 | cellular_component | centrosome |
| D | 0005832 | cellular_component | chaperonin-containing T-complex |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0042470 | cellular_component | melanosome |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| e | 0003730 | molecular_function | mRNA 3'-UTR binding |
| e | 0005515 | molecular_function | protein binding |
| e | 0005524 | molecular_function | ATP binding |
| e | 0005813 | cellular_component | centrosome |
| e | 0005832 | cellular_component | chaperonin-containing T-complex |
| e | 0005874 | cellular_component | microtubule |
| e | 0006457 | biological_process | protein folding |
| e | 0009615 | biological_process | response to virus |
| e | 0016887 | molecular_function | ATP hydrolysis activity |
| e | 0031681 | molecular_function | G-protein beta-subunit binding |
| e | 0044183 | molecular_function | protein folding chaperone |
| e | 0048027 | molecular_function | mRNA 5'-UTR binding |
| e | 0048487 | molecular_function | beta-tubulin binding |
| e | 0050821 | biological_process | protein stabilization |
| e | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| E | 0003730 | molecular_function | mRNA 3'-UTR binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005813 | cellular_component | centrosome |
| E | 0005832 | cellular_component | chaperonin-containing T-complex |
| E | 0005874 | cellular_component | microtubule |
| E | 0006457 | biological_process | protein folding |
| E | 0009615 | biological_process | response to virus |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0031681 | molecular_function | G-protein beta-subunit binding |
| E | 0044183 | molecular_function | protein folding chaperone |
| E | 0048027 | molecular_function | mRNA 5'-UTR binding |
| E | 0048487 | molecular_function | beta-tubulin binding |
| E | 0050821 | biological_process | protein stabilization |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| g | 0005524 | molecular_function | ATP binding |
| g | 0005737 | cellular_component | cytoplasm |
| g | 0005832 | cellular_component | chaperonin-containing T-complex |
| g | 0005874 | cellular_component | microtubule |
| g | 0006457 | biological_process | protein folding |
| g | 0016887 | molecular_function | ATP hydrolysis activity |
| g | 0044183 | molecular_function | protein folding chaperone |
| g | 0050821 | biological_process | protein stabilization |
| g | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005832 | cellular_component | chaperonin-containing T-complex |
| G | 0005874 | cellular_component | microtubule |
| G | 0006457 | biological_process | protein folding |
| G | 0016887 | molecular_function | ATP hydrolysis activity |
| G | 0044183 | molecular_function | protein folding chaperone |
| G | 0050821 | biological_process | protein stabilization |
| G | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| h | 0005515 | molecular_function | protein binding |
| h | 0005524 | molecular_function | ATP binding |
| h | 0005737 | cellular_component | cytoplasm |
| h | 0005832 | cellular_component | chaperonin-containing T-complex |
| h | 0005874 | cellular_component | microtubule |
| h | 0006457 | biological_process | protein folding |
| h | 0016887 | molecular_function | ATP hydrolysis activity |
| h | 0044183 | molecular_function | protein folding chaperone |
| h | 0050821 | biological_process | protein stabilization |
| h | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| H | 0005515 | molecular_function | protein binding |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005832 | cellular_component | chaperonin-containing T-complex |
| H | 0005874 | cellular_component | microtubule |
| H | 0006457 | biological_process | protein folding |
| H | 0016887 | molecular_function | ATP hydrolysis activity |
| H | 0044183 | molecular_function | protein folding chaperone |
| H | 0050821 | biological_process | protein stabilization |
| H | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| q | 0005524 | molecular_function | ATP binding |
| q | 0005737 | cellular_component | cytoplasm |
| q | 0005813 | cellular_component | centrosome |
| q | 0005832 | cellular_component | chaperonin-containing T-complex |
| q | 0006457 | biological_process | protein folding |
| q | 0016887 | molecular_function | ATP hydrolysis activity |
| q | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| Q | 0005524 | molecular_function | ATP binding |
| Q | 0005737 | cellular_component | cytoplasm |
| Q | 0005813 | cellular_component | centrosome |
| Q | 0005832 | cellular_component | chaperonin-containing T-complex |
| Q | 0006457 | biological_process | protein folding |
| Q | 0016887 | molecular_function | ATP hydrolysis activity |
| Q | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| z | 0005524 | molecular_function | ATP binding |
| z | 0005737 | cellular_component | cytoplasm |
| z | 0005832 | cellular_component | chaperonin-containing T-complex |
| z | 0005874 | cellular_component | microtubule |
| z | 0006457 | biological_process | protein folding |
| z | 0016887 | molecular_function | ATP hydrolysis activity |
| z | 0044183 | molecular_function | protein folding chaperone |
| z | 0050821 | biological_process | protein stabilization |
| z | 0071987 | molecular_function | WD40-repeat domain binding |
| z | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| Z | 0005524 | molecular_function | ATP binding |
| Z | 0005737 | cellular_component | cytoplasm |
| Z | 0005832 | cellular_component | chaperonin-containing T-complex |
| Z | 0005874 | cellular_component | microtubule |
| Z | 0006457 | biological_process | protein folding |
| Z | 0016887 | molecular_function | ATP hydrolysis activity |
| Z | 0044183 | molecular_function | protein folding chaperone |
| Z | 0050821 | biological_process | protein stabilization |
| Z | 0071987 | molecular_function | WD40-repeat domain binding |
| Z | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
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 | VAL95-LYS120 |
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AIADTGANVVVT |
| Chain | Residue | Details |
| Q | ALA282-THR293 |
| site_id | PS00750 |
| Number of Residues | 13 |
| Details | TCP1_1 Chaperonins TCP-1 signature 1. KStLGPkGmdKIL |
| Chain | Residue | Details |
| B | LYS40-LEU52 | |
| Q | ARG44-VAL56 | |
| G | ARG38-LEU50 | |
| Z | ARG35-LEU47 | |
| A | LYS33-LEU45 | |
| E | LYS49-MET61 | |
| D | ARG52-ILE64 | |
| H | ARG37-ILE49 |
| site_id | PS00751 |
| Number of Residues | 17 |
| Details | TCP1_2 Chaperonins TCP-1 signature 2. VTNDGATILknIgVdNP |
| Chain | Residue | Details |
| B | VAL63-PRO79 | |
| Q | VAL65-PRO81 | |
| G | MET59-PRO75 | |
| Z | LEU56-PRO72 | |
| A | ILE54-PRO70 | |
| E | VAL70-GLN86 | |
| D | ILE73-PRO89 | |
| H | ILE58-PRO74 |
| site_id | PS00995 |
| Number of Residues | 9 |
| Details | TCP1_3 Chaperonins TCP-1 signature 3. QDdeVGDGT |
| Chain | Residue | Details |
| B | GLN91-THR99 | |
| Q | GLN93-THR101 | |
| G | GLN87-THR95 | |
| Z | GLN84-THR92 | |
| A | GLN82-THR90 | |
| E | GLN98-THR106 | |
| D | GLN101-THR109 | |
| H | GLN86-THR94 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P17987","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P17987","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P17987","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17987","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11983","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P78371","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P78371","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P78371","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P50991","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P50991","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P80315","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50991","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P50991","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P80318","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q99832","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99832","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"Q99832","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P40227","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI30 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P80317","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI31 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P40227","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI32 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P40227","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
