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Literature summary extracted from
- The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring (2018), Biochem. J., 475, 3009-3034 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | drug development | development of cell-based CCT inhibitors using peptide reagents and HSF1A, a benzyl-pyrazole-based small molecule | Candida albicans |
| 3.6.4.B10 | medicine | subunit CCT2 is a chemotherapeutic target in uterine cancer | Homo sapiens |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.6.4.B10 | gene CCT1-8, cloning of mouse testis CCT genes | Mus musculus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.6.4.B10 | homology model of the FAB1 apical domain and the top scoring model was with the 2.2 A resolution mouse CCTgamma apical domain template, PDB ID 1GML | Mus musculus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | C450Y | naturally occuring mutation in subunit CCT4 | Rattus norvegicus |
| 3.6.4.B10 | H147R | naturally occuring mutation of subunit CCT5 | Homo sapiens |
| 5.6.1.7 | H147R | the mutation is associated with hereditary sensory neuropathies | Homo sapiens |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Bos taurus | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Homo sapiens | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Saccharomyces cerevisiae | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Mus musculus | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Drosophila melanogaster | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Danio rerio | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Dictyostelium discoideum | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Caenorhabditis elegans | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Rattus norvegicus | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Arabidopsis thaliana | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Plasmodium falciparum | |
| 3.6.4.B10 | additional information | - |
additional information | chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics | Candida albicans |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.6.4.B10 | basement membrane | - |
Caenorhabditis elegans | 5604 | - |
| 3.6.4.B10 | cytosol | - |
Bos taurus | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Homo sapiens | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Mus musculus | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Drosophila melanogaster | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Danio rerio | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Dictyostelium discoideum | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Caenorhabditis elegans | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Rattus norvegicus | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Arabidopsis thaliana | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Plasmodium falciparum | 5829 | - |
| 3.6.4.B10 | cytosol | - |
Candida albicans | 5829 | - |
| 3.6.4.B10 | microvillus | - |
Caenorhabditis elegans | 5902 | - |
| 3.6.4.B10 | myofibril | - |
Danio rerio | 30016 | - |
| 3.6.4.B10 | sarcomere | - |
Danio rerio | 30017 | - |
| 5.6.1.7 | cytoplasm | - |
Homo sapiens | 5737 | - |
| 5.6.1.7 | nucleolus | - |
Homo sapiens | 5730 | - |
| 5.6.1.7 | plasma membrane | - |
Homo sapiens | 5886 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.4.B10 | Mg2+ | required | Bos taurus |  |
| 3.6.4.B10 | Mg2+ | required | Homo sapiens | |
| 3.6.4.B10 | Mg2+ | required | Saccharomyces cerevisiae | |
| 3.6.4.B10 | Mg2+ | required | Mus musculus | |
| 3.6.4.B10 | Mg2+ | required | Drosophila melanogaster | |
| 3.6.4.B10 | Mg2+ | required | Danio rerio | |
| 3.6.4.B10 | Mg2+ | required | Dictyostelium discoideum | |
| 3.6.4.B10 | Mg2+ | required | Caenorhabditis elegans | |
| 3.6.4.B10 | Mg2+ | required | Rattus norvegicus | |
| 3.6.4.B10 | Mg2+ | required | Arabidopsis thaliana | |
| 3.6.4.B10 | Mg2+ | required | Plasmodium falciparum | |
| 3.6.4.B10 | Mg2+ | required | Candida albicans | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.4.B10 | ATP + H2O | Bos taurus | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Homo sapiens | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Saccharomyces cerevisiae | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Mus musculus | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Drosophila melanogaster | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Danio rerio | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Dictyostelium discoideum | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Caenorhabditis elegans | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Rattus norvegicus | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Arabidopsis thaliana | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Plasmodium falciparum | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Candida albicans | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Rattus norvegicus Sprague-Dawley | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Candida albicans ATCC MYA-2876 | - |
ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | Saccharomyces cerevisiae ATCC 204508 | - |
ADP + phosphate | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded actin | Mus musculus | - |
ATP + H2O + folded actin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded actin | Homo sapiens | - |
ATP + H2O + folded actin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded actin | Saccharomyces cerevisiae | - |
ATP + H2O + folded actin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded actin | Bos taurus | - |
ATP + H2O + folded actin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded tubulin | Mus musculus | - |
ATP + H2O + folded tubulin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded tubulin | Homo sapiens | - |
ATP + H2O + folded tubulin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded tubulin | Saccharomyces cerevisiae | - |
ATP + H2O + folded tubulin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded tubulin | Bos taurus | - |
ATP + H2O + folded tubulin | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.6.4.B10 | Arabidopsis thaliana | P28769 AND Q940P8 AND Q84WV1 AND Q9LV21 AND O04450 AND Q9M888 AND Q9SF16 AND Q94K05 | genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Bos taurus | Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9 | genes CCT1-5, 6A, 7, and 8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Caenorhabditis elegans | P41988 AND P47207 AND Q9N4J8 AND P47208 AND P47209 AND P46550 AND Q9TZS5 AND Q9N358 | genes cct-1 to cct-8 encoding subunits TCP-1-alpha, TCP-1-beta, TCP-1-gamma, TCP-1-delta, TCP-1-epsilon, TCP-1-zeta, TCP-1-eta, and TCP-1-theta | - |
| 3.6.4.B10 | Candida albicans | Q59QB7 AND Q59YC4 AND Q5AK16 AND Q59Z12 AND A0A1D8PMN9 AND Q59YH4 AND P47828 | genes CCT1-5, and 6-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Candida albicans ATCC MYA-2876 | Q59QB7 AND Q59YC4 AND Q5AK16 AND Q59Z12 AND A0A1D8PMN9 AND Q59YH4 AND P47828 | genes CCT1-5, and 6-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Danio rerio | Q9PW76 AND Q6PBW6 AND Q7T2P2 AND Q6P123 AND Q6NVI6 AND E9QGU4 AND B3DKJ0 AND A0A0R4IJT8 | genes CCT1-5, 6a, 7, and 8 encoding subunits CCT-alpha (TCP-1 protein), CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Dictyostelium discoideum | Q55BM4 AND Q54ES9 AND Q54TH8 AND Q54CL2 AND Q54TD3 AND Q76NU3 AND Q54ER7 AND Q552J0 | genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon or CCT5 isoform A, CCT-zeta, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Drosophila melanogaster | P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0 | genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon or CCT5 isoform A, CCT-zeta, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Homo sapiens | P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990 | genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Mus musculus | P11983 AND P80314 AND P80318 AND P80315 AND P80316 AND P80317 AND P80313 AND P42932 | genes CCT1-8 encoding subunits TCP-1-alpha, TCP-1-beta, TCP-1-gamma, TCP-1-delta, TCP-1-epsilon, TCP-1-zeta, TCP-1-eta, and TCP-1-theta | - |
| 3.6.4.B10 | Plasmodium falciparum | Q8II43 AND O97247 AND Q8I5C4 AND C0H5I7 AND O97282 AND C6KST5 AND O77323 AND O96220 | genes encoding subunits alpha, beta, gamma, delta, epsilon, zeta, eta, and theta | - |
| 3.6.4.B10 | Rattus norvegicus | P28480 AND Q5XIM9 AND Q6P502 AND Q7TPB1 AND Q68FQ0 AND Q3MHS9 AND D4AC23 AND D4ACB8 | genes CCT1-5, 6A, 7, and 8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Rattus norvegicus Sprague-Dawley | P28480 AND Q5XIM9 AND Q6P502 AND Q7TPB1 AND Q68FQ0 AND Q3MHS9 AND D4AC23 AND D4ACB8 | genes CCT1-5, 6A, 7, and 8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Saccharomyces cerevisiae | P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079 | genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
| 3.6.4.B10 | Saccharomyces cerevisiae ATCC 204508 | P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079 | genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
| 5.6.1.7 | Bos taurus | - |
- |
- |
| 5.6.1.7 | Homo sapiens | - |
- |
- |
| 5.6.1.7 | Mus musculus | - |
- |
- |
| 5.6.1.7 | Saccharomyces cerevisiae | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.6.4.B10 | intestinal epithelium | - |
Caenorhabditis elegans | - |
| 3.6.4.B10 | skeletal muscle | - |
Danio rerio | - |
| 3.6.4.B10 | testis | - |
Mus musculus | - |
| 3.6.4.B10 | testis | - |
Danio rerio | - |
| 5.6.1.7 | breast | - |
Homo sapiens | - |
| 5.6.1.7 | kidney | - |
Homo sapiens | - |
| 5.6.1.7 | liver | - |
Homo sapiens | - |
| 5.6.1.7 | additional information | signaling of CCT in many different cancer types, review: breast cancer cell, glioma cell, colorectal cancer cell, head and neck cancer cell, lymphoma cell, uterine cancer cell, small cell lung cancer cell, hepatocellular cancer cell | Homo sapiens | - |
| 5.6.1.7 | testis | - |
Mus musculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.4.B10 | ATP + H2O | - |
Bos taurus | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Homo sapiens | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Saccharomyces cerevisiae | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Mus musculus | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Drosophila melanogaster | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Danio rerio | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Dictyostelium discoideum | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Caenorhabditis elegans | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Rattus norvegicus | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Arabidopsis thaliana | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Plasmodium falciparum | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Candida albicans | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Rattus norvegicus Sprague-Dawley | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Candida albicans ATCC MYA-2876 | ADP + phosphate | - |
? | |
| 3.6.4.B10 | ATP + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | ADP + phosphate | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded actin | - |
Mus musculus | ATP + H2O + folded actin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded actin | - |
Homo sapiens | ATP + H2O + folded actin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded actin | - |
Saccharomyces cerevisiae | ATP + H2O + folded actin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded actin | - |
Bos taurus | ATP + H2O + folded actin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded tubulin | - |
Mus musculus | ATP + H2O + folded tubulin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded tubulin | - |
Homo sapiens | ATP + H2O + folded tubulin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded tubulin | - |
Saccharomyces cerevisiae | ATP + H2O + folded tubulin | - |
? | |
| 5.6.1.7 | ADP + phosphate + unfolded tubulin | - |
Bos taurus | ATP + H2O + folded tubulin | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | heterohexadecamer | - |
Homo sapiens |
| 3.6.4.B10 | heterohexadecamer | - |
Rattus norvegicus |
| 3.6.4.B10 | More | both subunits CCT4 and CCT5 can be assembled into homomeric hexadecamers which allow them to be studied individually in the context of an assembled ring system | Homo sapiens |
| 3.6.4.B10 | More | both subunits CCT4 and CCT5 can be assembled into homomeric hexadecamers which allow them to be studied individually in the context of an assembled ring system | Rattus norvegicus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | CCT | - |
Bos taurus |
| 3.6.4.B10 | CCT | - |
Homo sapiens |
| 3.6.4.B10 | CCT | - |
Saccharomyces cerevisiae |
| 3.6.4.B10 | CCT | - |
Mus musculus |
| 3.6.4.B10 | CCT | - |
Drosophila melanogaster |
| 3.6.4.B10 | CCT | - |
Danio rerio |
| 3.6.4.B10 | CCT | - |
Dictyostelium discoideum |
| 3.6.4.B10 | CCT | - |
Caenorhabditis elegans |
| 3.6.4.B10 | CCT | - |
Rattus norvegicus |
| 3.6.4.B10 | CCT | - |
Arabidopsis thaliana |
| 3.6.4.B10 | CCT | - |
Plasmodium falciparum |
| 3.6.4.B10 | CCT | - |
Candida albicans |
| 3.6.4.B10 | CCT ATPase | - |
Bos taurus |
| 3.6.4.B10 | CCT ATPase | - |
Homo sapiens |
| 3.6.4.B10 | CCT ATPase | - |
Saccharomyces cerevisiae |
| 3.6.4.B10 | CCT ATPase | - |
Mus musculus |
| 3.6.4.B10 | CCT ATPase | - |
Drosophila melanogaster |
| 3.6.4.B10 | CCT ATPase | - |
Danio rerio |
| 3.6.4.B10 | CCT ATPase | - |
Dictyostelium discoideum |
| 3.6.4.B10 | CCT ATPase | - |
Caenorhabditis elegans |
| 3.6.4.B10 | CCT ATPase | - |
Rattus norvegicus |
| 3.6.4.B10 | CCT ATPase | - |
Arabidopsis thaliana |
| 3.6.4.B10 | CCT ATPase | - |
Plasmodium falciparum |
| 3.6.4.B10 | CCT ATPase | - |
Candida albicans |
| 3.6.4.B10 | CCT/TRiC | - |
Bos taurus |
| 3.6.4.B10 | CCT/TRiC | - |
Homo sapiens |
| 3.6.4.B10 | CCT/TRiC | - |
Saccharomyces cerevisiae |
| 3.6.4.B10 | CCT/TRiC | - |
Mus musculus |
| 3.6.4.B10 | CCT/TRiC | - |
Drosophila melanogaster |
| 3.6.4.B10 | CCT/TRiC | - |
Danio rerio |
| 3.6.4.B10 | CCT/TRiC | - |
Dictyostelium discoideum |
| 3.6.4.B10 | CCT/TRiC | - |
Caenorhabditis elegans |
| 3.6.4.B10 | CCT/TRiC | - |
Rattus norvegicus |
| 3.6.4.B10 | CCT/TRiC | - |
Arabidopsis thaliana |
| 3.6.4.B10 | CCT/TRiC | - |
Plasmodium falciparum |
| 3.6.4.B10 | CCT/TRiC | - |
Candida albicans |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Bos taurus |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Homo sapiens |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Saccharomyces cerevisiae |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Mus musculus |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Drosophila melanogaster |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Danio rerio |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Dictyostelium discoideum |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Caenorhabditis elegans |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Rattus norvegicus |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Arabidopsis thaliana |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Plasmodium falciparum |
| 3.6.4.B10 | eukaryotic chaperonin | - |
Candida albicans |
| 3.6.4.B10 | TCP-1 | - |
Bos taurus |
| 3.6.4.B10 | TCP-1 | - |
Homo sapiens |
| 3.6.4.B10 | TCP-1 | - |
Saccharomyces cerevisiae |
| 3.6.4.B10 | TCP-1 | - |
Mus musculus |
| 3.6.4.B10 | TCP-1 | - |
Drosophila melanogaster |
| 3.6.4.B10 | TCP-1 | - |
Danio rerio |
| 3.6.4.B10 | TCP-1 | - |
Dictyostelium discoideum |
| 3.6.4.B10 | TCP-1 | - |
Caenorhabditis elegans |
| 3.6.4.B10 | TCP-1 | - |
Rattus norvegicus |
| 3.6.4.B10 | TCP-1 | - |
Arabidopsis thaliana |
| 3.6.4.B10 | TCP-1 | - |
Plasmodium falciparum |
| 3.6.4.B10 | TCP-1 | - |
Candida albicans |
| 5.6.1.7 | CCT ATPase | - |
Mus musculus |
| 5.6.1.7 | CCT ATPase | - |
Homo sapiens |
| 5.6.1.7 | CCT ATPase | - |
Saccharomyces cerevisiae |
| 5.6.1.7 | CCT ATPase | - |
Bos taurus |
| 5.6.1.7 | CCT1 | subunit | Mus musculus |
| 5.6.1.7 | CCT1 | subunit | Homo sapiens |
| 5.6.1.7 | CCT1 | subunit | Saccharomyces cerevisiae |
| 5.6.1.7 | CCT1 | subunit | Bos taurus |
| 5.6.1.7 | CCT2 | subunit | Mus musculus |
| 5.6.1.7 | CCT2 | subunit | Homo sapiens |
| 5.6.1.7 | CCT2 | subunit | Saccharomyces cerevisiae |
| 5.6.1.7 | CCT2 | subunit | Bos taurus |
| 5.6.1.7 | CCT3 | subunit | Mus musculus |
| 5.6.1.7 | CCT3 | subunit | Homo sapiens |
| 5.6.1.7 | CCT3 | subunit | Saccharomyces cerevisiae |
| 5.6.1.7 | CCT3 | subunit | Bos taurus |
| 5.6.1.7 | CCT4 | subunit | Mus musculus |
| 5.6.1.7 | CCT4 | subunit | Homo sapiens |
| 5.6.1.7 | CCT4 | subunit | Saccharomyces cerevisiae |
| 5.6.1.7 | CCT4 | subunit | Bos taurus |
| 5.6.1.7 | CCT5 | subunit | Mus musculus |
| 5.6.1.7 | CCT5 | subunit | Homo sapiens |
| 5.6.1.7 | CCT5 | subunit | Saccharomyces cerevisiae |
| 5.6.1.7 | CCT5 | subunit | Bos taurus |
| 5.6.1.7 | CCT6 | subunit | Mus musculus |
| 5.6.1.7 | CCT6 | subunit | Homo sapiens |
| 5.6.1.7 | CCT6 | subunit | Saccharomyces cerevisiae |
| 5.6.1.7 | CCT6 | subunit | Bos taurus |
| 5.6.1.7 | CCT7 | subunit | Mus musculus |
| 5.6.1.7 | CCT7 | subunit | Homo sapiens |
| 5.6.1.7 | CCT7 | subunit | Saccharomyces cerevisiae |
| 5.6.1.7 | CCT7 | subunit | Bos taurus |
| 5.6.1.7 | CCT8 | subunit | Mus musculus |
| 5.6.1.7 | CCT8 | subunit | Homo sapiens |
| 5.6.1.7 | CCT8 | subunit | Saccharomyces cerevisiae |
| 5.6.1.7 | CCT8 | subunit | Bos taurus |
| 5.6.1.7 | chaperonin-containing TCP-1 | - |
Mus musculus |
| 5.6.1.7 | chaperonin-containing TCP-1 | - |
Homo sapiens |
| 5.6.1.7 | chaperonin-containing TCP-1 | - |
Saccharomyces cerevisiae |
| 5.6.1.7 | chaperonin-containing TCP-1 | - |
Bos taurus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.4.B10 | phosducin I | - |
Homo sapiens | |
| 3.6.4.B10 | phosducin I | - |
Dictyostelium discoideum | |
| 3.6.4.B10 | phosducin II | - |
Homo sapiens | |
| 3.6.4.B10 | phosducin II | - |
Saccharomyces cerevisiae | |
| 3.6.4.B10 | phosducin II | - |
Dictyostelium discoideum | |
| 3.6.4.B10 | phosducin III | - |
Homo sapiens | |
| 3.6.4.B10 | phosducin III | - |
Saccharomyces cerevisiae | |
| 3.6.4.B10 | phosducin III | - |
Dictyostelium discoideum | |
| 3.6.4.B10 | phosducin III | - |
Caenorhabditis elegans | |
| 3.6.4.B10 | phosducin-like cofactor protein | three different phosducin-like cofactor proteins | Plasmodium falciparum |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Bos taurus |
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Homo sapiens |
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Saccharomyces cerevisiae |
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Mus musculus |
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Drosophila melanogaster |
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Dictyostelium discoideum |
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Caenorhabditis elegans |
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Rattus norvegicus |
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Arabidopsis thaliana |
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Plasmodium falciparum |
| 3.6.4.B10 | evolution | co-evolution of CCT and the eukaryotic cytoskeleton, overview | Candida albicans |
| 3.6.4.B10 | evolution | three BBS proteins which have homology to chaperonins, BBS6, BBS10 and BBS12, and a sub-complex of CCT proteins (CCT1, 2, 3, 4, 5 and 8) mediate the association of two beta-propeller domain-containing proteins, BBS7 and BBS2, during the assembly process of the BBSome. BBS6, -10 and -12 are vertebrate-specific proteins and it may be an evolutionary connection that one of the two absent CCT subunits in the BBS-CCT complex, CCT6, has a vertebrate-specific isoform, CCT6B, which is abundant in testis CCT. CCT6 self-interacts across the CCT rings which probably permits isoform interchange, and therefore, it is possible that one of the BBS subunits has hijacked this mechanism and is able to slot into the CCT6 position in the CCT ring system. Co-evolution of CCT and the eukaryotic cytoskeleton, overview | Danio rerio |
| 3.6.4.B10 | malfunction | deletion of the phosducin III gene causes embryo division arrest with astral microtubule defects | Caenorhabditis elegans |
| 3.6.4.B10 | malfunction | gene deletion of the gene encoding cofactor phosducin I in Dictyostelium discoideum causes inhibition of G-protein signalling and Gbetagamma dimer formation, deletion of the phosducin II gene is lethal with cell division collapse after 5 days, while deletion of phosducin IIII gene causes no phenotype | Dictyostelium discoideum |
| 3.6.4.B10 | malfunction | knockdown of cct1 and cct2 in zebrafish leads to BBS-like phenotypes | Danio rerio |
| 3.6.4.B10 | malfunction | knockdown of the CCT8/theta subunit leads to a severe growth defect in asexual development but does not alter protein trafficking in the red blood cell compartment | Plasmodium falciparum |
| 3.6.4.B10 | malfunction | mutations of subunit CCT5 are involved in sensory neuropathy. Mutation C450Y of subunit CCT4 is involved in hereditary sensory neuropathies that show degeneration of the fibres in the sensory periphery neurons | Rattus norvegicus |
| 3.6.4.B10 | malfunction | mutations of subunit CCT5 are involved in sensory neuropathy. Mutation H147R of subunit CCT5 is involved in hereditary sensory neuropathies that show degeneration of the fibres in the sensory periphery neurons | Homo sapiens |
| 3.6.4.B10 | metabolism | CCT-actin system, overview | Bos taurus |
| 3.6.4.B10 | metabolism | CCT-actin system, overview | Homo sapiens |
| 3.6.4.B10 | metabolism | CCT-actin system, overview | Mus musculus |
| 3.6.4.B10 | metabolism | CCT-actin system, overview | Drosophila melanogaster |
| 3.6.4.B10 | metabolism | CCT-actin system, overview | Danio rerio |
| 3.6.4.B10 | metabolism | CCT-actin system, overview | Rattus norvegicus |
| 3.6.4.B10 | metabolism | CCT-actin system, overview. Interactions between CCT, actin and Plp2p in yeast: the actin map shows the CCT-binding sites, I, II and III and hinges, and the essential actin-binding D244 residue located in actin subdomain 4, which biochemically cross-links to the CCT8 subunit. Yeast actin (ACT1) binding to yeast CCT induces protease resistance in Cct4p and Cct8p. The PLP2 component shows its interactions with CCT subunits, CCT1, CCT4 and CCT8 | Saccharomyces cerevisiae |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview | Bos taurus |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview | Homo sapiens |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview | Drosophila melanogaster |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview | Danio rerio |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview | Dictyostelium discoideum |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview | Caenorhabditis elegans |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview | Rattus norvegicus |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview | Arabidopsis thaliana |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview | Candida albicans |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview. CCT protein recognition sequences and structure | Mus musculus |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview. The individual CCT subunits have different functions in cells. CCT-folding activity stalls at low ATP concentrations. Binding of the non-hydrolysable ATP analog adenosine 5'-(beta,gamma-imino)-triphosphate to the ternary complex leads to 3fold faster release of actin from CCT following the addition of ATP, suggesting a two-step folding process with a conformational change occurring upon closure of the cavity and a subsequent near-final folding step involving packing of the C-terminus to the native-like state. Proposed one-dimensional free-energy landscape for actin folding, overview. Actin folding and unfolding behaviour in vitro and thermodynamics | Saccharomyces cerevisiae |
| 3.6.4.B10 | additional information | structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview. The Plasmodium falciparum actin proteins are more divergent compared with other eukaryotic actins, about 80% homologous, and so are their eight CCT complex and three phosducin-like cofactor proteins. CCT subunits and actin and tubulin are ART molecular target(s) in the asexual stages of the malaria parasite | Plasmodium falciparum |
| 3.6.4.B10 | physiological function | CCT is a key modulator of echinocandin susceptibility | Candida albicans |
| 3.6.4.B10 | physiological function | subunit CCT1 is involved in fragile X-linked and cell identity, subunit CCT5 is required for autophagy | Drosophila melanogaster |
| 3.6.4.B10 | physiological function | subunit CCT5 is involved in thin filament assembly at the sarcomere Z-disk. Three BBS proteins which have homology to chaperonins, BBS6, BBS10 and BBS12, and a sub-complex of CCT proteins (CCT1, 2, 3, 4, 5 and 8) mediate the association of two beta-propeller domain-containing proteins, BBS7 and BBS2, during the assembly process of the BBSome. BBS6, -10 and -12 are vertebrate-specific proteins and it may be an evolutionary connection that one of the two absent CCT subunits in the BBS-CCT complex, CCT6, has a vertebrate-specific isoform, CCT6B, which is abundant in testis CCT. CCT6 self-interacts across the CCT rings which probably permits isoform interchange, and therefore, it is possible that one of the BBS subunits has hijacked this mechanism and is able to slot into the CCT6 position in the CCT ring system | Danio rerio |
| 3.6.4.B10 | physiological function | subunit CCT8 and the CCT complex are involved in Ras signalling and morphogenesis, and in the polarisome and cell polarity, respectively | Saccharomyces cerevisiae |
| 3.6.4.B10 | physiological function | subunits CCT1, CCT3, CCT4 and CCT8 are all essential for spermatogenesis. The CCT3/gamma domain in FAB1p is involved in autophagy | Mus musculus |
| 3.6.4.B10 | physiological function | subunits CCT2 and CCT7 interact with tumour suppressors p53 and VHL, respectively. The enzyme is involved in breast cancer signaling via STAT3, and in apoptosis via CCT2 and PDC5, or BAG3. Subunit CCT8 interacts with AML-ETO in leukemia. Subunits CCT2, 3, and 8 are involved in mRNA overexpression in cancer cells. Subunit CCT7 is involved in fibroblast motility. Subunits CCT2, 5, and 7 are required for autophagy. The CCT complex is involved in disassembly of the mitotic checkpoint, artherosclerosis, and cell survival, and in several other cellular processes, overview | Homo sapiens |
| 3.6.4.B10 | physiological function | the enzyme complex CCT is involved in stem cell identity and protein translocation | Arabidopsis thaliana |
| 3.6.4.B10 | physiological function | the enzyme is involved in invasion and lifespan extension | Caenorhabditis elegans |
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Release 2023.1 (January 2023)
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