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Information on EC 3.6.4.B10 - chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)

for references in articles please use BRENDA:EC3.6.4.B10
preliminary BRENDA-supplied EC number
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UNIPROT: P28480 not found.
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Word Map
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Reaction Schemes
Synonyms
tcp-1, t-complex protein 1, cct complex, tric/cct, chaperonin containing tcp-1, eukaryotic chaperonin, cct/tric, cct chaperonin, chaperonin tric/cct, chaperonin tric, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha/beta-thermosome
-
-
archaeal chaperonin
-
CCT ATPase
CCT chaperonin
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
CCT complex
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
CCT/TRiC
CCT/TRiC chaperonin
CCT/TRiC complex
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
CCT2
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
chaperonin B
-
-
chaperonin containing t-complex polypeptide-1
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
-
chaperonin containing TCP-1
chaperonin containing TCP1
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
chaperonin TCP-1 ring complex
chaperonin TRiC
chaperonin TRiC/CCT
chaperonin-containing t-complex polypeptide 1
CtCCT
Thermochaetoides thermophila
-
-
cytosolic chaperonin TRiC
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
eukaryotic chaperone complex
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
eukaryotic chaperonin
eukaryotic chaperonin TRiC
eukaryotic group II chaperonin
GaTRiC
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
-
group II chaperonin
group II chaperonin CCT/TRiC
Thermochaetoides thermophila
-
-
HsTRiC
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
PfTRiC
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
PhCPN
Plasmodium TRiC
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
protein P45
-
-
T-complex polypeptide-1 ring complex
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
T-complex protein 1
T-complex protein 1 ring complex
T-complex protein-1 ring complex
TCP-1 ring complex
Thermochaetoides thermophila
-
-
TCP1
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
TCP1 ring complex
-
thermosome
TKS1-CPN
TRiC chaperonin
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
TRiC chaperonin complex
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
TRiC/CCT
type II chaperonin
additional information
ordered locus name: PH0017
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
CTP + H2O
CDP + phosphate
show the reaction diagram
GTP + H2O
GDP + phosphate
show the reaction diagram
UTP + H2O
UDP + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosducin I
-
phosducin II
-
phosducin III
-
phosducin-like cofactor protein
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
three different phosducin-like cofactor proteins
-
prefoldin
-
additional information
the group II CPNs do not require a GroES-like co-CPN but have a built-in lid that is composed of a helical protrusion in the apical domain. The rate of transfer of a substrate protein from PFD to CPN correlates with the strength of the PFD-CPN interaction
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activates
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP-PNP
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
ADP (or ATP, with a minor likelihood) remains bound on the CCT6 side of TRiC in the presence of excess AMP-PNP (10 mM), although some of the ADP may be replaced by AMP-PNP
prefoldin
-
inhibits the GFP protein refolding by interacting with intermediates
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
prefoldin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
-
assay at
7.4 - 7.5
Thermochaetoides thermophila
-
assay at
7.5 - 8
thermal protection assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
assay at
30
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
assay at
35
Thermochaetoides thermophila
-
assay at
4
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
refolding/ATPase
50
mutants Q533G and E530G
60 - 70
wild-type enzyme and mutant P538G
70
mutants P533M, D545M, and E530M
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 30
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
activity range, profile overview
30 - 90
activity range of wild-type and mutant enzymes, profiles overview
70 - 85
70°C: about 60% of maximal actiovity, 85°C: about 40% of maximal activity
70 - 95
70°C: about 70% of maximal activity, 95°C: about 50% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q9YDK6: alpha-subunit, Q9YA66: beta-subunit
SwissProt
Manually annotated by BRENDA team
genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
UniProt
Manually annotated by BRENDA team
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
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
UniProt
Manually annotated by BRENDA team
genes CCT1-5, and 6-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
UniProt
Manually annotated by BRENDA team
genes CCT1-5, and 6-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
UniProt
Manually annotated by BRENDA team
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
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
UniProt
Manually annotated by BRENDA team
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
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
UniProt
Manually annotated by BRENDA team
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
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
UniProt
Manually annotated by BRENDA team
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
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
UniProt
Manually annotated by BRENDA team
genes encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
UniProt
Manually annotated by BRENDA team
genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
UniProt
Manually annotated by BRENDA team
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
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
UniProt
Manually annotated by BRENDA team
genes encoding subunits alpha, beta, gamma, delta, epsilon, zeta, eta, and theta
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
UniProt
Manually annotated by BRENDA team
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
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
UniProt
Manually annotated by BRENDA team
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
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
UniProt
Manually annotated by BRENDA team
Thermochaetoides thermophila
-
-
-
Manually annotated by BRENDA team
gene CPKB
SwissProt
Manually annotated by BRENDA team
thermosome subunits alpha and beta; KS-1
UniProt
Manually annotated by BRENDA team
alpha-subunit
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
HBMEC
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
Manually annotated by BRENDA team
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
upon heat stress, human TRiC-alpha translocates from the cytosolic fraction and associates with the cytoskeleton
Manually annotated by BRENDA team
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
Manually annotated by BRENDA team
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
-
Manually annotated by BRENDA team
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THSB_THEK1
Thermococcus sp. (strain JCM 11816 / KS-1)
546
0
59174
Swiss-Prot
-
THS_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
549
0
59693
Swiss-Prot
other Location (Reliability: 2)
TCPA_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
559
0
60481
Swiss-Prot
-
THSA_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
545
0
58281
Swiss-Prot
-
THSB_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
543
0
58480
Swiss-Prot
-
THSA_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
548
0
59170
Swiss-Prot
-
THSA_THEK1
Thermococcus sp. (strain JCM 11816 / KS-1)
548
0
59170
Swiss-Prot
other Location (Reliability: 1)
TCPA_BOVIN
556
0
60206
Swiss-Prot
-
THSB_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
546
0
59158
Swiss-Prot
-
Q877G8_METMI
543
0
58215
TrEMBL
-
THSB_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
548
0
60430
Swiss-Prot
-
THSA_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
554
0
60374
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
-
10 * 55000, SDS-PAGE, assembles into a large ring-shaped oligomeric complex comprising about 10 subunits
550000
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
about, recombinant heterohexadecameric myc-tagged subunit theta complex, native PAGE
59140
x * 59140, calculatzed from sequence
60000
60700
61200
900000
about, Mm-cpn protein complex, gel filtration and native PAGE
950000
Thermochaetoides thermophila
-
purified recombinant CCT complex, about, sequence calculation
970000
Thermochaetoides thermophila
-
purified recombinant CCT complex, about, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
-
10 * 55000, SDS-PAGE, assembles into a large ring-shaped oligomeric complex comprising about 10 subunits
heterohexadecamer
hexadecamer
octamer
oligomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
InR/PI3K/Akt network in Drosophila dynamically phosphorylates sbunit CCT8 in response to insulin stimulation
ubiquitination
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
VRK2 is important for the eukaryotic chaperonin TRiC protein degradation pathway and is involved in polyQ protein aggregation. Ubiquitin-specific protease 25 (USP25) is a VRK2 substrate that acts on TRiC deubiquitination. USP25 deubiquitinates TRiC subunit CCT4. TRiC ubiquitination is induced by inhibition of USP25 and E3 ligase COP1 is recruited. Subsequently, TRiC protein levels are decreased. USP25 knockdown enhances CCT4 polyubiquitination and reduces CCT4 protein levels
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure analysis of the open conformation of the mammalian chaperonin CCT in complex with tubulin, overview
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
cryo-specimen preparation of AML-1-ETO DNA-binding domain (AML1-175), with TRiC and Hsp70, and cryo-EM imaging, three-dimensional cryo-EM map reconstruction, modelling, method, overview. TRiC can refold denatured AML1-175 (DBD) and restore its DNA binding activity in vitro. Reconstructed the TRiC-AML1-175 complex forms in the presence of Ni2+-gold nanoparticles capable of binding to the His-tag on AML1-175. Ni-affinity nanogold particles reveal the location of AML1-175 on TRiC
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
structure analysis of the open conformation of the mammalian chaperonin CCT in complex with tubulin, overview
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
crystal structure analysis, PDB ID 3KFK
crystal structure analysis, PDB IDs 3IYF and 3LOS, enzyme in open and closed state conformation
-
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
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
cryo-EM structures of Saccharomyces cerevisiae TRiC in a nucleotide partially preloaded (NPP) state and in the ATP-bound state at 4.7 A and 4.6 A resolution, respectively
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
crystal structure analysis, PDB ID 4D8Q
recombinant enzyme, removal of all surface exposed cysteine residues for diffracted X-ray tracking experiment, and addition of cysteine residues at the tip of helical protrusions of selected two subunits. Gold nanocrystals are attached onto CtCCTs via gold-thiol bonds and applied for the analysis by diffracted X-ray tracking
Thermochaetoides thermophila
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H147R
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
naturally occuring mutation of subunit CCT5
D386A
site-directed mutagenesis, introduction of D386A into Mm-cpn significantly reduces its ability to complement for loss of GroES and GroEL, loss of ATPase activity severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins
G160S
-
the TRiC-like mutant G160S of MmCpn has a drastically slower rate of ATP hydrolysis, roughly equivalent to the steady-state hydrolysis of eukaryotic TRiC
K216A
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216C
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216D
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216E
random mutagenesis, growth for the mutants is clearly faster than for wild-type Mm-cpn organisms under GroES/GroEL-limiting conditions, improved phenotype in Escherichia coli under GroEL- and GroES-depleting conditions. The mutant can effectively hydrolyze ATP
K216E/D386A
site-directed mutagenesis, introduction of D386A into Mm-cpn significantly reduces its ability to complement for loss of GroES and GroEL, loss of ATPase activity severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins
K216F
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216G
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216L
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216P
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216Q
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216R
site-directed mutagenesis, the mutant enzyme slightly complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216S
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216T
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216V
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216Y
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
M223E
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223F
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223G
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223I
M223I/D386A
site-directed mutagenesis, introduction of D386A into Mm-cpn significantly reduces its ability to complement for loss of GroES and GroEL, loss of ATPase activity severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins
M223L
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223R
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223S
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223V
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223W
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223Y
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
C450Y
G345D
D545G
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
D545M
site-directed mutagenesis, the mutant shows slightly higher stabilities than that of wild-type CpkA
E530G
site-directed mutagenesis, the mutant strain DA4 shows increased ATPase activity. The CpkA-E530G mutation prevents cold denaturation of proteins under cold-stress conditions, thereby enabling cells to grow in cooler environments
E530M
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
P538G
site-directed mutagenesis, the mutant shows slightly higher stabilities than that of wild-type CpkA
P538M
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
Q533G
site-directed mutagenesis
Q533M
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
D64A/D393A
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change
D64A/D393A/K485W
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview
K165A/K485W
site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner
K485W
L265W
site-directed mutagenesis, replacement of amino acid L265 with Trp partially impairs the protein folding activity, eight Trp residues are thought to come close in the closed conformation. The resulting steric hindrance might interrupt the conformational changes required for protein folding. Although ATP hydrolysis activity is almost completely lost in the absence of K+, slight ATP-dependent folding activity is observed
L56W
site-directed mutagenesis, the mutant exhibits nearly the same level of protein folding activity as the wild-type protein
D64A/D393A
-
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change
-
D64A/D393A/K485W
-
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview
-
K165A/K485W
-
site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner
-
K485W
L265W
-
site-directed mutagenesis, replacement of amino acid L265 with Trp partially impairs the protein folding activity, eight Trp residues are thought to come close in the closed conformation. The resulting steric hindrance might interrupt the conformational changes required for protein folding. Although ATP hydrolysis activity is almost completely lost in the absence of K+, slight ATP-dependent folding activity is observed
-
L56W
-
site-directed mutagenesis, the mutant exhibits nearly the same level of protein folding activity as the wild-type protein
-
K165A/K485W
-
site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner
-
K485W
-
site-directed mutagenesis, the mutant shows ATP binding and conformational change upon ATP binding
-
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Vaccinia-related kinase 2 controls the stability of the eukaryotic chaperonin TRiC/CCT by inhibiting the deubiquitinating enzyme USP25
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
each of the recombinant alpha- and beta- subunits is purified to 92% and 94% by using anion exchange chromatography
native enzyme by anion exchange chromatography and gel filtration
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
native enzyme by calmodulin affinity chromatography and gel filtration
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
native enzyme from bovine testes by anion exchange chromatography and gel filtration
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
native enzyme from HeLa cells by anion exchange chromatography and gel filtration
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
native enzyme is purified from HeLa cells by a process including anion exchange chromatography and gel filtration
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
recombinant alpha-subunit from Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) by heat shock treatment and anion exchange chromatography
recombinant beta-subunit from Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) by heat shock treatment and anion exchange chromatography
recombinant chaperonin Mm-cpn from Escherichia coli strain BL21(DE3) by anion exchange chromatography, ammonium sulfate fractionation, and gel filtation, followed by ultrafiltration
recombinant enzyme
-
recombinant enzyme CPN from Escherichia coli strain BLR(DE3)/pET23a by heat treatment for 15 min at 90°C, anion exchange chromatography, ultrafiltration, and gel filtration
-
recombinant His-tagged wild-type and mutant enzyme oligomer rings from Escherichia coli
recombinant Strep-tagged wild-type and mutant CCT complexes from Escherichia coli strain BL21 Star(DE3)pRARE by affinity and anion exchange chromatography, and gel filtration
Thermochaetoides thermophila
-
recombinant subunit alpha and subunit beta
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, and gel filtration
the recombinant enzyme is purified to 91% by heat-shock treatment and anion-exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ApCpnA and ApCpnB chaperonin genes are overexpressed in Escherichia coli Rosetta and Codonplus (DE3), respectively
expressed in Escherichia coli
expression in Escherichia coli
expression of ApCpnA (subunit alpha) and ApCpnB (subunit beta) in Escherichia coli Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) cells
gene CCT1-8, cloning of mouse testis CCT genes
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
gene cpkA, recombinant expression of the chimeric chaperonin CpkBA in Escherichia coli
gene cpkB, recombinant expression of the chimeric chaperonin CpkBA in Escherichia coli
gene thsA, recombinant expression of alpha-subunit in Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3)
gene thsB, recombinant expression of beta-subunit in Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3)
genes cct1-8
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
genes CCT1-8, recombinant expression of GFP-tagged subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta in insect cells, method overview. Examination if recombinant hTRiC and or hTRiC-GFP are assembled into the correct and evolutionarily conserved subunit arrangement using disuccinimidyl suberate (DSS) XL-MS
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
genes cct1-8, recombinant overexpression of Strep-tagged wild-type and mutant CCT complexes in Escherichia coli strain BL21 Star(DE3)pRARE
Thermochaetoides thermophila
-
genes encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta, DNA and amino acid sequence determination, sequences comparisons, quantitative real-time PCR expression analysis at different temperatures, overview. GaTRiC subunits are constitutively expressed at all temperatures with the exception of GaTRiCbeta subunit at 20°C reaching 4.5fold expression compared to optimal growth at 12°C
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
quantitative real-time reverse transcription-PCR expression analysis
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
recombinant ectopic overexpression in in Plasmodium falciparum of each of the N-terminally GFP-tagged PfTRiC subunits, under the expression of the strong, constitutively active HSP86 promoter, the subunits are additionally C-terminally tagged with a ten amino acid flexible linker sequence (PRPGAAHYAA) between the TRiC C-terminus and GFP to avoid disruption of heterohexadecamer formation. All GFP-tagged subunits are successfully overexpressed, except the PfTRiC-zeta subunit, where the GFP signal gets lost
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
recombinant expression of archaeal group II chaperonin Mm-cpn in Escherichia coli strain TAB21 lacking its group I chaperonin GroEL, and wild-type and mutant enzymes overexpression in Escherichia coli strain BL21(DE3)
recombinant expression of enzyme CPN in Escherichia coli strain BLR(DE3)/pET23a
-
recombinant expression of His-tagged wild-type and mutant enzyme oligomer rings in Escherichia coli
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) RIL
subcloned into vector pET21a. The constructed pET21a-ApCpnB is transformed into Escherichia coli BL21 Codonplus (DE3)
-
the chaperonin gene PhCpn is amplified by PCR from the genomic DNA, subcloned into pET21a vector, and expressed in three Escherichia coli host cells such as BL21, Rosetta, and Codonplus (DE3)DE3. Among these host cells, Escherichia coli Rosetta shows the highest expression level of recombinant PhCpn at induction with 1 mM isopropyl beta-D-thiogalactoside
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cardiac-specific upregulation of CCT components under time restricted feeding (TRF)
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
expression of CCT is not induced by stress conditions
Thermochaetoides thermophila
-
induced when halophilic cells are exposed to a low salt stress
-
possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively
role of AKT in regulating TCP1 downstream of FGFR2, Akt inhibition results in downregulation of TCP1 protein as well as reduced levels of Akt and RPS6 phosphorylation
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
subunit CCT1 is transcriptionally modulated by the driver oncogene, phosphatidylinositide 3-kinases (PI3K)
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
the TCP1 subunit of TRiC is regulated by fibroblast growth factor receptor 2 (FGFR2), the induction of TCP1 by FGFR2 is inhibited by PD173074, i.e. N-[2-[[4-(diethylamino)butyl]amino-6-(3,5-dimethoxyphenyl)pyrido[2,3-d]pyrimidin-7-yl]-N'-(1,1-dimethylethyl)urea], an ATP-competitive inhibitor. FGFR2 signals through PI3K and Akt to regulate TCP1 expression
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
TRiC can refold denatured AML1-175 (DBD) and restore its DNA binding activity in vitro. The reconstructed the TRiC-AML1-175 complex is formed in the presence of Ni2+-gold nanoparticles capable of binding to the His-tag on AML1-175. While AML1-175 is folded by TRiC to achieve its native function, ATP hydrolysis does not suffice to trigger its release from the chaperonin
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
synthesis
-
ApCpnB has both foldase and holdase activities and can be used as a powerful molecular machinery for the production of recombinant proteins as soluble and active forms in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shin, E.J.; Lee, J.W.; Kim, J.H.; Jeon, S.J.; Kim, Y.H.; Nam, S.W.
Overexpression, purification, and characterization of beta-subunit group II chaperonin from hyperthermophilic Aeropyrum pernix K1
J. Microbiol. Biotechnol.
20
542-549
2010
Aeropyrum pernix K1
Manually annotated by BRENDA team
Yan, Z.; Fujiwara, S.; Kohda, K.; Takagi, M.; Imanaka, T.
In vitro stabilization and in vivo solubilization of foreign proteins by the beta subunit of a chaperonin from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1
Appl. Environ. Microbiol.
63
785-789
1997
Thermococcus kodakarensis (Q52500)
Manually annotated by BRENDA team
Okochi, M.; Matsuzaki, H.; Nomura, T.; Ishii, N.; Yohda, M.
Molecular characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3
Extremophiles
9
127-134
2004
Pyrococcus horikoshii (O57762), Pyrococcus horikoshii OT-3 (O57762)
Manually annotated by BRENDA team
Franzetti, B.; Schoehn, G.; Ebel, C.; Gagnon, J.; Ruigrok, R.W.; Zaccai, G.
Characterization of a novel complex from halophilic archaebacteria, which displays chaperone-like activities in vitro
J. Biol. Chem.
276
29906-29914
2001
Haloarcula marismortui
Manually annotated by BRENDA team
Kim, J.H.; Lee, J.W.; Shin, E.J.; Nam, S.W.
Cooperativity of alpha- and beta-subunits of group II chaperonin from the hyperthermophilic archaeum Aeropyrum pernix K1
J. Microbiol. Biotechnol.
21
212-217
2011
Aeropyrum pernix (Q9YDK6 and Q9YA66), Aeropyrum pernix, Aeropyrum pernix DSM 11879 (Q9YDK6 and Q9YA66)
Manually annotated by BRENDA team
Lee, J.W.; Kim, S.W.; Kim, J.H.; Jeon, S.J.; Kwon, H.J.; Kim, B.W.; Nam, S.W.
Functional characterization of the alpha- and beta-subunits of a group II chaperonin from Aeropyrum pernix K1
J. Microbiol. Biotechnol.
23
818-825
2013
Aeropyrum pernix (Q9YA66), Aeropyrum pernix (Q9YDK6), Aeropyrum pernix (Q9YDK6 and Q9YA66), Aeropyrum pernix DSM 11879 (Q9YDK6 and Q9YA66)
Manually annotated by BRENDA team
Gao, L.; Danno, A.; Fujii, S.; Fukuda, W.; Imanaka, T.; Fujiwara, S.
Indole-3-glycerol-phosphate synthase is recognized by a cold-inducible group II chaperonin in Thermococcus kodakarensis
Appl. Environ. Microbiol.
78
3806-3815
2012
Thermococcus kodakarensis (P61111), Thermococcus kodakarensis (Q52500)
Manually annotated by BRENDA team
Jayasinghe, M.; Shrestha, P.; Wu, X.; Tehver, R.; Stan, G.
Weak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysis
Biophys. J.
103
1285-1295
2012
Thermoplasma acidophilum (P48424), Thermoplasma acidophilum (P48425), Thermoplasma acidophilum ATCC 25905 (P48424), Thermoplasma acidophilum ATCC 25905 (P48425)
Manually annotated by BRENDA team
Cong, Y.; Schroeder, G.; Meyer, A.; Jakana, J.; Ma, B.; Dougherty, M.; Schmid, M.; Reissmann, S.; Levitt, M.; Ludtke, S.; Frydman, J.; Chiu, W.
Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
EMBO J.
31
720-730
2012
Bos taurus
Manually annotated by BRENDA team
Skjaerven, L.; Cuellar, J.; Martinez, A.; Valpuesta, J.M.
Dynamics, flexibility, and allostery in molecular chaperonins
FEBS Lett.
589
2522-2532
2015
Saccharomyces cerevisiae (P12612), Thermoplasma acidophilum (P48424), Thermoplasma acidophilum (P48425), Bos taurus (Q32L40), Methanococcus maripaludis (Q877G8), Saccharomyces cerevisiae ATCC 204508 (P12612), Thermoplasma acidophilum ATCC 25905 (P48424), Thermoplasma acidophilum ATCC 25905 (P48425)
Manually annotated by BRENDA team
Gao, L.; Imanaka, T.; Fujiwara, S.
A mutant chaperonin that is functional at lower temperatures enables hyperthermophilic Archaea to grow under cold-stress conditions
J. Bacteriol.
197
2642-2652
2015
Thermococcus kodakarensis (P61111), Thermococcus kodakarensis (Q52500), Thermococcus kodakarensis KU216 (Q52500)
Manually annotated by BRENDA team
Hongo, K.; Itai, H.; Mizobata, T.; Kawata, Y.
Varied effects of Pyrococcus furiosus prefoldin and P. furiosus chaperonin on the refolding reactions of substrate proteins
J. Biochem.
151
383-390
2012
Pyrococcus furiosus
Manually annotated by BRENDA team
Yamamoto, Y.Y.; Abe, Y.; Moriya, K.; Arita, M.; Noguchi, K.; Ishii, N.; Sekiguchi, H.; Sasaki, Y.C.; Yohda, M.
Inter-ring communication is dispensable in the reaction cycle of group II chaperonins
J. Mol. Biol.
426
2667-2678
2014
Thermococcus sp. (O24730), Thermococcus sp. (P61112), Thermococcus sp. KS-1 (O24730), Thermococcus sp. KS1 (P61112)
Manually annotated by BRENDA team
Nakagawa, A.; Moriya, K.; Arita, M.; Yamamoto, Y.; Kitamura, K.; Ishiguro, N.; Kanzaki, T.; Oka, T.; Makabe, K.; Kuwajima, K.; Yohda, M.
Dissection of the ATP-dependent conformational change cycle of a group II chaperonin
J. Mol. Biol.
426
447-459
2014
Thermococcus sp. (O24730), Thermococcus sp. (P61112), Thermococcus sp. KS-1 (O24730), Thermococcus sp. KS-1 (P61112)
Manually annotated by BRENDA team
Lopez, T.; Dalton, K.; Frydman, J.
The mechanism and function of group II chaperonins
J. Mol. Biol.
427
2919-2930
2015
Saccharomyces cerevisiae, Methanococcus maripaludis, Thermoplasma acidophilum
Manually annotated by BRENDA team
Sekiguchi, H.; Nakagawa, A.; Moriya, K.; Makabe, K.; Ichiyanagi, K.; Nozawa, S.; Sato, T.; Adachi, S.; Kuwajima, K.; Yohda, M.; Sasaki, Y.C.
ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking
PLoS ONE
8
e64176
2013
Thermococcus sp. (O24730), Thermococcus sp. (P61112), Thermococcus sp. KS-1 (O24730), Thermococcus sp. KS-1 (P61112)
Manually annotated by BRENDA team
Kim, J.; Shin, E.; Jeon, S.; Kim, Y.; Kim, P.; Lee, C.; Nam, S.
Overexpression, purification, and functional characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3
Biotechnol. Bioprocess Eng.
14
551-558
2009
Pyrococcus horikoshii (O57762)
-
Manually annotated by BRENDA team
Willison, K.R.
The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring
Biochem. J.
475
3009-3034
2018
Arabidopsis thaliana (P28769 AND Q940P8 AND Q84WV1 AND Q9LV21 AND O04450 AND Q9M888 AND Q9SF16 AND Q94K05), Bos taurus (Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9), Caenorhabditis elegans (P41988 AND P47207 AND Q9N4J8 AND P47208 AND P47209 AND P46550 AND Q9TZS5 AND Q9N358), Candida albicans (Q59QB7 AND Q59YC4 AND Q5AK16 AND Q59Z12 AND A0A1D8PMN9 AND Q59YH4 AND P47828), Candida albicans ATCC MYA-2876 (Q59QB7 AND Q59YC4 AND Q5AK16 AND Q59Z12 AND A0A1D8PMN9 AND Q59YH4 AND P47828), Danio rerio (Q9PW76 AND Q6PBW6 AND Q7T2P2 AND Q6P123 AND Q6NVI6 AND E9QGU4 AND B3DKJ0 AND A0A0R4IJT8), Dictyostelium discoideum (Q55BM4 AND Q54ES9 AND Q54TH8 AND Q54CL2 AND Q54TD3 AND Q76NU3 AND Q54ER7 AND Q552J0), Drosophila melanogaster (P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0), Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Mus musculus (P11983 AND P80314 AND P80318 AND P80315 AND P80316 AND P80317 AND P80313 AND P42932), Plasmodium falciparum (Q8II43 AND O97247 AND Q8I5C4 AND C0H5I7 AND O97282 AND C6KST5 AND O77323 AND O96220), Rattus norvegicus (P28480 AND Q5XIM9 AND Q6P502 AND Q7TPB1 AND Q68FQ0 AND Q3MHS9 AND D4AC23 AND D4ACB8), Rattus norvegicus Sprague-Dawley (P28480 AND Q5XIM9 AND Q6P502 AND Q7TPB1 AND Q68FQ0 AND Q3MHS9 AND D4AC23 AND D4ACB8), Saccharomyces cerevisiae (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079), Saccharomyces cerevisiae ATCC 204508 (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079)
Manually annotated by BRENDA team
Korobko, I.; Nadler-Holly, M.; Horovitz, A.
Transient kinetic analysis of ATP hydrolysis by the CCT/TRiC chaperonin
J. Mol. Biol.
428
4520-4527
2016
Saccharomyces cerevisiae (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079), Saccharomyces cerevisiae ATCC 204508 (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079)
Manually annotated by BRENDA team
Araki, K.; Suenaga, A.; Kusano, H.; Tanaka, R.; Hatta, T.; Natsume, T.; Fukui, K.
Functional profiling of asymmetrically-organized human CCT/TRiC chaperonin
Biochem. Biophys. Res. Commun.
481
232-238
2016
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Homo sapiens
Manually annotated by BRENDA team
Roh, S.H.; Kasembeli, M.M.; Galaz-Montoya, J.G.; Chiu, W.; Tweardy, D.J.
Chaperonin TRiC/CCT recognizes fusion oncoprotein AML1-ETO through subunit-specific interactions
Biophys. J.
110
2377-2385
2016
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
Manually annotated by BRENDA team
Balchin, D.; Milicic, G.; Strauss, M.; Hayer-Hartl, M.; Hartl, F.U.
Pathway of actin folding directed by the eukaryotic chaperonin TRiC
Cell
174
1507-1521.e16
2018
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
Manually annotated by BRENDA team
Gestaut, D.; Roh, S.H.; Ma, B.; Pintilie, G.; Joachimiak, L.A.; Leitner, A.; Walzthoeni, T.; Aebersold, R.; Chiu, W.; Frydman, J.
The chaperonin TRiC/CCT associates with prefoldin through a conserved electrostatic interface essential for cellular proteostasis
Cell
177
751-765.e15
2019
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
Manually annotated by BRENDA team
Berger, J.; Berger, S.; Li, M.; Jacoby, A.S.; Arner, A.; Bavi, N.; Stewart, A.G.; Currie, P.D.
In vivo function of the chaperonin TRiC in beta-actin folding during sarcomere assembly
Cell Rep.
22
313-322
2018
Danio rerio (Q9PW76 AND Q6PBW6 AND Q7T2P2 AND Q6P123 AND Q6NVI6 AND E9QGU4 AND B3DKJ0 AND A0A0R4IJT8)
Manually annotated by BRENDA team
Yusof, N.A.; Kamaruddin, S.; Abu Bakar, F.D.; Mahadi, N.M.; Abdul Murad, A.M.
Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica
Cell Stress Chaperones
24
351-368
2019
Glaciozyma antarctica (A0A1S6LQX4 AND A0A1S6LQU3 AND A0A1S6LQU0 AND A0A1S6LQU6 AND A0A1S6LQU1 AND A0A1S6LQU9 AND A0A1S6LQW6 AND A0A1S6LQW7), Glaciozyma antarctica
Manually annotated by BRENDA team
Spillman, N.J.; Beck, J.R.; Ganesan, S.M.; Niles, J.C.; Goldberg, D.E.
The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol
Cell. Microbiol.
19
e12719
2017
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Plasmodium falciparum (Q8II43 AND O97247 AND Q8I5C4 AND C0H5I7 AND O97282 AND C6KST5 AND O77323 AND O96220), Plasmodium falciparum
Manually annotated by BRENDA team
Guest, S.T.; Kratche, Z.R.; Bollig-Fischer, A.; Haddad, R.; Ethier, S.P.
Two members of the TRiC chaperonin complex, CCT2 and TCP1 are essential for survival of breast cancer cells and are linked to driving oncogenes
Exp. Cell Res.
332
223-235
2015
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Homo sapiens
Manually annotated by BRENDA team
Melkani, G.C.; Bhide, S.; Han, A.; Vyas, J.; Livelo, C.; Bodmer, R.; Bernstein, S.I.
TRiC/CCT chaperonins are essential for maintaining myofibril organization, cardiac physiological rhythm, and lifespan
FEBS Lett.
591
3447-3458
2017
Drosophila melanogaster (P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0)
Manually annotated by BRENDA team
Roh, S.H.; Kasembeli, M.; Bakthavatsalam, D.; Chiu, W.; Tweardy, D.J.
Contribution of the type II chaperonin, TRiC/CCT, to oncogenesis
Int. J. Mol. Sci.
16
26706-26720
2015
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Bos taurus (Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9)
Manually annotated by BRENDA team
Shah, R.; Large, A.T.; Ursinus, A.; Lin, B.; Gowrinathan, P.; Martin, J.; Lund, P.A.
Replacement of GroEL in Escherichia coli by the group II chaperonin from the archaeon Methanococcus maripaludis
J. Bacteriol.
198
2692-2700
2016
Methanococcus maripaludis (Q877G8)
Manually annotated by BRENDA team
Roh, S.H.; Kasembeli, M.; Galaz-Montoya, J.G.; Trnka, M.; Lau, W.C.; Burlingame, A.; Chiu, W.; Tweardy, D.J.
Chaperonin TRiC/CCT modulates the folding and activity of leukemogenic fusion oncoprotein AML1-ETO
J. Biol. Chem.
291
4732-4741
2016
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Bos taurus (Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9)
Manually annotated by BRENDA team
Zako, T.; Sahlan, M.; Fujii, S.; Yamamoto, Y.Y.; Tai, P.T.; Sakai, K.; Maeda, M.; Yohda, M.
Contribution of the C-terminal region of a group II chaperonin to its interaction with prefoldin and substrate transfer
J. Mol. Biol.
428
2405-2417
2016
Thermococcus sp. JCM 11816 (P61112 AND O24730)
Manually annotated by BRENDA team
Kim, S.; Lee, D.; Lee, J.; Song, H.; Kim, H.J.; Kim, K.T.
Vaccinia-related kinase 2 controls the stability of the eukaryotic chaperonin TRiC/CCT by inhibiting the deubiquitinating enzyme USP25
Mol. Cell. Biol.
35
1754-1762
2015
Mus musculus (P11983 AND P80314 AND P80318 AND P80315 AND P80316 AND P80317 AND P80313 AND P42932)
Manually annotated by BRENDA team
Knowlton, J.J.; Fernandez de Castro, I.; Ashbrook, A.W.; Gestaut, D.R.; Zamora, P.F.; Bauer, J.A.; Forrest, J.C.; Frydman, J.; Risco, C.; Dermody, T.S.
The TRiC chaperonin controls reovirus replication through outer-capsid folding
Nat. Microbiol.
3
481-493
2018
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
Manually annotated by BRENDA team
Zang, Y.; Jin, M.; Wang, H.; Cui, Z.; Kong, L.; Liu, C.; Cong, Y.
Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM
Nat. Struct. Mol. Biol.
23
1083-1091
2016
Saccharomyces cerevisiae (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kim, A.R.; Choi, K.W.
TRiC/CCT chaperonins are essential for organ growth by interacting with insulin/TOR signaling in Drosophila
Oncogene
38
4739-4754
2019
Drosophila melanogaster (P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0)
Manually annotated by BRENDA team
Ohhara, Y.; Nakamura, A.; Kato, Y.; Yamakawa-Kobayashi, K.
Chaperonin TRiC/CCT supports mitotic exit and entry into endocycle in Drosophila
PLoS Genet.
15
e1008121
2019
Drosophila melanogaster (P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0), Drosophila melanogaster Oregon R (P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0)
Manually annotated by BRENDA team
Yamamoto, Y.Y.; Uno, Y.; Sha, E.; Ikegami, K.; Ishii, N.; Dohmae, N.; Sekiguchi, H.; Sasaki, Y.C.; Yohda, M.
Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC
PLoS ONE
12
e0176054
2017
Thermochaetoides thermophila
Manually annotated by BRENDA team
Moparthi, S.B.; Carlsson, U.; Vincentelli, R.; Jonsson, B.H.; Hammarstroem, P.; Wenger, J.
Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components
Sci. Rep.
6
28386
2016
Bos taurus (Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9)
Manually annotated by BRENDA team