3.6.4.B10: chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)

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For detailed information about chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing), go to the full flat file.

Reaction

Synonyms

alpha/beta-thermosome, ApCpnB, archaeal chaperonin, CCT, CCT ATPase, CCT chaperonin, CCT complex, CCT/TRiC, CCT/TRiC chaperonin, CCT/TRiC complex, CCT2, chaperonin B, chaperonin containing t-complex polypeptide-1, chaperonin containing TCP-1, chaperonin containing TCP1, chaperonin TCP-1 ring complex, chaperonin TRiC, chaperonin TRiC/CCT, chaperonin-containing t-complex polypeptide 1, cPKA, CpkB, CtCCT, cytosolic chaperonin TRiC, eukaryotic chaperone complex, eukaryotic chaperonin, eukaryotic chaperonin TRiC, eukaryotic group II chaperonin, GaTRiC, group II chaperonin, group II chaperonin CCT/TRiC, group II CPN, HsTRiC, Mm-cpn, MmCpn, More, PfCPN, PfTRiC, PhCPN, Plasmodium TRiC, protein P45, T-complex polypeptide-1 ring complex, T-complex protein 1, T-complex protein 1 ring complex, T-complex protein-1 ring complex, TCP-1, TCP-1 ring complex, TCP1, TCP1 ring complex, thermosome, TKS1-CPN, TriC, TRiC chaperonin, TRiC chaperonin complex, TRiC/CCT, type II chaperonin

ECTree

     3 Hydrolases

         3.6 Acting on acid anhydrides

             3.6.4 Acting on acid anhydrides to facilitate cellular and subcellular movement

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

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Results	in table
3	Activating Compound
12	AA Sequence
7	Application
21	Cloned(Commentary)
13	Cofactor
9	Crystallization (Commentary)
242	Disease/ Diagnostics
8	Expression
184	General Information
1	General Stability
2	Inhibitors
14	KM Value [mM]
40	Localization
52	Metals/Ions
16	Molecular Weight [Da]
67	Natural Substrates/ Products (Substrates)
106	Organism
15	pH Optimum
2	Posttranslational Modification
74	Protein Variants
19	Purification (Commentary)
2	Reaction
86	Reference
1	Renatured (Commentary)
34	Source Tissue
105	Substrates and Products (Substrate)
43	Subunits
224	Synonyms
18	Temperature Optimum [°C]
4	Temperature Range [°C]
1	Temperature Stability [°C]

Posttranslational Modification

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

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

phosphoprotein

Drosophila melanogaster

P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0

InR/PI3K/Akt network in Drosophila dynamically phosphorylates sbunit CCT8 in response to insulin stimulation

757875

ubiquitination

Mus musculus

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

757660