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AAA ATPases C

Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).

Overview

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AAA or AAA+ (ATPases Associated with diverse cellular Activities) proteins couple chemical energy provided by ATP hydrolysis to the remodeling or translocation of macromolecules. They are involved in a wide range of cellular processes, including DNA replication, protein degradation, membrane fusion, microtubule severing, peroxisome biogenesis, signal transduction and the regulation of gene expression.

Enzymes

3273
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caseinolytic mitochondrial matrix peptidase proteolytic subunit Show summary »


Target Id 3273
Nomenclature caseinolytic mitochondrial matrix peptidase proteolytic subunit
Genes CLPP (Hs), Clpp (Mm), Clpp (Rn)
Ensembl ID ENSG00000125656 (Hs), ENSMUSG00000002660 (Mm), ENSRNOG00000047052 (Rn)
UniProtKB AC Q16740 (Hs), O88696 (Mm)
Activators
compound 16z [PMID: 35609303] pEC50 6.7 [2]
Allosteric modulators
ONC201 (Activation) [9]
Comment Caseinolytic mitochondrial matrix peptidase (ClpP) is an ATP-dependent protease that plays an important role in maintaining mitochondrial protein homeostasis. It is a validated target for the development of anti-tumour drugs. The functional enzyme is a complex of two identical cylindrical heptameric 'pores' of CLPP catalytic subunits that are apically capped by chaperone subunits (CLPX) that regulate substrate recognition, unfolding and translocation [3-4].

katanin catalytic subunit A1 Show summary » More detailed page go icon to follow link

lon peptidase 1, mitochondrial Show summary »

References

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How to cite this family page

Database page citation:

AAA ATPases. Accessed on 29/04/2024. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=933.

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Fabbro D, Kelly E, Mathie AA, Peters JA, Veale EL, Armstrong JF, Faccenda E, Harding SD, Davies JA et al. (2023) The Concise Guide to PHARMACOLOGY 2023/24: Enzymes. Br J Pharmacol. 180 Suppl 2:S289-373.