Aliases for CLPX Gene
- Caseinolytic Mitochondrial Matrix Peptidase Chaperone Subunit 2 3 5
- ATP-Dependent Clp Protease ATP-Binding Subunit ClpX-Like, Mitochondrial 3
- ClpX (Caseinolytic Protease X, E. Coli) Homolog 2
- ClpX Caseinolytic Peptidase X Homolog (E. Coli) 2
- ClpX Caseinolytic Protease X Homolog (E. Coli) 2
- Energy-Dependent Regulator Of Proteolysis 3
- ClpX Caseinolytic Peptidase X Homolog 3
- ClpX Caseinolytic Protease X Homolog 3
External Ids for CLPX Gene
Previous GeneCards Identifiers for CLPX Gene
The protein encoded by this gene is part of a protease found in mitochondria. This protease is ATP-dependent and targets specific proteins for degradation. The protease consists of two heptameric rings of the CLPP catalytic subunit sandwiched between two hexameric rings of the chaperone subunit encoded by this gene. Targeted proteins are unwound by this protein and then passed on to the CLPP subunit for degradation. Two transcript variants, one protein-coding and the other non-protein coding, have been found for this gene. [provided by RefSeq, Nov 2015]
GeneCards Summary for CLPX Gene
CLPX (Caseinolytic Mitochondrial Matrix Peptidase Chaperone Subunit) is a Protein Coding gene. Diseases associated with CLPX include Tick-Borne Relapsing Fever and Relapsing Fever. Gene Ontology (GO) annotations related to this gene include transcription factor binding and unfolded protein binding.
UniProtKB/Swiss-Prot for CLPX Gene
ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex (PubMed:11923310, PubMed:22710082). Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure (PubMed:22841477). ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through upregulation of heme biosynthesis (PubMed:25957689).