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- Table of Contents
7 Q&As
Facts about ATP-dependent Clp protease proteolytic subunit, mitochondrial.
The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and could be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. .
| Human | |
|---|---|
| Gene Name: | CLPP |
| Uniprot: | Q16740 |
| Entrez: | 8192 |

| Belongs to: |
|---|
| peptidase S14 family |

ATP-dependent protease ClpAP, proteolytic subunit, human; ClpP (caseinolytic protease, ATP-dependent, proteolytic subunit, E. coli)homolog; ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog (E.coli); ClpP caseinolytic protease, ATP-dependent, proteolytic subunit homolog (E.coli); ClpP caseinolytic protease, ATP-dependent, proteolytic subunit homolog; EC 3.4.21.92; Endopeptidase Clp; putative ATP-dependent Clp protease proteolytic subunit, mitochondrial
Mass (kDA):
30.18 kDA

| Human | |
|---|---|
| Location: | 19p13.3 |
| Sequence: | 19; NC_000019.10 (6361531..6370242) |
Detected in liver (at protein level). Predominantly expressed in skeletal muscle. Intermediate levels in heart, liver and pancreas. Low in brain, placenta, lung and kidney.
Mitochondrion matrix.





PMID: 8543061 by Bross P., et al. Human ClpP protease: cDNA sequence, tissue-specific expression and chromosomal assignment of the gene.
PMID: 19892738 by Xu G., et al. Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini.