Search Results
Overview
| Uniprot ID | Q16740 |
|---|---|
| Protein Name | ATP-dependent Clp protease proteolytic subunit, mitochondrial |
| Gene Name | CLPP |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 203 | EEIMKLKKQLYNIYA |
Function
Protease component of the ClpXP complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The ClpXP complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates (PubMed:11923310, PubMed:15522782). Cleaves PINK1 in the mitochondrion (PubMed:22354088)
Protein Sequence
10
MWPGILVGGA
20
RVASCRYPAL
30
GPRLAAHFPA
40
QRPPQRTLQN
50
GLALQRCLHA
60
TATRALPLIP
70
IVVEQTGRGE
80
RAYDIYSRLL
90
RERIVCVMGP
100
IDDSVASLVI
110
AQLLFLQSES
120
NKKPIHMYIN
130
SPGGVVTAGL
140
AIYDTMQYIL
150
NPICTWCVGQ
160
AASMGSLLLA
170
AGTPGMRHSL
180
PNSRIMIHQP
190
SGGARGQATD
200
IAIQAEEIMK
210
LKKQLYNIYA
220
KHTKQSLQVI
230
ESAMERDRYM
240
SPMEAQEFGI
250
LDKVLVHPPQ
260
DGEDEPTLVQ
270
KEPVEAAPAA
EPVPAST
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0009368 | endopeptidase Clp complex |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0004176 | ATP-dependent peptidase activity |
| Molecular Function | GO:0051117 | ATPase binding |
| Molecular Function | GO:0004175 | endopeptidase activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0008233 | peptidase activity |
| Molecular Function | GO:0004252 | serine-type endopeptidase activity |
| Biological Process | GO:0033619 | membrane protein proteolysis |
| Biological Process | GO:0035694 | mitochondrial protein catabolic process |
| Biological Process | GO:0006515 | protein quality control for misfolded or incompletely synthesized proteins |
| Biological Process | GO:0006508 | proteolysis |
| Biological Process | GO:0051603 | proteolysis involved in protein catabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.