BAIT
CLPP
DFNB81, PRLTS3
caseinolytic mitochondrial matrix peptidase proteolytic subunit
GO Process (1)
GO Function (3)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
HSD17B4
DBP, MFE-2, MPF-2, PRLTS1, SDR8C1
hydroxysteroid (17-beta) dehydrogenase 4
GO Process (15)
GO Function (6)
GO Component (5)
Gene Ontology Biological Process
- alpha-linolenic acid metabolic process [TAS]
- androgen metabolic process [IDA]
- bile acid biosynthetic process [TAS]
- bile acid metabolic process [TAS]
- cellular lipid metabolic process [TAS]
- estrogen metabolic process [IDA]
- fatty acid beta-oxidation [IDA]
- fatty acid beta-oxidation using acyl-CoA oxidase [TAS]
- medium-chain fatty-acyl-CoA metabolic process [IDA]
- metabolic process [IDA]
- osteoblast differentiation [IDA]
- oxidation-reduction process [IDA, IMP]
- small molecule metabolic process [TAS]
- unsaturated fatty acid metabolic process [TAS]
- very long-chain fatty-acyl-CoA metabolic process [IDA]
Gene Ontology Molecular Function- 17-beta-hydroxysteroid dehydrogenase (NAD+) activity [IDA]
- 3-hydroxyacyl-CoA dehydrogenase activity [IDA, IMP, TAS]
- 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity [TAS]
- long-chain-enoyl-CoA hydratase activity [IDA, TAS]
- protein homodimerization activity [IDA]
- receptor binding [IPI]
- 17-beta-hydroxysteroid dehydrogenase (NAD+) activity [IDA]
- 3-hydroxyacyl-CoA dehydrogenase activity [IDA, IMP, TAS]
- 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity [TAS]
- long-chain-enoyl-CoA hydratase activity [IDA, TAS]
- protein homodimerization activity [IDA]
- receptor binding [IPI]
Gene Ontology Cellular Component
Homo sapiens
Proximity Label-MS
An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.
Publication
Inhibition of the Mitochondrial Protease ClpP as a Therapeutic Strategy for Human Acute Myeloid Leukemia.
From an shRNA screen, we identified ClpP as a member of the mitochondrial proteome whose knockdown reduced the viability of K562 leukemic cells. Expression of this mitochondrial protease that has structural similarity to the cytoplasmic proteosome is increased in leukemic cells from approximately half of all patients with AML. Genetic or chemical inhibition of ClpP killed cells from both human ... [more]
Cancer Cell Jun. 08, 2015; 27(6);864-76 [Pubmed: 26058080]
Throughput
- High Throughput
Curated By
- BioGRID