Page last updated: 2024-08-07 20:48:24

Lon protease homolog, mitochondrial

A Lon protease, mitochondrial that is encoded in the genome of human. [PRO:DNx, UniProtKB:P36776]

Synonyms

EC 3.4.21.53;
LONHs;
Lon protease-like protein;
LONP;
Mitochondrial ATP-dependent protease Lon;
Serine protease 15

Research

Bioassay Publications (1)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's1 (100.00)2.80

Compounds (1)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
bortezomibHomo sapiens (human)IC500.183011

Enables

This protein enables 14 target(s):

TargetCategoryDefinition
single-stranded RNA bindingmolecular functionBinding to single-stranded RNA. [GOC:jl]
ATP-dependent peptidase activitymolecular functionCatalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. [GOC:mah]
serine-type endopeptidase activitymolecular functionCatalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
ATP bindingmolecular functionBinding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732]
ATP hydrolysis activitymolecular functionCatalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. [RHEA:13065]
PH domain bindingmolecular functionBinding to a PH domain (pleckstrin homology) of a protein, a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton. [GOC:jl, Pfam:PF00169]
identical protein bindingmolecular functionBinding to an identical protein or proteins. [GOC:jl]
ADP bindingmolecular functionBinding to ADP, adenosine 5'-diphosphate. [GOC:jl]
insulin receptor substrate bindingmolecular functionBinding to an insulin receptor substrate (IRS) protein, an adaptor protein that bind to the transphosphorylated insulin and insulin-like growth factor receptors, are themselves phosphorylated and in turn recruit SH2 domain-containing signaling molecules to form a productive signaling complex. [PMID:12829233]
sequence-specific DNA bindingmolecular functionBinding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. [GOC:jl]
G-quadruplex DNA bindingmolecular functionBinding to G-quadruplex DNA structures, in which groups of four guanines adopt a flat, cyclic Hoogsteen hydrogen-bonding arrangement known as a guanine tetrad. The stacking of guanine tetrads results in G-quadruplex DNA structures. G-quadruplex DNA can form under physiological conditions from some G-rich sequences, such as those found in telomeres, immunoglobulin switch regions, gene promoters, fragile X repeats, and the dimerization domain in the human immunodeficiency virus (HIV) genome. [PMID:16142245, PMID:9512530]
DNA polymerase bindingmolecular functionBinding to a DNA polymerase. [GOC:BHF, GOC:mah]
single-stranded DNA bindingmolecular functionBinding to single-stranded DNA. [GOC:elh, GOC:vw, PMID:22976174]

Located In

This protein is located in 6 target(s):

TargetCategoryDefinition
nucleoplasmcellular componentThat part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653]
mitochondrioncellular componentA semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732]
mitochondrial matrixcellular componentThe gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. [GOC:as, ISBN:0198506732]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
membranecellular componentA lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194]
mitochondrial nucleoidcellular componentThe region of a mitochondrion to which the DNA is confined. [GOC:jl]

Active In

This protein is active in 2 target(s):

TargetCategoryDefinition
mitochondrioncellular componentA semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732]
mitochondrial matrixcellular componentThe gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. [GOC:as, ISBN:0198506732]

Involved In

This protein is involved in 13 target(s):

TargetCategoryDefinition
mitochondrial genome maintenancebiological processThe maintenance of the structure and integrity of the mitochondrial genome; includes replication and segregation of the mitochondrial chromosome. [GOC:ai, GOC:vw]
response to hypoxiabiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. [GOC:hjd]
mitochondrion organizationbiological processA process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components. [GOC:dph, GOC:jl, GOC:mah, GOC:sgd_curators, PMID:9786946]
protein catabolic processbiological processThe chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. [GOC:mah]
mitochondrial DNA metabolic processbiological processThe chemical reactions and pathways involving mitochondrial DNA. [GOC:mah]
cellular response to oxidative stressbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. [GOC:mah]
mitochondrial protein catabolic processbiological processThe chemical reactions and pathways resulting in the breakdown of a mitochondrial protein. This process is necessary to maintain the healthy state of mitochondria and is thought to occur via the induction of an intramitochondrial lysosome-like organelle that acts to eliminate the damaged oxidised mitochondrial proteins without destroying the mitochondrial structure. [GOC:sp, PMID:21264221, PMID:21264228]
negative regulation of insulin receptor signaling pathwaybiological processAny process that stops, prevents, or reduces the frequency, rate or extent of insulin receptor signaling. [GOC:bf]
regulation of peptidyl-tyrosine phosphorylationbiological processAny process that modulates the frequency, rate or extent of the phosphorylation of peptidyl-tyrosine. [GOC:ai]
proteolysis involved in protein catabolic processbiological processThe hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells. [GOC:ai, GOC:dph, GOC:tb]
oxidation-dependent protein catabolic processbiological processThe chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the oxidation of one or more amino acid residues in the protein. [GOC:mah]
protein quality control for misfolded or incompletely synthesized proteinsbiological processThe chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins. [GOC:jl]
chaperone-mediated protein complex assemblybiological processThe aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex. [GOC:ai]