Gene Symbol | LONP2 |
Entrez ID | 83752 |
Uniprot ID | Q86WA8 |
Description | lon peptidase 2, peroxisomal |
Chromosomal Location | chr16: 48,244,296-48,363,122 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0006515 |
misfolded or incompletely synthesized protein catabolic process |
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins. |
IBA |
BP |
GO:0006625 |
protein targeting to peroxisome |
The process of directing proteins towards the peroxisome, usually using signals contained within the protein. |
IMP |
BP |
GO:0007031 |
peroxisome organization |
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a peroxisome. A peroxisome is a small, membrane-bounded organelle that uses dioxygen (O2) to oxidize organic molecules. |
NAS |
BP |
GO:0014070 |
response to organic cyclic compound |
Any 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 an organic cyclic compound stimulus. |
IEA |
BP |
GO:0016485 |
protein processing |
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. |
IMP |
BP |
GO:0016558 |
protein import into peroxisome matrix |
The import of proteins into the peroxisomal matrix. A peroxisome targeting signal (PTS) binds to a soluble receptor protein in the cytosol, and the resulting complex then binds to a receptor protein in the peroxisome membrane and is imported. The cargo protein is then released into the peroxisome matrix. |
IEA |
BP |
GO:0031998 |
regulation of fatty acid beta-oxidation |
Any process that modulates the frequency, rate or extent of fatty acid bbeta-oxidation. |
IMP |
CC |
GO:0005634 |
nucleus |
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
IEA |
CC |
GO:0005777 |
peroxisome |
A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism. |
IDA |
CC |
GO:0005782 |
peroxisomal matrix |
The volume contained within the membranes of a peroxisome; in many cells the matrix contains a crystalloid core largely composed of urate oxidase. |
IBA |
CC |
GO:0016020 |
membrane |
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
IDA |
MF |
GO:0002020 |
protease binding |
Interacting selectively and non-covalently with any protease or peptidase. |
IPI |
MF |
GO:0004176 |
ATP-dependent peptidase activity |
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the hydrolysis of peptide bonds. |
IBA |
MF |
GO:0004252 |
serine-type endopeptidase activity |
Catalysis 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). |
IEA |
MF |
GO:0005102 |
receptor binding |
Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. |
IPI |
MF |
GO:0005515 |
protein binding |
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). |
IPI |
MF |
GO:0005524 |
ATP binding |
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
IEA |
MF |
GO:0008233 |
peptidase activity |
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. |
IDA |
MF |
GO:0019899 |
enzyme binding |
Interacting selectively and non-covalently with any enzyme. |
IPI |
Domain ID | Description |
---|---|
IPR003111 |
Lon, substrate-binding domain |
IPR003593 |
AAA+ ATPase domain |
IPR003959 |
ATPase, AAA-type, core |
IPR004815 |
Lon protease, bacterial/eukaryotic-type |
IPR008268 |
Peptidase S16, active site |
IPR008269 |
Peptidase S16, Lon proteolytic domain |
IPR014721 |
Ribosomal protein S5 domain 2-type fold, subgroup |
IPR015947 |
PUA-like domain |
IPR020568 |
Ribosomal protein S5 domain 2-type fold |
IPR027065 |
Lon protease |
IPR027417 |
P-loop containing nucleoside triphosphate hydrolase |
IPR027501 |
Lon protease homologue 2, peroxisomal |
Tissue | Cell Type |
---|---|
caudate |
glial cells |
cervix, uterine |
glandular cells |
endometrium |
glandular cells |
esophagus |
squamous epithelial cells |
fallopian tube |
glandular cells |
kidney |
cells in glomeruli |
kidney |
cells in tubules |
salivary gland |
glandular cells |
testis |
cells in seminiferous ducts |
thyroid gland |
glandular cells |
tonsil |
squamous epithelial cells |
Pubmed ID | Author | Year | Title |
---|---|---|---|
22617121 |
Ouandaogo et al. |
2012 |
Differences in transcriptomic profiles of human cumulus cells isolated from oocytes at GV, MI and MII stages after in vivo andin vitro oocyte maturation |
22951915 |
Haozi et al. |
2012 |
Altered gene expression profile in cumulus cells of mature MII oocytes from patients with polycystic ovary syndrome |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
PEX14 |
5195 |
O75381 |
0.52 |
DCN |
1634 |
P07585 |
0.63 |
ELAVL1 |
1994 |
Q15717 |
0.63 |
IL17A |
3605 |
Q16552 |
0.63 |
RB1CC1 |
9821 |
Q8TDY2 |
0.63 |
OS9 |
10956 |
Q13438 |
0.63 |
FBXW11 |
23291 |
Q9UKB1 |
0.63 |
WWOX |
51741 |
Q9NZC7 |
0.63 |
TYSND1 |
219743 |
Q2T9J0 |
0.63 |
RSPH9 |
221421 |
Q9H1X1 |
0.63 |
PEX5 |
5830 |
P50542 |
0.73 |
AMOT |
154796 |
Q4VCS5 |
0.76 |