A lysyl oxidase homolog 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9Y4K0]
EC 1.4.3.13;
Lysyl oxidase-like protein 2;
Lysyl oxidase-related protein 2;
Lysyl oxidase-related protein WS9-14
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 4 (80.00) | 24.3611 |
| 2020's | 1 (20.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| phenethylamine | Homo sapiens (human) | IC50 | 60.1000 | 1 | 1 |
| pyrithione | Homo sapiens (human) | IC50 | 18.0000 | 1 | 1 |
| aminopropionitrile | Homo sapiens (human) | IC50 | 0.5650 | 13 | 13 |
| disulfiram | Homo sapiens (human) | IC50 | 0.1500 | 1 | 1 |
| thiram | Homo sapiens (human) | IC50 | 0.1700 | 1 | 1 |
| benzylamine | Homo sapiens (human) | IC50 | 64.7000 | 1 | 1 |
| 4-nitrobenzylamine | Homo sapiens (human) | IC50 | 0.7190 | 1 | 1 |
| 4-fluorobenzylamine | Homo sapiens (human) | IC50 | 26.0000 | 1 | 1 |
| 4-pyridylmethylamine | Homo sapiens (human) | IC50 | 1.2200 | 1 | 1 |
This protein enables 5 target(s):
| Target | Category | Definition |
|---|---|---|
| protein-lysine 6-oxidase activity | molecular function | Catalysis of the reaction: peptidyl-L-lysyl-peptide + H2O + O2 = peptidyl-allysyl-peptide + NH3 + hydrogen peroxide. [EC:1.4.3.13] |
| copper ion binding | molecular function | Binding to a copper (Cu) ion. [GOC:ai] |
| calcium ion binding | molecular function | Binding to a calcium ion (Ca2+). [GOC:ai] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| oligosaccharide binding | molecular function | Binding to an oligosaccharide, a molecule with between two and (about) 20 monosaccharide residues connected by glycosidic linkages. [GOC:mah] |
This protein is located in 7 target(s):
| Target | Category | Definition |
|---|---|---|
| basement membrane | cellular component | A collagen-containing extracellular matrix consisting of a thin layer of dense material found in various animal tissues interposed between the cells and the adjacent connective tissue. It consists of the basal lamina plus an associated layer of reticulin fibers. [ISBN:0198547684, PMID:22505934] |
| extracellular space | cellular component | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. [ISBN:0198547684] |
| nucleus | cellular component | 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. [GOC:go_curators] |
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| endoplasmic reticulum | cellular component | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732] |
| membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
| collagen-containing extracellular matrix | cellular component | An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells. [GOC:BHF, GOC:rph, PMID:21123617] |
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|---|---|
| collagen-containing extracellular matrix | cellular component | An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells. [GOC:BHF, GOC:rph, PMID:21123617] |
| extracellular space | cellular component | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. [ISBN:0198547684] |
This protein is part of 1 target(s):
| Target | Category | Definition |
|---|---|---|
| chromatin | cellular component | The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome. [GOC:elh, PMID:20404130] |
This protein is involved in 15 target(s):
| Target | Category | Definition |
|---|---|---|
| negative regulation of transcription by RNA polymerase II | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II. [GOC:go_curators, GOC:txnOH] |
| response to hypoxia | biological process | 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 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] |
| epithelial to mesenchymal transition | biological process | A transition where an epithelial cell loses apical/basolateral polarity, severs intercellular adhesive junctions, degrades basement membrane components and becomes a migratory mesenchymal cell. [GOC:dph, PMID:14701881] |
| endothelial cell proliferation | biological process | The multiplication or reproduction of endothelial cells, resulting in the expansion of a cell population. Endothelial cells are thin flattened cells which line the inside surfaces of body cavities, blood vessels, and lymph vessels, making up the endothelium. [GOC:add, ISBN:0781735149] |
| sprouting angiogenesis | biological process | The extension of new blood vessels from existing vessels into avascular tissues, this process includes the specialization of endothelial cells into leading tip and stalk cells, proliferation and migration of the endothelial cells and cell adhesion resulting in angiogenic sprout fusion or lumen formation. [PMID:16391003, PMID:23031691] |
| positive regulation of epithelial to mesenchymal transition | biological process | Any process that increases the rate, frequency, or extent of epithelial to mesenchymal transition. Epithelial to mesenchymal transition is where an epithelial cell loses apical/basolateral polarity, severs intercellular adhesive junctions, degrades basement membrane components and becomes a migratory mesenchymal cell. [GOC:BHF, GOC:dph, GOC:tb] |
| peptidyl-lysine oxidation | biological process | The oxidation of the terminal amino-methylene groups of peptidyl-L-lysine or peptidyl-5-hydroxy-L-lysine to aldehyde groups to form allysine or hydroxyallysine residues, respectively; these are intermediates in the formation of covalent cross-links between adjacent polypeptide chains in proteins such as collagens. [ISBN:0198547684, RESID:AA0121] |
| collagen fibril organization | biological process | Any process that determines the size and arrangement of collagen fibrils within an extracellular matrix. [GOC:mah, ISBN:0815316194] |
| positive regulation of chondrocyte differentiation | biological process | Any process that activates or increases the frequency, rate or extent of chondrocyte differentiation. [GOC:mah] |
| protein modification process | biological process | The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). [GOC:bf, GOC:jl] |
| endothelial cell migration | biological process | The orderly movement of an endothelial cell into the extracellular matrix to form an endothelium. [GOC:go_curators] |
| negative regulation of DNA-templated transcription | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH] |
| response to copper ion | biological process | 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 a copper ion stimulus. [GOC:ai] |
| heterochromatin organization | biological process | Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic heterochromatin, a compact and highly condensed form of chromatin. [GOC:mah] |
| negative regulation of stem cell population maintenance | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of stem cell population maintenance. [GOC:hjd, GOC:TermGenie, PMID:22969033] |