Page last updated: 2024-08-07 18:49:06
Egl nine homolog 1
An egl nine homolog 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9GZT9]
Synonyms
EC 1.14.11.29;
Hypoxia-inducible factor prolyl hydroxylase 2;
HIF-PH2;
HIF-prolyl hydroxylase 2;
HPH-2;
Prolyl hydroxylase domain-containing protein 2;
PHD2;
SM-20
Research
Bioassay Publications (24)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (12.50) | 29.6817 |
2010's | 15 (62.50) | 24.3611 |
2020's | 6 (25.00) | 2.80 |
Compounds (21)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Drugs with Other Measurements
Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors.Journal of medicinal chemistry, , Jan-24, Volume: 56, Issue:2, 2013
Using NMR solvent water relaxation to investigate metalloenzyme-ligand binding interactions.Journal of medicinal chemistry, , Jan-28, Volume: 53, Issue:2, 2010
Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one?Nature chemical biology, , Volume: 3, Issue:3, 2007
Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors.Journal of medicinal chemistry, , Jan-24, Volume: 56, Issue:2, 2013
Using NMR solvent water relaxation to investigate metalloenzyme-ligand binding interactions.Journal of medicinal chemistry, , Jan-28, Volume: 53, Issue:2, 2010
Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases.Journal of medicinal chemistry, , Nov-27, Volume: 51, Issue:22, 2008
Plant growth regulator daminozide is a selective inhibitor of human KDM2/7 histone demethylases.Journal of medicinal chemistry, , Jul-26, Volume: 55, Issue:14, 2012
2-Oxoglutarate analogue inhibitors of prolyl hydroxylase domain 2.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 19, Issue:21, 2009
Inhibition of a viral prolyl hydroxylase.Bioorganic & medicinal chemistry, , 06-15, Volume: 27, Issue:12, 2019
Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors.Journal of medicinal chemistry, , Jan-24, Volume: 56, Issue:2, 2013
Design, synthesis, enzyme-inhibitory activity, and effect on human cancer cells of a novel series of jumonji domain-containing protein 2 histone demethylase inhibitors.Journal of medicinal chemistry, , Aug-12, Volume: 53, Issue:15, 2010
Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases.Journal of medicinal chemistry, , Nov-27, Volume: 51, Issue:22, 2008
Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors.Journal of medicinal chemistry, , Jan-24, Volume: 56, Issue:2, 2013
Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases.Journal of medicinal chemistry, , Nov-27, Volume: 51, Issue:22, 2008
Inhibition of a viral prolyl hydroxylase.Bioorganic & medicinal chemistry, , 06-15, Volume: 27, Issue:12, 2019
Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors.Journal of medicinal chemistry, , Jan-24, Volume: 56, Issue:2, 2013
Inhibition of a viral prolyl hydroxylase.Bioorganic & medicinal chemistry, , 06-15, Volume: 27, Issue:12, 2019
Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors.Journal of medicinal chemistry, , Jan-24, Volume: 56, Issue:2, 2013
Lysine demethylases inhibitors.Journal of medicinal chemistry, , Dec-22, Volume: 54, Issue:24, 2011
Inhibitors of histone demethylases.Bioorganic & medicinal chemistry, , Jun-15, Volume: 19, Issue:12, 2011
Design, synthesis, enzyme-inhibitory activity, and effect on human cancer cells of a novel series of jumonji domain-containing protein 2 histone demethylase inhibitors.Journal of medicinal chemistry, , Aug-12, Volume: 53, Issue:15, 2010
Using NMR solvent water relaxation to investigate metalloenzyme-ligand binding interactions.Journal of medicinal chemistry, , Jan-28, Volume: 53, Issue:2, 2010
2-Oxoglutarate analogue inhibitors of prolyl hydroxylase domain 2.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 19, Issue:21, 2009
Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases.Journal of medicinal chemistry, , Nov-27, Volume: 51, Issue:22, 2008
Synthesis and biological evaluation of (4-hydroxy-2-(substitued sulfonamido)pyrimidine-5-carbonyl)glycines as oral erythropoietin secretagogues.Bioorganic & medicinal chemistry letters, , 11-15, Volume: 76, 2022
Novel PHD2/HDACs hybrid inhibitors protect against cisplatin-induced acute kidney injury.European journal of medicinal chemistry, , Feb-15, Volume: 230, 2022
Tetrahydropyridin-4-ylpicolinoylglycines as novel and orally active prolyl hydroxylase 2 (PHD2) inhibitors for the treatment of renal anemia.European journal of medicinal chemistry, , Aug-05, Volume: 238, 2022
Discovery of a Highly Selective and H435R-Sensitive Thyroid Hormone Receptor β Agonist.Journal of medicinal chemistry, , 05-26, Volume: 65, Issue:10, 2022
[no title available]Journal of medicinal chemistry, , 09-10, Volume: 63, Issue:17, 2020
Inhibition of a viral prolyl hydroxylase.Bioorganic & medicinal chemistry, , 06-15, Volume: 27, Issue:12, 2019
Photoactivatable Prolyl Hydroxylase 2 Inhibitors for Stabilizing the Hypoxia-Inducible Factor with Light.Journal of medicinal chemistry, , 08-22, Volume: 62, Issue:16, 2019
Click Chemistry-Based Discovery of [3-Hydroxy-5-(1 H-1,2,3-triazol-4-yl)picolinoyl]glycines as Orally Active Hypoxia-Inducing Factor Prolyl Hydroxylase Inhibitors with Favorable Safety Profiles for the Treatment of Anemia.Journal of medicinal chemistry, , 06-28, Volume: 61, Issue:12, 2018
Discovery of N-[Bis(4-methoxyphenyl)methyl]-4-hydroxy-2-(pyridazin-3-yl)pyrimidine-5-carboxamide (MK-8617), an Orally Active Pan-Inhibitor of Hypoxia-Inducible Factor Prolyl Hydroxylase 1-3 (HIF PHD1-3) for the Treatment of Anemia.Journal of medicinal chemistry, , 12-22, Volume: 59, Issue:24, 2016
Affinity-Based Fluorescence Polarization Assay for High-Throughput Screening of Prolyl Hydroxylase 2 Inhibitors.ACS medicinal chemistry letters, , Dec-10, Volume: 6, Issue:12, 2015
Small-Molecule Modulators of the Hypoxia-Inducible Factor Pathway: Development and Therapeutic Applications.Journal of medicinal chemistry, , 06-27, Volume: 62, Issue:12, 2019
Inhibition of a viral prolyl hydroxylase.Bioorganic & medicinal chemistry, , 06-15, Volume: 27, Issue:12, 2019
Inhibition of the Oxygen-Sensing Asparaginyl Hydroxylase Factor Inhibiting Hypoxia-Inducible Factor: A Potential Hypoxia Response Modulating Strategy.Journal of medicinal chemistry, , 06-10, Volume: 64, Issue:11, 2021
Inhibition of a viral prolyl hydroxylase.Bioorganic & medicinal chemistry, , 06-15, Volume: 27, Issue:12, 2019
Prolyl Hydroxylase Inhibitors: A Breakthrough in the Therapy of Anemia Associated with Chronic Diseases.Journal of medicinal chemistry, , 08-23, Volume: 61, Issue:16, 2018
Affinity-Based Fluorescence Polarization Assay for High-Throughput Screening of Prolyl Hydroxylase 2 Inhibitors.ACS medicinal chemistry letters, , Dec-10, Volume: 6, Issue:12, 2015
Enables
This protein enables 8 target(s):
Target | Category | Definition |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
ferrous iron binding | molecular function | Binding to a ferrous iron ion, Fe(II). [GOC:ai] |
2-oxoglutarate-dependent dioxygenase activity | molecular function | Catalysis of the reaction: A + 2-oxoglutarate + O2 = B + succinate + CO2. This is an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from 2-oxoglutarate and one other donor, and one atom of oxygen is incorporated into each donor. [GOC:mah] |
enzyme binding | molecular function | Binding to an enzyme, a protein with catalytic activity. [GOC:jl] |
L-ascorbic acid binding | molecular function | Binding to L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species. [GOC:mah] |
peptidyl-proline dioxygenase activity | molecular function | Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl hydroxy-L-proline + succinate + CO2. [GOC:mah, GOC:vw, PMID:24550447, PMID:24550462] |
hypoxia-inducible factor-proline dioxygenase activity | molecular function | Catalysis of the reaction: 2-oxoglutarate + L-prolyl-[hypoxia-inducible factor alpha subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-inducible factor alpha subunit]. [PMID:11595184, PMID:11598268] |
peptidyl-proline 4-dioxygenase activity | molecular function | Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl trans-4-hydroxy-L-proline + succinate + CO2. [GOC:mah] |
Located In
This protein is located in 5 target(s):
Target | Category | Definition |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
postsynaptic density | cellular component | An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components. [GOC:BHF, GOC:dos, GOC:ef, GOC:jid, GOC:pr, GOC:sjp, http://molneuro.kaist.ac.kr/psd, PMID:14532281, Wikipedia:Postsynaptic_density] |
intracellular membrane-bounded organelle | cellular component | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators] |
glutamatergic synapse | cellular component | A synapse that uses glutamate as a neurotransmitter. [GOC:dos] |
Active In
This protein is active in 2 target(s):
Target | Category | Definition |
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] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
Involved In
This protein is involved in 16 target(s):
Target | Category | Definition |
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] |
intracellular iron ion homeostasis | biological process | A homeostatic process involved in the maintenance of a steady state level of iron ions within a cell. [GOC:ai, GOC:mah] |
intracellular oxygen homeostasis | biological process | A homeostatic process involved in the maintenance of a steady state level of oxygen within a cell. [GOC:rph] |
negative regulation of DNA-binding transcription factor activity | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of a transcription factor, any factor involved in the initiation or regulation of transcription. [GOC:jl] |
regulation of angiogenesis | biological process | Any process that modulates the frequency, rate or extent of angiogenesis. [GOC:go_curators] |
positive regulation of transcription by RNA polymerase II | biological process | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH] |
negative regulation of cyclic-nucleotide phosphodiesterase activity | biological process | Any process that stops or reduces the rate of cyclic nucleotide phosphodiesterase activity, the catalysis of the reaction: nucleotide 3',5'-cyclic phosphate + H2O = nucleotide 5'-phosphate. [GOC:ai, GOC:tb] |
cardiac muscle tissue morphogenesis | biological process | The process in which the anatomical structures of cardiac muscle tissue are generated and organized. [GOC:devbiol] |
heart trabecula formation | biological process | The process of creating a trabecula in the heart. A trabecula is a tissue element in the form of a small beam, strut or rod. [GOC:dph] |
ventricular septum morphogenesis | biological process | The developmental process in which a ventricular septum is generated and organized. A ventricular septum is an anatomical structure that separates the lower chambers (ventricles) of the heart from one another. [GOC:dph] |
labyrinthine layer development | biological process | The process in which the labyrinthine layer of the placenta progresses, from its formation to its mature state. [GOC:dph] |
response to nitric oxide | 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 nitric oxide stimulus. [GOC:mah, GOC:yaf] |
regulation of modification of postsynaptic structure | biological process | Any process that modulates the frequency, rate or extent of modification of postsynaptic structure. [GOC:dos] |
regulation protein catabolic process at postsynapse | biological process | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein at the postsynapse. [PMID:17062563] |
peptidyl-proline hydroxylation to 4-hydroxy-L-proline | biological process | The modification of peptidyl-proline to form 4-hydroxy-L-proline; catalyzed by procollagen-proline,2-oxoglutarate-4-dioxygenase. [RESID:AA0030] |
cellular response to hypoxia | biological process | Any 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 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:mah] |