Proteins > Transmembrane prolyl 4-hydroxylase
Page last updated: 2024-08-07 13:46:38
Transmembrane prolyl 4-hydroxylase
A transmembrane prolyl 4-hydroxylase that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9NXG6]
Synonyms
P4H-TM;
EC 1.14.11.29;
Hypoxia-inducible factor prolyl hydroxylase 4;
HIF-PH4;
HIF-prolyl hydroxylase 4;
HPH-4
Research
Bioassay Publications (4)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (75.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 1 (25.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Compounds (9)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Novel inhibitors of prolyl 4-hydroxylase. 5. The intriguing structure-activity relationships seen with 2,2'-bipyridine and its 5,5'-dicarboxylic acid derivatives.Journal of medicinal chemistry, , Nov-26, Volume: 36, Issue:24, 1993
Novel inhibitors of prolyl 4-hydroxylase.Journal of medicinal chemistry, , Mar-06, Volume: 35, Issue:5, 1992
Novel inhibitors of prolyl 4-hydroxylase. 5. The intriguing structure-activity relationships seen with 2,2'-bipyridine and its 5,5'-dicarboxylic acid derivatives.Journal of medicinal chemistry, , Nov-26, Volume: 36, Issue:24, 1993
Novel inhibitors of prolyl 4-hydroxylase.Journal of medicinal chemistry, , Mar-06, Volume: 35, Issue:5, 1992
Novel inhibitors of prolyl 4-hydroxylase. 2. 5-Amide substituted pyridine-2-carboxylic acids.Journal of medicinal chemistry, , Mar-06, Volume: 35, Issue:5, 1992
Enables
This protein enables 6 target(s):
Target | Category | Definition |
iron ion binding | molecular function | Binding to an iron (Fe) ion. [GOC:ai] |
calcium ion binding | molecular function | Binding to a calcium ion (Ca2+). [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] |
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] |
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] |
procollagen-proline 4-dioxygenase activity | molecular function | Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2. [EC:1.14.11.2] |
Located In
This protein is located in 1 target(s):
Target | Category | Definition |
endoplasmic reticulum membrane | cellular component | The lipid bilayer surrounding the endoplasmic reticulum. [GOC:mah] |
Active In
This protein is active in 1 target(s):
Target | Category | Definition |
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] |
Involved In
This protein is involved in 2 target(s):
Target | Category | Definition |
regulation of erythrocyte differentiation | biological process | Any process that modulates the frequency, rate or extent of erythrocyte differentiation. [GOC:go_curators] |
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] |