Proteins > Prolyl 4-hydroxylase subunit alpha-1
Page last updated: 2024-08-08 00:46:37
Prolyl 4-hydroxylase subunit alpha-1
A prolyl 4-hydroxylase subunit alpha-1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P13674]
Synonyms
4-PH alpha-1;
EC 1.14.11.2;
Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
Research
Bioassay Publications (2)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 1 (50.00) | 29.6817 |
2010's | 1 (50.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Compounds (3)
Drugs with Inhibition Measurements
Drugs with Other Measurements
Enables
This protein enables 5 target(s):
Target | Category | Definition |
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] |
iron ion binding | molecular function | Binding to an iron (Fe) ion. [GOC:ai] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
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] |
identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
Located In
This protein is located in 5 target(s):
Target | Category | Definition |
mitochondrion | cellular component | A 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] |
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] |
endoplasmic reticulum lumen | cellular component | The volume enclosed by the membranes of the endoplasmic reticulum. [ISBN:0198547684] |
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] |
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] |
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] |
Part Of
This protein is part of 1 target(s):
Target | Category | Definition |
procollagen-proline 4-dioxygenase complex | cellular component | A protein complex that catalyzes the formation of procollagen trans-4-hydroxy-L-proline and succinate from procollagen L-proline and 2-oxoglutarate, requiring Fe2+ and ascorbate. Contains two alpha subunits that contribute to most parts of the catalytic sites, and two beta subunits that are identical to protein-disulfide isomerase. [PMID:14500733, PMID:7753822] |
Involved In
This protein is involved in 2 target(s):
Target | Category | Definition |
collagen fibril organization | biological process | Any process that determines the size and arrangement of collagen fibrils within an extracellular matrix. [GOC:mah, ISBN:0815316194] |
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] |