A vitamin K epoxide reductase complex subunit 1-like protein 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q8N0U8]
VKORC1-like protein 1;
EC 1.17.4.4
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 | 1 (100.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
---|---|---|---|---|---|
warfarin | Homo sapiens (human) | Ki | 21.7500 | 1 | 4 |
This protein enables 3 target(s):
Target | Category | Definition |
---|---|---|
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
vitamin-K-epoxide reductase (warfarin-sensitive) activity | molecular function | Catalysis of the reaction: phylloquinol + a protein with a disulfide bond = phylloquinone + a protein with reduced L-cysteine residues. [RHEA:57744] |
quinone binding | molecular function | Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds. [ISBN:0198506732] |
This protein is located in 2 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] |
endoplasmic reticulum membrane | cellular component | The lipid bilayer surrounding the endoplasmic reticulum. [GOC:mah] |
This protein is involved in 3 target(s):
Target | Category | Definition |
---|---|---|
peptidyl-glutamic acid carboxylation | biological process | The gamma-carboxylation of peptidyl-glutamic acid; catalyzed by the vitamin K dependent gamma-glutamyl carboxylase. [RESID:AA0032] |
cellular response to oxidative stress | 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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. [GOC:mah] |
vitamin K metabolic process | biological process | The chemical reactions and pathways involving any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals. Vitamin K substances share a methylated naphthoquinone ring structure and vary in the aliphatic side chains attached to the molecule. [GOC:jl, http://www.dentistry.leeds.ac.uk/biochem/thcme/vitamins.html#k] |