A ribonuclease H1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O60930]
RNase H1;
EC 3.1.26.4;
Ribonuclease H type II
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| beta-thujaplicinol | Homo sapiens (human) | IC50 | 0.6300 | 2 | 2 |
| 3-hydroxy-quinazoline-2,4-dione | Homo sapiens (human) | IC50 | 5.9500 | 2 | 2 |
| 2-hydroxy-4h-isoquinoline-1,3-dione | Homo sapiens (human) | IC50 | 0.1275 | 2 | 2 |
| nsc 727447 | Homo sapiens (human) | IC50 | 28.7750 | 1 | 4 |
This protein enables 6 target(s):
| Target | Category | Definition |
|---|---|---|
| magnesium ion binding | molecular function | Binding to a magnesium (Mg) ion. [GOC:ai] |
| nucleic acid binding | molecular function | Binding to a nucleic acid. [GOC:jl] |
| RNA binding | molecular function | Binding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah] |
| RNA-DNA hybrid ribonuclease activity | molecular function | Catalysis of the endonucleolytic cleavage of RNA in RNA-DNA hybrids to 5'-phosphomonoesters. [EC:3.1.26.4] |
| RNA nuclease activity | molecular function | Catalysis of the hydrolysis of phosphodiester bonds in chains of RNA. [GOC:mah, ISBN:0198547684] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
This protein is located in 1 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] |
This protein is involved in 2 target(s):
| Target | Category | Definition |
|---|---|---|
| RNA catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. [ISBN:0198506732] |
| DNA replication, removal of RNA primer | biological process | Removal of the Okazaki RNA primer from the lagging strand of replicating DNA, by a combination of the actions of DNA polymerase, DNA helicase and an endonuclease. [GOC:jl, PMID:12424238] |