ASNS asparagine synthetase (glutamine-hydrolyzing)
ENSG00000070669 · protein coding · Open Targets profile
Catalyzes the ATP-dependent synthesis of L-asparagine from L- aspartate, using L-glutamine as a source of nitrogen (PubMed:2564390, PubMed:2573597). Can also use ammonia as the nitrogen source in vitro (PubMed:2564390, PubMed:2573597). {ECO:0000269|PubMed:2564390, ECO:0000269|PubMed:2573597}.
Each row is a cancer, strongest overall evidence first. The two dots show how strong the inherited (germline) and tumour-mutation (somatic) evidence is; the line between them is the gap.
Scores run from 0 (no evidence) to 1 (strongest). A missing dot at 0 means Open Targets holds no evidence of that kind. Source: Open Targets Platform, fetched live.
Tractability
- Small molecule
- Structure with Ligand, High-Quality Ligand
- PROTAC
- Database Ubiquitination, Half-life Data, Small Molecule Binder
gnomAD loss of function constraint: o/e 0.5910000205039978 (upper bound 0.7774900197982788). Low values mean loss of function is poorly tolerated, a safety flag for inhibition.
Who runs trials of these drugs
No named investigators on registry trials of ASNS's approved or late-stage drugs in the last three years.
No terminated, withdrawn or suspended trials of ASNS's drugs are registered
All 0 drugs and clinical candidates as a table
Each drug, stage and indication links to its Open Targets record, where the trials and approvals behind it are listed. Salt forms (for example a mesylate) are listed as Open Targets records them, as separate entries.
| Drug | Type | Highest stage | Indications | Source records |
|---|---|---|---|---|
| No drugs or clinical candidates recorded. | ||||