{
 "meta": {
  "api_version": "1.0.0",
  "dataset_version": "2.0.1",
  "corpus_snapshot": "2026-10-12T22:59:14+0200",
  "source_commit": "93739c9d195dc39e47eecfabc3cab2565a2f256f",
  "license": "CC-BY-4.0",
  "cite": "Barton O. Oliver's mTOR Atlas. doi:10.5281/zenodo.22059963",
  "docs": "https://mtor-atlas.org/api/"
 },
 "data": {
  "id": "GATOR1-RAG",
  "claim": "GATOR1 inhibits Rag GTPases",
  "source": {
   "name": "GATOR1",
   "entity": "gator1"
  },
  "target": {
   "name": "Rag GTPases",
   "entity": "rag-gtpases"
  },
  "effect": "inhibits",
  "type": "gap-activity",
  "directness": "direct",
  "timescale": "seconds",
  "compartment": "lyso",
  "map_band": "lyso",
  "species": [
   "human cells"
  ],
  "mechanism": "GATOR1 acts as a GAP: it forces RagA/B to hydrolyse GTP, flipping the Rag heterodimer into the inactive shape that cannot hold mTORC1.",
  "mechanism_beginner": "GATOR1 forces the Rag proteins into their \"off\" shape, so they can no longer hold onto mTORC1.",
  "context": null,
  "boundary": "Human cell biochemistry with cancer genomics (BAR2013) and a cryo-EM structure (SHE2018). GAP activity is shown on purified and cellular Rags; the cited studies do not test it in whole animals or in people.",
  "note": null,
  "consensus_contested": false,
  "curation_contested": false,
  "contested": false,
  "confidence": {
   "mechanistic": "high",
   "human_relevance": "plausible",
   "consensus": "established"
  },
  "evidence": {
   "kind": "Direct biochemical",
   "strongest": {
    "code": "M",
    "label": "Molecular — cells, biochemistry, structure"
   },
   "supporting": [
    "BAR2013",
    "SHE2018"
   ],
   "conflicting": []
  },
  "external_refs": [],
  "reviewed": null,
  "updated": null,
  "checked": null,
  "review_status": "unreviewed",
  "reviewer": null,
  "curation_status": "Proposed",
  "url": "https://mtor-atlas.org/relation/GATOR1-RAG/",
  "api_url": "https://mtor-atlas.org/api/v1/relations/GATOR1-RAG.json"
 }
}