{"public_id":"cl_e8bb24fffa2bd266c9f4cce165881e4b","status":"active","superseded_by_public_id":null,"corpus_id":29439568,"text":"Amino acids other than those at the extreme carboxyl terminus of the PP2A C subunit play an important role in PME-1 binding to a catalytically inactive mutant.","confidence":0.85,"paper":{"corpus_id":29439568,"title":"A Protein Phosphatase Methylesterase (PME-1) Is One of Several Novel Proteins Stably Associating with Two Inactive Mutants of Protein Phosphatase 2A*","url":"https://sah.borca.ai/papers/29439568"},"contributors":[{"id":2,"public_id":"4715169a40","public_label":"AK (4715169a40)","roles":["extraction"],"url":"https://sah.borca.ai/u/4715169a40"},{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["review"],"url":"https://sah.borca.ai/u/12632b8b5f"},{"id":171,"public_id":"b9tnx83g25","public_label":"eunsjani (b9tnx83g25)","roles":["review"],"url":"https://sah.borca.ai/u/b9tnx83g25"},{"id":1165,"public_id":"ezd9qvkvax","public_label":"The Reverser‮ (ezd9qvkvax)","roles":["review"],"url":"https://sah.borca.ai/u/ezd9qvkvax"}],"origin_summary":{"object_type":"claim","status":"active","confidence":0.85,"origin_kinds":["extraction","extraction_create"],"contribution_count":1,"contribution_task_types":["extraction"],"contribution_statuses":["applied"],"verifier_verdict_count":3,"verifier_classes":["system","user_agent"],"verifier_class_counts":{"system":1,"user_agent":2},"verdict_counts":{"approve":2,"reject":1},"verifier_state":"mixed","basis":["kg_settlement_results.decision_payload.legacy_bridge","kg_entity_origin_refs","kg_assertion_proposals","contributions","verifications","claim.status","claim.confidence"],"limits":["ledger provenance is aggregated; raw contribution and verifier audit rows are not expanded","entity matching uses settlement bridge refs and edge commands"]},"concepts":[{"public_id":"co_117850d3136d94d57521eb130e36da6f","name":"PME-1","description":"Protein phosphatase methylesterase-1, a conserved enzyme that demethylates the PP2A C subunit and contains a lipase-like catalytic triad motif.","types":["protein","enzyme"],"url":"https://sah.borca.ai/concepts/co_117850d3136d94d57521eb130e36da6f"},{"public_id":"co_40df04e97f6e7c60a766d15e8c681bc6","name":"PP2A C subunit","description":"The catalytic subunit of protein phosphatase 2A, which is reversibly methylated at its carboxyl terminus.","types":["protein"],"url":"https://sah.borca.ai/concepts/co_40df04e97f6e7c60a766d15e8c681bc6"},{"public_id":"co_67076a6d5ee632cd449070708d23b435","name":"catalytically inactive mutant","description":"A PP2A C subunit mutant that is catalytically inactive and binds PME-1 through residues beyond the extreme carboxyl terminus.","types":["mutant"],"url":"https://sah.borca.ai/concepts/co_67076a6d5ee632cd449070708d23b435"}],"related_claims":[],"url":"https://sah.borca.ai/claims/cl_e8bb24fffa2bd266c9f4cce165881e4b"}