{"gene":"TRAPPC14","run_date":"2026-04-28T21:42:59","timeline":{"discoveries":[{"year":2019,"finding":"TRAPPC14 (C7orf43/MAP11) directly binds to Rabin8 and is required for Rabin8 preciliary centrosome accumulation during ciliogenesis; knockdown of TRAPPC14 diminishes Rabin8 centrosomal recruitment.","method":"MS-based interactome, direct binding assay, knockdown with centrosomal accumulation readout","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 — reciprocal/MS-based identification plus direct binding plus functional KD phenotype, multiple orthogonal methods in one study","pmids":["31467083"],"is_preprint":false},{"year":2019,"finding":"TRAPPC14 (C7orf43) co-sediments with TRAPPII complex subunits and directly interacts with TRAPPC proteins, establishing it as a TRAPPII-specific complex component; it is dispensable for TRAPPII complex integrity but mediates Rabin8 association with the TRAPPII complex.","method":"Co-sedimentation, direct interaction assays, complex integrity analysis","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1-2 — direct biochemical reconstitution of interactions with multiple orthogonal methods in a single rigorous study","pmids":["31467083"],"is_preprint":false},{"year":2019,"finding":"TRAPPC14 interacts with distal appendage proteins FBF1 and CEP83, which are required for GFP-Rabin8 centrosomal accumulation, supporting a role for the TRAPPII complex in tethering preciliary vesicles to the mother centriole.","method":"Co-immunoprecipitation, knockdown with centrosomal accumulation readout","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 — Co-IP and functional KD, single lab with multiple methods","pmids":["31467083"],"is_preprint":false},{"year":2019,"finding":"TRAPPC14 (MAP11/C7orf43) associates with mitotic spindles, co-localizing and physically associating with α-tubulin during mitosis; it also co-localizes with PLK1 at edges of microtubule extensions of daughter cells post-cytokinesis abscission, implicating roles in spindle dynamics and regulation of cell abscission.","method":"Immunofluorescence, co-immunoprecipitation in SH-SY5Y cells; CRISPR/Cas9 knockout zebrafish model","journal":"Brain : a journal of neurology","confidence":"Medium","confidence_rationale":"Tier 2 — Co-IP plus co-localization plus loss-of-function in two systems (human cells and zebrafish)","pmids":["30715179"],"is_preprint":false},{"year":2019,"finding":"MAP11 (TRAPPC14) expression precedes α-tubulin in gap formation of cell abscission at the midbody, and lentiviral silencing of MAP11 diminishes SH-SY5Y cell viability by reducing proliferation rather than affecting apoptosis.","method":"Lentiviral shRNA knockdown, cell viability and proliferation assays, immunofluorescence","journal":"Brain : a journal of neurology","confidence":"Medium","confidence_rationale":"Tier 2 — clean KD with specific cellular phenotype readout distinguishing proliferation from apoptosis","pmids":["30715179"],"is_preprint":false},{"year":2019,"finding":"TRAPPC14 (C7orf43) is required for ciliation in both human cells and zebrafish embryos, as demonstrated by knockdown/knockout causing ciliogenesis defects.","method":"siRNA knockdown in human cells, CRISPR/Cas9 knockout in zebrafish embryos with ciliogenesis phenotype readout","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 — loss-of-function in two independent model systems with defined cellular phenotype","pmids":["31467083"],"is_preprint":false},{"year":2019,"finding":"C7orf43 (TRAPPC14) upregulates TERT expression through Yes-associated protein 1 (YAP1), with the C7orf43-responsive site mapped to between base pairs -169 and -59 in the TERT promoter.","method":"Genome-wide shRNA screen, promoter assays","journal":"Cancer science","confidence":"Low","confidence_rationale":"Tier 3 — single lab, promoter assay with limited mechanistic follow-up on YAP1 link","pmids":["30447097"],"is_preprint":false}],"current_model":"TRAPPC14 (C7orf43/MAP11) is a TRAPPII-specific complex component that directly binds Rabin8 to mediate its preciliary centrosomal accumulation and interact with distal appendage proteins FBF1 and CEP83, thereby tethering preciliary vesicles to the mother centriole during ciliogenesis; it also associates with α-tubulin and PLK1 at the mitotic spindle and midbody to regulate spindle dynamics and cytokinetic abscission, with loss of function causing microcephaly through impaired neuronal proliferation."},"narrative":{"teleology":[{"year":2019,"claim":"Establishing TRAPPC14 as a TRAPPII-specific subunit and Rabin8 effector resolved how the TRAPPII complex recruits Rabin8 to the centrosome during early ciliogenesis — a previously undefined targeting mechanism.","evidence":"MS-based interactome, co-sedimentation with TRAPPII subunits, direct binding assays, and siRNA knockdown with centrosomal Rabin8 accumulation readout in human cells","pmids":["31467083"],"confidence":"High","gaps":["Structural basis of the TRAPPC14–Rabin8 interaction is unknown","Whether TRAPPC14 contributes to TRAPPII GEF activation of Rab11 is untested","Temporal regulation of TRAPPC14 incorporation into TRAPPII is not defined"]},{"year":2019,"claim":"Demonstration that TRAPPC14 interacts with distal appendage proteins FBF1 and CEP83 provided a physical link between the TRAPPII vesicle-trafficking complex and the centriolar docking machinery, explaining how preciliary vesicles are tethered to the mother centriole.","evidence":"Co-immunoprecipitation of TRAPPC14 with FBF1 and CEP83; knockdown of these DAPs phenocopied loss of centrosomal Rabin8","pmids":["31467083"],"confidence":"Medium","gaps":["Interactions with FBF1 and CEP83 rely on Co-IP without reciprocal validation or domain mapping","Whether TRAPPC14 directly contacts distal appendage proteins or bridges through other TRAPPII subunits is unresolved"]},{"year":2019,"claim":"Parallel work revealed a distinct mitotic function: TRAPPC14 associates with α-tubulin on the spindle and with PLK1 at the midbody, and its depletion reduces neuronal cell proliferation, establishing a dual role in both ciliogenesis and cell division.","evidence":"Immunofluorescence and Co-IP in SH-SY5Y cells; lentiviral shRNA knockdown with proliferation versus apoptosis discrimination; CRISPR knockout in zebrafish","pmids":["30715179"],"confidence":"Medium","gaps":["Whether TRAPPC14 functions at the spindle as part of the TRAPPII complex or independently is unknown","The mechanism by which TRAPPC14 regulates abscission timing is not defined","Causal link between midbody function and the microcephaly phenotype awaits direct demonstration"]},{"year":2019,"claim":"An shRNA screen identified a role for TRAPPC14 in upregulating TERT expression through YAP1, suggesting a potential link to telomerase regulation in cancer cells.","evidence":"Genome-wide shRNA screen and promoter-reporter assays in cancer cell lines","pmids":["30447097"],"confidence":"Low","gaps":["Single-lab finding without independent replication or detailed mechanistic follow-up on the YAP1 connection","Relationship between TERT regulation and known TRAPPII/ciliogenesis functions is unexplored"]},{"year":null,"claim":"Key open questions include whether TRAPPC14's spindle and ciliogenesis functions represent independent or coordinated activities, the structural basis of its interactions, and whether loss-of-function mutations cause human ciliopathy or microcephaly.","evidence":"","pmids":[],"confidence":"High","gaps":["No human genetic disease formally linked via causative mutation in the available timeline evidence","No structural or cryo-EM data on TRAPPC14 within the TRAPPII complex","Whether ciliogenesis and mitotic roles are cell-type or cell-cycle dependent is unresolved"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,1]}],"localization":[{"term_id":"GO:0005815","term_label":"microtubule organizing center","supporting_discovery_ids":[0,2,3]},{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[3,4]},{"term_id":"GO:0005929","term_label":"cilium","supporting_discovery_ids":[0,2,5]}],"pathway":[{"term_id":"R-HSA-5653656","term_label":"Vesicle-mediated transport","supporting_discovery_ids":[0,1,2]},{"term_id":"R-HSA-1852241","term_label":"Organelle biogenesis and maintenance","supporting_discovery_ids":[2,5]},{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[3,4]}],"complexes":["TRAPPII"],"partners":["RABIN8","FBF1","CEP83","TUBA1A","PLK1"],"other_free_text":[]},"mechanistic_narrative":"TRAPPC14 (C7orf43/MAP11) is a TRAPPII-specific complex subunit that functions at the intersection of ciliogenesis and mitotic cell division. It co-sediments with TRAPPII subunits and, while dispensable for overall complex integrity, directly binds Rabin8 and mediates its association with the TRAPPII complex, thereby driving Rabin8 preciliary centrosomal accumulation required for ciliogenesis; it also interacts with the distal appendage proteins FBF1 and CEP83, supporting a vesicle-tethering role at the mother centriole [PMID:31467083]. In mitosis, TRAPPC14 associates with α-tubulin on the mitotic spindle and co-localizes with PLK1 at the midbody during cytokinetic abscission, and its silencing reduces neuronal cell proliferation without affecting apoptosis [PMID:30715179]. Loss of TRAPPC14 function causes ciliogenesis defects in both human cells and zebrafish embryos [PMID:31467083]."},"prefetch_data":{"uniprot":{"accession":"Q8WVR3","full_name":"Trafficking protein particle complex subunit 14","aliases":["Microtubule-associated protein 11"],"length_aa":580,"mass_kda":62.6,"function":"Specific subunit of the TRAPP (transport protein particle) II complex, a highly conserved vesicle tethering complex that functions in late Golgi trafficking as a membrane tether (PubMed:30715179, PubMed:31467083). TRAPP II complex also has GEF activity toward RAB1A (By similarity). TRAPPC14 is dispensable for TRAPPII complex integrity but mediates RAB3IP preciliary vesicle trafficking to the mother centriole during ciliogenesis (PubMed:31467083). Modulates YAP1 activity as transcriptional regulator (PubMed:30447097)","subcellular_location":"Cytoplasm, cytoskeleton, spindle; Vesicle; Midbody; Cytoplasm","url":"https://www.uniprot.org/uniprotkb/Q8WVR3/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/TRAPPC14","classification":"Not Classified","n_dependent_lines":10,"n_total_lines":1208,"dependency_fraction":0.008278145695364239},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/TRAPPC14","total_profiled":1310},"omim":[{"mim_id":"618351","title":"MICROCEPHALY 25, PRIMARY, AUTOSOMAL RECESSIVE; MCPH25","url":"https://www.omim.org/entry/618351"},{"mim_id":"618350","title":"TRAFFICKING PROTEIN PARTICLE COMPLEX, SUBUNIT 14; TRAPPC14","url":"https://www.omim.org/entry/618350"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Enhanced","locations":[{"location":"Vesicles","reliability":"Enhanced"},{"location":"Plasma membrane","reliability":"Additional"},{"location":"Centriolar satellite","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/TRAPPC14"},"hgnc":{"alias_symbol":["FLJ10925"],"prev_symbol":["C7orf43","MAP11"]},"alphafold":{"accession":"Q8WVR3","domains":[{"cath_id":"2.60.40.10","chopping":"6-56_71-91_134-221","consensus_level":"high","plddt":79.3482,"start":6,"end":221},{"cath_id":"2.60.40,2.60.40","chopping":"225-366","consensus_level":"high","plddt":79.2809,"start":225,"end":366},{"cath_id":"2.60.40.10","chopping":"371-479_564-577","consensus_level":"high","plddt":81.5041,"start":371,"end":577}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8WVR3","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q8WVR3-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q8WVR3-F1-predicted_aligned_error_v6.png","plddt_mean":70.19},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=TRAPPC14","jax_strain_url":"https://www.jax.org/strain/search?query=TRAPPC14"},"sequence":{"accession":"Q8WVR3","fasta_url":"https://rest.uniprot.org/uniprotkb/Q8WVR3.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q8WVR3/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8WVR3"}},"corpus_meta":[{"pmid":"30715179","id":"PMC_30715179","title":"Mutations in the microtubule-associated protein MAP11 (C7orf43) cause microcephaly in humans and zebrafish.","date":"2019","source":"Brain : a journal of neurology","url":"https://pubmed.ncbi.nlm.nih.gov/30715179","citation_count":32,"is_preprint":false},{"pmid":"15087135","id":"PMC_15087135","title":"Characterization of a major outer membrane protein multigene family in Ehrlichia ruminantium.","date":"2004","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/15087135","citation_count":32,"is_preprint":false},{"pmid":"15995193","id":"PMC_15995193","title":"Transcription analysis of the major antigenic protein 1 multigene family of three in vitro-cultured Ehrlichia ruminantium isolates.","date":"2005","source":"Journal of bacteriology","url":"https://pubmed.ncbi.nlm.nih.gov/15995193","citation_count":30,"is_preprint":false},{"pmid":"12039046","id":"PMC_12039046","title":"Transcriptional analysis of the major antigenic protein 1 multigene family of Cowdria ruminantium.","date":"2002","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/12039046","citation_count":27,"is_preprint":false},{"pmid":"31467083","id":"PMC_31467083","title":"The C7orf43/TRAPPC14 component links the TRAPPII complex to Rabin8 for preciliary vesicle tethering at the mother centriole during ciliogenesis.","date":"2019","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/31467083","citation_count":25,"is_preprint":false},{"pmid":"30447097","id":"PMC_30447097","title":"Identification of genes involved in the regulation of TERT in hepatocellular carcinoma.","date":"2019","source":"Cancer science","url":"https://pubmed.ncbi.nlm.nih.gov/30447097","citation_count":18,"is_preprint":false},{"pmid":"17321077","id":"PMC_17321077","title":"Differential transcription of the major antigenic protein 1 multigene family of Ehrlichia ruminantium in Amblyomma variegatum ticks.","date":"2007","source":"Veterinary microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/17321077","citation_count":17,"is_preprint":false},{"pmid":"12381577","id":"PMC_12381577","title":"Major outer membrane proteins of Ehrlichia ruminantium encoded by a multigene family.","date":"2002","source":"Annals of the New York Academy of Sciences","url":"https://pubmed.ncbi.nlm.nih.gov/12381577","citation_count":3,"is_preprint":false},{"pmid":"38138609","id":"PMC_38138609","title":"Exploring Thiazolopyridine AV25R: Unraveling of Biological Activities, Selective Anti-Cancer Properties and In Silico Target and Binding Prediction in Hematological Neoplasms.","date":"2023","source":"Molecules (Basel, Switzerland)","url":"https://pubmed.ncbi.nlm.nih.gov/38138609","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5949,"output_tokens":1534,"usd":0.020428},"stage2":{"model":"claude-opus-4-6","input_tokens":4799,"output_tokens":1665,"usd":0.09843},"total_usd":0.118858,"stage1_batch_id":"msgbatch_01RPbVc9PDH9zQmYK5Hs6srm","stage2_batch_id":"msgbatch_01JVbVLzeKN2yVrsGp3zC8aM","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2019,\n      \"finding\": \"TRAPPC14 (C7orf43/MAP11) directly binds to Rabin8 and is required for Rabin8 preciliary centrosome accumulation during ciliogenesis; knockdown of TRAPPC14 diminishes Rabin8 centrosomal recruitment.\",\n      \"method\": \"MS-based interactome, direct binding assay, knockdown with centrosomal accumulation readout\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — reciprocal/MS-based identification plus direct binding plus functional KD phenotype, multiple orthogonal methods in one study\",\n      \"pmids\": [\"31467083\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"TRAPPC14 (C7orf43) co-sediments with TRAPPII complex subunits and directly interacts with TRAPPC proteins, establishing it as a TRAPPII-specific complex component; it is dispensable for TRAPPII complex integrity but mediates Rabin8 association with the TRAPPII complex.\",\n      \"method\": \"Co-sedimentation, direct interaction assays, complex integrity analysis\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 — direct biochemical reconstitution of interactions with multiple orthogonal methods in a single rigorous study\",\n      \"pmids\": [\"31467083\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"TRAPPC14 interacts with distal appendage proteins FBF1 and CEP83, which are required for GFP-Rabin8 centrosomal accumulation, supporting a role for the TRAPPII complex in tethering preciliary vesicles to the mother centriole.\",\n      \"method\": \"Co-immunoprecipitation, knockdown with centrosomal accumulation readout\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — Co-IP and functional KD, single lab with multiple methods\",\n      \"pmids\": [\"31467083\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"TRAPPC14 (MAP11/C7orf43) associates with mitotic spindles, co-localizing and physically associating with α-tubulin during mitosis; it also co-localizes with PLK1 at edges of microtubule extensions of daughter cells post-cytokinesis abscission, implicating roles in spindle dynamics and regulation of cell abscission.\",\n      \"method\": \"Immunofluorescence, co-immunoprecipitation in SH-SY5Y cells; CRISPR/Cas9 knockout zebrafish model\",\n      \"journal\": \"Brain : a journal of neurology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — Co-IP plus co-localization plus loss-of-function in two systems (human cells and zebrafish)\",\n      \"pmids\": [\"30715179\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"MAP11 (TRAPPC14) expression precedes α-tubulin in gap formation of cell abscission at the midbody, and lentiviral silencing of MAP11 diminishes SH-SY5Y cell viability by reducing proliferation rather than affecting apoptosis.\",\n      \"method\": \"Lentiviral shRNA knockdown, cell viability and proliferation assays, immunofluorescence\",\n      \"journal\": \"Brain : a journal of neurology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — clean KD with specific cellular phenotype readout distinguishing proliferation from apoptosis\",\n      \"pmids\": [\"30715179\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"TRAPPC14 (C7orf43) is required for ciliation in both human cells and zebrafish embryos, as demonstrated by knockdown/knockout causing ciliogenesis defects.\",\n      \"method\": \"siRNA knockdown in human cells, CRISPR/Cas9 knockout in zebrafish embryos with ciliogenesis phenotype readout\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — loss-of-function in two independent model systems with defined cellular phenotype\",\n      \"pmids\": [\"31467083\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"C7orf43 (TRAPPC14) upregulates TERT expression through Yes-associated protein 1 (YAP1), with the C7orf43-responsive site mapped to between base pairs -169 and -59 in the TERT promoter.\",\n      \"method\": \"Genome-wide shRNA screen, promoter assays\",\n      \"journal\": \"Cancer science\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 — single lab, promoter assay with limited mechanistic follow-up on YAP1 link\",\n      \"pmids\": [\"30447097\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"TRAPPC14 (C7orf43/MAP11) is a TRAPPII-specific complex component that directly binds Rabin8 to mediate its preciliary centrosomal accumulation and interact with distal appendage proteins FBF1 and CEP83, thereby tethering preciliary vesicles to the mother centriole during ciliogenesis; it also associates with α-tubulin and PLK1 at the mitotic spindle and midbody to regulate spindle dynamics and cytokinetic abscission, with loss of function causing microcephaly through impaired neuronal proliferation.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"TRAPPC14 (C7orf43/MAP11) is a TRAPPII-specific complex subunit that functions at the intersection of ciliogenesis and mitotic cell division. It co-sediments with TRAPPII subunits and, while dispensable for overall complex integrity, directly binds Rabin8 and mediates its association with the TRAPPII complex, thereby driving Rabin8 preciliary centrosomal accumulation required for ciliogenesis; it also interacts with the distal appendage proteins FBF1 and CEP83, supporting a vesicle-tethering role at the mother centriole [PMID:31467083]. In mitosis, TRAPPC14 associates with α-tubulin on the mitotic spindle and co-localizes with PLK1 at the midbody during cytokinetic abscission, and its silencing reduces neuronal cell proliferation without affecting apoptosis [PMID:30715179]. Loss of TRAPPC14 function causes ciliogenesis defects in both human cells and zebrafish embryos [PMID:31467083].\",\n  \"teleology\": [\n    {\n      \"year\": 2019,\n      \"claim\": \"Establishing TRAPPC14 as a TRAPPII-specific subunit and Rabin8 effector resolved how the TRAPPII complex recruits Rabin8 to the centrosome during early ciliogenesis — a previously undefined targeting mechanism.\",\n      \"evidence\": \"MS-based interactome, co-sedimentation with TRAPPII subunits, direct binding assays, and siRNA knockdown with centrosomal Rabin8 accumulation readout in human cells\",\n      \"pmids\": [\"31467083\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis of the TRAPPC14–Rabin8 interaction is unknown\",\n        \"Whether TRAPPC14 contributes to TRAPPII GEF activation of Rab11 is untested\",\n        \"Temporal regulation of TRAPPC14 incorporation into TRAPPII is not defined\"\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Demonstration that TRAPPC14 interacts with distal appendage proteins FBF1 and CEP83 provided a physical link between the TRAPPII vesicle-trafficking complex and the centriolar docking machinery, explaining how preciliary vesicles are tethered to the mother centriole.\",\n      \"evidence\": \"Co-immunoprecipitation of TRAPPC14 with FBF1 and CEP83; knockdown of these DAPs phenocopied loss of centrosomal Rabin8\",\n      \"pmids\": [\"31467083\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Interactions with FBF1 and CEP83 rely on Co-IP without reciprocal validation or domain mapping\",\n        \"Whether TRAPPC14 directly contacts distal appendage proteins or bridges through other TRAPPII subunits is unresolved\"\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Parallel work revealed a distinct mitotic function: TRAPPC14 associates with α-tubulin on the spindle and with PLK1 at the midbody, and its depletion reduces neuronal cell proliferation, establishing a dual role in both ciliogenesis and cell division.\",\n      \"evidence\": \"Immunofluorescence and Co-IP in SH-SY5Y cells; lentiviral shRNA knockdown with proliferation versus apoptosis discrimination; CRISPR knockout in zebrafish\",\n      \"pmids\": [\"30715179\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Whether TRAPPC14 functions at the spindle as part of the TRAPPII complex or independently is unknown\",\n        \"The mechanism by which TRAPPC14 regulates abscission timing is not defined\",\n        \"Causal link between midbody function and the microcephaly phenotype awaits direct demonstration\"\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"An shRNA screen identified a role for TRAPPC14 in upregulating TERT expression through YAP1, suggesting a potential link to telomerase regulation in cancer cells.\",\n      \"evidence\": \"Genome-wide shRNA screen and promoter-reporter assays in cancer cell lines\",\n      \"pmids\": [\"30447097\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Single-lab finding without independent replication or detailed mechanistic follow-up on the YAP1 connection\",\n        \"Relationship between TERT regulation and known TRAPPII/ciliogenesis functions is unexplored\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Key open questions include whether TRAPPC14's spindle and ciliogenesis functions represent independent or coordinated activities, the structural basis of its interactions, and whether loss-of-function mutations cause human ciliopathy or microcephaly.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"No human genetic disease formally linked via causative mutation in the available timeline evidence\",\n        \"No structural or cryo-EM data on TRAPPC14 within the TRAPPII complex\",\n        \"Whether ciliogenesis and mitotic roles are cell-type or cell-cycle dependent is unresolved\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [0, 2, 3]},\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [3, 4]},\n      {\"term_id\": \"GO:0005929\", \"supporting_discovery_ids\": [0, 2, 5]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-5653656\", \"supporting_discovery_ids\": [0, 1, 2]},\n      {\"term_id\": \"R-HSA-1852241\", \"supporting_discovery_ids\": [2, 5]},\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [3, 4]}\n    ],\n    \"complexes\": [\n      \"TRAPPII\"\n    ],\n    \"partners\": [\n      \"RABIN8\",\n      \"FBF1\",\n      \"CEP83\",\n      \"TUBA1A\",\n      \"PLK1\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```"}