CEP120 is a centriolar microtubule-binding component with separable roles in centriole elongation, distal-component recruitment and basal-body competence. The review preserves all 21 normal source assertions, their qualifiers and partners, and the three UniProt products Q8N960-1, Q8N960-2 and Q8N960-3. No source row was assigned an invented isoform. The primary human full-length construct in the 2013 study is 986 residues, matching the displayed product's length; this does not establish identical functions for the alternative products.
The sole generic binding assertion concerns CEP162. Its exact source-linked machine records are provided in CEP120-source-evidence.json. Three positive tagged co-immunoprecipitation records and three positive BioID records involve the human pair in HEK293 cells. They support association, with reciprocal bait configurations, but do not establish purified binary affinity. The campaign instruction to retain supported generic binding as non-core applies. The CEP162 interaction is not replaced by the distinct microtubule-binding activity, and no redundant binding descendant is added as a NEW assertion.
[PMID:23857771, "CEP120 cooperates with CPAP to regulate centriole elongation"] reports human CEP120 constructs amplified from HEK293T RNA. Selected Results, Figure4/5 descriptions and Methods distinguish purified GST-tagged N-terminal fragments from cellular full-length constructs. The N-terminal 1–209 region binds polymerized microtubules; K76A impairs this interaction and reduces overexpression-induced centriole elongation. The C-terminal regions contribute localization and self-association. The microtubule-binding molecular-function core is grounded in CEP120's own assay, rather than inferred from a partner's role. This study does not by itself establish a full-length single-molecule polymerase mechanism.
PMID:20956381 resolves endogenous CEP120 enrichment on daughter centrioles in human RPE1 cells. Its depletion/rescue study includes human RPE1 cells rescued with mouse Cep120; detailed multiciliated tracheal-epithelium and many cycling-cell experiments are mouse. Recruitment of SAS6 can persist despite the loss of normal centriole duplication, distinguishing early cartwheel assembly from later structural construction. Human loss/rescue and direct binding studies support the centrosome is_active_in assertion beyond mere localization.
The current mouse Q7TSG1 source chain links centrosome-cycle, positive-duplication and positive-cilium-assembly annotations to PMID:25251415. The complete current donor query and selected literal records are linked in the evidence JSON. Selected full Methods and Figure7 Results establish mouse knockout, primary embryonic fibroblast centriolar defects and failure to form cilia; cerebellar and ependymal outcomes are mouse developmental context. These observations are consistent with, but not substitutes for, independent human evidence. Current donor records do not reconstruct every historical Ensembl, ARBA or PAINT decision. A PAINT target appearing among descendant evidence is legitimate, not circular support.
PMID:27185865 examines CEP120-induced overextension in the CEP295 pathway, but its Figure7D and Results explicitly report [PMID:27185865, "depletion of CPAP, but not CEP120, centrobin or SPICE, substantially blocked the targeting of CEP295 to centrioles"]. The relevant Methods use human U2OS PLK4-inducible cells and siRNA. The study's Figure5 also shows that a CEP295 N-terminal fragment disrupts CEP120 localization; that reverse direction does not demonstrate CEP120-dependent CEP295 recruitment. The source therefore supports an elongation context while leaving a claim-specific problem for the original positive-protein-localization citation. Its IMP tuple is preserved, not silently reassigned.
Independent human PMID:30988386 resolves the broader functional question. Selected Figures1–5 show shortened centrioles and deficient appendages in CEP120/p53-null RPE1 cells, with p53-null controls and wild-type-p53 depletion experiments. CEP295 and RTTN recruitment remain detectable; SPICE, centrobin, POC1B, POC5, C2CD3 and TALPID3 recruitment are affected. Tagged co-IP and GST-fragment pull-down of in-vitro-translated partners map C2CD3 and TALPID3 associations. These are not all purified two-component affinity measurements or a proven single simultaneous complex. The positive-protein-localization process is retained on this independent evidence, expressly excluding the unsupported CEP295 recruitment paraphrase.
PMID:30988386 Figure6 reports loss of ciliation in the human CEP120 knockout models. Wild-type re-expression restores appendage markers but only partially rescues ciliation; excess CEP120 can also impair ciliation and overextend centrioles. Disease variants can retain overexpression-induced elongation while differing in ciliation rescue and partner recruitment. Thus the positive assembly role is conditional on proper protein level and architecture, not a universal monotonic effect of overexpression.
PMID:29847808 independently examines genome-engineered human RPE1 V194A/A199P variants, protein stability, distal markers and ciliation. Reduced ciliation need not imply abolished centriole duplication. Its domain structures have distinct species: C2A from zebrafish, C2B from tilapia and C2C from mouse; human mutant biochemical and cellular measurements are separate. No calcium-binding or membrane-binding activity is inferred merely from the C2 fold.
PMID:29741480 adds a different quiescent-cell role. Selected mouse fibroblast depletion, rescue, domain and MT-regrowth assays show excess PCM accumulation and altered satellite distribution after Cep120 loss. Its 988-residue mouse constructs are distinguished from the human RPE1 cells also listed in its Methods. Restraint of premature PCM maturation is compatible with a positive role in centriole construction during cycling. The direction-neutral protein-localization assertion can encompass both contexts.
All primary cache files are authentic normal outputs or exact existing-main bytes. PMID:21399614's existing full HTML-derived cache was read selectively; the exact CEP120 supplementary assay entry was not independently recovered, but its location is established by later primary human imaging. PMID:26638075 remains an abstract cache; exact source/method/partner linkage was read in authentic IntAct records rather than claimed from uninspected paper supplements. PMID:36590171's selected full localization Results and immunofluorescence Methods support centrosomal location; this does not confer USP54 deubiquitinase activity on CEP120.
PMID:29398280 is an authentic abstract-only cache. Independent consultation recovered the original publisher’s indexed cloning Methods, identifying human C2A1–151, C2B160–340, C2C450–610 and coiled-coil707–925 bacterial constructs (publisher preview). The full assembly Methods/Results remained inaccessible. The report of increased MT formation does not by itself distinguish nucleation, stabilization, bundling or the specifically defined plus-end tubulin-dimer transfer of GO:0061863. The final core is therefore microtubule binding, not a polymerase assertion; the unresolved mechanistic specificity is retained as a question. The independent peer also confirmed the direct human GST-N5 binding assay in PMID:23857771 and noted that its brain-tubulin species is unspecified in the inspected Methods.
A genuine bounded Falcon research attempt timed out; the explicit perplexity-lite fallback returned insufficient-quota HTTP401. No provider report was produced and none was authored in its name. This manual journal and the primary-source assessments are the scientific record. Three broad electronic process annotations are refined to the demonstrated duplication, elongation and cilium-assembly terms; there are no NEW biological-process or molecular-function rows. Molecular-function core synthesis is separate from preserving the CEP162 source assertion.
The applicable binding exception is the frozen ClinGen campaign instruction. Normal validation's generic-binding advisory is expected under that instruction. Its suggestion to add microtubule binding as NEW is not followed because the existing protein-binding ancestor is already present; the independently established activity is represented in core_functions without manufacturing a redundant source row.
This append updates the earlier broad localization disposition while preserving the preceding journal verbatim. Reinspection of the full cached PMID:30988386 Results and Figure 2–3 legends confirms that human RPE1 CEP120 loss reduces recruitment of C2CD3, TALPID3, SPICE, centrobin, POC1B and POC5 to nascent centrioles. CEP295 and RTTN recruitment remain intact in the same comparison. The positive source assertion is therefore refined with MODIFY to GO:1904781 positive regulation of protein localization to centrosome, and the core uses that same term. The original IMP/PMID:27185865 source object remains unchanged. Its Figure 7D limitation still applies, while its separate CEP120 elongation evidence and accepted elongation row remain valid.
The neutral ARBA protein-localization row is refined with MODIFY to GO:1904779 regulation of protein localization to centrosome. Full cached PMID:29741480 Results, Figures 2–4 and the depletion/rescue passages establish excess centrosomal PCM in quiescent mouse fibroblasts after Cep120 loss, with rescue and dose-dependent restraint after overexpression. This is a localization outcome, rather than a general increase in protein expression, and it is not relabeled as a human measurement. The neutral destination-specific parent preserves the distinction from the positive recruitment observed in cycling human cells. The standalone description now retains the mouse quiescent-cell boundary without presenting it as an assay report.
Official QuickGO term, ancestor and child responses retrieved on 2026-10-10 verify both active biological-process terms. GO:1904779 is a descendant of GO:0032880 and the parent of GO:1904781. GO:1904781 is not a formal descendant of GO:1904951 in the inspected is_a/part_of hierarchy: that replacement is a destination-specific semantic refinement supported by the recruitment assay, not a claim about that ancestry. Both changes review existing source assertions; neither adds a NEW row. No binding annotation is added or redirected: the CEP162 interaction and the existing microtubule-binding core keep their distinct evidence and the standing campaign/ancestor constraint. The MISCITED assessment of PMID:27185865 remains explicitly claim-specific in reference_review; it does not invalidate the paper's elongation results.
All 21 original source objects, three product records, 18 reference identities, original source caches and the preceding notes bytes are preserved. No new primary-source quotations are introduced in this follow-up.