CEP120

Summary: CEP120 associates with CEP162 in human cell interaction assays.

Reason: Exact source-linked IntAct records EBI-11357643, EBI-11357763 and EBI-11362825 report positive tagged co-immunoprecipitation in human HEK293 cells; three additional records report proximity labeling. The reciprocal bait configurations corroborate association but do not establish a purified binary interface. Retain this partner-specific generic binding under the campaign instruction. CEP120 microtubule binding does not replace the distinct CEP162 association.

Summary: The centrosome is a supported site of CEP120 activity.

Reason: This PAINT inference is consistent with target-specific microtubule binding, centriole elongation and distal-component recruitment in human cells. Those activities support is_active_in beyond localization alone. The original PTN001090653 and descendant evidence, including the target itself, are preserved; no uninspected ancestral-node reconstruction or donor-count criticism is asserted.

Summary: CEP120 localizes to the centrosome and its centrioles.

Reason: The original human centrosome-proteomics/localization source is retained. Its selected main text was inspected, but the exact CEP120 supplementary target entry was not independently resolved. Independent endogenous CEP120 imaging in human RPE1 cells in PMID:20956381 Figure2 and PMID:30988386 Figure4 directly supports this core location.

Summary: Human CEP120 is detected at centrosomes in the cited cell study.

Reason: The cited study uses CEP120 and gamma-tubulin immunofluorescence with centrosomal phenotyping in human cell lines. Its Methods and selected Results were inspected. This localization agrees with independent human RPE1 imaging; the location annotation does not imply that CEP120 itself catalyzes PLK4 deubiquitination.

Summary: The combined electronic centrosome mapping agrees with direct human evidence.

Reason: The original ARBA, mouse ortholog, Ensembl and UniProt location sources are unchanged. Human endogenous immunofluorescence and centriole-localized activity support the centrosome assignment independently; no detailed historical ARBA decision path is claimed.

Summary: Centriolar localization is a defining property of CEP120.

Reason: The source immunofluorescence annotation is retained. Independent human RPE1 endogenous imaging resolves CEP120 at centrioles, enriched on daughters, and later super-resolution imaging places portions of its signal around the distal end and centriole wall. This supports the location without inventing a product-specific distribution.

Summary: The electronic centriole assignment is biologically supported.

Reason: The exact combined electronic assertion is preserved. Human centriolar imaging independently supports it, and the currently inspected mouse source includes experimental centriolar localization. Family membership is not used as a substitute for those observations.

Summary: The mouse-to-human centriolar location transfer agrees with human observations.

Reason: Current mouse Q7TSG1 records link centriole localization to PMID:25251415. That study uses mouse embryonic fibroblasts; its species scope is retained. Human RPE1 imaging independently establishes the corresponding location, so the original ISS transfer remains sound.

Summary: CEP120 contributes to the centrosome cycle through centriole construction.

Reason: The term includes centrosome duplication as well as separation; it does not require that CEP120 independently perform both. The PAINT inference agrees with human depletion/rescue and centriole elongation studies. No loss or divergence contradicting the inferred conserved role is identified, and the ancestral node is not reinterpreted as a pairwise similarity transfer.

Summary: The conserved centrosome-cycle role is supported by mouse and human studies.

Reason: The original Ensembl orthology transfer is preserved. Current mouse Q7TSG1 links this process to PMID:25251415, whose knockout experiments demonstrate failed centriole duplication. Human depletion/rescue and elongation evidence independently supports the same functional scope.

Summary: The manually transferred centrosome-cycle annotation is supported.

Reason: Mouse PMID:25251415 provides experimental duplication evidence, and human CEP120 depletion causes centriole loss that can be rescued by mouse Cep120 in PMID:20956381. This cross-species rescue and direct human elongation evidence support conservation while leaving the original ISS source fields intact.

Summary: CEP120 promotes centrosome duplication through centriole assembly.

Reason: The directionless electronic regulation term can be refined to positive regulation of centrosome duplication. Loss/depletion impairs duplication and rescue restores it; independent human experiments establish a centriole-construction role. Quiescent-cell restraint of premature PCM accumulation is a different outcome and does not reverse this duplication-specific direction.

Proposed replacements: positive regulation of centrosome duplication

Summary: CEP120 positively supports centrosome duplication.

Reason: Current mouse donor records identify PMID:25251415 knockout evidence for this term. Human depletion/rescue and human centriole assembly/elongation studies corroborate the transferred positive role. Preserve the IEA orthology source rather than replacing it with an authored experimental assertion.

Summary: The positive centrosome-duplication transfer is consistent with human function.

Reason: The mouse experiments establish impaired centriole duplication after Cep120 loss; human RPE1 depletion and cross-species rescue provide independent conservation evidence. CEP120 contributes the microtubule-associated centriole machinery rather than merely being a marker of cell proliferation.

Summary: CEP120 regulates protein localization to centrosomes in distinct cell-state contexts.

Reason: Refine the broad localization term to GO:1904779 regulation of protein localization to centrosome. Human RPE1 CEP120 loss reduces recruitment of C2CD3, TALPID3, SPICE, centrobin, POC1B and POC5 to nascent centrioles in PMID:30988386 Figures 2–3. In contrast, quiescent mouse fibroblasts in PMID:29741480 Figures 2–4 accumulate excess centrosomal PCM after Cep120 depletion; rescue and overexpression support a restraining role in that context. The shared destination is the centrosome, while the direction-neutral parent preserves these distinct effects and their species/cell-state limits. The original ARBA assertion is unchanged; its historical rule is not reconstructed.

Proposed replacements: regulation of protein localization to centrosome

Summary: CEP120 promotes the formation of cilia by building competent basal-body architecture.

Reason: The mouse donor process is experimentally grounded in PMID:25251415. Human CEP120-null RPE1 cells in PMID:30988386 lack normal appendages and fail ciliogenesis; wild-type CEP120 re-expression restores appendage markers but only partially rescues ciliation, and overexpression can itself impair ciliation. Association and recruitment of distal centriolar factors connect CEP120 to the assembly work, beyond disease necessity alone.

Summary: The conserved positive contribution to cilium assembly is supported.

Reason: The original mouse ISS source remains unchanged. Mouse knockout and independent human loss/rescue experiments support a role in assembling cilia-competent centrioles. Ciliopathy variants can preserve overexpression-induced elongation while impairing ciliogenesis, so these outcomes are not treated as interchangeable.

Summary: The relevant cell-cycle process is centrosome duplication.

Reason: The broad electronic positive-cell-cycle-process term is best expressed as the demonstrated positive regulation of centrosome duplication. The evidence concerns centriole construction within the centrosome cycle, not a generic stimulation of every cell-cycle phase or an inferred autonomous mitogenic activity.

Proposed replacements: positive regulation of centrosome duplication

Summary: CEP120 positively regulates specific centriole and cilium assembly processes.

Reason: The electronic organelle-assembly term is broader than the documented work. Refine it to positive regulation of centriole elongation and positive regulation of cilium assembly, supported by human depletion/overexpression, knockout/rescue and recruitment experiments. These are source-specific refinements of an existing assertion, not new process additions.

Proposed replacements: positive regulation of centriole elongation positive regulation of cilium assembly

Summary: CEP120 promotes centriole elongation in cooperation with other centriolar proteins.

Reason: PMID:27185865 tests CEP120-induced centriole overextension and its dependence on CEP295, including Figure5 and FigureS2. Independent PMID:23857771 directly tests CEP120 and its microtubule-binding mutant; PMID:30988386 adds endogenous-loss and rescue evidence. The phenotype is therefore not assigned from the CEP295 title or from overexpression alone.

Summary: CEP120 positively regulates recruitment of specific proteins to centrosomes.

Reason: Replace the broad recruitment term with GO:1904781 positive regulation of protein localization to centrosome. The human RPE1 comparison in PMID:30988386 Figures 2–3 measures reduced centriolar recruitment of C2CD3, TALPID3, SPICE, centrobin, POC1B and POC5 after CEP120 loss; mapped associations with C2CD3 and TALPID3 further support the recruitment role. This destination-specific semantic refinement is not claimed to be a formal descendant of GO:1904951. The original PMID:27185865 linkage retains its claim-specific limitation: Figure 7D reports that CEP120 depletion did not substantially block CEP295 targeting, and PMID:30988386 Figure 2a likewise finds CEP295 recruitment preserved. The original IMP assertion is unchanged; the refinement uses the separately identified human recruitment evidence and does not assert CEP120-dependent CEP295 recruitment.

Proposed replacements: positive regulation of protein localization to centrosome