CEP250

Summary: C-Nap1 undergoes cell-cycle-dependent redistribution and contributes to the centrosomal structural cycle.

Reason: The original human-cell study measures C-Nap1 mitotic phosphorylation/dissociation, phosphatase-sensitive antibody recognition and overexpression effects on microtubule organization; it does not show that C-Nap1 is degraded or catalyzes the cell-cycle transition. Retain the broad existing process with independent evidence that C-Nap1 itself maintains interphase centriole cohesion. The more descriptive core is the structural cohesion function, not an intrinsic kinase or an absolute requirement for all mitoses.

Summary: Mouse photoreceptor outer-segment localization supports a bounded conserved retinal context.

Reason: The mouse Q60952 donor has an experimental localization assertion from PMID:28005958. The full primary retinal staining is in postnatal mouse retina, whereas its human-cell experiment tests CEP250 A609V and cilium length. Retain the source orthology inference without relabeling that mouse staining as direct human photoreceptor evidence or making it part of the centrosomal core. Figure 4A/B uses the commercial anti-CEP250 antibody AB_2076918 in P60 mouse retina. The inspected Methods and figure legend do not report a knockout or peptide-block specificity control for this outer-segment signal; retain the reported localization with that antibody-specificity limitation.

Summary: Mouse photoreceptor outer-segment localization supports a bounded conserved retinal context.

Reason: The mouse Q60952 donor has an experimental localization assertion from PMID:28005958. The full primary retinal staining is in postnatal mouse retina, whereas its human-cell experiment tests CEP250 A609V and cilium length. Retain the source orthology inference without relabeling that mouse staining as direct human photoreceptor evidence or making it part of the centrosomal core. Figure 4A/B uses the commercial anti-CEP250 antibody AB_2076918 in P60 mouse retina. The inspected Methods and figure legend do not report a knockout or peptide-block specificity control for this outer-segment signal; retain the reported localization with that antibody-specificity limitation.

Summary: The exact photoreceptor inner-segment transfer remains unadjudicated.

Reason: The current mouse Q60952 provenance links the inner-segment assertion to PMID:30998843. Its abstract supports retinal involvement, but the primary localization panels and antibody controls were not recovered after bounded access attempts. Outer-segment staining in PMID:28005958 does not establish this distinct compartment. Preserve the original orthology/source assertion pending the exact evidence rather than call it incorrect.

Summary: The exact photoreceptor inner-segment transfer remains unadjudicated.

Reason: The current mouse Q60952 provenance links the inner-segment assertion to PMID:30998843. Its abstract supports retinal involvement, but the primary localization panels and antibody controls were not recovered after bounded access attempts. Outer-segment staining in PMID:28005958 does not establish this distinct compartment. Preserve the original orthology/source assertion pending the exact evidence rather than call it incorrect.

Summary: The documented NEK2 association is more informative as protein kinase binding.

Reason: The source abstract explicitly identifies a C-Nap1–NEK2–PP1 ternary complex and C-Nap1 as a substrate. Independent full PMID:9647649 establishes the human C-Nap1/NEK2 interaction and fragment assays. Refine the partner class to protein kinase binding while retaining the original source and P51955 partner. This does not make C-Nap1 a kinase, phosphatase or activator; the complete PMID:10880350 body was not recovered.

Proposed replacements: protein kinase binding

Summary: CEP250 associates with the proximal-centriolar platform CEP135.

Reason: Human endogenous reciprocal co-IP and terminal-fragment experiments support association with CEP135. The source recruitment direction is CEP135 to C-Nap1. Retain generic binding under the project instruction without inventing catalysis or dimerization.

Summary: The conductin/Axin2 interaction is retained with its source partner and cross-species scope.

Reason: The original selected Results document conductin–C-Nap1 co-immunoprecipitation and C-Nap1-dependent conductin centrosomal recruitment, including endogenous human-cell localization. The GOA partner O88566 is mouse Axin2 and is preserved as supplied; the tested transfection/fragment record is not relabeled as a purified native human pair. These observations support association, not intrinsic Wnt signaling catalysis or a newly inferred molecular mechanism.

Summary: CEP250 binds the protein kinase SIK2.

Reason: The full source Figure 4 tests a C-Nap1 C-terminal fragment with endogenous SIK2 in human cells and identifies SIK2-mediated C-Nap1 phosphorylation. Exact source-linked IntAct records independently preserve the human pair and assay fields. Protein kinase binding captures CEP250's own binding role; phosphorylation is catalyzed by SIK2, not by CEP250, and the fragment/overexpression context is retained.

Proposed replacements: protein kinase binding

Summary: Ninein association is positive, with a remaining construct-to-isoform mapping limit.

Reason: The genuine primary Figure 3H includes endogenous Ninein–CEP250 co-immunoprecipitation in HeLa cells, and the tested NPC-versus-neuronal C-terminal forms differ in association. The exact GOA partner Q8N4C6-7 is preserved. Table S6 was not recovered to independently map every recombinant construct to that accession, so this is not a claim that all Ninein isoforms bind or that human host cells establish the species of every transgene. Supported human association is retained as non-core under the project instruction.

Summary: C-Nap1 associates with the linker component CCDC102B.

Reason: Endogenous human-cell co-IP and full-length/terminal-fragment experiments support CCDC102B association. The Discussion allows an indirect rootletin contribution. Retain association without a purified binary-interface or enzyme claim.

Summary: The source-specific OPTN interaction is supported at screening resolution.

Reason: Exact positive IntAct records for human Q9BV73–Q96CV9 and PMID:32814053 include pooled, arrayed and validated yeast two-hybrid assays. Their shared source and representations are not independent biological replication. Retain the supported low-resolution association under the project instruction without transferring optineurin functions to CEP250 or asserting a native disease mechanism.

Summary: The SARS-CoV-2 nsp3-chain association is retained as a tested viral interaction.

Reason: Exact positive source-linked yeast two-hybrid records join human Q9BV73 to the supplied P0DTD1-PRO_0000449631 viral chain. Preserve that chain identifier and viral-versus-human taxon scope. This screen does not establish CEP250's normal cellular function, infection-dependent necessity, or an enzymatic role. No narrower host molecular activity follows from the partner identity alone.

Summary: The NEK2 interaction supports protein kinase binding.

Reason: The full primary identifies human C-Nap1 from a NEK2 interaction screen and assays its C-terminal fragment with active/inactive NEK2. The interaction and phosphorylation are distinct: CEP250 binds the kinase and is its substrate, but does not thereby possess kinase activity. Preserve the original IPI source and exact P51955 partner while refining the generic term.

Proposed replacements: protein kinase binding

Summary: Centrosomal activity is central to CEP250's inherited and directly observed structural role.

Reason: Preserve the PAINT assertion and is_active_in qualifier. The target appearing in WITH/FROM is legitimate descendant evidence, not circularity. Human endogenous imaging and perturbation independently establish active structural cohesion at proximal centrosomal centrioles. The full ancestral-node history was not reconstructed, so no claim about its precise origin or loss is added.

Summary: Centrosomal localization is independently verified and core.

Reason: Retain the immunofluorescence curation assertion. Multiple human-cell primary assays localize native C-Nap1 to proximal centrioles within the centrosome, where it performs structural work; the conclusion does not rely on an inference from the protein name.

Summary: The centrosomal annotation is consistent with direct independent human evidence.

Reason: The cited proteomic/localization paper is preserved as the original IDA source, but its exact CEP250 supplementary identification was not independently recovered from the selected main text. The location itself is directly established by human immunolocalization and endogenous tagging in other primary sources. Accept the correct core compartment without claiming that the original target-level supplementary record was reverified.

Summary: CEP250 functions as a centrosomal anchor in the Ninein study.

Reason: Figure 3 and its human HeLa endogenous interaction panel, together with CEP250-dependent Ninein localization, support the centrosomal context. Preserve is_active_in; this is not a claim that every neural construct was human or that CEP250 performs the splicing reaction. Independent human structural work supports activity at this site.

Summary: Human-cell proximal-centrosomal C-Nap1 staining supports the core location.

Reason: The full Cep44 paper uses C-Nap1 as a proximal centriole marker in human U2OS/RPE1 microscopy, including Figure 1. This is genuine target localization despite a title centered on another protein. No Cep44 biochemical activity is transferred to CEP250.

Summary: The original human C-Nap1 study establishes its centrosomal localization.

Reason: The primary immunofluorescence and electron-microscopy work identifies C-Nap1 at proximal centriolar ends, with cell-cycle-dependent association. The centrosome remains a core site even though the protein dissociates during mitosis.

Summary: The UniProt centrosome mapping agrees with direct primary localization.

Reason: The curated subcellular-location mapping is retained and independently corroborated by the original human study and later functional endogenous tagging. No evidence-rank penalty is applied to a correct core location.

Summary: Active structural cohesion occurs at proximal centrioles.

Reason: Preserve the phylogenetic is_active_in assertion rather than reduce it to generic colocalization. Human endogenous C-Nap1 assemblies contact proximal centrioles and contribute to their cohesion. The PAINT node and donor list are retained without guessing a reconstructed node-placement history.

Summary: Immunoelectron microscopy supports the supplied centriole colocalization.

Reason: The original human-cell study places C-Nap1 near proximal parental centriole tips. Preserve the colocalizes_with qualifier and do not reinterpret this as localization inside a nascent procentriole or cartwheel. This spatial evidence is consistent with the structural core.

Summary: C-Nap1 is localized at proximal centriolar ends in the CEP135 study.

Reason: The source's endogenous human-cell imaging and proximal localization support the annotation. CEP135 provides the platform for C-Nap1 localization in those perturbations; the localization of C-Nap1 is a direct observation, independent of that recruitment direction.

Summary: C-Nap1 marks the proximal centriole in human RPE1 cells.

Reason: The full Talpid3/CEP290 paper explicitly uses anti-C-Nap1 in Figure 2B and Methods to distinguish the proximal site from the distal Talpid3 region. Accept this actual target observation without assigning Talpid3/CEP290 ciliary functions to C-Nap1.

Summary: The MDM1 study directly distinguishes proximal C-Nap1 from a luminal marker.

Reason: Human-cell 3D-SIM uses C-Nap1 as a proximal centriole marker in Figure 2, separate from MDM1's distribution. This supports the precise existing location and does not imply that CEP250 is the microtubule-binding protein assayed elsewhere in that paper.

Summary: Human RPE1 microscopy places C-Nap1 at proximal centrioles.

Reason: The genuine full author article shows C-Nap1 alongside Girdin at proximal centrioles in Figure 5C. The human-cell evidence is distinct from the paper's separate nematode experiments. The location is consistent with the cohesion core.

Summary: Endogenous human C-Nap1 directly marks and bridges proximal centriole contacts.

Reason: Functional endogenous tagging, validated anti-C-Nap1 expansion microscopy and cell-type replication localize C-Nap1 at proximal ends. Some centriole pairs are bridged and others spatially separate; the study does not establish a permanent continuous bridge in every cell.

Summary: The mouse-to-human centriole inference is independently corroborated in human cells.

Reason: Preserve the original mouse donor chain. Direct human microscopy establishes the same proximal-centriolar location, so a complete reinspection of every mouse assay is unnecessary for this correct core compartment.

Summary: The microtubule-organizing-center description is correct but less specific than the centrosomal core.

Reason: C-Nap1 is a proximal centrosomal structural component in the cited primary study. The broad location is retained without interpreting it as microtubule nucleation or polymerase activity by C-Nap1 itself. The core uses centrosome and direct centriole cohesion.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The curated cytosolic context is retained without transferring reaction chemistry.

Reason: Preserve this source-specific Reactome TAS location. The official human CEP250 physical entity R-HSA-380263 maps Q9BV73 to cytosol, documenting the compartment provenance within the same Reactome source, rather than providing an independent localization experiment. The cited event is pathway/complex context rather than a claim that CEP250 catalyzes every reaction in that event. Proximal centrosomal assemblies are the more informative core location; no enzyme activity or new process is inferred from shared pathway membership.

Summary: The established protein-localization role is more specifically centrosomal.

Reason: The original CEP135 study primarily demonstrates CEP135-dependent recruitment of C-Nap1, so its causal direction is not inverted. Independent human C-Nap1 depletion experiments in PMID:24554434 and PMID:30404835 establish C-Nap1-dependent maintenance of centlein/Cep68/rootletin or CCDC102B at centrosomes. Refine the correct broad protein-localization role to its observed destination while preserving the original source assertion and stating that the independent studies supply the outgoing recruitment evidence.

Proposed replacements: protein localization to centrosome

Summary: Centrosomal recruitment gives a supported destination-specific refinement.

Reason: The selected full 3D-SIM paper uses C-Nap1 as a proximal marker, but the exact perturbation supporting this original IMP assertion was not located. Do not claim a wrong-gene annotation from that limit. Independent full human studies directly show loss of centrosomal linker components after C-Nap1 depletion, supporting protein localization to centrosome. Preserve the original source object and distinguish the independent functional support from the unresolved source-specific attribution.

Proposed replacements: protein localization to centrosome

Summary: C-Nap1 directly contributes cohesive structure between parental centrioles.

Reason: Human endogenous C-Nap1 forms proximal centriole contact bridges, and its cohesive assemblies and rootlet-terminal association perform structural work maintaining centriole pairing. Ectopic retargeting and partial rescue of rootletin-depletion phenotypes support an intrinsic cohesive contribution; they do not establish native activity at the retargeted organelles. True phase separation and purified full-length material properties remain unresolved.

Summary: Human interference experiments establish C-Nap1-dependent centriole cohesion.

Reason: Antibody interference in human Hs68 fibroblasts and dominant-negative C-Nap1 fragments in U2OS disrupt parental centriole cohesion. Combined with direct later structural/functional imaging this supports own cohesion activity, rather than merely a requirement to be phosphorylated. The paper does not establish that C-Nap1 spans every inter-centriolar distance or joins parental centrioles to procentrioles.

Summary: Human C-Nap1 depletion disrupts centriole cohesion.

Reason: The selected full original CEP135 study includes C-Nap1 depletion in HeLa cells and centrosome-splitting measurements, not merely CEP135 perturbation. Those experiments converge with independent antibody interference and endogenous structural imaging. Retain the core cohesion annotation without treating C-Nap1 as a kinase.

Summary: Centriole cohesion is directly established, although this exact cited perturbation remains unresolved.

Reason: The selected full PMID:23213374 text contains proximal C-Nap1 marker localization; its exact source-specific IMP cohesion experiment was not located. Preserve the curator's assertion and source rather than infer misattribution. Independent human interference and physical bridge/functional experiments directly establish this core role, which is why the biological annotation is accepted; the unresolved citation linkage is recorded separately.

Summary: Human C-Nap1 depletion impairs the centrosomal linker and centriole cohesion.

Reason: The selected full centlein study tests human C-Nap1 RNAi, centrosome splitting and the dependency of centlein/Cep68/rootletin centrosomal accumulation. This is its own structural organization work, not merely necessity as a substrate for another enzyme.

Summary: Mapped centlein/C-Nap1 domains support this association.

Reason: The full original Results map centlein and C-Nap1 fragments and show endogenous co-immunoprecipitation. GST-fragment pull-downs use partner-containing cell extracts, so a completely purified binary interface is not claimed. Retain the already informative domain-specific binding assertion; it supports linker organization but is not treated as a distinct catalytic core.

Summary: C-Nap1 participates in a regulated structural linker system.

Reason: The original source establishes human proximal-centriolar C-Nap1 and phosphorylation of its C-terminal fragment by NEK2 in vitro and after U2OS coexpression; it presents the timing and consequences for cohesion as a working model. Independent human interference and direct physical-cohesion studies establish C-Nap1 as a structural participant. The regulation term explicitly includes assembly/disassembly of a proteinaceous linker, so this broad regulatory assertion is defensible with the original source limit stated. Do not describe the 1998 assay as C-Nap1 catalysis or definitive demonstration of phosphorylation-triggered linker dissolution.

Summary: The precise spindle-pole centrosome transfer remains unresolved.

Reason: The mouse Q60952 donor links this site to PMID:19117032, whose full localization experiment was not recovered. Direct human studies emphasize interphase proximal-centriolar C-Nap1 and its mitotic dissociation; that temporal contrast does not itself refute a particular mouse developmental assay or establish functional loss. Preserve the electronic source pending verification of stage, localization and transfer scope.

Summary: The source supports a C-Nap1-containing kinase/phosphatase complex.

Reason: The authentic abstract explicitly reports a ternary C-Nap1–NEK2–PP1 complex, supporting broad complex membership even though the complete original body was unavailable. Preserve the original IMP and part_of fields. This does not make C-Nap1 either enzyme and does not establish a named stable holoenzyme beyond the source's assay scope.

Summary: The basal-body context is compatible with proximal-centriolar C-Nap1.

Reason: Retain the supplied localization/inference as a non-core ciliary context. Direct human imaging observes C-Nap1 at proximal centriole bases in ciliated cells, independently supporting the broad location. The mouse donor's PMID:30998843 localization panels were not recovered, so this is not a claim that the exact mouse experiment or a matrix subcompartment was newly verified; basal-body localization does not establish an essential cilium-assembly function.

Summary: The basal-body context is compatible with proximal-centriolar C-Nap1.

Reason: Retain the supplied localization/inference as a non-core ciliary context. Direct human imaging observes C-Nap1 at proximal centriole bases in ciliated cells, independently supporting the broad location. The mouse donor's PMID:30998843 localization panels were not recovered, so this is not a claim that the exact mouse experiment or a matrix subcompartment was newly verified; basal-body localization does not establish an essential cilium-assembly function.

Summary: The basal-body context is compatible with proximal-centriolar C-Nap1.

Reason: Retain the supplied localization/inference as a non-core ciliary context. Direct human imaging observes C-Nap1 at proximal centriole bases in ciliated cells, independently supporting the broad location. The mouse donor's PMID:30998843 localization panels were not recovered, so this is not a claim that the exact mouse experiment or a matrix subcompartment was newly verified; basal-body localization does not establish an essential cilium-assembly function.

Summary: Perinuclear cytoplasmic location is a coarse description of the centrosomal pool.

Reason: Preserve the supplied UniProt location-vocabulary mapping. The original human study observes centrosomal/perinuclear C-Nap1, and the established proximal-centriolar assemblies lie in that general cellular region. This broad located_in assertion is not promoted to an independent cytoplasmic molecular function.

Summary: The exact mouse IMP donor establishes retinal dysfunction, but a distinct light-detection role remains unresolved.

Reason: The electronic orthology transfer cites mouse Q60952 and ENSMUSP00000091988; its exact historical Ensembl transfer chain is not reconstructed. The current Q60952 record is an IMP annotation from PMID:30998843, not merely a protein-class prediction. Official GO:0050908 concerns reception of a light stimulus and its conversion into a molecular signal, with an is_a path to light detection and a part_of link to visual perception. The authentic primary abstract reports reduced retinal thickness and ERG responses in homozygous knock-in mice. These coupled structural and functional endpoints do not distinguish a proximal detection contribution from reduced responses secondary to photoreceptor degeneration. The full assays needed to adjudicate that distinction remain unavailable after renewed bounded attempts. CEP250 structural identity does not exclude a structural contribution to detection, and neither the donor experiment nor its transfer is shown to be erroneous. Retain UNDECIDED because the specific biological role is unresolved, not because the retinal phenotype is doubted or the source is assumed wrong.

Summary: The exact mouse IMP donor establishes retinal dysfunction, but a distinct light-detection role remains unresolved.

Reason: The sequence-similarity transfer cites mouse Q60952. The current Q60952 record is an IMP annotation from PMID:30998843, not merely a protein-class prediction. Official GO:0050908 concerns reception of a light stimulus and its conversion into a molecular signal, with an is_a path to light detection and a part_of link to visual perception. The authentic primary abstract reports reduced retinal thickness and ERG responses in homozygous knock-in mice. These coupled structural and functional endpoints do not distinguish a proximal detection contribution from reduced responses secondary to photoreceptor degeneration. The full assays needed to adjudicate that distinction remain unavailable after renewed bounded attempts. CEP250 structural identity does not exclude a structural contribution to detection, and neither the donor experiment nor its transfer is shown to be erroneous. Retain UNDECIDED because the specific biological role is unresolved, not because the retinal phenotype is doubted or the source is assumed wrong.

Summary: The inherited cilium-assembly assertion remains unresolved in the conflicting human evidence.

Reason: The PAINT inference is preserved as a phylogenetic assertion at PANTHER:PTN000570270; target self-inclusion in WITH/FROM is legitimate and is not circular or weak evidence. Human CEP250 perturbations provide ciliary evidence, including the A609V length phenotype (PMID:28005958), but the assembly mechanism and its physiological scope remain unresolved. PMID:23789104 reports reduced formation after C-Nap1 RNAi, whereas PMID:28100636 reports normal ciliation in validated human RPE1 null cells and demonstrates off-target ciliation effects for the earlier Conroy 2012 reagent. The latter reagent has not been equated to the 2013 reagent, and knockout nonessentiality alone does not disprove involvement or the PAINT node. The node history and complete descendant evidence have not been reconstructed; retain UNDECIDED rather than infer target-specific loss or declare the ancestral assertion false.

Summary: A609V-associated cilium elongation is demonstrated, but its relationship to the annotated assembly process is unresolved.

Reason: PMID:28005958 Figure 4 and Methods compare C-terminally IT6-tagged human full-length WT and A609V CEP250 in serum-starved ARPE-19 cells with endogenous CEP250 still present; mutant-expressing cells have longer cilia. This is a real mutant-associated ciliary phenotype, but the endpoint length comparison does not distinguish altered assembly, disassembly or another determinant of steady-state length. It therefore does not resolve the precise existing cilium-assembly assertion, and it does not justify a replacement asserting regulatory direction or kinetics. This is not a depletion/rescue assay or evidence that native CEP250 initiates cilia; the separate retinal localization experiment is in mouse. PMID:28100636 reports normal ciliation in validated human null cells and considers divergent length findings compatible with clonal variation. Those data limit an essential-assembly interpretation without proving that CEP250 cannot participate in assembly. Preserve the IMP source and use UNDECIDED consistently with the unresolved ciliary evidence.

Summary: The original human urinary-exosome dataset detects CEP250.

Reason: The authentic authors' NHLBI database lists CEP250/NP_009117 as centrosomal protein 2 isoform 1 with one peptide and reference 2, explicitly the PMID:19056867 study. This is positive target-level detection, not a missing-target inference from a generic proteomic title. Retain the HDA compartment at that detection resolution without inferring secretion, an extracellular physiological function or high-confidence vesicle-surface topology.

Summary: C-Nap1 maintains CCDC102B at centrosomes as part of linker organization.

Reason: The selected original Results show C-Nap1-dependent centrosomal CCDC102B in human U2OS cells; the reverse dependency is not equivalent. C-Nap1 depletion also affects total CCDC102B and the paper allows an indirect rootletin contribution. The destination-specific role is accepted as part of the core structural organization, without inventing a purified transport or direct binary recruitment mechanism.

Summary: C-Nap1 promotes centrosomal accumulation of Girdin in human cells.

Reason: The genuine full original human RPE1 experiments show loss of centriolar Girdin intensity after C-Nap1 depletion, with centrosome-splitting confirmation. This supports the supplied directional localization process. Keep it as a specific supporting dependency rather than duplicate the broader core protein-localization process or transfer the separate Girdin/nematode ciliogenesis mechanism to CEP250.

Summary: The original C-Nap1 RNAi experiment directly reports impaired non-motile cilium formation, but the source-specific conflict with later knockout evidence remains unresolved.

Reason: PMID:23789104 genuinely assays C-Nap1 in human RPE1 cells despite its Cep123-focused title. Figure 4 reports 64% fewer ciliated cells in the formation protocol and 30% fewer in the maintenance protocol; depletion and proliferation/stress controls were measured. PMID:28100636 subsequently observes normal ciliation in C-NAP1-null cells and shows that its reused Conroy 2012 siRNA reduces ciliation even in null cells. The 2013 Table S2 target sequences were not recovered, so it is not established that the 2013 C-Nap1 reagent is the same off-target pool. The observations therefore warrant UNDECIDED, not a claim that this exact experimental annotation has been disproved or that CEP250 can never participate in ciliary biology.

Summary: C-Nap1 itself contributes structural integrity to the centrosomal linker.

Reason: Functional endogenous human tagging and expansion microscopy identify proximal centriole contact bridges; rootlet-terminal association, altered cohesion with truncations and partial rescue of rootletin-depletion splitting establish C-Nap1's own cohesive structural work. Ectopic organelle retargeting corroborates cohesive capacity but is not native localization at those organelles. The checked structural MF is neither an ancestor nor descendant of any seeded term, including generic binding, and adds an experimentally demonstrated molecular role without adding a process. True phase separation and purified full-length material properties remain unresolved.