C2CD3

Summary: C2CD3 associates with OFD1 in a centriole-length regulatory context.

Reason: PMID:24997988 reports endogenous C2CD3–OFD1 co-immunoprecipitation in human RPE cells and OFD1-fragment capture of cell-expressed C2CD3. These support the exact O75665 partner assertion without establishing purified binary affinity or an enzyme activity. Retain the supported generic interaction under the standing task instruction; no finer activity follows from this association alone.

Summary: The curated C2CD3–OFD1 screen association agrees with independent target-specific evidence.

Reason: The complete PMID:26496610 abstract describes quantitative affinity-purification proteomics of near-endogenous GFP-tagged proteins in HeLa cells; its individual C2CD3–OFD1 record was not inspected. Defer to that curated experimental edge because the same exact partner interaction is independently supported by human-cell experiments in PMID:24997988. This does not claim the source-specific supplementary entry was verified, and generic binding is retained as non-core under the standing task instruction.

Summary: C2CD3 is a centrosomal protein concentrated at distal centrioles.

Reason: The curated immunofluorescence annotation is consistent with human endogenous and tagged-protein localization in PMID:24997988 and human U2OS epitope mapping in PMID:41364719. Retain the broader centrosome location alongside its more precise centriolar localization. The original individual atlas image was not independently reviewed.

Summary: The centrosome assignment agrees with independently established C2CD3 localization.

Reason: PMID:21399614 combines human centrosomal proteomics and localization, but its exact C2CD3 target image/table was not recovered from the inspected cache. Retain the reliable experimental assertion with curator deference and independent target-specific support from PMID:24997988 and PMID:41364719; a full-text flag is not treated as proof of target-panel inspection.

Summary: C2CD3 has a conserved distal-centriolar localization.

Reason: The PAINT assertion at PTN001082712 is biologically concordant with human localization and mouse C2cd3 experiments in PMID:24997988, and with human epitope mapping in PMID:41364719. The target in WITH/FROM is legitimate descendant evidence, not circularity. This assessment uses convergent biology and does not claim an independent tree/alignment audit.

Summary: Human C2CD3 participates in distal centriole formation and localizes to centrioles.

Reason: The complete PMID:23769972 abstract explicitly reports human-cell functional genomics and detailed C2CD3 distal-centriole follow-up. Exact target localization images and the listed erratum content remain uninspected; retain the curated IDA with independent localization support from PMID:24997988 and PMID:41364719. The erratum listing alone does not establish invalidation.

Summary: The electronic centriole location matches experimental C2CD3 biology.

Reason: The combined ARBA, mouse ortholog and UniProt location sources agree with independently inspected human and mouse C2CD3 localization. No target-specific divergence contradicts the mapping; retain the term without claiming a separate audit of every electronic rule.

Summary: C2CD3 acts at the centrosomal microtubule-organizing center through its centriolar pool.

Reason: This broader PAINT location is consistent with the directly established centriole and basal-body locations. It does not assign microtubule nucleation, polymerase activity or centrosomal kinase activity to C2CD3. PTN001082711 is retained on concordant biology rather than donor counting.

Summary: Cytosol is a broad compartment assignment in the curated ciliogenesis pathway.

Reason: The preserved Reactome-derived GOA assertion assigns the cytosol location. The complete cached event summary supplies reaction context but does not independently resolve a diffuse versus centriolar pool. RAB3IP-mediated nucleotide exchange on RAB8A is the activity of RAB3IP, not C2CD3. Retain this broad location as non-core; the specific structural work of C2CD3 occurs at the distal centriole/basal body, and this location annotation is not an assertion that C2CD3 catalyzes the named reaction.

Summary: Cytosol is a broad compartment assignment in the curated ciliogenesis pathway.

Reason: The preserved Reactome-derived GOA assertion assigns the cytosol location. The complete cached event summary supplies reaction context but does not independently resolve a diffuse versus centriolar pool. The source describes recruitment of C2CD3 to the mother centriole. Retain this broad location as non-core; the specific structural work of C2CD3 occurs at the distal centriole/basal body, and this location annotation is not an assertion that C2CD3 catalyzes the named reaction.

Summary: Cytosol is a broad compartment assignment in the curated ciliogenesis pathway.

Reason: The preserved Reactome-derived GOA assertion assigns the cytosol location. The complete cached event summary supplies reaction context but does not independently resolve a diffuse versus centriolar pool. The source describes distal-appendage recruitment in the C2CD3/OFD1 context. Retain this broad location as non-core; the specific structural work of C2CD3 occurs at the distal centriole/basal body, and this location annotation is not an assertion that C2CD3 catalyzes the named reaction.

Summary: Cytosol is a broad compartment assignment in the curated ciliogenesis pathway.

Reason: The preserved Reactome-derived GOA assertion assigns the cytosol location. The complete cached event summary supplies reaction context but does not independently resolve a diffuse versus centriolar pool. The source describes removal of CP110 and CEP97 during initiation of ciliogenesis. Retain this broad location as non-core; the specific structural work of C2CD3 occurs at the distal centriole/basal body, and this location annotation is not an assertion that C2CD3 catalyzes the named reaction.

Summary: Cytosol is a broad compartment assignment in the curated ciliogenesis pathway.

Reason: The preserved Reactome-derived GOA assertion assigns the cytosol location. The complete cached event summary supplies reaction context but does not independently resolve a diffuse versus centriolar pool. TTBK2 recruitment and kinase action must not be transferred to C2CD3. Retain this broad location as non-core; the specific structural work of C2CD3 occurs at the distal centriole/basal body, and this location annotation is not an assertion that C2CD3 catalyzes the named reaction.

Summary: Cytosol is a broad compartment assignment in the curated ciliogenesis pathway.

Reason: The preserved Reactome-derived GOA assertion assigns the cytosol location. The complete cached event summary supplies reaction context but does not independently resolve a diffuse versus centriolar pool. The source describes transition-zone recruitment downstream of distal maturation. Retain this broad location as non-core; the specific structural work of C2CD3 occurs at the distal centriole/basal body, and this location annotation is not an assertion that C2CD3 catalyzes the named reaction.

Summary: Cytosol is a broad compartment assignment in the curated ciliogenesis pathway.

Reason: The preserved Reactome-derived GOA assertion assigns the cytosol location. The complete cached event summary supplies reaction context but does not independently resolve a diffuse versus centriolar pool. MARK4–ODF2 regulation is a partner reaction, not a C2CD3 kinase activity. Retain this broad location as non-core; the specific structural work of C2CD3 occurs at the distal centriole/basal body, and this location annotation is not an assertion that C2CD3 catalyzes the named reaction.

Summary: Cytosol is a broad compartment assignment in the curated ciliogenesis pathway.

Reason: The preserved Reactome-derived GOA assertion assigns the cytosol location. The complete cached event summary supplies reaction context but does not independently resolve a diffuse versus centriolar pool. CEP164-dependent recruitment of RAB3IP-associated vesicles supplies pathway context rather than a C2CD3 transport enzyme activity. Retain this broad location as non-core; the specific structural work of C2CD3 occurs at the distal centriole/basal body, and this location annotation is not an assertion that C2CD3 catalyzes the named reaction.

Summary: A centriolar-satellite pool accompanies the principal centriolar C2CD3 pool.

Reason: The PAINT satellite location agrees with localization evidence summarized in PMID:24469809 and the low-level tagged mouse IMCD3 experiments in PMID:24997988. Retain the conserved location as non-core; neither this location nor its inheritance establishes that C2CD3 is required for satellite integrity. No independent PAINT node-placement audit is claimed.

Summary: C2cd3 colocalizes with the centriolar-satellite marker PCM1 in the inspected model.

Reason: PMID:24997988 reports low-level GFP-C2cd3 expression in mouse IMCD3 cells and PCM1 colocalization, while C2CD3 depletion/mutation did not disrupt satellite integrity in the tested systems. Retain the curated human localization by curator deference and conserved target biology, explicitly distinguishing the inspected mouse tagged-protein assay from a human target image. The satellite pool is auxiliary to the distal-centriolar structural function.

Summary: Electronic satellite localization is consistent with the experimentally observed C2cd3 pool.

Reason: The mouse-ortholog/ARBA sources agree with the satellite localization in PMID:24997988 and PMID:24469809. The term remains a location claim, not evidence of satellite assembly or integrity activity; no loss/divergence evidence justifies rejecting the propagation.

Summary: C2CD3 acts at the ciliary basal body during primary-cilium assembly.

Reason: The curated immunofluorescence assignment is consistent with the mother-centriole/basal-body functions reported in PMID:23769972 and PMID:24469809. Retain the location while acknowledging that the original individual atlas image was not inspected; it does not imply localization within the ciliary axoneme.

Summary: The basal-body location is supported by the conserved ciliogenesis mechanism.

Reason: Mouse ortholog and electronic annotation sources agree with recruitment and appendage-assembly experiments summarized in PMID:24469809, with human distal-centriole localization corroborated by PMID:24997988 and PMID:41364719. A basal-body role does not require assigning C2CD3 to the ciliary lumen.

Summary: C2CD3 contributes structural organization and recruitment needed for cilium assembly.

Reason: The PAINT inference at PTN001082711 agrees with human C2CD3 follow-up in PMID:23769972, mammalian distal-appendage assembly in PMID:24469809 and human architectural evidence in PMID:41364719. C2CD3 performs organizing work at the basal body rather than merely serving as a downstream disease marker. Target self-inclusion is not circular evidence.

Summary: The electronic cilium-assembly annotation agrees with the established target function.

Reason: Independent target experiments support distal maturation, appendage recruitment and primary-cilium assembly. Retain the broader ARBA assertion; no evidence suggests the target has lost this function. This does not transfer motor, kinase or guanine-nucleotide-exchange activity from downstream ciliogenesis proteins.

Summary: C2CD3 participates in conserved centriole elongation.

Reason: The PAINT assertion is corroborated by shortened centrioles in mutant mouse fibroblasts and C2CD3-induced centriole extensions in human cells in PMID:24997988, with further human depletion evidence in PMID:41364719. The evidence supports a structural elongation role without assigning a tubulin-polymerizing enzyme activity. No independent phylogenetic placement audit is claimed.

Summary: Loss and gain of C2CD3 perturb centriole length in opposite directions.

Reason: PMID:24997988 combines mutant mouse-cell ultrastructure with human-cell overexpression and correlative microscopy of continuous centriolar extensions. These experiments support participation in centriole elongation; OFD1 antagonism and altered appendages are mechanistic context. The overexpression structures are not treated as proof of a purified microtubule-polymerase activity.

Summary: Electronic centriole elongation is consistent with direct target experiments.

Reason: The combined mouse-ortholog and ARBA sources agree with the experimentally established C2CD3 length phenotype and its structural role at the distal centriole. Retain the biological assertion while preserving the original electronic provenance.

Summary: C2CD3 supports recruitment or maintenance of distal centrosomal proteins.

Reason: The PAINT protein-localization assertion is consistent with loss of distal components after C2CD3 perturbation in PMID:24997988 and human depletion in PMID:41364719. GO:0071539 includes maintenance at the centrosome as well as transport, so C2CD3 need not be a motor or transport catalyst to perform this organizing role.

Summary: C2CD3 supports distal-centriolar retention and recruitment of multiple proteins.

Reason: PMID:24997988 reports loss of centriolar components and appendages in C2cd3-mutant cells. Independent PMID:41364719 human-cell imaging shows disruption of the luminal network, DISCO recruitment and distal microtubule-cap components. Retain the broad localization process; not every affected protein is shown to bind C2CD3 directly, and MNR cellular displacement is distinct from purified binary binding.

Summary: The ARBA localization process agrees with C2CD3 architectural and recruitment functions.

Reason: Independent human and mammalian evidence supports recruitment or maintenance of proteins at the centrosome. This process does not imply that C2CD3 itself phosphorylates TTBK2 substrates, activates RAB8 or carries ciliary vesicles.

Summary: C2CD3 distal-centriole function supports primary, non-motile cilium assembly.

Reason: The PMID:23769972 abstract reports target-specific distal-centriole follow-up and primary-cilium templating in human cells. Full target Methods/images and the erratum contents remain unavailable; retain the curated IMP in conjunction with independent ciliogenesis and appendage evidence from PMID:24469809. No exact target follow-up cell line is inferred from general indexing.

Summary: C2CD3 contributes to the structural organization of the distal-centriolar luminal network.

Reason: PMID:41364719 combines human C2CD3 epitope mapping in a radial arrangement with loss of luminal and appendage-recruitment architecture after depletion. Physical placement within that architecture plus its organizing effect supports a cytoskeletal structural function, beyond a ciliogenesis-necessity phenotype alone. Mouse cryo-electron tomography is complementary structural context; it does not identify every ring node or hook as C2CD3. GO:0005200 specifically concerns structural integrity of a cytoskeletal structure; the distal centriole is that structure here. It is a child of structural molecule activity and does not require direct tubulin affinity. This specifies the demonstrated architectural role without asserting a finer protein adapter, catalytic activity or calcium-dependent lipid binding. This is a new molecular-function assertion, not an additional process annotation.