CEP83

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005515 protein binding	IPI PMID:23530209 CCDC41 is required for ciliary vesicle docking to the mother...	REMOVE	Summary: IPI with IFT20 (Q8IY31) from the CCDC41/CEP83 study; the abstract reports co-localization of a CEP83 pool with IFT20 at the Golgi and that CEP83 knockdown blocks IFT20 recruitment to the centrosome. Reason: Bare protein binding carries no functional information. The CEP83-IFT20 association is plausible and is reflected in the review through cilium assembly and protein localization to centrosome annotations; no specific molecular function term is supported by the interaction alone. Removal does not dispute the interaction. Supporting Evidence: PMID:23530209 a pool of CCDC41 colocalizes with intraflagellar transport protein 20 (IFT20) subunit of the intraflagellar transport particle at the Golgi complex. PMID:23530209 knockdown of CCDC41 inhibits the recruitment of IFT20 to the centrosome.
GO:0005515 protein binding	IPI PMID:23530209 CCDC41 is required for ciliary vesicle docking to the mother...	REMOVE	Summary: IPI with CEP164 (Q9UPV0) from the CCDC41/CEP83 study. Reason: Bare protein binding is uninformative. The CEP83-CEP164 interaction is consistent with the distal appendage assembly hierarchy (CEP83 at the appendage root, CEP164 at the tip), but no more specific MF term is justified; the structural role is captured by the ciliary transition fiber annotation and core function. Supporting Evidence: PMID:23530209 CCDC41 specifically localizes to the distal end of the mother centriole and interacts with centrosomal protein 164 (Cep164), a distal appendage component.
GO:0005794 Golgi apparatus	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: IBA propagation of Golgi apparatus localization, with CEP83 itself among the experimental sources. Reason: A minor Golgi-associated pool co-localizing with IFT20 was reported for human CEP83, and CEP83 appearing in the WITH/FROM is expected for an IBA grounded in its own experimental data. The HPA atlas also lists Golgi apparatus and vesicles as main locations. The functionally defining location is the distal appendage; the Golgi pool is retained as non-core. Supporting Evidence: PMID:23530209 a pool of CCDC41 colocalizes with intraflagellar transport protein 20 (IFT20) subunit of the intraflagellar transport particle at the Golgi complex.
GO:0005794 Golgi apparatus	IDA PMID:23530209 CCDC41 is required for ciliary vesicle docking to the mother...	KEEP AS NON CORE	Summary: IDA: a pool of CEP83 (CCDC41) co-localizes with IFT20 at the Golgi complex. Reason: Direct observation in the cited study supports a Golgi pool, but its functional significance is unclear relative to the well-established distal appendage location. Retained as non-core. Supporting Evidence: PMID:23530209 a pool of CCDC41 colocalizes with intraflagellar transport protein 20 (IFT20) subunit of the intraflagellar transport particle at the Golgi complex.
GO:0005813 centrosome	IBA GO_REF:0000033	ACCEPT	Summary: IBA centrosome location. Reason: CEP83 localizes to the distal appendages of the mother centriole, a part of the centrosome; the propagated location is correct though less specific than ciliary transition fiber. Supporting Evidence: PMID:23530209 CCDC41 specifically localizes to the distal end of the mother centriole and interacts with centrosomal protein 164 (Cep164), a distal appendage component. PMID:23348840 we identified five DAP components, including one previously described (CEP164), one partially characterized (CEP89 [ccdc123]), and three novel (CEP83 [ccdc41], SCLT1, and FBF1) DAP proteins
GO:0005814 centriole	IBA GO_REF:0000033	ACCEPT	Summary: IBA centriole location, grounded in human and mouse experimental data. Reason: CEP83 sits at the root of the distal appendage blades on the mother centriole. Correct, although ciliary transition fiber is the more precise term. Supporting Evidence: PMID:29789620 CEP83, CEP89, SCLT1, and CEP164 form the backbone of pinwheel blades, with CEP83 confined at the root and CEP164 extending to the tip near the membrane-docking site.
GO:0005814 centriole	IDA PMID:23348840 Centriole distal appendages promote membrane docking, leadin...	ACCEPT	Summary: IDA from the distal appendage proteomics/super-resolution study identifying CEP83 as a DAP component. Reason: Direct localization to the distal appendages of the mother centriole. Supporting Evidence: PMID:23348840 we identified five DAP components, including one previously described (CEP164), one partially characterized (CEP89 [ccdc123]), and three novel (CEP83 [ccdc41], SCLT1, and FBF1) DAP proteins
GO:0005814 centriole	IDA PMID:23530209 CCDC41 is required for ciliary vesicle docking to the mother...	ACCEPT	Summary: IDA: CCDC41/CEP83 localizes specifically to the distal end of the mother centriole. Reason: Direct localization evidence in human cells. Supporting Evidence: PMID:23530209 CCDC41 specifically localizes to the distal end of the mother centriole and interacts with centrosomal protein 164 (Cep164), a distal appendage component.
GO:0005814 centriole	IEA GO_REF:0000120	ACCEPT	Summary: IEA (Ensembl Compara/UniProt subcellular location transfer) centriole location. Reason: Consistent with abundant direct human evidence for centriolar distal appendage localization. Supporting Evidence: PMID:23348840 we identified five DAP components, including one previously described (CEP164), one partially characterized (CEP89 [ccdc123]), and three novel (CEP83 [ccdc41], SCLT1, and FBF1) DAP proteins
GO:0005829 cytosol	TAS Reactome:R-HSA-5617816	KEEP AS NON CORE	Summary: Reactome places this distal appendage protein in its 'cytosol' compartment for a ciliogenesis reaction; Reactome has no centriole/distal-appendage compartment, so centrosomal reactions are modelled in cytosol. Reason: This TAS row reflects a Reactome compartment convention rather than an independent localization experiment. The protein is a structural component of the centriolar distal appendages (ciliary transition fibers), which are part of the centrosome in the cytoplasm rather than the soluble cytosol. The location is broadly compatible (the centrosome lies in the cytoplasm and is not membrane-bounded) but uninformative, so it is retained only as non-core; the informative location is ciliary transition fiber.
GO:0005829 cytosol	TAS Reactome:R-HSA-5626223	KEEP AS NON CORE	Summary: Reactome places this distal appendage protein in its 'cytosol' compartment for a ciliogenesis reaction; Reactome has no centriole/distal-appendage compartment, so centrosomal reactions are modelled in cytosol. Reason: This TAS row reflects a Reactome compartment convention rather than an independent localization experiment. The protein is a structural component of the centriolar distal appendages (ciliary transition fibers), which are part of the centrosome in the cytoplasm rather than the soluble cytosol. The location is broadly compatible (the centrosome lies in the cytoplasm and is not membrane-bounded) but uninformative, so it is retained only as non-core; the informative location is ciliary transition fiber.
GO:0005829 cytosol	TAS Reactome:R-HSA-5626227	KEEP AS NON CORE	Summary: Reactome places this distal appendage protein in its 'cytosol' compartment for a ciliogenesis reaction; Reactome has no centriole/distal-appendage compartment, so centrosomal reactions are modelled in cytosol. Reason: This TAS row reflects a Reactome compartment convention rather than an independent localization experiment. The protein is a structural component of the centriolar distal appendages (ciliary transition fibers), which are part of the centrosome in the cytoplasm rather than the soluble cytosol. The location is broadly compatible (the centrosome lies in the cytoplasm and is not membrane-bounded) but uninformative, so it is retained only as non-core; the informative location is ciliary transition fiber.
GO:0005829 cytosol	TAS Reactome:R-HSA-5626228	KEEP AS NON CORE	Summary: Reactome places this distal appendage protein in its 'cytosol' compartment for a ciliogenesis reaction; Reactome has no centriole/distal-appendage compartment, so centrosomal reactions are modelled in cytosol. Reason: This TAS row reflects a Reactome compartment convention rather than an independent localization experiment. The protein is a structural component of the centriolar distal appendages (ciliary transition fibers), which are part of the centrosome in the cytoplasm rather than the soluble cytosol. The location is broadly compatible (the centrosome lies in the cytoplasm and is not membrane-bounded) but uninformative, so it is retained only as non-core; the informative location is ciliary transition fiber.
GO:0005829 cytosol	TAS Reactome:R-HSA-5626681	KEEP AS NON CORE	Summary: Reactome places this distal appendage protein in its 'cytosol' compartment for a ciliogenesis reaction; Reactome has no centriole/distal-appendage compartment, so centrosomal reactions are modelled in cytosol. Reason: This TAS row reflects a Reactome compartment convention rather than an independent localization experiment. The protein is a structural component of the centriolar distal appendages (ciliary transition fibers), which are part of the centrosome in the cytoplasm rather than the soluble cytosol. The location is broadly compatible (the centrosome lies in the cytoplasm and is not membrane-bounded) but uninformative, so it is retained only as non-core; the informative location is ciliary transition fiber.
GO:0005829 cytosol	TAS Reactome:R-HSA-5626699	KEEP AS NON CORE	Summary: Reactome places this distal appendage protein in its 'cytosol' compartment for a ciliogenesis reaction; Reactome has no centriole/distal-appendage compartment, so centrosomal reactions are modelled in cytosol. Reason: This TAS row reflects a Reactome compartment convention rather than an independent localization experiment. The protein is a structural component of the centriolar distal appendages (ciliary transition fibers), which are part of the centrosome in the cytoplasm rather than the soluble cytosol. The location is broadly compatible (the centrosome lies in the cytoplasm and is not membrane-bounded) but uninformative, so it is retained only as non-core; the informative location is ciliary transition fiber.
GO:0005829 cytosol	TAS Reactome:R-HSA-5638009	KEEP AS NON CORE	Summary: Reactome places this distal appendage protein in its 'cytosol' compartment for a ciliogenesis reaction; Reactome has no centriole/distal-appendage compartment, so centrosomal reactions are modelled in cytosol. Reason: This TAS row reflects a Reactome compartment convention rather than an independent localization experiment. The protein is a structural component of the centriolar distal appendages (ciliary transition fibers), which are part of the centrosome in the cytoplasm rather than the soluble cytosol. The location is broadly compatible (the centrosome lies in the cytoplasm and is not membrane-bounded) but uninformative, so it is retained only as non-core; the informative location is ciliary transition fiber.
GO:0051660 establishment of centrosome localization	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: IBA establishment of centrosome localization, sourced from mouse Cep83. Reason: In mouse radial glial progenitors, removal of CEP83 eliminates distal appendages and disrupts anchoring of the centrosome to the apical membrane. This is a downstream structural consequence of distal appendage loss (anchoring rather than directed movement of the centrosome), so it is retained as non-core rather than a core function. Supporting Evidence: PMID:32238932 Selective removal of centrosomal protein 83 (CEP83) eliminates these distal appendages and disrupts the anchorage of the centrosome to the apical membrane
GO:0060271 cilium assembly	IBA GO_REF:0000033	ACCEPT	Summary: IBA cilium assembly with CEP83 itself among the experimental sources. Reason: CEP83 is required for primary cilium assembly as the root distal appendage component; it supports centriole-to-membrane docking. Supporting Evidence: PMID:23348840 All five DAP components are essential for ciliogenesis; loss of CEP83 specifically blocks centriole-to-membrane docking.
GO:0060271 cilium assembly	IMP PMID:23348840 Centriole distal appendages promote membrane docking, leadin...	ACCEPT	Summary: IMP: CEP83 depletion blocks ciliogenesis and centriole-to-membrane docking. Reason: CEP83 is a structural component of the distal appendages that directly mediate membrane docking of the mother centriole, the first step of cilium assembly; this is participation, not only upstream necessity. Supporting Evidence: PMID:23348840 All five DAP components are essential for ciliogenesis; loss of CEP83 specifically blocks centriole-to-membrane docking. PMID:23348840 Undocked centrioles fail to recruit TTBK2 or release CP110, the two earliest modifications found on centrioles prior to cilia assembly
GO:0060271 cilium assembly	IMP PMID:23348840 Centriole distal appendages promote membrane docking, leadin...	ACCEPT	Summary: IMP: CEP83 depletion blocks ciliogenesis (duplicate row with involved_in qualifier). Reason: As above; CEP83 is essential for ciliogenesis and acts within the docking step. Supporting Evidence: PMID:23348840 All five DAP components are essential for ciliogenesis; loss of CEP83 specifically blocks centriole-to-membrane docking.
GO:0060271 cilium assembly	IMP PMID:23530209 CCDC41 is required for ciliary vesicle docking to the mother...	ACCEPT	Summary: IMP: CCDC41/CEP83 depletion arrests ciliogenesis at the ciliary vesicle docking step. Reason: Supports a direct role in the earliest step of cilium assembly. Supporting Evidence: PMID:23530209 depletion of CCDC41 or IFT20 inhibits ciliogenesis at the ciliary vesicle docking step
GO:0060271 cilium assembly	IMP PMID:23530209 CCDC41 is required for ciliary vesicle docking to the mother...	ACCEPT	Summary: IMP: CCDC41/CEP83 depletion arrests ciliogenesis at the ciliary vesicle docking step. Reason: Supports a direct role in the earliest step of cilium assembly. Supporting Evidence: PMID:23530209 depletion of CCDC41 or IFT20 inhibits ciliogenesis at the ciliary vesicle docking step
GO:0071539 protein localization to centrosome	IMP PMID:23348840 Centriole distal appendages promote membrane docking, leadin...	ACCEPT	Summary: IMP from the DAP study: CEP83 is required to recruit SCLT1 and CEP89 (and indirectly FBF1/CEP164) to centrioles, and for TTBK2 recruitment. Reason: CEP83 is the root of the distal appendage assembly hierarchy and is needed to localize the downstream DAP components to the mother centriole, a part of the centrosome. The term is acceptable, though it captures assembly of the appendage structure rather than a transport activity. Supporting Evidence: PMID:23348840 CEP83 recruits both SCLT1 and CEP89 to centrioles. Subsequent recruitment of FBF1 and CEP164 is independent of CEP89 but mediated by SCLT1.
GO:0071539 protein localization to centrosome	IMP PMID:23530209 CCDC41 is required for ciliary vesicle docking to the mother...	ACCEPT	Summary: IMP: CEP83 knockdown inhibits IFT20 recruitment to the centrosome. Reason: Supported by the cited abstract; consistent with CEP83 acting as an anchoring platform at the distal appendages. Supporting Evidence: PMID:23530209 knockdown of CCDC41 inhibits the recruitment of IFT20 to the centrosome.
GO:0097539 ciliary transition fiber	IBA GO_REF:0000033	ACCEPT	Summary: IBA ciliary transition fiber (distal appendage), grounded in CEP83 experimental data. Reason: Ciliary transition fiber is the GO term for distal appendages; CEP83 is a defining component. Supporting Evidence: PMID:29789620 CEP83, CEP89, SCLT1, and CEP164 form the backbone of pinwheel blades, with CEP83 confined at the root and CEP164 extending to the tip near the membrane-docking site.
GO:0097539 ciliary transition fiber	IDA PMID:23348840 Centriole distal appendages promote membrane docking, leadin...	ACCEPT	Summary: IDA: CEP83 is one of five distal appendage components identified by proteomics and super-resolution microscopy. Reason: Core location of CEP83. Supporting Evidence: PMID:23348840 we identified five DAP components, including one previously described (CEP164), one partially characterized (CEP89 [ccdc123]), and three novel (CEP83 [ccdc41], SCLT1, and FBF1) DAP proteins PMID:23348840 CEP83 recruits both SCLT1 and CEP89 to centrioles. Subsequent recruitment of FBF1 and CEP164 is independent of CEP89 but mediated by SCLT1.
GO:0005198 structural molecule activity	IDA PMID:29789620 Super-resolution architecture of mammalian centriole distal ...	NEW	Summary: Proposed: CEP83 contributes to the structural integrity of the distal appendage (ciliary transition fiber) blade, as one of the four proteins forming the blade backbone. Reason: Super-resolution mapping shows the protein forms part of the backbone of the distal appendage blades, and loss-of-function abolishes recruitment of downstream appendage components. No enzymatic or specific binding activity is known, so structural molecule activity is the most accurate available MF term. This is a molecular-function proposal, not a process term. Supporting Evidence: PMID:29789620 CEP83, CEP89, SCLT1, and CEP164 form the backbone of pinwheel blades, with CEP83 confined at the root and CEP164 extending to the tip near the membrane-docking site. PMID:23348840 CEP83 recruits both SCLT1 and CEP89 to centrioles. Subsequent recruitment of FBF1 and CEP164 is independent of CEP89 but mediated by SCLT1.

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