AURKC

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000775 chromosome, centromeric region	IEA GO_REF:0000044	ACCEPT	Summary: The UniProt centromere mapping agrees with human Aurora-C localization. Reason: PMID:27332895 reports full-length human Aurora-C around metaphase centromeres with CPC partners; deleting its distal C terminus disperses the construct. This supports the dynamic centromeric location of the kinase, without asserting constitutive residence or equal localization of every natural product.
GO:0000776 kinetochore	IBA GO_REF:0000033	UNDECIDED	Summary: The kinetochore IBA needs a more precise target-level spatial or phylogenetic assessment. Reason: The PTN000681968 IBD record was read, but the actual tree and alignment were not reconstructed. Human inner-centromere localization in PMID:27332895 does not by itself resolve localization or activity at the distinct kinetochore structure. The displayed Aurora-B and other donors do not establish erroneous propagation, so the source assertion is preserved without a confident rejection. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000681968 UNRESOLVED The ancestral assertion is present in the PAINT IBD table. Its full phylogenetic placement and target-specific experimental support remain unresolved; donor composition alone does not establish a propagation error.
GO:0000793 condensed chromosome	IDA PMID:15670791 Cloning and characterization of a novel human Aurora C splic...	ACCEPT	Summary: Aurora C-SV associates with condensed chromosomes during early mitosis. Reason: EGFP-tagged 290-residue Aurora C-SV associates with condensed chromosomes from prophase through metaphase in PMID:15670791. This establishes the location for the tested splice variant; identical localization of all three natural products has not been demonstrated. Supporting Evidence: PMID:15670791 Aurora C-SV-EGFP associated with chromosomes in prophase and metaphase
GO:0000922 spindle pole	IBA GO_REF:0000033	UNDECIDED	Summary: Spindle-pole placement remains unresolved for human AURKC. Reason: The PTN000681968 spindle-pole IBD is present in the complete local PAINT table. Aurora-A-containing donor lists alone cannot show that AURKC falls outside the inherited clade or lost the function. No target-specific pole experiment or full node-placement/MSA analysis was established in this consultation; central-spindle localization cannot simply substitute for pole evidence. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000681968 UNRESOLVED The ancestral assertion is present in the PAINT IBD table. Its full phylogenetic placement and target-specific experimental support remain unresolved; donor composition alone does not establish a propagation error.
GO:0004672 protein kinase activity	IDA PMID:15670791 Cloning and characterization of a novel human Aurora C splic...	ACCEPT	Summary: Aurora C-SV directly phosphorylates a protein substrate. Reason: The 290-residue Aurora C-SV protein phosphorylates MBP, with loss of activity after the T179A substitution (PMID:15670791). This directly supports the broad protein kinase assertion. Independent residue-specific studies establish the serine/threonine class, but the original MBP experiment need not be recast as a residue-specific assay.
GO:0004672 protein kinase activity	IEA GO_REF:0000002	MODIFY	Summary: The InterPro kinase-family mapping is less specific than the established catalytic activity. Reason: IPR008271/IPR030616 supply the original electronic kinase inference. Human Aurora-C assays in PMID:27332895 and the engineered kinase-domain experiments in PMID:31320618 establish serine/threonine-directed phosphotransfer, providing an independently justified specific replacement. This does not change the original InterPro identifiers or claim that those signatures alone distinguish every substrate specificity. Proposed replacements: protein serine/threonine kinase activity
GO:0004674 protein serine/threonine kinase activity	IEA GO_REF:0000003	ACCEPT	Summary: The EC mapping matches the experimentally supported serine/threonine kinase mechanism. Reason: EC:2.7.11.1 agrees with human Aurora-C phosphorylation of Survivin and INCENP in PMID:27332895 and ATP-dependent catalysis by the purified human kinase-domain complex in PMID:31320618. Retain this central molecular activity; recombinant fragments do not establish natural-product equivalence.
GO:0004712 protein serine/threonine/tyrosine kinase activity	IEA GO_REF:0000117	MODIFY	Summary: The ARBA dual-specificity label includes an unestablished tyrosine reaction. Reason: The official GO:0004712 definition requires serine, threonine and tyrosine phosphorylation. The independently inspected human Aurora-C experiments establish serine/threonine catalysis, providing GO:0004674 as a supported replacement. This is a specificity correction, not a claim that an exhaustive search disproved every possible tyrosine substrate or that the current term is a synonym for serine/threonine kinase. Proposed replacements: protein serine/threonine kinase activity
GO:0004712 protein serine/threonine/tyrosine kinase activity	TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle.	MODIFY	Summary: The review abstract and direct AURKC experiments support the serine/threonine class. Reason: PMID:19774610 explicitly describes Aurora kinases as serine/threonine kinases in its complete abstract. Its Aurora-A-focused title does not invalidate the AURKC TAS annotation, and its full text remains uninspected. The narrower catalytic replacement is independently established by PMID:27332895 and PMID:31320618; GO:0004712 additionally requires tyrosine catalysis, which was not established in the inspected experiments. Proposed replacements: protein serine/threonine kinase activity
GO:0005515 protein binding	IPI PMID:21988832 Toward an understanding of the protein interaction network o...	UNDECIDED	Summary: The liver-network AURKC–Survivin record has not been independently traced to its exact dataset entry. Reason: The complete PMID:21988832 abstract and cached article availability were inspected, but the source-specific interaction table and validation assignment were not recovered. Survivin binding is independently credible from PMID:27332895, yet that does not certify the exact original network record or its assay. Preserve the IPI/partner tuple without calling the screen false.
GO:0005515 protein binding	IPI PMID:27332895 Aurora-C Interactions with Survivin and INCENP Reveal Shared...	KEEP AS NON CORE	Summary: Direct binding to Survivin is experimentally supported but the generic MF does not describe the kinase mechanism. Reason: Human co-immunoprecipitation and recombinant binding experiments establish association with Survivin and identify a contribution from the Aurora-C C terminus (PMID:27332895). The generic interaction is supported but does not by itself describe an additional molecular activity beyond the kinase mechanism. Supporting Evidence: PMID:27332895 Aurora-C and Survivin in the same immune complexes
GO:0005515 protein binding	IPI PMID:27332895 Aurora-C Interactions with Survivin and INCENP Reveal Shared...	KEEP AS NON CORE	Summary: Aurora-C directly binds its INCENP regulator and substrate. Reason: Human Aurora-C binds INCENP fragments that activate the kinase and undergo phosphorylation (PMID:27332895). This is a supported interaction within the catalytic complex. A separate specialized binding activity has not been established.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: The binary-interactome pair with A2RRN7 remains source-table unresolved. Reason: PMID:32296183 is a human binary interaction resource; its complete abstract was read, but the precise AURKC–A2RRN7 experiment and supplementary record were not inspected. Retain uncertainty about this source-specific pair instead of removing a potentially genuine interaction or manufacturing a function from it.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: The P32243-2 partner-specific interaction needs its original pair record. Reason: The exact PMID:32296183 supplementary interaction and construct identity were not verified. Preserve P32243-2 as the source partner identifier: it is not an isoform assignment to AURKC. The general interactome abstract cannot determine this pair or justify a specific molecular-function replacement.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: The binary-interactome Q96CA5 pair remains unadjudicated. Reason: The original PMID:32296183 dataset entry and validation for this partner were not read. A large interactome survey is not evidence that a particular interaction is false, but its abstract cannot resolve the individual assertion; retain the source tuple and uncertainty.
GO:0005515 protein binding	IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro...	UNDECIDED	Summary: The kinase-network INCENP pair is plausible but its original record is unverified. Reason: PMID:32707033 provides mass-spectrometry kinase interaction data. Its complete abstract was read, while the exact AURKC bait/prey row and confidence context were not inspected. Independent INCENP experiments in PMID:27332895 do not replace verification of this particular source record; no wrong-pair claim is made.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	UNDECIDED	Summary: The BioPlex INCENP interaction needs its cell-line-specific source entry. Reason: PMID:33961781 reports distinct 293T and HCT116 interaction networks. The complete abstract was read, but the particular AURKC–INCENP entry and cell-line/assay attribution were not established. Preserve the reported partner and uncertainty despite independent evidence that these proteins interact.
GO:0005524 ATP binding	IEA GO_REF:0000002	ACCEPT	Summary: ATP binding is an intrinsic component of the kinase reaction. Reason: The ATP-containing radiometric reactions in PMID:27332895 and controlled ATP addition in the purified human kinase-domain assays of PMID:31320618 directly support this property. The structural inhibitor-bound complex alone is not being treated as an ATP-bound crystal or a natural full-length product assay.
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: The nuclear PAINT annotation is compatible with the chromosome-passenger kinase. Reason: The PTN000681967 nuclear assertion agrees with the chromosomal activity of human Aurora-C. Chromosome association and subsequent midzone/midbody redistribution describe different stages of the cell cycle, so the broad nuclear compartment remains compatible with the more precise mitotic locations.
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: The UniProt nuclear compartment is compatible with the dynamic kinase localization. Reason: Retain the nuclear location as cellular context for the chromosome-passenger kinase. It does not imply permanent nuclear residence throughout mitosis; direct chromosome-to-midzone/midbody redistribution is recorded separately in PMID:15670791. Replacing nucleus with a single mitotic structure would erase that temporal distinction rather than simply improve the original compartment assertion.
GO:0005694 chromosome	IEA GO_REF:0000044	ACCEPT	Summary: Chromosome association is supported independently of the more specific centromere location. Reason: Aurora C-SV associates with condensed chromosomes during prophase and metaphase (PMID:15670791), while full-length Aurora-C is detected around metaphase centromeres with CPC partners (PMID:27332895). The UniProt chromosome and centromeric-region records capture related but separately supported localization assertions. Retain the broader chromosome location.
GO:0005813 centrosome	IBA GO_REF:0000033	UNDECIDED	Summary: The centrosome IBA cannot be rejected from Aurora-A donor names alone. Reason: PTN001219008 is a genuine IBD in the local PAINT table. Its full tree/MSA placement and AURKC-specific retention or loss were not established. The reviewed Aurora-C studies emphasize CPC and central-spindle locations, which does not disprove an additional centrosomal role. Preserve uncertainty rather than assert paralog mispropagation. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN001219008 UNRESOLVED The ancestral assertion is present in the PAINT IBD table. Its full phylogenetic placement and target-specific experimental support remain unresolved; donor composition alone does not establish a propagation error.
GO:0005819 spindle	IEA GO_REF:0000044	ACCEPT	Summary: Aurora-C associates with the spindle during cell division. Reason: UniProt independently records spindle localization, with evidence from PMID:15938719. Aurora C-SV imaging in PMID:15670791 corroborates central-spindle association. Retain the broad spindle compartment alongside the separately supported spindle-midzone annotation; this does not imply localization to spindle poles.
GO:0005819 spindle	TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle.	ACCEPT	Summary: The broad spindle location is corroborated by independent direct imaging. Reason: Independent human Aurora C-SV imaging demonstrates central-spindle localization (PMID:15670791), supporting the broad spindle compartment recorded by this TAS annotation. The original review is available only as an abstract, so the direct experimental support is attributed to PMID:15670791.
GO:0005876 spindle microtubule	IBA GO_REF:0000033	ACCEPT	Summary: Spindle-microtubule association is consistent with the active midzone passenger complex. Reason: The PTN000681967 spindle-microtubule assertion agrees with UniProt localization to midzone microtubules and human Aurora C-SV imaging at the central spindle (PMID:15670791). Localization does not by itself establish direct microtubule binding or a microtubule-organizing activity.
GO:0006468 protein phosphorylation	IDA PMID:15670791 Cloning and characterization of a novel human Aurora C splic...	ACCEPT	Summary: Aurora C-SV directly phosphorylates a protein substrate. Reason: The complete PMID:15670791 abstract reports MBP kinase activity by the 290-residue C-SV protein and loss of activity in its T179A mutant. AURKC therefore performs phosphotransfer itself, rather than merely being required for another protein to do the reaction. The tested-product boundary is retained. Supporting Evidence: PMID:15670791 this Aurora C-SV phosphorylated MBP
GO:0007051 spindle organization	IEA GO_REF:0000117	UNDECIDED	Summary: The ARBA spindle-organization process needs a more direct target-level link. Reason: GO:0007051 concerns assembly, arrangement or disassembly of the spindle. The inspected human kinase/localization experiments and Survivin-mutant chromosome-alignment phenotypes do not by themselves establish which spindle-organization step AURKC performs. The broader curated UniProt CPC summary is supportive context, but the exact ARBA rationale and primary assembly endpoint remain unresolved; no contrary-function claim is made.
GO:0007052 mitotic spindle organization	IBA GO_REF:0000033	UNDECIDED	Summary: The mitotic-spindle-organization IBA remains unresolved at the target and ancestral node. Reason: The PTN000681967 IBD is real and its donor count is not a weakness. The full phylogeny/MSA and underlying target-relevant spindle-organization experiments were not reconstructed. CPC localization and kinase activity alone do not settle spindle assembly/organization, so retain uncertainty without declaring the inherited annotation erroneous. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000681967 UNRESOLVED The ancestral assertion is present in the PAINT IBD table. Its full phylogenetic placement and target-specific experimental support remain unresolved; donor composition alone does not establish a propagation error.
GO:0008608 attachment of spindle microtubules to kinetochore	TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle.	UNDECIDED	Summary: The review-derived kinetochore-attachment process needs its supporting experiment. Reason: The full PMID:19774610 discussion and cited primary attachment studies were not inspected. Centromeric kinase localization and chromosome misalignment do not alone establish the exact spindle-microtubule attachment step. Do not call this TAS record miscited merely because the abstract foregrounds Aurora A.
GO:0030496 midbody	IBA GO_REF:0000033	ACCEPT	Summary: The midbody IBA has concordant experimental grounding on AURKC itself. Reason: The PTN002806146 IBD includes Q9UQB9 among experimental descendants, which is expected and not circular. PMID:15670791 independently reports Aurora C-SV at the midbody during cytokinesis. Retain this location as a division-stage component of the kinase model.
GO:0030496 midbody	IDA PMID:15670791 Cloning and characterization of a novel human Aurora C splic...	ACCEPT	Summary: Aurora C-SV localizes to the midbody during cytokinesis. Reason: The EGFP-tagged 290-residue Aurora C-SV protein localizes to the midbody during cytokinesis (PMID:15670791). This directly supports the IDA compartment assertion for the tested variant.
GO:0030496 midbody	IEA GO_REF:0000117	ACCEPT	Summary: The ARBA midbody mapping agrees with direct Aurora C-SV localization. Reason: The electronic ARBA00033509 inference is independently corroborated by PMID:15670791. Midbody localization is a stage-specific part of the chromosome-passenger kinase mechanism, not constitutive residence or a claim that localization alone proves every cytokinetic process.
GO:0030496 midbody	TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle.	ACCEPT	Summary: The TAS midbody assertion agrees with independent direct localization. Reason: Human Aurora C-SV localizes to the midbody during cytokinesis (PMID:15670791), independently supporting this TAS compartment assertion. The original review is available only as an abstract, so its detailed experimental discussion remains unverified.
GO:0032133 chromosome passenger complex	IBA GO_REF:0000033	ACCEPT	Summary: AURKC is a catalytic component of a chromosome passenger complex. Reason: The PTN000681967 IBD agrees with human binding, reconstitution and cellular experiments in PMID:27332895. AURKC binds CPC components and is activated through INCENP-associated phosphorylation. Predominantly distinct AURKB- and AURKC-containing complexes were observed; membership does not require simultaneous B/C catalytic subunits in every complex.
GO:0032133 chromosome passenger complex	TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle.	ACCEPT	Summary: The review-derived CPC membership is independently supported. Reason: Human AURKC binds INCENP and Survivin and forms an active kinase complex (PMID:15316025; PMID:27332895), supporting CPC membership. Predominantly separate AURKB- and AURKC-containing complexes were observed in the tested somatic-cell system. The original TAS review is available only as an abstract. Supporting Evidence: PMID:15316025 human Aurora-C is a chromosomal passenger protein
GO:0032465 regulation of cytokinesis	IBA GO_REF:0000033	ACCEPT	Summary: Cytokinesis regulation is consistent with the inherited CPC kinase role. Reason: The PTN000681967 IBD is retained without donor-count or circularity arguments. Human primary PMID:15938719 reports cytokinesis interference by inactive Aurora-C and reciprocal rescue by active Aurora-B/C in the tested expression system. AURKC supplies catalytic activity to the regulatory machinery; this is not a gene-null rescue claim or evidence that it is uniquely required in every mammalian cell.
GO:0032467 positive regulation of cytokinesis	TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle.	ACCEPT	Summary: The positive cytokinesis role has independent human functional corroboration. Reason: Although PMID:19774610 is available only at the abstract-reading level here, PMID:15938719 directly describes inactive-kinase disruption of cytokinesis and reciprocal active-kinase rescue. This supports a positive regulatory role in the tested somatic expression context, with B/C compensation and dominant-negative limitations explicit; no direct human germ-cell assay is inferred.
GO:0051233 spindle midzone	IBA GO_REF:0000033	ACCEPT	Summary: The spindle-midzone IBA is supported by a target-grounded IBD and direct localization. Reason: Q9UQB9 in PTN000681967 is legitimate experimental grounding for the ancestral assertion, not circular evidence. PMID:15670791 documents C-SV redistribution to the central spindle midzone after chromosome separation. Preserve the dynamic kinase localization without asserting all natural products behave identically.
GO:0051233 spindle midzone	IDA PMID:15670791 Cloning and characterization of a novel human Aurora C splic...	ACCEPT	Summary: Aurora C-SV redistributes to the spindle midzone during anaphase. Reason: The complete PMID:15670791 abstract reports direct imaging of this change for the 290-residue EGFP-tagged variant. This supports the annotated compartment, while location alone is not treated as an experiment establishing midzone assembly.
GO:0051256 mitotic spindle midzone assembly	TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle.	UNDECIDED	Summary: Midzone localization does not by itself verify midzone assembly. Reason: The full PMID:19774610 review and the exact primary assembly study behind this TAS assertion were not inspected. PMID:15670791 supports localization at the midzone, but not necessarily a causal assembly endpoint. Retain the original assertion as unresolved rather than infer a wrong-paralog citation from the review title.
GO:0090068 positive regulation of cell cycle process	IEA GO_REF:0000117	ACCEPT	Summary: The broad positive cell-cycle role includes experimentally supported cytokinesis regulation. Reason: Aurora-C kinase activity supports cytokinesis in the human mitotic expression/rescue experiments of PMID:15938719. Cytokinesis is a cell-cycle process, so the broad positive-regulation assertion is biologically supported alongside the separately annotated, more specific cytokinesis term.
GO:0090267 positive regulation of mitotic cell cycle spindle assembly checkpoint	NAS PMID:31320618 Structural mechanism of synergistic activation of Aurora kin...	UNDECIDED	Summary: The cited structural paper does not itself resolve a human mitotic checkpoint assay. Reason: PMID:31320618 was read through selected original Introduction, Results and Methods. Its checkpoint discussion concerns prior mouse-oocyte meiosis and artificial mitotic substitution, while its own primary experiments characterize human recombinant kinase/INCENP structure and catalysis. Those are not interchangeable with a direct human mitotic spindle-checkpoint experiment. The cited underlying studies were not fully adjudicated, so preserve uncertainty rather than deny all checkpoint activity.
GO:0106310 protein serine kinase activity	IEA GO_REF:0000116	ACCEPT	Summary: Protein serine phosphorylation is directly demonstrated. Reason: The RHEA-derived serine-kinase assertion agrees with human Aurora-C phosphorylation of Survivin Ser20 in PMID:27332895 and serine-containing INCENP sites. This is a demonstrated part of the catalytic specificity and need not be replaced merely because the core uses the broader serine/threonine label.
GO:1903490 positive regulation of mitotic cytokinesis	NAS PMID:15316025 Direct association with inner centromere protein (INCENP) ac...	ACCEPT	Summary: Positive mitotic cytokinesis regulation is supported in a defined human expression system. Reason: PMID:15316025 establishes human INCENP association and activation in its complete abstract, but that abstract alone is not a direct cytokinesis assay. Independent PMID:15938719 reports inactive Aurora-C interference with cytokinesis and reciprocal active Aurora-B/C rescue. Retain the biologically supported NAS assertion with this distinction, without turning dominant-negative rescue into gene-null rescue or universal nonredundant necessity.

Gene Description

Existing Annotations Review

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