APC2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005515 protein binding	IPI PMID:12477395 Proteomics analysis identifies new components of the fission...	REMOVE	Summary: IntAct-derived IPI with Mnd2 (UniProtKB:P40577) from Yoon et al. 2002, a tandem-affinity purification/DALPC proteomics study that raised the yeast APC/C subunit count to 13 by identifying Mnd2 and Swm1. The 'interaction' is co-membership of Apc2 and Mnd2 in the purified 13-subunit complex, not a characterised pairwise binding activity. Reason: The cached abstract records a proteomic inventory of APC/C subunits, and the same paper already supports the informative GO:0005680 part_of IPI row for Apc2. Following the repository policy for GO:0005515, the generic term is removed rather than retained: it conveys no molecular-function information beyond what the GO:0005680 complex-membership annotations already state, and removal does not imply that the Apc2-Mnd2 co-association is false. The characterised molecular role of Apc2 (cullin-like scaffold that tethers Apc11 and Doc1 within the APC/C catalytic module) is captured by the proposed GO:0160072 ubiquitin ligase complex scaffold activity annotation instead. Supporting Evidence: PMID:12477395 Here, we have applied a tandem affinity purification approach coupled with direct analysis of the purified complexes by mass spectrometry (DALPC) to reveal additional subunits of both the S. pombe and S. cerevisiae APCs. PMID:12477395 Our data increase the total number of identified APC subunits to 13 in both yeasts and indicate that previous approaches were biased against the identification of small subunits.
GO:0005515 protein binding	IPI PMID:12609981 Mnd2 and Swm1 are core subunits of the Saccharomyces cerevis...	REMOVE	Summary: IntAct-derived IPI with Mnd2 (UniProtKB:P40577) from Hall et al. 2003, which identified Mnd2 and Swm1 as constitutive core APC/C subunits present in complexes from G1-, S- and M-arrested and meiotic cells. In the pairwise in vitro translation assays of that paper Mnd2 bound Cdc23, Apc5 and Apc1; a direct Apc2-Mnd2 contact was not reported, so the IntAct pair reflects co-purification within the complex. Reason: The evidence is co-complex membership (captured by the GO:0005680 rows), and the abstract explicitly names Cdc23, Apc5 and Apc1, not Apc2, as the subunits Mnd2 binds directly. Following the repository policy for GO:0005515, the generic term is removed rather than retained: it conveys no molecular-function information beyond what the GO:0005680 complex-membership annotations already state, and removal does not imply that the Apc2-Mnd2 co-association is false. The characterised molecular role of Apc2 (cullin-like scaffold that tethers Apc11 and Doc1 within the APC/C catalytic module) is captured by the proposed GO:0160072 ubiquitin ligase complex scaffold activity annotation instead. Supporting Evidence: PMID:12609981 Both proteins were present in APC preparations from haploid cells arrested in G(1), S, and M phases and from meiotic diploid cells, indicating that they are constitutive components of the complex throughout the yeast cell cycle. PMID:12609981 Mnd2 interacted strongly with Cdc23, Apc5, and Apc1 when coexpressed in an in vitro transcription/translation reaction.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	REMOVE	Summary: IntAct-derived IPI with Mnd2 (UniProtKB:P40577) from the proteome-wide affinity-enrichment mass-spectrometry map of Michaelis et al. 2023 (4,159 GFP pull-downs, 31,004 interactions). Apc2 and Mnd2 co-enrich as members of the APC/C; this is a high-throughput co-complex observation with no functional content specific to Apc2. Reason: A systematic interactome pull-down recapitulates known APC/C co-membership; the generic term adds nothing to the complex annotations. Following the repository policy for GO:0005515, the generic term is removed rather than retained: it conveys no molecular-function information beyond what the GO:0005680 complex-membership annotations already state, and removal does not imply that the Apc2-Mnd2 co-association is false. The characterised molecular role of Apc2 (cullin-like scaffold that tethers Apc11 and Doc1 within the APC/C catalytic module) is captured by the proposed GO:0160072 ubiquitin ligase complex scaffold activity annotation instead. Supporting Evidence: PMID:37968396 The 4,159 pull-downs generated a highly structured network of 3,927 proteins connected by 31,004 interactions, doubling the number of proteins and tripling the number of reliable interactions compared with existing interactome maps2.
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: UniProt subcellular-location mapping (SL-0191 nucleus), traceable to the genome-wide GFP localisation of Huh et al. 2003 (UniProt: Cytoplasm; Nucleus). The APC/C acts on nuclear substrates (Pds1/securin, Clb2) during the closed mitosis of budding yeast, and tagged core subunits (Cdc23, Apc9) are predominantly nuclear with kinetochore/spindle-associated foci. Reason: Nucleus is the compartment in which Apc2-containing APC/C performs its core function (ubiquitination of securin and mitotic cyclins that reside in the nucleus of budding yeast); the electronic mapping is consistent with direct GFP data for the protein and with localisation of the intact complex. Note that the most detailed localisation studies imaged other subunits rather than Apc2 itself. Supporting Evidence: file:yeast/APC2/APC2-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269\|PubMed:14562095}. Nucleus {ECO:0000269\|PubMed:14562095}. file:yeast/APC2/APC2-deep-research-falcon.md Cdc23 signal was predominantly nuclear throughout the cell cycle, with one or two nuclear foci; Apc9 showed a similar but weaker pattern. file:yeast/APC2/APC2-deep-research-falcon.md Because these studies visualized Cdc23 or Apc9 rather than Apc2, this is complex-level localization evidence and should not be overinterpreted as a directly measured Apc2 distribution.
GO:0005680 anaphase-promoting complex	IBA GO_REF:0000033	ACCEPT	Summary: PAINT IBA from ancestral node PTN000231994 of the ANAPC2 family (PTHR45957), with experimental descendants in human ANAPC2, fly, fission yeast and budding-yeast APC2 itself. APC/C membership is the defining, ancestral property of this cullin-family lineage. Reason: Apc2 is a constitutive core subunit of the 13-subunit APC/C: it was identified in the purified particle by mass spectrometry, co-immunoprecipitates with Cdc23, remains associated with Apc1-TAP, and forms with Apc11 and Doc1 one of the two subcomplexes bridged by Apc1. The IBA is a sound phylogenetic judgment; SGD:S000004117 (APC2 itself) appearing in the WITH/FROM list is expected, as its own IDA/IPI evidence contributed to placing the IBD node. Supporting Evidence: PMID:9469814 Apc2p, Apc5p, and the RING-finger protein Apc11p are conserved from yeast to humans. PMID:16481473 one that contains Apc2 (Cullin), Apc11 (RING), and Doc1/Apc10, and another that contains the three TPR subunits (Cdc27, Cdc16, and Cdc23)
GO:0005680 anaphase-promoting complex	IDA PMID:9469814 Mass spectrometric analysis of the anaphase-promoting comple...	ACCEPT	Summary: Zachariae et al. 1998 purified the budding-yeast APC/C particle and identified Apc2p by tandem mass spectrometry among at least 12 subunits, noting its similarity to the cullin Cdc53p of SCF-Cdc4; this is the founding identification of Apc2 as an APC/C subunit. Reason: Apc2 is a constitutive core subunit of the 13-subunit APC/C: it was identified in the purified particle by mass spectrometry, co-immunoprecipitates with Cdc23, remains associated with Apc1-TAP, and forms with Apc11 and Doc1 one of the two subcomplexes bridged by Apc1. Direct biochemical evidence for complex membership. Supporting Evidence: PMID:9469814 At least 12 different subunits were detected in the purified particle from budding yeast, including the previously identified proteins Apc1p, Cdc16p, Cdc23p, Cdc26p, and Cdc27p. PMID:9469814 Apc2p is similar to the cullin Cdc53p, which is a subunit of the ubiquitin-protein ligase complex SCFCdc4 required for the initiation of DNA replication.
GO:0005680 anaphase-promoting complex	IPI PMID:12477395 Proteomics analysis identifies new components of the fission...	ACCEPT	Summary: ComplexPortal-derived IPI from Yoon et al. 2002, whose TAP/DALPC purification of the S. cerevisiae APC/C recovered Apc2 together with the other core subunits and two new small subunits, giving the 13-subunit complex now curated as CPX-756. Reason: Apc2 is a constitutive core subunit of the 13-subunit APC/C: it was identified in the purified particle by mass spectrometry, co-immunoprecipitates with Cdc23, remains associated with Apc1-TAP, and forms with Apc11 and Doc1 one of the two subcomplexes bridged by Apc1. Independent proteomic confirmation of membership. Supporting Evidence: PMID:12477395 Our data increase the total number of identified APC subunits to 13 in both yeasts and indicate that previous approaches were biased against the identification of small subunits.
GO:0005680 anaphase-promoting complex	NAS PMID:11114178 Ama1p is a meiosis-specific regulator of the anaphase promot...	ACCEPT	Summary: ComplexPortal NAS row supporting the meiosis-specific APC/C-Ama1 variant (CPX-762); Cooper et al. 2000 showed that the Cdc20-family coactivator Ama1 co-immunoprecipitates with the APC/C in vivo. The paper does not assay Apc2 itself; the row asserts that the core complex, of which Apc2 is a constitutive subunit, is the ligase Ama1 activates. Reason: Apc2 is a constitutive core subunit of the 13-subunit APC/C: it was identified in the purified particle by mass spectrometry, co-immunoprecipitates with Cdc23, remains associated with Apc1-TAP, and forms with Apc11 and Doc1 one of the two subcomplexes bridged by Apc1. Apc2 is present in APC/C purified from meiotic diploid cells (Hall et al. 2003), so the complex-level statement is correct for Apc2 even though the evidence code is weak. Supporting Evidence: PMID:11114178 First, coimmunoprecipitation assays indicate that Ama1p associates with the APC/C in vivo. PMID:12609981 Both proteins were present in APC preparations from haploid cells arrested in G(1), S, and M phases and from meiotic diploid cells, indicating that they are constitutive components of the complex throughout the yeast cell cycle.
GO:0005680 anaphase-promoting complex	NAS PMID:16481473 An architectural map of the anaphase-promoting complex.	ACCEPT	Summary: ComplexPortal NAS row citing Thornton et al. 2006, who mapped APC/C architecture with Apc1-TAP purifications from strains deleted for each essential subunit: Apc2 sits with Apc11 and Doc1 in the cullin/catalytic subcomplex bound to Apc1, and apc2 deletion removes Apc11 and Doc1 from the complex. Reason: Apc2 is a constitutive core subunit of the 13-subunit APC/C: it was identified in the purified particle by mass spectrometry, co-immunoprecipitates with Cdc23, remains associated with Apc1-TAP, and forms with Apc11 and Doc1 one of the two subcomplexes bridged by Apc1. The cited paper is a direct architectural study of Apc2 within the complex. Supporting Evidence: PMID:16481473 one that contains Apc2 (Cullin), Apc11 (RING), and Doc1/Apc10, and another that contains the three TPR subunits (Cdc27, Cdc16, and Cdc23) PMID:16481473 Purifications from apc2 Δ strains, on the other hand, revealed the complete loss of Apc11 and Doc1 binding
GO:0005737 cytoplasm	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: UniProt subcellular-location mapping (SL-0086 cytoplasm) from the same genome-wide GFP localisation dataset (Huh et al. 2003), which scored Apc2-GFP in both cytoplasm and nucleus. Reason: The observation is genuine (Apc2 is detectable in the cytoplasm, and APC/C-Cdh1 acts on cytoplasmic substrates such as the actomyosin-ring component Iqg1 late in mitosis), but the core cell-cycle function on Pds1 and Clb cyclins is executed in the nucleus, and imaging of the intact complex shows a predominantly nuclear signal. Retain as a non-core location. Supporting Evidence: file:yeast/APC2/APC2-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269\|PubMed:14562095}. Nucleus {ECO:0000269\|PubMed:14562095}. file:yeast/APC2/APC2-deep-research-falcon.md Cdc23 signal was predominantly nuclear throughout the cell cycle, with one or two nuclear foci; Apc9 showed a similar but weaker pattern.
GO:0007091 metaphase/anaphase transition of mitotic cell cycle	IBA GO_REF:0000033	ACCEPT	Summary: PAINT IBA from node PTN000231994, seeded in part by the budding-yeast APC2 IGI evidence itself (SGD:S000004117). APC/C-driven destruction of securin is the ancestral trigger of the metaphase/anaphase transition across eukaryotes. Reason: Apc2 is an essential subunit of the ligase that ubiquitinates Pds1/securin; ts apc2 alleles arrest in metaphase and the arrest is bypassed by deleting PDS1. The IBA correctly reflects a conserved, ancestral function; APC2 in its own WITH/FROM is the expected marker of experimental grounding on the target. Supporting Evidence: PMID:9430641 Temperature-sensitive rsi1/apc2 mutants arrest in metaphase and are unable to degrade Clb2p, suggesting that Rsi1p/Apc2p is associated with the anaphase promoting complex (APC). PMID:9430641 Indeed, the anaphase block in rsi1/apc2 temperature-sensitive mutants is overcome by removal of PDS1, consistent with Rsi1p/Apc2p being part of the APC.
GO:0007091 metaphase/anaphase transition of mitotic cell cycle	IGI PMID:9430641 Budding yeast RSI1/APC2, a novel gene necessary for initiati...	ACCEPT	Summary: IGI with PDS1 (SGD:S000002520): Kramer et al. 1998 isolated rsi1/apc2 in a screen for mutations that make SIC1 essential, showed that temperature-sensitive rsi1/apc2 mutants arrest in metaphase with stabilised Clb2, and that deleting PDS1 (securin) allows the mutants to initiate anaphase - the canonical genetic signature of an APC/C subunit acting at the metaphase/anaphase transition. Reason: Direct genetic evidence in the gene's own organism that Apc2 is required for the transition and acts through Pds1 destruction; the epistasis with pds1 delta places Apc2 upstream of securin proteolysis, exactly as the GO term definition describes. Core function. Supporting Evidence: PMID:9430641 Temperature-sensitive rsi1/apc2 mutants arrest in metaphase and are unable to degrade Clb2p, suggesting that Rsi1p/Apc2p is associated with the anaphase promoting complex (APC). PMID:9430641 Indeed, the anaphase block in rsi1/apc2 temperature-sensitive mutants is overcome by removal of PDS1, consistent with Rsi1p/Apc2p being part of the APC. PMID:9430641 This is an E3 ubiquitin-ligase that controls anaphase initiation through degradation of Pds1p and mitotic exit via degradation of Clb cyclins.
GO:0007346 regulation of mitotic cell cycle	NAS PMID:16481473 An architectural map of the anaphase-promoting complex.	MODIFY	Summary: ComplexPortal NAS row attached to the APC/C core complex (CPX-756) citing Thornton et al. 2006. The statement is true but shallow: the APC/C does not merely modulate the mitotic cycle, it executes two irreversible transitions by ubiquitinating securin and B-type cyclins, which the paper identifies as the only obligatory APC/C targets. Reason: 'Regulation of mitotic cell cycle' is a broad grouping term; the specific processes this complex-level assertion stands for are already carried by Apc2 with experimental evidence (GO:0007091 metaphase/anaphase transition IGI; GO:0010458 exit from mitosis IGI). Re-express the row with those terms rather than keeping an uninformative ancestor; the biology is not in doubt. Proposed replacements: metaphase/anaphase transition of mitotic cell cycle exit from mitosis Supporting Evidence: PMID:16481473 Previously, we showed that the only obligatory targets of the APC for cell cycle progression are securin and the B-type cyclins PMID:9430641 This is an E3 ubiquitin-ligase that controls anaphase initiation through degradation of Pds1p and mitotic exit via degradation of Clb cyclins.
GO:0010458 exit from mitosis	IGI PMID:9430641 Budding yeast RSI1/APC2, a novel gene necessary for initiati...	ACCEPT	Summary: IGI with PDS1 (SGD:S000002520): in rsi1/apc2 ts cells Clb2 is not degraded, compromised alleles are lethal with sic1 delta (the CDK inhibitor becomes essential when Clb-kinase cannot be destroyed), and rsi1-8 pds1 delta cells that bypass the metaphase block go on to arrest in telophase, revealing a second, Pds1-independent requirement for Apc2 in mitotic exit. Reason: Exit from mitosis requires APC/C-mediated destruction of Clb2 (and Cdc20) via APC/C-Cdh1; Apc2 is part of the catalytic core of that ligase, and the genetics (Clb2 stabilisation, sic1 delta synthetic lethality, telophase arrest after PDS1 bypass) directly demonstrate the requirement. Core function. Supporting Evidence: PMID:9430641 Temperature-sensitive rsi1/apc2 mutants arrest in metaphase and are unable to degrade Clb2p, suggesting that Rsi1p/Apc2p is associated with the anaphase promoting complex (APC). PMID:9430641 In addition, like our rsi1/apc2 mutations, cdc23-1, encoding a known APC subunit, is also lethal with sic1Delta. PMID:9430641 This is an E3 ubiquitin-ligase that controls anaphase initiation through degradation of Pds1p and mitotic exit via degradation of Clb cyclins.
GO:0016567 protein ubiquitination	IDA PMID:16481473 An architectural map of the anaphase-promoting complex.	ACCEPT	Summary: Thornton et al. 2006 assayed ubiquitination of 35S-Pds1 (and 125I-cyclin B) by APC/C purified from strains lacking each essential subunit, using recombinant E1, E2 and Cdh1: complexes lacking Apc2 had no detectable activity, whereas only cdc27 delta complexes retained residual activity. Reason: Apc2 forms, with the RING subunit Apc11, the cullin-RING catalytic core of the APC/C; loss of Apc2 removes Apc11 and Doc1 from the complex and abolishes detectable ubiquitination activity, so Apc2 participates directly in the ubiquitination reaction as the scaffold that positions the RING/E2 machinery. Direct in vitro ubiquitination evidence with subunit-deleted complexes. Supporting Evidence: PMID:16481473 the resulting complexes were subjected to a substrate ubiquitination assay using recombinant E1, E2, Cdh1, and 35 S-Met-labeled Pds1 as a substrate. PMID:16481473 Of the mutant complexes, only cdc27 Δ APC displayed detectable activity against Pds1 PMID:16481473 Since Apc2 and Apc11 are thought to form the catalytic core of the APC, the enzyme should lack all activity and should be resistant to Cdh1 m11 .
GO:0016567 protein ubiquitination	IEA GO_REF:0000041	ACCEPT	Summary: UniPathway mapping (UPA00143, protein ubiquitination) from the UniProt PATHWAY line; the APC/C is an E3 ubiquitin ligase and Apc2 is its cullin subunit. Reason: Apc2 forms, with the RING subunit Apc11, the cullin-RING catalytic core of the APC/C; loss of Apc2 removes Apc11 and Doc1 from the complex and abolishes detectable ubiquitination activity, so Apc2 participates directly in the ubiquitination reaction as the scaffold that positions the RING/E2 machinery. The electronic mapping is correct, if general; the specific APC/C-dependent process is annotated separately. Supporting Evidence: file:yeast/APC2/APC2-uniprot.txt APC2 interacts directly with APC11 thereby anchoring APC11 to the core complex. PMID:16481473 The “catalytic core” subcomplex includes Apc2 and Apc11, the Cullin and RING-finger subunits that characterize the APC as a member of the multisubunit cullin-RING family of ubiquitin ligases.
GO:0016567 protein ubiquitination	IMP PMID:16481473 An architectural map of the anaphase-promoting complex.	ACCEPT	Summary: SGD IMP from the apc2 delta strain (viable only in the pds1 delta clb5 delta SIC1-10X background): APC/C purified from apc2 delta cells lacks ubiquitination activity, loses Apc11 and Doc1, and apc2 delta cells are resistant to the lethality of hyperactive GAL-CDH1-m11, consistent with an enzyme lacking its catalytic core. Reason: Apc2 forms, with the RING subunit Apc11, the cullin-RING catalytic core of the APC/C; loss of Apc2 removes Apc11 and Doc1 from the complex and abolishes detectable ubiquitination activity, so Apc2 participates directly in the ubiquitination reaction as the scaffold that positions the RING/E2 machinery. Mutant-phenotype evidence in the gene's own organism. Supporting Evidence: PMID:16481473 Purifications from apc2 Δ strains, on the other hand, revealed the complete loss of Apc11 and Doc1 binding PMID:16481473 Since Apc2 and Apc11 are thought to form the catalytic core of the APC, the enzyme should lack all activity and should be resistant to Cdh1 m11 .
GO:0016567 protein ubiquitination	NAS PMID:11114178 Ama1p is a meiosis-specific regulator of the anaphase promot...	ACCEPT	Summary: ComplexPortal NAS for the APC/C-Ama1 variant: Cooper et al. 2000 showed that ectopic Ama1 stimulates ubiquitination of Clb1 in vitro and its degradation in vivo, i.e. the Apc2-containing core complex is the ubiquitin ligase that the meiotic coactivator directs. Reason: Apc2 forms, with the RING subunit Apc11, the cullin-RING catalytic core of the APC/C; loss of Apc2 removes Apc11 and Doc1 from the complex and abolishes detectable ubiquitination activity, so Apc2 participates directly in the ubiquitination reaction as the scaffold that positions the RING/E2 machinery. The complex-level statement is correct for Apc2 as a constitutive core subunit, although the paper does not assay Apc2 itself. Supporting Evidence: PMID:11114178 Here we describe the yeast gene AMA1, a new member of the Cdc20 protein family that regulates the multisubunit ubiquitin ligase termed the anaphase promoting complex/cyclosome (APC/C). PMID:11114178 Second, Ama1p is required for the degradation of the B-type cyclin Clb1p, an APC/C substrate in both meiotic and mitotic cells.
GO:0016567 protein ubiquitination	NAS PMID:16481473 An architectural map of the anaphase-promoting complex.	ACCEPT	Summary: ComplexPortal NAS row for the core APC/C (CPX-756) citing the architectural map, which characterises the complex as a 13-subunit cullin-RING ubiquitin ligase with Apc2 and Apc11 as its catalytic core. Reason: Apc2 forms, with the RING subunit Apc11, the cullin-RING catalytic core of the APC/C; loss of Apc2 removes Apc11 and Doc1 from the complex and abolishes detectable ubiquitination activity, so Apc2 participates directly in the ubiquitination reaction as the scaffold that positions the RING/E2 machinery. Duplicates the IDA/IMP rows from the same paper; harmless. Supporting Evidence: PMID:16481473 The anaphase-promoting complex or cyclosome (APC) is an unusually complicated ubiquitin ligase, composed of 13 core subunits and either of two loosely associated regulatory subunits, Cdc20 and Cdh1. PMID:16481473 The “catalytic core” subcomplex includes Apc2 and Apc11, the Cullin and RING-finger subunits that characterize the APC as a member of the multisubunit cullin-RING family of ubiquitin ligases.
GO:0031145 anaphase-promoting complex-dependent catabolic process	IDA PMID:16481473 An architectural map of the anaphase-promoting complex.	ACCEPT	Summary: Direct assay: Cdh1-dependent ubiquitination of Pds1 and cyclin B by purified APC/C requires Apc2 (apc2 delta complexes are inactive), and the paper frames securin and the B-type cyclins as the only obligatory APC/C targets for cell-cycle progression. Reason: GO:0031145 is the precise process term for what the Apc2-containing ligase does: ubiquitination by the APC/C followed by proteasomal destruction of securin and B-type cyclins. Apc2 does the work as the cullin scaffold of the catalytic core, so 'involved_in' is appropriate. In vitro reconstitution with subunit-deleted complexes. Supporting Evidence: PMID:16481473 Of the mutant complexes, only cdc27 Δ APC displayed detectable activity against Pds1 PMID:16481473 Previously, we showed that the only obligatory targets of the APC for cell cycle progression are securin and the B-type cyclins
GO:0031145 anaphase-promoting complex-dependent catabolic process	IMP PMID:16481473 An architectural map of the anaphase-promoting complex.	ACCEPT	Summary: IMP from apc2 delta in the APC-nonessential background: the deletion removes Apc11 and Doc1 from the complex, abolishes activity, and renders cells resistant to hyperactive Cdh1, whereas cdc27 delta cells retain residual APC/C activity and lower Clb2/Cdc20 levels. Reason: GO:0031145 is the precise process term for what the Apc2-containing ligase does: ubiquitination by the APC/C followed by proteasomal destruction of securin and B-type cyclins. Apc2 does the work as the cullin scaffold of the catalytic core, so 'involved_in' is appropriate. Mutant phenotype in vivo. Supporting Evidence: PMID:16481473 Purifications from apc2 Δ strains, on the other hand, revealed the complete loss of Apc11 and Doc1 binding PMID:16481473 We also observed that total Clb2 and Cdc20 levels were lower in cdc27 Δ strains than in any other apc Δ strains
GO:0031145 anaphase-promoting complex-dependent catabolic process	IMP PMID:9430641 Budding yeast RSI1/APC2, a novel gene necessary for initiati...	ACCEPT	Summary: IMP from the original rsi1/apc2 ts alleles, which fail to degrade Clb2 and arrest in metaphase; the block is relieved by removing the APC/C substrate Pds1, and Rsi1/Apc2 co-immunoprecipitates with Cdc23. Reason: GO:0031145 is the precise process term for what the Apc2-containing ligase does: ubiquitination by the APC/C followed by proteasomal destruction of securin and B-type cyclins. Apc2 does the work as the cullin scaffold of the catalytic core, so 'involved_in' is appropriate. The founding genetic evidence for Apc2-dependent APC/C proteolysis. Supporting Evidence: PMID:9430641 Temperature-sensitive rsi1/apc2 mutants arrest in metaphase and are unable to degrade Clb2p, suggesting that Rsi1p/Apc2p is associated with the anaphase promoting complex (APC). PMID:9430641 Indeed, the anaphase block in rsi1/apc2 temperature-sensitive mutants is overcome by removal of PDS1, consistent with Rsi1p/Apc2p being part of the APC. PMID:9430641 Finally, we find that Rsi1p/Apc2p co-immunoprecipitates with Cdc23p.
GO:0031145 anaphase-promoting complex-dependent catabolic process	NAS PMID:11114178 Ama1p is a meiosis-specific regulator of the anaphase promot...	ACCEPT	Summary: ComplexPortal NAS for the APC/C-Ama1 variant: Ama1 is required for degradation of Clb1 in meiosis and its overexpression stimulates Clb1 ubiquitination in vitro, i.e. the Apc2-containing core executes APC/C-dependent proteolysis under meiotic coactivator control. Reason: GO:0031145 is the precise process term for what the Apc2-containing ligase does: ubiquitination by the APC/C followed by proteasomal destruction of securin and B-type cyclins. Apc2 does the work as the cullin scaffold of the catalytic core, so 'involved_in' is appropriate. Complex-level inference; Apc2 is present in meiotic APC/C preparations. Supporting Evidence: PMID:11114178 Second, Ama1p is required for the degradation of the B-type cyclin Clb1p, an APC/C substrate in both meiotic and mitotic cells. PMID:12609981 Both proteins were present in APC preparations from haploid cells arrested in G(1), S, and M phases and from meiotic diploid cells, indicating that they are constitutive components of the complex throughout the yeast cell cycle.
GO:0031145 anaphase-promoting complex-dependent catabolic process	NAS PMID:16481473 An architectural map of the anaphase-promoting complex.	ACCEPT	Summary: ComplexPortal NAS for the core APC/C (CPX-756) citing Thornton et al. 2006; duplicates the IDA and IMP rows from the same paper. Reason: GO:0031145 is the precise process term for what the Apc2-containing ligase does: ubiquitination by the APC/C followed by proteasomal destruction of securin and B-type cyclins. Apc2 does the work as the cullin scaffold of the catalytic core, so 'involved_in' is appropriate. Redundant with the experimental rows but correct. Supporting Evidence: PMID:16481473 Previously, we showed that the only obligatory targets of the APC for cell cycle progression are securin and the B-type cyclins PMID:16481473 Of the mutant complexes, only cdc27 Δ APC displayed detectable activity against Pds1
GO:0051445 regulation of meiotic cell cycle	NAS PMID:11114178 Ama1p is a meiosis-specific regulator of the anaphase promot...	KEEP AS NON CORE	Summary: ComplexPortal NAS attached to the meiosis-specific APC/C-Ama1 variant (CPX-762). Cooper et al. 2000 showed that Ama1 directs an APC/C required for meiosis I and spore-wall assembly; Apc2 is a constitutive core subunit present in APC/C from meiotic cells, but no Apc2-specific meiotic phenotype has been examined. Reason: The meiotic APC/C-Ama1 uses the same Apc2-Apc11 catalytic core, so the assertion is biologically reasonable for Apc2, but it is a coactivator-defined, developmental-stage context inferred at the complex level with a weak evidence code, and 'regulation of meiotic cell cycle' is a broad grouping term. Keep as non-core; the core role of Apc2 is the mitotic ligase function. Supporting Evidence: PMID:11114178 In conclusion, this study indicates that Ama1p directs a meiotic APC/C that functions solely outside mitotic cell division. PMID:12609981 Both proteins were present in APC preparations from haploid cells arrested in G(1), S, and M phases and from meiotic diploid cells, indicating that they are constitutive components of the complex throughout the yeast cell cycle.
GO:0061630 ubiquitin protein ligase activity	IMP PMID:16481473 An architectural map of the anaphase-promoting complex.	ACCEPT	Summary: SGD IMP with contributes_to: APC/C purified from apc2 delta strains has no detectable ubiquitin ligase activity toward Pds1, and apc2 delta cells resist hyperactive Cdh1; Apc2 and Apc11 are the cullin and RING subunits that constitute the catalytic core. Reason: The contributes_to qualifier is exactly right: ubiquitin ligase activity is a property of the Apc2-Apc11 module within the whole complex, Apc11 supplies the RING that activates the E2, and Apc2 supplies the cullin scaffold that anchors Apc11 and Doc1 and positions the E2 over coactivator-bound substrate. Apc11 alone can mediate ubiquitin transfer in a minimal in vitro system (Leverson et al. 2000), which is why Apc2 contributes to rather than enables the activity. Supporting Evidence: PMID:16481473 Since Apc2 and Apc11 are thought to form the catalytic core of the APC, the enzyme should lack all activity and should be resistant to Cdh1 m11 . PMID:16481473 Of the mutant complexes, only cdc27 Δ APC displayed detectable activity against Pds1 PMID:10888670 the results presented in Figure 5 demonstrate that Apc11p alone is capable of efficiently mediating ubiquitin transfer. PMID:10888670 While Apc2p was not required to effect ubiquitin transfer in vitro, it may function in a cellular context to tether Apc11p to APC core proteins, and to properly position the Apc11p RING-H2 finger with respect to its substrates.
GO:0070979 protein K11-linked ubiquitination	IBA GO_REF:0000033	MODIFY	Summary: PAINT IBA from node PTN000231994 whose only experimental donor for this term is human ANAPC2 (UniProtKB:Q9UJX6). K11-linked chain assembly by the human APC/C depends on the chain-elongating E2 UBE2S, which has no ortholog in S. cerevisiae; the budding-yeast APC/C instead uses Ubc4 to initiate and Ubc1 to elongate predominantly K48-linked chains (Rodrigo-Brenni and Morgan 2007, as summarised by Williamson et al. 2009). Reason: The IBD placement propagates a metazoan, UBE2S-dependent linkage specificity to the whole ANAPC2 family, but there is target-specific evidence of divergence: yeast lacks Ube2S and its APC/C-Ubc4/Ubc1 system builds K48-linked chains. The ancestral, lineage-independent claim is that Apc2-containing APC/C assembles polyubiquitin chains that target substrates to the proteasome; the linkage supported in this organism is K48. Re-express as protein K48-linked ubiquitination (GO:0070936), with protein polyubiquitination (GO:0000209) as the safe linkage-agnostic term, and suggest that the K11 IBD be re-placed at the node where UBE2S-dependent chain building arose. Propagation Review Root cause: PROPAGATION BAD Failure modes: FUNCTIONAL DIVERGENCE LINEAGE OR TAXON MISMATCH Sources checked: PANTHER:PTN000231994 SUPPORTS SOURCE BUT NOT TARGET IBD node in PTHR45957 carrying GO:0070979 on the strength of human ANAPC2 K11 evidence; the linkage specificity depends on UBE2S, which fungi lack, so the node is placed too deep for this term. UniProtKB:Q9UJX6 · ANAPC2 SUPPORTS SOURCE BUT NOT TARGET Human ANAPC2 has direct IDA evidence for K11-linked chains built by UBE2C/UBE2S; the yeast APC/C uses Ubc4/Ubc1 and assembles K48-linked chains. Proposed replacements: protein K48-linked ubiquitination protein polyubiquitination Supporting Evidence: PMID:19822757 The cooperation between Ube2S and UbcH10 is reminiscent of yeast APC/C, which uses a chain-initiating E2, Ubc4, and a chain-elongating E2, Ubc1 PMID:19822757 However, Ubc4 and Ubc1 function sequentially to assemble K48-linked ubiquitin chains, whereas human UbcH10 and Ube2S most likely bind APC/C at the same time.
GO:1903473 positive regulation of mitotic actomyosin contractile ring contraction	IMP PMID:19109423 The anaphase-promoting complex promotes actomyosin-ring disa...	MODIFY	Summary: SGD IMP from Tully et al. 2009: in the APC-nonessential background, apc2 delta cells leave persistent Myo1 patches for at least 10 min after the end of actomyosin-ring contraction, phenocopying cdh1 delta, in which ring contraction proceeds at a normal rate but ring constituents (Myo1, Iqg1) are not disassembled during or after contraction. Reason: The cited data concern disassembly of the ring after contraction, and the paper states explicitly that contraction itself is normal without APC/C-Cdh1; 'positive regulation of ring contraction' therefore misstates the phenotype. As for the matching CDH1 rows, GO has no dedicated mitotic actomyosin-ring disassembly term, so re-express under actomyosin contractile ring organization (GO:0044837), which explicitly covers disassembly. This is a genuine but non-core, late-mitotic output of APC/C-Cdh1 substrate turnover (Iqg1). Proposed replacements: actomyosin contractile ring organization Supporting Evidence: PMID:19109423 In the apc2 Δ strain, Myo1 patches persisted for ≥10 min after the end of ring contraction (Supplemental Figure S3B), supporting the hypothesis that the APC, with its activator Cdh1, is required for proper disassembly of Myo1-containing structures after actomyosin-ring contraction. PMID:19109423 In cells lacking the APC activator Cdh1, the actomyosin ring contracts at a normal rate, but ring constituents are not disassembled normally during or after contraction.
GO:0160072 ubiquitin ligase complex scaffold activity	IDA PMID:16481473 An architectural map of the anaphase-promoting complex.	NEW	Summary: Proposed annotation capturing the characterised molecular role of Apc2 that the generic protein-binding rows fail to express. Thornton et al. 2006 showed with subunit-deleted Apc1-TAP purifications that Apc2 independently tethers the RING ligase subunit Apc11 and the substrate co-receptor Doc1/Apc10 to the complex (apc2 delta loses both; apc11 delta only partially reduces Apc2 and Doc1), and that Apc2 is required for efficient binding of the substrate adaptor Cdh1. Leverson et al. 2000 had proposed exactly this tethering/positioning role after finding that Apc11 alone can transfer ubiquitin in vitro. Reason: GO:0160072 is defined as the binding activity that brings together a ubiquitin ligase and a ubiquitin ligase-substrate adaptor so that they function in a coordinated way, which is precisely what the cullin-family Apc2 does within the APC/C: it holds the Apc11 RING and the degron co-receptor Doc1 and contributes to coactivator (Cdh1) binding, positioning the E2-charged RING over receptor-bound substrate. The same term was adopted for the human ortholog ANAPC2 in this repository; the yeast evidence is direct (co-purification dependencies in the gene's own organism), so IDA rather than IC is proposed. This is a molecular-function refinement, not a new process claim. Supporting Evidence: PMID:16481473 Purifications from apc2 Δ strains, on the other hand, revealed the complete loss of Apc11 and Doc1 binding PMID:16481473 These data suggest that Apc2 independently tethers Doc1 and Apc11. PMID:16481473 These data suggest that Apc2 is required for efficient Cdh1 binding to the APC. PMID:10888670 While Apc2p was not required to effect ubiquitin transfer in vitro, it may function in a cellular context to tether Apc11p to APC core proteins, and to properly position the Apc11p RING-H2 finger with respect to its substrates. file:yeast/APC2/APC2-uniprot.txt APC2 interacts directly with APC11 thereby anchoring APC11 to the core complex.

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