ACIN1 encodes Acinus, a predominantly nuclear RNA-binding protein in the RNPS1-SAP18-Acinus ASAP complex and peripheral exon-junction-complex machinery. It regulates pre-mRNA splicing, including intron and exon selection, and occupies nucleoplasm and nuclear speckles. Caspase-generated Acinus fragments can promote apoptotic chromatin condensation in experimental systems, and phosphorylation regulates their production. Acinus dependence of nuclear remodeling varies between models; its RNA-processing activity also affects transcripts such as DFFA/ICAD.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0008380 RNA splicing | IBA GO_REF:0000033 | ACCEPT | Summary: RNA splicing is a core ACIN1 process. Reason: ACIN1 is an ASAP/EJC-associated splicing factor and participates in spliceosome-linked RNA processing. Direct human iCLIP and depletion RNA-seq evidence (PMID:27365209) shows Acinus binds pre-mRNAs and spliced mRNAs and is required for inclusion of specific alternative cassette exons and faithful splicing of a subset of introns, supporting a direct role in exon/intron definition. Supporting Evidence: PMID:16314458 identified two novel EJC components, Acinus and SAP18 PMID:16314458 Acinus binds directly to another EJC component, RNPS1 file:human/ACIN1/ACIN1-uniprot.txt Auxiliary component of the splicing-dependent multiprotein exon junction complex PMID:22388736 transcriptional regulation, pre-mRNA splicing and mRNA quality control |
| GO:0061574 ASAP complex | IBA GO_REF:0000033 | ACCEPT | Summary: ASAP complex membership is a core ACIN1 cellular-component annotation. Reason: ACIN1 is a defining Acinus subunit of the RNPS1-SAP18-ACIN1 ASAP complex; this captures the specific complex context better than generic protein binding. Supporting Evidence: PMID:12665594 ASAP complexes are composed of the polypeptides SAP18 and RNPS1 and different isoforms of the Acinus protein PMID:20966198 RNPS1, Acinus, and SAP18 form the apoptosis- and splicing-associated protein (ASAP) complex PMID:16314458 identified two novel EJC components, Acinus and SAP18 PMID:16314458 Acinus binds directly to another EJC component, RNPS1 |
| GO:0003676 nucleic acid binding | IEA GO_REF:0000002 | MODIFY | Summary: Nucleic acid binding is too broad for the reviewed ACIN1 evidence. Reason: The specific supported molecular function is RNA binding in the ASAP/EJC splicing context, not generic nucleic acid binding. Proposed replacements: RNA binding Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt Component of the ASAP complexes which bind RNA PMID:22388736 both RNA- and protein-binding properties file:human/ACIN1/ACIN1-uniprot.txt Auxiliary component of the splicing-dependent multiprotein exon junction complex PMID:22388736 transcriptional regulation, pre-mRNA splicing and mRNA quality control |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: nucleus is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005654 nucleoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: nucleoplasm is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0016607 nuclear speck | IEA GO_REF:0000044 | ACCEPT | Summary: nuclear speck is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0031981 nuclear lumen | IEA GO_REF:0000117 | MODIFY | Summary: The nuclear-lumen location is correct but can be refined to demonstrated nuclear compartments. Reason: Nucleoplasm and nuclear speckles are supported for Acinus and already represented in this review. Refine the broad lumen term to both supported locations. Proposed replacements: nucleoplasm nuclear speck Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005515 protein binding | IPI PMID:17332742 Composition and three-dimensional EM structure of double aff... | REMOVE | Summary: The SF3A2 interaction does not define a separate ACIN1 molecular function. Reason: The source places ACIN1 near SF3A2 in purified prespliceosomal A complexes. This fits the reviewed spliceosome/EJC context, but the generic GO:0005515 term adds no molecular-function information and the abstract-only local record does not resolve a sharper ACIN1 activity. |
| GO:0005515 protein binding | IPI PMID:20195357 A comprehensive resource of interacting protein regions for ... | REMOVE | Summary: The PCBD1 interaction does not define a separate ACIN1 molecular function. Reason: This high-throughput mRNA-display interaction-region resource supports an ACIN1-PCBD1 edge at most. The interaction does not map to ACIN1's established RNA-binding, ASAP-complex or apoptotic-chromatin-condensation activities, so only the uninformative generic binding term is removed. |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | REMOVE | Summary: The SRPK2 interaction does not define a separate ACIN1 molecular function. Reason: The source is a human spliceosomal protein-interaction matrix. The SRPK2 edge is plausible regulatory context, but this row does not identify a specific ACIN1 molecular function; ACIN1's reviewed functions remain RNA binding, ASAP/EJC splicing and apoptotic chromatin condensation. |
| GO:0005515 protein binding | IPI PMID:23602568 The protein interaction landscape of the human CMGC kinase g... | REMOVE | Summary: The SRPK2 interaction does not define a separate ACIN1 molecular function. Reason: The CMGC-kinase interactome row supports an SRPK2 association, but ACIN1 is the regulated substrate rather than the kinase. The paper does not support replacing generic binding with a more informative ACIN1 molecular function. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: The PNN interaction does not define a separate ACIN1 molecular function. Reason: BioPlex 2.0 provides AP-MS co-complex information. Pinin is useful PSAP/EJC-neighborhood context, but this broad interactome row does not establish a specific ACIN1 activity. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: The PNN interaction does not define a separate ACIN1 molecular function. Reason: The nuclear crosslinking-MS source supports chromatin-proximal interaction context. It does not show a distinct ACIN1 molecular function, so the generic PNN binding row is not retained. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The SRPK2 interaction does not define a separate ACIN1 molecular function. Reason: BioPlex AP-MS can support an SRPK2 co-association, but the interaction row is still only a proteome-scale protein edge. It does not license a distinct ACIN1 activity beyond the accepted RNA-processing and apoptosis functions. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: The SF3A2 interaction does not define a separate ACIN1 molecular function. Reason: OpenCell reports a broad endogenous-tagging and interaction cartography dataset. The SF3A2 edge is compatible with ACIN1 nuclear splicing biology, but does not establish a specific ACIN1 molecular function beyond existing RNA-binding and ASAP/EJC splicing annotations. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: The SRPK2 interaction does not define a separate ACIN1 molecular function. Reason: The U2OS multimodal cell-map source provides large-scale AP-MS and imaging context. The SRPK2 edge is not a specific ACIN1 molecular function and should not be promoted to a binding activity. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: nucleoplasm is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005634 nucleus | IDA PMID:12665594 ASAP, a novel protein complex involved in RNA processing and... | ACCEPT | Summary: nucleus is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0043065 positive regulation of apoptotic process | IDA PMID:12665594 ASAP, a novel protein complex involved in RNA processing and... | KEEP AS NON CORE | Summary: Positive regulation of apoptotic process is supported for ACIN1/ASAP. Reason: ASAP complex microinjection accelerates cell death, and ACIN1 is a caspase-activated apoptosis-associated factor. ACIN1 additionally couples its splicing activity to apoptosis by regulating splicing of the DFFA/ICAD transcript, a major regulator of apoptotic DNA fragmentation (PMID:27365209); caspase-3 cleavage of ACIN1 is restrained by the API5/AAC-11 interaction (PMID:38275765, review). This is a context-dependent prodeath effect alongside the constitutive RNA-processing role; Acinus depletion does not universally prevent apoptotic chromatin condensation (PMID:16537548). Supporting Evidence: PMID:12665594 microinjection of ASAP complexes into mammalian cells resulted in acceleration of cell death PMID:12665594 after induction of apoptosis the ASAP complex disassembles PMID:10490026 induces apoptotic chromatin condensation after cleavage by caspase-3 PMID:10490026 essential for apoptotic chromatin condensation in vitro |
| GO:0050684 regulation of mRNA processing | IDA PMID:12665594 ASAP, a novel protein complex involved in RNA processing and... | MODIFY | Summary: Regulation of mRNA processing is sound but can be made more specific. Reason: ASAP complexes inhibit RNA processing in vitro splicing reactions; UniProt already represents this as negative regulation of mRNA splicing via spliceosome. Proposed replacements: negative regulation of mRNA splicing, via spliceosome Supporting Evidence: PMID:12665594 Addition of ASAP isoforms to in vitro splicing reactions inhibits RNA processing file:human/ACIN1/ACIN1-uniprot.txt The ASAP complex can inhibit RNA processing during in vitro splicing reactions PMID:12665594 ASAP complexes are composed of the polypeptides SAP18 and RNPS1 and different isoforms of the Acinus protein PMID:20966198 RNPS1, Acinus, and SAP18 form the apoptosis- and splicing-associated protein (ASAP) complex |
| GO:0061574 ASAP complex | IPI PMID:12665594 ASAP, a novel protein complex involved in RNA processing and... | ACCEPT | Summary: ASAP complex membership is a core ACIN1 cellular-component annotation. Reason: ACIN1 is a defining Acinus subunit of the RNPS1-SAP18-ACIN1 ASAP complex; this captures the specific complex context better than generic protein binding. Supporting Evidence: PMID:12665594 ASAP complexes are composed of the polypeptides SAP18 and RNPS1 and different isoforms of the Acinus protein PMID:20966198 RNPS1, Acinus, and SAP18 form the apoptosis- and splicing-associated protein (ASAP) complex PMID:16314458 identified two novel EJC components, Acinus and SAP18 PMID:16314458 Acinus binds directly to another EJC component, RNPS1 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770131 | ACCEPT | Summary: nucleoplasm is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770141 | ACCEPT | Summary: nucleoplasm is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770142 | ACCEPT | Summary: nucleoplasm is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770145 | ACCEPT | Summary: nucleoplasm is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770236 | ACCEPT | Summary: nucleoplasm is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770847 | ACCEPT | Summary: nucleoplasm is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9794542 | ACCEPT | Summary: nucleoplasm is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | ACCEPT | Summary: RNA binding is consistent with ACIN1/ASAP complex function. Reason: ACIN1 confers RNA-binding to the ASAP complex and is supported by RNA-binding proteome datasets, so the HDA RNA-binding rows are appropriate. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt Component of the ASAP complexes which bind RNA PMID:22388736 both RNA- and protein-binding properties PMID:12665594 ASAP complexes are composed of the polypeptides SAP18 and RNPS1 and different isoforms of the Acinus protein PMID:20966198 RNPS1, Acinus, and SAP18 form the apoptosis- and splicing-associated protein (ASAP) complex |
| GO:0003723 RNA binding | HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ... | ACCEPT | Summary: RNA binding is consistent with ACIN1/ASAP complex function. Reason: ACIN1 confers RNA-binding to the ASAP complex and is supported by RNA-binding proteome datasets, so the HDA RNA-binding rows are appropriate. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt Component of the ASAP complexes which bind RNA PMID:22388736 both RNA- and protein-binding properties PMID:12665594 ASAP complexes are composed of the polypeptides SAP18 and RNPS1 and different isoforms of the Acinus protein PMID:20966198 RNPS1, Acinus, and SAP18 form the apoptosis- and splicing-associated protein (ASAP) complex |
| GO:0061574 ASAP complex | IDA PMID:12665594 ASAP, a novel protein complex involved in RNA processing and... | ACCEPT | Summary: ASAP complex membership is a core ACIN1 cellular-component annotation. Reason: ACIN1 is a defining Acinus subunit of the RNPS1-SAP18-ACIN1 ASAP complex; this captures the specific complex context better than generic protein binding. Supporting Evidence: PMID:12665594 ASAP complexes are composed of the polypeptides SAP18 and RNPS1 and different isoforms of the Acinus protein PMID:20966198 RNPS1, Acinus, and SAP18 form the apoptosis- and splicing-associated protein (ASAP) complex PMID:16314458 identified two novel EJC components, Acinus and SAP18 PMID:16314458 Acinus binds directly to another EJC component, RNPS1 |
| GO:0016607 nuclear speck | IDA PMID:20966198 Human SAP18 mediates assembly of a splicing regulatory multi... | ACCEPT | Summary: nuclear speck is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005829 cytosol | TAS Reactome:R-HSA-201630 | UNDECIDED | Summary: The source-model cytosolic Acinus pool remains unresolved. Reason: Reactome R-HSA-201630 describes caspase-mediated Acinus cleavage but the cached reaction summary does not resolve localization of the reaction participants. Strong nuclear localization does not disprove a transient cytosolic pool. The original full paper remains inaccessible, so the prior over-annotation judgment based only on predominantly nuclear localization is not sustained. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0005515 protein binding | IPI PMID:18951082 Death by splicing: tumor suppressor RBM5 freezes splice-site... | REMOVE | Summary: The RBM5 interaction does not define a separate ACIN1 molecular function. Reason: The local RBM5 source is an abstract-only commentary on Fas pre-mRNA splice-site pairing. Retain uncertainty about the exact curated edge rather than calling it false, but remove the generic binding term because it does not define an ACIN1 function. |
| GO:0003676 nucleic acid binding | NAS PMID:10490026 Acinus is a caspase-3-activated protein required for apoptot... | MODIFY | Summary: Nucleic acid binding is too broad for the reviewed ACIN1 evidence. Reason: The specific supported molecular function is RNA binding in the ASAP/EJC splicing context, not generic nucleic acid binding. Proposed replacements: RNA binding Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt Component of the ASAP complexes which bind RNA PMID:22388736 both RNA- and protein-binding properties file:human/ACIN1/ACIN1-uniprot.txt Auxiliary component of the splicing-dependent multiprotein exon junction complex PMID:22388736 transcriptional regulation, pre-mRNA splicing and mRNA quality control |
| GO:0005634 nucleus | IDA PMID:10490026 Acinus is a caspase-3-activated protein required for apoptot... | ACCEPT | Summary: nucleus is a supported ACIN1 nuclear localization. Reason: ACIN1 localizes to nucleus, nucleoplasm, and nuclear speckles, matching its ASAP/EJC splicing regulatory role. Supporting Evidence: file:human/ACIN1/ACIN1-uniprot.txt SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. PMID:20966198 nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus |
| GO:0016887 ATP hydrolysis activity | NAS PMID:10490026 Acinus is a caspase-3-activated protein required for apoptot... | UNDECIDED | Summary: The original non-traceable author statement cannot be resolved from the accessible source. Reason: Live GO defines ATP hydrolysis as catalytic ATP-to-ADP/phosphate conversion. The accessible original Acinus abstract and publisher figure previews establish caspase-dependent condensation but do not resolve an ATP-hydrolysis assay. Its full text remains restricted. Absence of an ATPase claim from later summaries does not demonstrate that the NAS assertion is false. Supporting Evidence: |
| GO:0019899 enzyme binding | NAS PMID:10490026 Acinus is a caspase-3-activated protein required for apoptot... | UNDECIDED | Summary: The original non-traceable author statement cannot be resolved from the accessible source. Reason: Live GO defines enzyme binding simply as binding an enzyme; it is not covered by the special bare-protein-binding removal policy. Caspase cleavage establishes a substrate relationship, but the accessible original abstract and figure previews do not resolve the specific enzyme-binding observation. The full source remains restricted, so the previous confident removal is replaced with uncertainty. Supporting Evidence: |
| GO:0030218 erythrocyte differentiation | IEP PMID:11208865 Caspase activation is required for terminal erythroid differ... | KEEP AS NON CORE | Summary: Erythrocyte differentiation is a non-core caspase-substrate context for ACIN1. Reason: Human erythroid differentiation involves transient caspase activation and Acinus cleavage, but the annotation reflects a broader differentiation program rather than ACIN1's core RNA-processing/apoptotic-chromatin-condensation function. Supporting Evidence: PMID:11208865 cleave proteins involved in nucleus integrity (lamin B) and chromatin condensation (acinus)without inducing cell death PMID:11208865 normal erythroid differentiation requires the transient activation of several caspases |
| GO:0030263 apoptotic chromosome condensation | IDA PMID:10490026 Acinus is a caspase-3-activated protein required for apoptot... | KEEP AS NON CORE | Summary: Cleaved Acinus promotes chromatin condensation in defined systems, but is not universally required. Reason: PMID:10490026 reports recombinant-factor, immunodepletion and antisense evidence for Acinus-dependent condensation. Full PMID:16177823 shows phosphorylation-dependent cleavage and condensation phenotypes in HEK293/PC12 systems. In contrast, PMID:16537548 reports that inducible Acinus knockdown did not block condensation in intact cells or cell-free assays, while DNA fragmentation was impaired. Retain the experimental process as contextual; neither a universal requirement nor rejection of the original phenotype follows. RNA binding is not established as the molecular mechanism of condensation. Supporting Evidence: PMID:10490026 induces apoptotic chromatin condensation after cleavage by caspase-3 PMID:10490026 essential for apoptotic chromatin condensation in vitro PMID:16177823 Acinus S422, 573D, a mutant mimicking phosphorylation, resists against apoptotic cleavage and prevents chromatin condensation. PMID:16537548 down-regulation of Acinus did not inhibit apoptotic chromatin condensation either in intact cells or in a cell-free system. |
| GO:0045657 positive regulation of monocyte differentiation | IEP PMID:12393560 Specific involvement of caspases in the differentiation of m... | KEEP AS NON CORE | Summary: Positive regulation of monocyte differentiation is a non-core caspase-substrate context for ACIN1. Reason: The evidence shows Acinus cleavage during caspase-dependent monocyte-to-macrophage differentiation, but this is secondary to the core ACIN1 functions reviewed here. Supporting Evidence: PMID:12393560 leads to the cleavage of the protein acinus PMID:12393560 caspase activation specifically contributes to the differentiation of monocytes into macrophages |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | REMOVE | Summary: The RNPS1 interaction does not define a separate ACIN1 molecular function. Reason: The source reports a large human spliceosomal Y2H/co-immunoprecipitation matrix. The RNPS1 interaction is already represented by accepted ASAP-complex membership, so this duplicate generic binding row adds no separate molecular function. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The RNPS1 interaction does not define a separate ACIN1 molecular function. Reason: BioPlex AP-MS can support RNPS1 co-association, but the informative RNPS1 relationship is ACIN1's membership in the RNPS1-SAP18-ACIN1 ASAP complex. No separate generic binding term is needed. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The PNN interaction does not define a separate ACIN1 molecular function. Reason: BioPlex AP-MS can support a PNN co-association in the RNPS1/SAP18/PSAP neighborhood, but it does not establish a molecular function for ACIN1 more specific than protein binding. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: The RNPS1 interaction does not define a separate ACIN1 molecular function. Reason: The U2OS multimodal cell-map source supplies a large-scale RNPS1 interaction edge. ASAP-complex membership already captures the functional complex context, so the generic protein-binding row is removed. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: The PNN interaction does not define a separate ACIN1 molecular function. Reason: The U2OS multimodal cell-map source contributes a large-scale AP-MS edge for PNN. That is useful interactome context but not an ACIN1-specific activity term. |
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Download this section (compressed HTML)Q: Does human ACIN1 retain the Drosophila Acinus basal-autophagy/autophagosome-maturation role suggested by the PN context, or is that function lineage- or tissue-specific?
Suggested experts: GO autophagy editors, Drosophila autophagy experts, human RNA-processing curators
Q: Should broad ACIN1 protein-binding interaction rows be replaced by more specific complex membership and RNA-binding/splicing annotations?
Suggested experts: GO molecular-function editors, ComplexPortal curators
Q: Does ACIN1-dependent splicing of DFFA/ICAD constitute a direct regulatory link between its RNA-processing and apoptosis functions that warrants a distinct annotation (e.g., regulation of an apoptosis-related splicing target)?
Suggested experts: GO apoptosis editors, human RNA-processing curators
Experiment: Test basal autophagic flux, autophagosome maturation, and lysosomal cargo clearance in human ACIN1 knockout/rescue cells using endogenous ACIN1 isoforms and Drosophila-aligned phosphorylation/caspase-site mutants.
Hypothesis: The Drosophila Acinus basal-autophagy function is conserved in human ACIN1 only under specific stress, neuronal, or proteotoxic contexts.
Type: cell biology/autophagy flux assay
Experiment: Map ACIN1-dependent RNA targets and splicing changes after ACIN1 depletion, with rescue by ASAP-complex-binding mutants, and compare them with apoptosis/autophagy pathway transcripts.
Hypothesis: ACIN1 affects proteostasis-related phenotypes indirectly through ASAP/EJC-mediated RNA processing rather than as a direct autophagy machinery component.
Type: RNA-seq/splicing reporter
Experiment: Quantify DFFA/ICAD intron retention and functional ICAD/CAD output in ACIN1-depleted cells versus cells rescued with RNA-binding-competent ACIN1, and assay downstream apoptotic DNA fragmentation, including under API5 overexpression that blocks caspase-3 cleavage of ACIN1.
Hypothesis: ACIN1 couples its splicing activity to apoptotic DNA fragmentation via DFFA/ICAD splicing, and this axis is modulated by API5-dependent protection of ACIN1 from caspase-3 cleavage.
Type: splicing reporter/apoptosis DNA-fragmentation assay
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