C1QBP (p32/gC1qR) is an acidic, predominantly mitochondrial RNA-associated protein with distinct extramitochondrial pools. The mature homotrimer supports mitochondrial protein synthesis through RNA and mitoribosome association. In a separate RNA-clearance pathway, C1QBP recognizes m5C-marked mitochondrial transcripts and recruits PNPT1 for turnover, helping limit the accumulation and cytosolic release of mitochondrial double-stranded RNA. At the cell surface, extrinsic C1QBP binds the globular region of C1q and high-molecular-weight kininogen, modulating complement and contact-system assemblies in cooperation with other surface proteins. Smaller nuclear and cytoplasmic pools regulate splicing, transcription, preribosome remodeling and MRE11-dependent DNA repair. Biallelic C1QBP defects cause mitochondrial disease with respiratory-chain deficiency and cardiomyopathy.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005634 nucleus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: A nuclear C1QBP pool supports context-dependent nuclear functions. Reason: The human HeLa study reports nuclear as well as cytoplasmic p32 and partial colocalization with CBF-B. This supports the inherited location despite predominant mitochondrial localization. The minor nuclear pool is retained as non-core; rat splenic immunoreactivity is not treated as a human localization experiment. |
| GO:0042256 cytosolic ribosome assembly | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: C1QBP participates in nucleolar preribosome remodeling. Reason: The p32 study reports competitive Nop52/fibrillarin interactions, association with preribosomal particles and precursor rRNA, and impaired processing after depletion. This is mechanistic participation in ribosome biogenesis. GO:0042256 includes nuclear and nucleolar stages of cytosolic ribosome assembly, so the location is compatible. Retain as a secondary function rather than equating it with mitochondrial translation. |
| GO:0001849 complement component C1q complex binding | IBA GO_REF:0000033 | ACCEPT | Summary: C1QBP directly recognizes the globular region of C1q. Reason: Purified cell-derived and recombinant human p32 bind C1q in the original study, independently supporting the inherited molecular function. This is recognition by C1QBP, not complement-protease activity. The historical apparent oligomer-size estimate is not used to override the established homotrimer. |
| GO:0003714 transcription corepressor activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: C1QBP can repress CBF/NF-Y-dependent transcription. Reason: The human study reports interaction with CBF-B and inhibition of CBF-mediated transcription in a reconstituted system. This supports corepressor activity without assigning sequence-specific DNA recognition or a general transcriptional role in every cellular context. Retain the nuclear mechanism as non-core. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: A peripheral plasma-membrane pool participates in extracellular ligand recognition. Reason: Human cell-surface detection and the characterized endothelial ligand-binding pool support membrane association. The protein need not span the membrane: UniProt identifies a peripheral extracellular-side pool alongside predominant mitochondrial localization. Retain this location for the surface recognition functions, without inventing a transmembrane segment. |
| GO:0009986 cell surface | IBA GO_REF:0000033 | ACCEPT | Summary: Cell-surface C1QBP provides a binding site for extracellular ligands. Reason: The human surface-display observations and endothelial p33 isolation support a genuine surface-associated pool. This is compatible with the mitochondrial pool and does not establish that all C1QBP is surface exposed or autonomously transduces signals. |
| GO:0030449 regulation of complement activation | IBA GO_REF:0000033 | ACCEPT | Summary: C1q binding by C1QBP can regulate complement activation. Reason: The original human-protein study reports inhibition of complement-dependent hemolysis in human serum after C1q recognition. C1QBP performs the recognition/regulatory work; it is not merely a passive complement substrate and is not assigned protease activity. The existing regulatory annotation is supported within the tested context. |
| GO:0030984 kininogen binding | IBA GO_REF:0000033 | MODIFY | Summary: C1QBP directly binds high-molecular-weight kininogen. Reason: The inherited source specifies kininogen binding, while purified endothelial p33 and recombinant human protein distinguish high- from low-molecular-weight kininogen and identify D5H-mediated recognition. Refine this target claim to the verified HMW child using direct human specificity evidence. The historical IBD tree/node was not independently inspected, so this does not assert that all descendants inherited the narrower specificity or that the original node placement was incorrect. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN008506808 UNRESOLVED The exact source node is preserved from GOA. Its IBD tree/MSA was unavailable, so no independent placement or narrower ancestral specificity is claimed. UniProtKB:Q07021 · C1QBP SUPPORTS TRANSFER The target is a legitimate experimental descendant source, not circular evidence. Human purified/recombinant protein distinguishes HMW from LMW kininogen, supporting refinement of this target annotation rather than a claim that all descendants share that narrower specificity. Proposed replacements: high molecular weight kininogen binding |
| GO:0048025 negative regulation of mRNA splicing, via spliceosome | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: C1QBP can inhibit SRSF1-dependent splicing through regulation of SRSF1 RNA engagement. Reason: The human p32 study reports inhibition of stable ASF/SF2 (SRSF1) RNA association and its phosphorylation. This supplies a mechanism for negative regulation in the assayed splicing contexts. It does not establish universal suppression of all splicing or direct phosphatase catalysis by C1QBP; retain as a secondary nuclear function. |
| GO:0002250 adaptive immune response | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: C1QBP modulates adaptive immune responses in defined cellular contexts. Reason: The keyword-derived term is broad but biologically supported: ligating gC1qR on human dendritic cells suppresses IL-12 and consequently Th1 differentiation and IFN-gamma production in cocultured T cells. This is contextual regulatory participation, not evidence that C1QBP is an antigen receptor or that a broad annotation is false merely because it is uninformative. |
| GO:0002376 immune system process | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: C1QBP participates in immune regulation. Reason: C1q recognition, complement regulation and ligand-dependent immune-cell signaling support the broad process. Retain it outside the core synthesis rather than removing a correct parent-level keyword inference. |
| GO:0005576 extracellular region | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: A soluble extracellular C1QBP pool occurs in defined cell contexts. Reason: The preserved UniProt location and the primary release study support extracellular C1QBP. This does not make secretion universal across cell types or confuse release of a POLGARF fragment with secretion of C1QBP itself. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: A nuclear C1QBP pool supports secondary nuclear functions. Reason: Human HeLa localization and transcription-factor interaction support a real nuclear pool despite predominant mitochondrial localization. Nuclear presence is not discarded because an earlier study emphasized mitochondria. |
| GO:0005730 nucleolus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: C1QBP can occupy nucleoli during ribosome-biogenesis and interaction contexts. Reason: The Nop52/fibrillarin study reports p32 association with preribosomal particles and precursor rRNA; the POLGARF study provides an additional nucleolar interaction context. Neither establishes that all mature C1QBP is nucleolar. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: C1QBP has a context-dependent cytoplasmic pool. Reason: Human cell localization and the preserved UniProt record support cytoplasmic protein in addition to the predominant mitochondrial pool. Retain this broad location as secondary rather than infer uniform cytosolic residence from overexpression. |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000120 | ACCEPT | Summary: The mitochondrial matrix is a principal site of C1QBP RNA functions. Reason: The electronic inference agrees with fractionation and imaging of human p32 and with the mitochondrial RNA studies. This accepts the matrix location without extending the older exclusively mitochondrial interpretation to all tissues and conditions. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: A genuine plasma-membrane-associated C1QBP pool binds extracellular ligands. Reason: Surface antibody detection and isolation of extrinsic endothelial membrane p33 independently support this mapping. C1QBP has no inferred transmembrane receptor topology and need not itself span the membrane to associate with it. |
| GO:0006397 mRNA processing | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: C1QBP regulates mRNA processing through a splicing-factor interaction. Reason: The ASF/SF2 study reports an inhibitory complex affecting SRSF1 RNA engagement and phosphorylation. This supports contextual mRNA-processing regulation, not intrinsic RNA-processing catalysis or a universal effect on every transcript. |
| GO:0006915 apoptotic process | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: C1QBP participates in context-dependent apoptotic regulation. Reason: Hrk binding, colocalization, mutant interference and p32 depletion support an apoptotic regulatory role in the tested model. The process is not rejected merely as a secondary phenotype, but the historical pore-forming interpretation is not made a core molecular activity. |
| GO:0006958 complement activation, classical pathway | IEA GO_REF:0000043 | MODIFY | Summary: C1QBP recognition of C1q regulates complement rather than constituting the activation cascade. Reason: The human-protein study directly reports inhibition of complement-mediated hemolysis after C1q binding. GO:0006958 describes the classical activation steps; C1QBP is neither a C1q recognition chain nor the complement protease. Refine this broad keyword mapping to the already represented regulation of complement activation, rather than infer activation from the protein name. Proposed replacements: regulation of complement activation |
| GO:0006974 DNA damage response | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: C1QBP regulates the MRE11-dependent DNA-damage response. Reason: The accessible primary abstract describes MRE11/RAD50 stabilization and inhibition before damage, followed by ATM-dependent release. Both excess and insufficient C1QBP impair recruitment and repair. This is a dosage- and phase-dependent regulatory function, not C1QBP nuclease activity. |
| GO:0008380 RNA splicing | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: C1QBP can regulate RNA splicing by sequestering SRSF1. Reason: The human p32 study identifies an inhibitory splicing-factor complex and reduced stable SRSF1 RNA binding. Retain the broad splicing inference as a secondary function; C1QBP is not assigned the spliceosomal catalytic reaction. |
| GO:0042254 ribosome biogenesis | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: C1QBP participates in nucleolar preribosome remodeling. Reason: Competitive Nop52/fibrillarin binding, preribosomal association and precursor-rRNA processing defects support actual structural/regulatory participation. This cytosolic-ribosome biogenesis context is distinct from mitochondrial translation. |
| GO:0045087 innate immune response | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: C1QBP modulates innate immune signaling in several defined contexts. Reason: The MAVS and gC1qR-ligation studies provide direct regulatory mechanisms. Retain this broad keyword annotation outside the core synthesis rather than imply an autonomous pathogen receptor or transfer partner enzymatic activities. |
| GO:0005515 protein binding | IPI PMID:10831594 Protein kinase C [micro] is regulated by the multifunctional... | MODIFY | Summary: C1QBP binds the protein kinase C family member PRKCZ. Reason: The complete PMID:10831594 abstract explicitly identifies binding to PKC-zeta among the tested isoforms. The source partner Q05513 is PRKCZ, not the PKC-mu/PRKD1 protein studied in greater mechanistic detail. GO:0005080 is an evidence-backed refinement for this exact partner; do not transfer the detailed PKC-mu substrate-inhibition result to PRKCZ. Proposed replacements: protein kinase C binding |
| GO:0005515 protein binding | IPI PMID:11086025 Interaction between complement receptor gC1qR and hepatitis ... | KEEP AS NON CORE | Summary: C1QBP associates with the processed HCV core protein. Reason: PMID:11086025 explicitly describes a human T-cell-library screen, mapped core–gC1qR binding and antibody-sensitive inhibition of T-cell proliferation. Preserve P27958-PRO_0000037566, rather than substituting the entire viral polyprotein or asserting every viral protein binds. The source supports association; a distinct receptor/signaling mechanism beyond this contextual interaction is not assigned from the abstract alone. |
| GO:0005515 protein binding | IPI PMID:12034482 The N-terminal conserved domain of rubella virus capsid inte... | KEEP AS NON CORE | Summary: Human C1QBP binds the rubella capsid N-terminal region. Reason: PMID:12034482 explicitly reports human WI-38-derived p32 binding to the conserved rubella capsid N-terminal domain and maps the p32 region. Preserve the source processed product P07566-PRO_0000041308. Enhanced infectivity after overexpression does not by itself define a new autonomous C1QBP viral-replication activity. |
| GO:0005515 protein binding | IPI PMID:12220632 The cytoplasmic tail peptide sequence of membrane type-1 mat... | MODIFY | Summary: C1QBP directly associates with the cytoplasmic tail of MMP14/MT1-MMP. Reason: The complete PMID:12220632 abstract explicitly reports direct tail association with the protease MMP14, supporting protease binding. The paper states that the functional link is uncertain; no peptidase regulator or chaperone activity is inferred merely from the proposed cell-surface-trafficking role. Proposed replacements: protease binding |
| GO:0005515 protein binding | IPI PMID:14743216 A physical and functional map of the human TNF-alpha/NF-kapp... | UNDECIDED | Summary: The specific O00221 interaction remains unresolved in the accessible source. Reason: PMID:14743216 provides a tandem-affinity-purification/mass-spectrometry pathway framework but its normal cache is abstract-only and the O00221–C1QBP target entry was not inspected. O00221 is also present in another curated screen row, but no independently read target assay or matching interaction entry in the inspected UniProt INTERACTION block resolves this pair. Preserve uncertainty; the pathway title is not evidence of wrong-gene curation. |
| GO:0005515 protein binding | IPI PMID:15031724 Physical and functional interaction between BH3-only protein... | KEEP AS NON CORE | Summary: C1QBP associates with HRK in mitochondrial apoptosis experiments. Reason: PMID:15031724 explicitly reports yeast two-hybrid identification, in-vitro binding, co-immunoprecipitation and colocalization of Hrk/p32. Retain the exact O00198 interaction as non-core generic binding; the abstract’s proposed p32 channel interpretation is not independently established here and is not transferred into the recommendation. |
| GO:0005515 protein binding | IPI PMID:16721827 CDC2L5, a Cdk-like kinase with RS domain, interacts with the... | MODIFY | Summary: C1QBP binds the serine/threonine kinase CDK13/CDC2L5. Reason: The complete PMID:16721827 abstract explicitly describes direct CDC2L5–p32 interaction and a splicing context. Refine to serine/threonine kinase binding. Preserve the original Q14004 versus Q14004-2 distinction; the latter exact product is independently represented in UniProt/IntAct, while the abstract does not resolve individual construct sequences. No kinase activity or isoform-exclusive function is assigned to C1QBP. Proposed replacements: protein serine/threonine kinase binding |
| GO:0005515 protein binding | IPI PMID:17486078 The autophagic inducer smARF interacts with and is stabilize... | KEEP AS NON CORE | Summary: C1QBP binds a short mitochondrial ARF product in the tested species. Reason: PMID:17486078 explicitly reports interaction with both human and murine smARF, mitochondrial colocalization and stabilization of the short form. Preserve murine Q64364 as a cross-species partner, rather than silently changing it to human CDKN2A. The abstract distinguishes short smARF from predominantly nucleolar full-length p19ARF. Do not generalize a short-product interaction to every ARF product or turn stabilization into C1QBP catalysis. |
| GO:0005515 protein binding | IPI PMID:18676636 Human p32 is a novel FOXC1-interacting protein that regulate... | MODIFY | Summary: C1QBP binds the FOXC1 forkhead transcription factor. Reason: PMID:18676636 explicitly reports human-library identification, Ni-pulldown and immunoprecipitation, maps binding to the FOXC1 forkhead domain, and measures altered FOXC1 transcriptional activation without altered DNA binding. This supports DNA-binding transcription factor binding for exact partner Q12948; C1QBP itself is not assigned sequence-specific DNA recognition. Proposed replacements: DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:19164550 Inhibition of RIG-I and MDA5-dependent antiviral response by... | KEEP AS NON CORE | Summary: C1QBP associates with MAVS in antiviral-signaling experiments. Reason: The complete PMID:19164550 abstract explicitly describes gC1qR–VISA/MAVS association following viral/dsRNA stimulation and suppression of RIG-I/MDA5 signaling. Preserve Q7Z434. The interaction is supported, but a specific adapter molecular activity of C1QBP is not established merely because its partner MAVS is an adapter. |
| GO:0005515 protein binding | IPI PMID:21653829 Protein interactome reveals converging molecular pathways am... | KEEP AS NON CORE | Summary: The YBX1–C1QBP association is independently established and the curated source edge is retained. Reason: PMID:21653829 is a Y2H-centered autism-interactome source; its inspected validation framework tests a subset in mammalian cells. The original partner P67809 is retained with experimental curator deference. Independent targeted interaction evidence in PMID:23986595 and PMID:25497084 and the exact UniProt/IntAct edge support the claim. This does not pretend that the original target supplement or a direct binary interface was inspected, or assign YBX1’s RNA-binding/transcription activities to C1QBP. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | UNDECIDED | Summary: The exact O00221 liver-interactome association remains unresolved. Reason: The PMID:21988832 abstract and accessible source narrative establish a human liver yeast-two-hybrid screen with validation of subsets. No C1QBP–O00221 target table entry was inspected, and the other curated screen row does not supply an independently read target assay. Retain UNDECIDED without claiming absence, misattribution or that high-throughput evidence is intrinsically invalid. The cache full-text flag does not mean its target supplement was read. |
| GO:0005515 protein binding | IPI PMID:22118625 NONO and RALY proteins are required for YB-1 oxaliplatin ind... | KEEP AS NON CORE | Summary: The YBX1–C1QBP association is independently established and the curated source edge is retained. Reason: PMID:22118625 reports tagged YB-1 co-purification, and the accessible Table 1 text includes C1QBP/Q07021 among potential YB-1 partners. The original partner P67809 is retained with experimental curator deference. Independent targeted interaction evidence in PMID:23986595 and PMID:25497084 and the exact UniProt/IntAct edge support the claim. This does not pretend that the original target supplement or a direct binary interface was inspected, or assign YBX1’s RNA-binding/transcription activities to C1QBP. |
| GO:0005515 protein binding | IPI PMID:22238231 Binding of cellular p32 protein to the rubella virus P150 re... | KEEP AS NON CORE | Summary: C1QBP binds the rubella P150 replicase proline-rich region. Reason: PMID:22238231 explicitly describes GST-PRR pulldown, motif mutations that abolish binding and infected-cell colocalization. Preserve O40955-PRO_0000240177. The paper reports little overlap with RNA replication complexes and leaves the replication role unresolved, so binding is retained without a direct viral RNA-synthesis role. |
| GO:0005515 protein binding | IPI PMID:23986595 A host YB-1 ribonucleoprotein complex is hijacked by hepatit... | KEEP AS NON CORE | Summary: C1QBP is a validated YBX1-associated factor in the HCV cell model. Reason: PMID:23986595 explicitly identifies C1QBP among YB-1 partners after quantitative proteomics and extensive interaction/functional validation, with redistribution to core-containing lipid droplets. Retain P67809 association, not a claim that C1QBP is the viral core protein or that every co-purification proves a purified binary interface. |
| GO:0005515 protein binding | IPI PMID:24955142 Exploration of panviral proteome: high-throughput cloning an... | KEEP AS NON CORE | Summary: C1QBP binding to rubella capsid is supported by the source’s targeted validation. Reason: The full relevant PMID:24955142 Results passage describes a C1QBP NAPPA signal, independent bead-based pulldown and capsid colocalization in HeLa cells. Preserve P08563-PRO_0000041302; do not replace the processed viral partner with a different strain/product. The source’s broader panviral scope does not invalidate this directly discussed target interaction. |
| GO:0005515 protein binding | IPI PMID:25497084 C1QBP negatively regulates the activation of oncoprotein YBX... | KEEP AS NON CORE | Summary: C1QBP associates with YBX1 in renal carcinoma cells. Reason: The complete PMID:25497084 abstract explicitly reports co-immunoprecipitation/mass spectrometry followed by targeted immunoprecipitation/Western confirmation of C1QBP–YBX1. Retain P67809 binding outside the core synthesis. Changes in YBX1 phosphorylation after C1QBP depletion do not make C1QBP a kinase or phosphatase. |
| GO:0005515 protein binding | IPI PMID:25852190 Integrative analysis of kinase networks in TRAIL-induced apo... | MODIFY | Summary: The curated PRKCZ interaction is consistent with independently established PKC binding. Reason: PMID:25852190 supplies a protein-interaction network framework; the individual PRKCZ–C1QBP assay/table entry was not independently inspected. Preserve the original source and exact Q05513 partner with curator deference, supported by the explicit PKC-zeta binding in PMID:10831594 and matching UniProt/IntAct edge. Refine the claim to PKC binding without claiming verification of the original network cell or transferring the PKC-mu inhibition assay to PRKCZ. Proposed replacements: protein kinase C binding |
| GO:0005515 protein binding | IPI PMID:26184334 Comprehensive Protein Interactome Analysis of a Key RNA Heli... | KEEP AS NON CORE | Summary: The YBX1–C1QBP association is independently established and the curated source edge is retained. Reason: PMID:26184334 centers on DDX6; inspected Results identify C1QBP in the larger splicing-protein complex, but the exact YBX1 pairwise assay was not independently read. The original partner P67809 is retained with experimental curator deference. Independent targeted interaction evidence in PMID:23986595 and PMID:25497084 and the exact UniProt/IntAct edge support the claim. This does not pretend that the original target supplement or a direct binary interface was inspected, or assign YBX1’s RNA-binding/transcription activities to C1QBP. |
| GO:0005515 protein binding | IPI PMID:26816005 Homologous Transcription Factors DUX4 and DUX4c Associate wi... | KEEP AS NON CORE | Summary: C1QBP associates with the source DUX4c-related product. Reason: The exact source identifier Q6RFH8 is labeled DUX4L9 in the preserved UniProt interaction record, while the primary papers use DUX4c nomenclature. Inspected PMID:26816005 Results report C1QBP in HaloTag-DUX4c precipitates and distinguish this from DUX4 homeodomain co-immunoprecipitation experiments. Retain the exact source partner and association without rewriting it to another DUX4 accession, inferring a sequence-specific C1QBP DNA-binding activity, or treating proximity as proof of a purified binary interface. These source contexts emphasize RNA-protein assemblies rather than establishing a distinct transcription-regulatory molecular activity of C1QBP. |
| GO:0005515 protein binding | IPI PMID:27499296 Mitochondrial Protein Interaction Mapping Identifies Regulat... | KEEP AS NON CORE | Summary: The curated PRSS35 association is retained with source-specific limits. Reason: PMID:27499296 provides a mitochondrial affinity-enrichment/MS framework, but the preserved body contains limited narrative and does not expose the C1QBP–PRSS35 target table. The exact Q8N3Z0 pair is independently curated in UniProt/IntAct. Retain the experimental edge with curator deference, without claiming target-table verification, a purified binary interaction, or protease-binding specificity from an unverified catalytic state. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | KEEP AS NON CORE | Summary: C1QBP–vitronectin association is independently supported. Reason: The inspected 28514442 abstract/source framework describes affinity-purification/MS co-complex detection; the individual target entry remains uninspected. The exact P04004 partner is curated in UniProt/IntAct and independently supported by the direct purified binding experiments summarized in PMID:8900153. Retain this source edge with curator deference, while distinguishing the multimeric vitronectin form tested in the targeted study from every circulating form. |
| GO:0005515 protein binding | IPI PMID:28565870 C1QBP is upregulated in colon cancer and binds to apolipopro... | MODIFY | Summary: C1QBP associates with apolipoprotein A-I in the studied cell model. Reason: The complete normal PMID:28565870 abstract explicitly reports C1QBP pull-down/MS followed by reverse-immunoprecipitation confirmation of APOA1 association. The official apolipoprotein-binding parent record identifies GO:0034186 as apolipoprotein A-I binding. Preserve P02647 and do not assign lipid transfer or APOA1 enzymatic activity. The original paper remains abstract-only; its explicit targeted confirmation is sufficient for this binding refinement. Proposed replacements: apolipoprotein A-I binding |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: The curated PRKCZ interaction is consistent with independently established PKC binding. Reason: PMID:31980649 supplies a protein-interaction network framework; the individual PRKCZ–C1QBP assay/table entry was not independently inspected. Preserve the original source and exact Q05513 partner with curator deference, supported by the explicit PKC-zeta binding in PMID:10831594 and matching UniProt/IntAct edge. Refine the claim to PKC binding without claiming verification of the original network cell or transferring the PKC-mu inhibition assay to PRKCZ. Proposed replacements: protein kinase C binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The curated C1QBP–KLF1 HuRI edge is retained with assay-context limits. Reason: PMID:32296183 supplies a repeated Y2H/pairwise-retesting framework and the exact Q13351 pair is present in the UniProt/IntAct interaction record. The individual supplementary record was not read. Retain supported generic binding with experimental curator deference; a physiological KLF1 transcription-regulation mechanism is not claimed from the screen alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: C1QBP–vitronectin association is independently supported. Reason: The inspected 33961781 abstract/source framework describes affinity-purification/MS co-complex detection; the individual target entry remains uninspected. The exact P04004 partner is curated in UniProt/IntAct and independently supported by the direct purified binding experiments summarized in PMID:8900153. Retain this source edge with curator deference, while distinguishing the multimeric vitronectin form tested in the targeted study from every circulating form. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The YBX1–C1QBP association is independently established and the curated source edge is retained. Reason: PMID:35271311 uses endogenous tagging and interaction profiling; the preserved body is partial and its individual C1QBP–YBX1 entry was not inspected. The original partner P67809 is retained with experimental curator deference. Independent targeted interaction evidence in PMID:23986595 and PMID:25497084 and the exact UniProt/IntAct edge support the claim. This does not pretend that the original target supplement or a direct binary interface was inspected, or assign YBX1’s RNA-binding/transcription activities to C1QBP. |
| GO:0005515 protein binding | IPI PMID:36882853 The double homeodomain protein DUX4c is associated with rege... | KEEP AS NON CORE | Summary: C1QBP associates with the source DUX4c-related product. Reason: The exact source identifier Q6RFH8 is labeled DUX4L9 in the preserved UniProt interaction record, while the primary papers use DUX4c nomenclature. Inspected PMID:36882853 Results identify C1QBP as a major HaloTag-DUX4c partner across replicate purifications and report endogenous proximity ligation in human muscle cells. Retain the exact source partner and association without rewriting it to another DUX4 accession, inferring a sequence-specific C1QBP DNA-binding activity, or treating proximity as proof of a purified binary interface. These source contexts emphasize RNA-protein assemblies rather than establishing a distinct transcription-regulatory molecular activity of C1QBP. |
| GO:0005515 protein binding | IPI PMID:8710908 Identification of the zinc-dependent endothelial cell bindin... | MODIFY | Summary: C1QBP binds coagulation factor XII in zinc-dependent biochemical assays. Reason: The complete PMID:8710908 abstract reports zinc-dependent ligand- and dot-blot binding of factor XII to isolated HUVEC protein and recombinant gC1qR. The exact source partner P00748 is factor XII, separately preserved from the kininogen partner. GO:0002020 specifies binding to a protease or peptidase and does not require a catalytic-regulator mechanism. Refine the partner-class term consistently with the MMP14 interaction. The inspected abstract does not settle the factor XII activation state; no activation, inhibition or clotting-protease activity is assigned to C1QBP. Proposed replacements: protease binding |
| GO:0005515 protein binding | IPI PMID:8900153 The binding protein for globular heads of complement C1q, gC... | KEEP AS NON CORE | Summary: C1QBP binds the multimeric heparin-binding form of vitronectin. Reason: The complete PMID:8900153 abstract describes purified-system binding to multimeric vitronectin, saturability and glycosaminoglycan competition; the plasma vitronectin form did not bind in the reported assay. Retain P04004 with this conformation boundary. Do not generalize to every vitronectin-containing state or infer particle clearance as a directly demonstrated C1QBP process. |
| GO:0001849 complement component C1q complex binding | IEA GO_REF:0000107 | ACCEPT | Summary: The rat-derived C1q-binding inference agrees with direct human evidence. Reason: The donor identifiers resolve to rat C1qbp. Independently, purified and recombinant human C1QBP bind C1q in the original human study. Retain the existing orthology assertion without claiming that the exact rat assay underlying the Ensembl transfer was reconstructed. |
| GO:0005080 protein kinase C binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: C1QBP has a supported secondary PKC-binding function. Reason: The donor study identifies rat p32 and tests recombinant p32 interaction with PKC isoforms, with binding controls. Human UniProt also records PRKCZ interaction. This supports retention of the existing binding inference; it neither makes C1QBP a PKC substrate nor establishes a new kinase-regulator core. |
| GO:0005615 extracellular space | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: An extracellular soluble C1QBP pool is supported in defined cell contexts. Reason: Human UniProt records a secreted form, and the primary release study detects soluble gC1qR from Raji cells. The specific release conditions should not be generalized to every lymphocyte. Retain extracellular space as non-core; secretion of the POLGARF fragment in a different study is not evidence that C1QBP itself was secreted. Supporting Evidence: GO_REF:0000107 file:human/C1QBP/C1QBP-uniprot.txt PMID:9191880 gC1q-R was releasable only from Raji cells |
| GO:0031690 adrenergic receptor binding | IEA GO_REF:0000107 | MODIFY | Summary: The transferred receptor-binding function can be specified as alpha-1B adrenergic receptor binding. Reason: The complete PMID:10409668 abstract describes a rat-liver cDNA-library interaction with the alpha-1B receptor cytoplasmic tail, deletion mapping to residues 369-378, and confirmation with full-length receptor in transfected COS-7 cells. GO:0031692 is the verified alpha-1B child of adrenergic receptor binding. Human UniProt records ADRA1B association by similarity. Refine this existing orthology-based assertion to the assayed subtype while preserving the rat donor and original evidence code; no independent human binding experiment, intrinsic receptor activity or general adrenergic-signaling core is claimed. This remains a secondary interaction outside the four core functions. Proposed replacements: alpha-1B adrenergic receptor binding |
| GO:0048786 presynaptic active zone | IEA GO_REF:0000107 | UNDECIDED | Summary: The rat-derived presynaptic active zone location remains unresolved at the source-assay level. Reason: The source correctly identifies rat C1qbp, and its official record lists presynaptic active zone. However, the precise donor publication and localization experiment underlying this transferred compartment were not recovered. General mitochondrial, cytoplasmic or neuronal presence does not settle this fine location. Keep the assertion unresolved rather than declaring the location false or demanding an additional human experiment as a prerequisite for orthology. Supporting Evidence: GO_REF:0000107 |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | UNDECIDED | Summary: The rat-derived glutamatergic synapse location remains unresolved at the source-assay level. Reason: The source correctly identifies rat C1qbp, and its official record lists glutamatergic synapse. However, the precise donor publication and localization experiment underlying this transferred compartment were not recovered. General mitochondrial, cytoplasmic or neuronal presence does not settle this fine location. Keep the assertion unresolved rather than declaring the location false or demanding an additional human experiment as a prerequisite for orthology. Supporting Evidence: GO_REF:0000107 |
| GO:0098982 GABA-ergic synapse | IEA GO_REF:0000107 | UNDECIDED | Summary: The rat-derived GABA-ergic synapse location remains unresolved at the source-assay level. Reason: The source correctly identifies rat C1qbp, and its official record lists GABA-ergic synapse. However, the precise donor publication and localization experiment underlying this transferred compartment were not recovered. General mitochondrial, cytoplasmic or neuronal presence does not settle this fine location. Keep the assertion unresolved rather than declaring the location false or demanding an additional human experiment as a prerequisite for orthology. Supporting Evidence: GO_REF:0000107 |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | ACCEPT | Summary: C1QBP localizes to mitochondria. Reason: Retain the curated immunofluorescence assertion with independent human fractionation and imaging support. The original GO_REF-linked image was not separately inspected; the biological location is independently established. |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | ACCEPT | Summary: C1QBP is present at the plasma membrane in appropriate cellular contexts. Reason: Retain the curated immunofluorescence assertion with independent surface-antibody and endothelial membrane isolation evidence. This is a surface-associated pool rather than an assumed transmembrane topology. |
| GO:0000957 mitochondrial RNA catabolic process | IDA PMID:39019044 RNA 5-methylcytosine marks mitochondrial double-stranded RNA... | ACCEPT | Summary: C1QBP promotes turnover of methylated mitochondrial RNAs by recruiting PNPT1. Reason: The primary report assigns NSUN4 the methylation step and PNPT1 the degradative activity; C1QBP recognizes the marked RNA and recruits the nuclease. This is molecular participation in RNA clearance, not a necessity-only inference or nuclease activity assigned to C1QBP. Selected cellular Results/Methods were inspected in addition to the cached abstract. The complete institutional copy of the 2025 correction concerns copyediting of reagent names/citations, not the C1QBP assays. Supporting Evidence: |
| GO:0005759 mitochondrial matrix | IDA PMID:39019044 RNA 5-methylcytosine marks mitochondrial double-stranded RNA... | ACCEPT | Summary: C1QBP acts on mitochondrial RNA in the matrix. Reason: The source places the reader/turnover mechanism in mitochondria, and independent fractionation and imaging directly establish matrix localization. Neither this annotation nor the independent study is treated as excluding all extramitochondrial C1QBP. |
| GO:0062153 C5-methylcytidine-containing RNA reader activity | IDA PMID:39019044 RNA 5-methylcytosine marks mitochondrial double-stranded RNA... | ACCEPT | Summary: C1QBP is reported to recognize m5C-containing mitochondrial RNA and recruit its turnover machinery. Reason: The methylated-versus-unmodified RNA pulldown uses precleared total cell lysate; cellular crosslinking/RNA immunoprecipitation and PNPT1 association support the reader/adaptor model. These assays do not establish purified binary affinity, an intrinsic recognition site, or C1QBP nuclease catalysis. Retain the source-supported reader activity with these assay bounds. The subsequently accessed institutional correction changes reagent naming/citation text, not the C1QBP findings. Supporting Evidence: PMID:39019044 These m5C-modified RNAs are recognized by complement C1q-binding protein |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | ACCEPT | Summary: C1QBP is a mitochondrial protein. Reason: The MitoCOP primary framework profiles human mitochondrial proteins by complementary approaches. The exact C1QBP target table was not independently inspected, so retain the experimental curator assertion with strong independent mitochondrial localization evidence rather than claim a table read. |
| GO:0004857 enzyme inhibitor activity | IDA PMID:31353207 C1QBP Promotes Homologous Recombination by Stabilizing MRE11... | MODIFY | Summary: C1QBP inhibits MRE11 deoxyribonuclease activity in the pre-damage complex. Reason: The complete primary abstract explicitly reports an MRE11/RAD50/C1QBP complex that inhibits MRE11 nuclease activity by preventing DNA/chromatin engagement. GO:0060703 captures the experimentally identified enzyme class more precisely than generic enzyme inhibitor activity. The phase-dependent inhibition is contextual; C1QBP neither cleaves DNA nor becomes a constitutive inhibitor under every condition. Proposed replacements: deoxyribonuclease inhibitor activity Supporting Evidence: PMID:31353207 nuclease activity by preventing its binding to DNA or chromatin |
| GO:2000042 negative regulation of double-strand break repair via homologous recombination | IDA PMID:31353207 C1QBP Promotes Homologous Recombination by Stabilizing MRE11... | KEEP AS NON CORE | Summary: C1QBP restrains homologous-recombination machinery in a regulated pre-damage state. Reason: The primary abstract describes MRE11 inhibition within a stabilizing complex and its release after ATM phosphorylation. Thus the title emphasizing repair promotion does not contradict the inhibitory phase. Retain the contextual negative regulation; both excess and insufficient protein impair repair, so a universal anti-repair role would be misleading. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32958672 Unusually efficient CUG initiation of an overlapping reading... | KEEP AS NON CORE | Summary: C1QBP associates with the alternative-frame product POLGARF. Reason: The complete PMID:32958672 abstract explicitly names C1QBP as an interacting partner of unprocessed POLGARF in nucleoli. Preserve A0A3B3IS91 and distinguish the alternative-frame protein from the canonical POLG DNA-polymerase enzyme and from the secreted cleaved POLGARF fragment. No DNA-polymerase binding/activity is inferred. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9645692 | ACCEPT | Summary: C1QBP has a mitochondrial matrix pool in the ARF interaction context. Reason: The Reactome event uses C1QBP in p14ARF trafficking, while independent human experiments establish the matrix location. The cache also records uncertainty over the precise ARF/C1QBP complex location; accept C1QBP matrix residence without asserting that every ARF complex was proven to occupy that compartment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9645692 | KEEP AS NON CORE | Summary: A cytosolic C1QBP pool is compatible with the curated ARF event. Reason: The ARF mitochondrial-trafficking Reactome record provides a pathway context for cytosolic C1QBP, supported independently by human cell localization. Conflicting reports about ARF complex distribution do not make all cytosolic C1QBP incorrect. Mutations in the ARF partner are not silently transferred to wild-type C1QBP. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9645694 | KEEP AS NON CORE | Summary: A cytosolic C1QBP pool is compatible with the curated ARF event. Reason: The ARF binding Reactome record provides a pathway context for cytosolic C1QBP, supported independently by human cell localization. Conflicting reports about ARF complex distribution do not make all cytosolic C1QBP incorrect. Mutations in the ARF partner are not silently transferred to wild-type C1QBP. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9645766 | KEEP AS NON CORE | Summary: A cytosolic C1QBP pool is compatible with the curated ARF event. Reason: The ARF-mutant comparison Reactome record provides a pathway context for cytosolic C1QBP, supported independently by human cell localization. Conflicting reports about ARF complex distribution do not make all cytosolic C1QBP incorrect. Mutations in the ARF partner are not silently transferred to wild-type C1QBP. |
| GO:0005515 protein binding | IPI PMID:18191643 Novel tyrosine phosphorylated and cardiolipin-binding protei... | KEEP AS NON CORE | Summary: C1QBP associates with PLEKHN1/CLPABP. Reason: The complete PMID:18191643 abstract identifies SF2p32 as a binding protein required for the characteristic CLPABP granule localization. Preserve Q494U1. CLPABP phospholipid-binding and proposed RNA-transport functions belong to that protein/complex context and are not transferred to C1QBP merely from association. |
| GO:0005759 mitochondrial matrix | IDA PMID:9305894 p32 protein, a splicing factor 2-associated protein, is loca... | ACCEPT | Summary: Human p32 is localized to the mitochondrial matrix. Reason: Fractionation, fluorescent immunocytochemistry and electron-microscopic immunostaining support the matrix location. Preserve the source part_of qualifier. The study’s exclusive-location interpretation is bounded by later evidence for specific extramitochondrial pools; its yeast loss/rescue experiments are not described as human knockout assays. Supporting Evidence: PMID:9305894 p32 is exclusively localized in the mitochondrial matrix |
| GO:0005739 mitochondrion | IDA PMID:11083468 Localization of P32 protein (gC1q-R) in mitochondria and at ... | ACCEPT | Summary: C1QBP predominantly localizes to mitochondria while additional pools are context dependent. Reason: The primary study examines human cell lines and rat tissues by immunogold/electron microscopy and reports predominant mitochondrial localization with selected extramitochondrial sites. Preserve the source part_of qualifier and distinguish rat tissue observations from human experiments. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-158218 | ACCEPT | Summary: Surface-associated C1QBP presents kininogen in the curated contact-system event. Reason: Endothelial p33 isolation and recombinant binding support the plasma-membrane-associated pool used by this Reactome event. Kallikrein, factor XII and prolylcarboxypeptidase perform their own proteolytic steps; their catalytic activities are not transferred to C1QBP. Historical apparent tetramer terminology in the cached pathway does not establish current oligomer stoichiometry. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-158251 | ACCEPT | Summary: Surface-associated C1QBP presents kininogen in the curated contact-system event. Reason: Endothelial p33 isolation and recombinant binding support the plasma-membrane-associated pool used by this Reactome event. Kallikrein, factor XII and prolylcarboxypeptidase perform their own proteolytic steps; their catalytic activities are not transferred to C1QBP. Historical apparent tetramer terminology in the cached pathway does not establish current oligomer stoichiometry. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-158311 | ACCEPT | Summary: Surface-associated C1QBP presents kininogen in the curated contact-system event. Reason: Endothelial p33 isolation and recombinant binding support the plasma-membrane-associated pool used by this Reactome event. Kallikrein, factor XII and prolylcarboxypeptidase perform their own proteolytic steps; their catalytic activities are not transferred to C1QBP. Historical apparent tetramer terminology in the cached pathway does not establish current oligomer stoichiometry. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-158313 | ACCEPT | Summary: Surface-associated C1QBP presents kininogen in the curated contact-system event. Reason: Endothelial p33 isolation and recombinant binding support the plasma-membrane-associated pool used by this Reactome event. Kallikrein, factor XII and prolylcarboxypeptidase perform their own proteolytic steps; their catalytic activities are not transferred to C1QBP. Historical apparent tetramer terminology in the cached pathway does not establish current oligomer stoichiometry. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-158354 | ACCEPT | Summary: Surface-associated C1QBP presents kininogen in the curated contact-system event. Reason: Endothelial p33 isolation and recombinant binding support the plasma-membrane-associated pool used by this Reactome event. Kallikrein, factor XII and prolylcarboxypeptidase perform their own proteolytic steps; their catalytic activities are not transferred to C1QBP. Historical apparent tetramer terminology in the cached pathway does not establish current oligomer stoichiometry. |
| GO:0000122 negative regulation of transcription by RNA polymerase II | IDA PMID:15243141 Human p32, interacts with B subunit of the CCAAT-binding fac... | KEEP AS NON CORE | Summary: C1QBP inhibits NF-Y/CBF-mediated transcription in vitro. Reason: The human HeLa study isolates p32 with CBF, identifies interaction with the B subunit and measures inhibition of transcriptional activation. Retain the contextual negative regulation without assigning sequence-specific DNA recognition or universal transcriptional repression. Supporting Evidence: |
| GO:0003714 transcription corepressor activity | IDA PMID:15243141 Human p32, interacts with B subunit of the CCAAT-binding fac... | KEEP AS NON CORE | Summary: C1QBP acts as a transcriptional corepressor in the NF-Y/CBF assay. Reason: CBF-B association and inhibition of CBF-mediated transcription support the source-defined corepressor activity. This is a secondary nuclear function and is not conflated with the mitochondrial RNA-binding activities. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:15243141 Human p32, interacts with B subunit of the CCAAT-binding fac... | KEEP AS NON CORE | Summary: A nuclear p32 pool is observed in the human CBF study. Reason: Immunostaining in HeLa cells reports nuclear and cytoplasmic p32 with partial CBF-B colocalization. This is compatible with a predominant mitochondrial pool and supports a contextual nuclear location. Supporting Evidence: |
| GO:0005829 cytosol | IDA PMID:15243141 Human p32, interacts with B subunit of the CCAAT-binding fac... | KEEP AS NON CORE | Summary: A cytosolic p32 pool is observed in the human CBF study. Reason: The reported human cell localization supports a cytoplasmic/cytosolic pool accompanying the nuclear transcriptional context. Retain with experimental curator deference; the abstract does not supply an exhaustive subcellular fractionation map. Supporting Evidence: |
| GO:0008134 transcription factor binding | IDA PMID:15243141 Human p32, interacts with B subunit of the CCAAT-binding fac... | MODIFY | Summary: C1QBP binds the DNA-binding transcription factor NF-Y/CBF. Reason: The primary study directly identifies the CBF-B interaction and transcriptional inhibition. The established DNA-binding transcription factor binding term is a justified refinement of generic transcription factor binding. C1QBP itself is not assigned NF-Y sequence-specific DNA recognition. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0043065 positive regulation of apoptotic process | IMP PMID:15031724 Physical and functional interaction between BH3-only protein... | KEEP AS NON CORE | Summary: C1QBP supports Hrk-induced apoptosis in the tested model. Reason: Hrk/p32 binding, colocalization and interference by p32 mutants or depletion support regulatory participation. A secondary or model-dependent apoptotic role can be valid; do not remove it solely for pleiotropy. The historical channel hypothesis is not established as a core p32 molecular activity. Supporting Evidence: |
| GO:0048025 negative regulation of mRNA splicing, via spliceosome | IDA PMID:10022843 The splicing factor-associated protein, p32, regulates RNA s... | KEEP AS NON CORE | Summary: C1QBP negatively regulates SRSF1-dependent splicing. Reason: The primary study reports an inhibitory complex, prevention of stable SRSF1 RNA binding and reduced phosphorylation. These observations establish regulation in the tested splicing system without assigning C1QBP a kinase, phosphatase or universal splicing-suppression activity. Supporting Evidence: PMID:10022843 an ASF/SF2 inhibitory factor |
| GO:0001849 complement component C1q complex binding | IDA PMID:8195709 Isolation, cDNA cloning, and overexpression of a 33-kD cell ... | ACCEPT | Summary: C1QBP binds the globular heads of C1q. Reason: Raji-derived protein and recombinant mature residues 74–282 bind C1q, independently supporting the direct molecular function. The available cached abstract is itself marked truncated; no complete Methods or universal cell-surface stoichiometry is claimed. Supporting Evidence: PMID:8195709 bind to the globular "heads" of C1q molecules |
| GO:0003729 mRNA binding | ISS GO_REF:0000024 | ACCEPT | Summary: C1QBP binds mitochondrial mRNAs as part of its mitochondrial RNA function. Reason: The primary donor study combines recombinant RNA binding with mitochondrial mRNA association, supporting the existing mRNA-binding inference. The assayed RNA-binding mutant links that activity to translation. The separate stress-dependent m5C study includes noncoding mitochondrial RNA targets and is not substituted for this mRNA-specific evidence. Supporting Evidence: GO_REF:0000024 file:human/C1QBP/C1QBP-uniprot.txt PMID:22904065 Recombinant p32 binds RNA, not DNA |
| GO:0005540 hyaluronic acid binding | IDA PMID:8567680 Molecular cloning of human fibroblast hyaluronic acid-bindin... | KEEP AS NON CORE | Summary: Recombinant human C1QBP binds hyaluronic acid. Reason: The primary abstract reports expression, ligand affinity and competition experiments, not merely sequence homology to a motif. Retain a supported secondary ligand-binding activity without inferring hyaluronan catalysis or a universal extracellular-matrix role. Supporting Evidence: |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: A cytoplasmic pool is supported independently of the predominant mitochondrial pool. Reason: Human HeLa localization in the CBF study supports cytoplasmic as well as nuclear p32, and UniProt records cytoplasm. The rat receptor-interaction study provides additional context. Retain this broad secondary location without treating transient overexpression as proof that the mature protein is uniformly cytosolic. |
| GO:0005739 mitochondrion | IDA PMID:19164550 Inhibition of RIG-I and MDA5-dependent antiviral response by... | ACCEPT | Summary: C1QBP associates with mitochondria in the antiviral-signaling context. Reason: Viral/dsRNA stimulation promotes an outer-mitochondrial-membrane C1QBP pool interacting with MAVS. This does not negate the predominant matrix pool or establish identical topology in unstimulated cells. Supporting Evidence: |
| GO:0009986 cell surface | IDA PMID:17881511 HCV core protein interaction with gC1q receptor inhibits Th1... | ACCEPT | Summary: Human dendritic cells display surface C1QBP that can be ligated. Reason: The study uses HCV core protein and anti-gC1qR ligation in human monocyte-derived dendritic cells. Surface availability is supported within this context; C1QBP is not presumed to be an autonomous transmembrane signaling receptor. Supporting Evidence: |
| GO:0016020 membrane | IDA PMID:8662673 Isolation and characterization of the kininogen-binding prot... | MODIFY | Summary: Endothelial C1QBP provides an extrinsic cell-surface ligand-binding site. Reason: The complete PMID:8662673 abstract identifies purified endothelial p33 as extrinsic membrane gC1qR, demonstrates HMW-kininogen binding and reports competition with ligand binding to EA.hy926 cells. This supports the cell-surface site more specifically than generic membrane association. GO:0009986 includes externally attached or loosely bound proteins, so the refinement does not imply a transmembrane segment or exclude intracellular pools. The full paper was not inspected in this follow-up. Proposed replacements: cell surface Supporting Evidence: |
| GO:0030449 regulation of complement activation | IDA PMID:8195709 Isolation, cDNA cloning, and overexpression of a 33-kD cell ... | ACCEPT | Summary: C1QBP can inhibit complement activation after binding C1q. Reason: Cell-derived and recombinant mature human protein inhibit complement-mediated sheep-erythrocyte lysis by human serum. C1QBP performs the binding/regulatory step, not complement-protease catalysis. The direction is specific to the tested biochemical conditions. Supporting Evidence: |
| GO:0030984 kininogen binding | IDA PMID:8662673 Isolation and characterization of the kininogen-binding prot... | MODIFY | Summary: C1QBP specifically binds high-molecular-weight kininogen. Reason: Purified endothelial p33 and recombinant protein bind high-molecular-weight but not low-molecular-weight kininogen, with D5H peptide competition. Refine the generic ligand-class annotation to the experimentally established HMW child. This binding/site-presentation role is not kininogen-cleaving activity. Proposed replacements: high molecular weight kininogen binding Supporting Evidence: PMID:8662673 p33 binds H-kininogen, but not L-kininogen |
| GO:0031690 adrenergic receptor binding | ISS GO_REF:0000024 | MODIFY | Summary: The transferred receptor-binding function can be specified as alpha-1B adrenergic receptor binding. Reason: The complete PMID:10409668 abstract describes a rat-liver cDNA-library interaction with the alpha-1B receptor cytoplasmic tail, deletion mapping to residues 369-378, and confirmation with full-length receptor in transfected COS-7 cells. GO:0031692 is the verified alpha-1B child of adrenergic receptor binding. Human UniProt records ADRA1B association by similarity. Refine this existing orthology-based assertion to the assayed subtype while preserving the rat donor and original evidence code; no independent human binding experiment, intrinsic receptor activity or general adrenergic-signaling core is claimed. This remains a secondary interaction outside the four core functions. Proposed replacements: alpha-1B adrenergic receptor binding |
| GO:0032689 negative regulation of type II interferon production | IDA PMID:17881511 HCV core protein interaction with gC1q receptor inhibits Th1... | KEEP AS NON CORE | Summary: gC1qR ligation suppresses downstream T-cell IFN-gamma production through dendritic-cell regulation. Reason: HCV core/anti-gC1qR treatment reduces human dendritic-cell IL-12 and consequent Th1 differentiation/IFN-gamma in coculture; IL-12 supplementation rescues the response. This supports non-cell-autonomous regulation, not direct cytokine synthesis or autonomous C1QBP signaling. Supporting Evidence: |
| GO:0032695 negative regulation of interleukin-12 production | IDA PMID:16177118 gC1q receptor ligation selectively down-regulates human IL-1... | KEEP AS NON CORE | Summary: gC1qR ligation reduces IL-12 production in the tested human myeloid-cell system. Reason: The primary abstract reports reduced TLR4-induced IL-12 after receptor crosslinking, dependent on PI3K activation. The published correction replaces the accidentally duplicated IL-6 panel in Figure 3c; the corrected image was not inspected. Retain the stated IL-12 result with this access bound rather than infer a withdrawal not present in the notice. Supporting Evidence: PMID:16177118 was dependent on PI3K activation |
| GO:0032695 negative regulation of interleukin-12 production | IDA PMID:17881511 HCV core protein interaction with gC1q receptor inhibits Th1... | KEEP AS NON CORE | Summary: gC1qR engagement reduces dendritic-cell IL-12 in the HCV-core context. Reason: The human monocyte-derived dendritic-cell experiment links gC1qR ligation to reduced TLR-induced IL-12 and altered T-cell differentiation. This is a defined regulatory role, not universal suppression across all immune cells. Supporting Evidence: |
| GO:0039534 negative regulation of MDA-5 signaling pathway | IDA PMID:19164550 Inhibition of RIG-I and MDA5-dependent antiviral response by... | KEEP AS NON CORE | Summary: C1QBP negatively regulates MDA-5 signaling through MAVS association. Reason: The primary study reports stimulus-dependent C1QBP/MAVS association at mitochondria and suppression of downstream antiviral signaling, with opposite effects after depletion. Retain the contextual MDA-5 regulation without assigning C1QBP the RNA sensor, GTPase or partner adaptor activity. Supporting Evidence: |
| GO:0039536 negative regulation of RIG-I signaling pathway | IDA PMID:19164550 Inhibition of RIG-I and MDA5-dependent antiviral response by... | KEEP AS NON CORE | Summary: C1QBP negatively regulates RIG-I signaling through MAVS association. Reason: The primary study reports stimulus-dependent C1QBP/MAVS association at mitochondria and suppression of downstream antiviral signaling, with opposite effects after depletion. Retain the contextual RIG-I regulation without assigning C1QBP the RNA sensor, GTPase or partner adaptor activity. Supporting Evidence: |
| GO:0042256 cytosolic ribosome assembly | IMP PMID:21536856 Splicing factor 2-associated protein p32 participates in rib... | KEEP AS NON CORE | Summary: C1QBP participates in nucleolar assembly/remodeling of cytosolic preribosomes. Reason: The source reports Nop52/fibrillarin interactions, association with pre-rRNA/preribosomal particles and processing delays after depletion. GO:0042256 includes nuclear/nucleolar assembly stages, so the nucleolar context is compatible with cytosolic ribosome assembly. This mechanism is distinct from mitochondrial translation. Supporting Evidence: |
| GO:0043491 phosphatidylinositol 3-kinase/protein kinase B signal transduction | IMP PMID:16177118 gC1q receptor ligation selectively down-regulates human IL-1... | KEEP AS NON CORE | Summary: gC1qR ligation engages the PI3K/Akt pathway in the tested immune-cell context. Reason: The source reports PI3K dependence and subsequent Akt phosphorylation during suppression of IL-12. C1QBP participates as the ligated surface component, not the PI3K or Akt catalytic enzyme. The corrected Figure 3c cytokine panel was not independently inspected. Supporting Evidence: |
| GO:0045785 positive regulation of cell adhesion | IMP PMID:20810993 An alternative role of C1q in cell migration and tissue remo... | KEEP AS NON CORE | Summary: C1QBP contributes to C1q-dependent trophoblast adhesion in the tested human system. Reason: Human trophoblast p33 and integrin blocking experiments support a receptor/co-receptor contribution to adhesion. The separate C1q-deficient mouse placental phenotype is not described as a human C1QBP knockout experiment. Supporting Evidence: |
| GO:0050687 negative regulation of defense response to virus | IMP PMID:19164550 Inhibition of RIG-I and MDA5-dependent antiviral response by... | KEEP AS NON CORE | Summary: C1QBP can suppress antiviral defense through the MAVS pathway. Reason: The source reports viral/dsRNA-dependent association and signaling suppression, with depletion enhancing antiviral responses. This supports contextual negative regulation rather than a constitutive whole-organism susceptibility claim. Supporting Evidence: |
| GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | IMP PMID:16177118 gC1q receptor ligation selectively down-regulates human IL-1... | KEEP AS NON CORE | Summary: gC1qR ligation positively regulates PI3K/Akt signaling in a defined cellular response. Reason: The primary study connects surface crosslinking to PI3K-dependent Akt phosphorylation and IL-12 suppression. This is regulation of the kinase pathway, not kinase activity of C1QBP. The correction concerns an IL-6 comparison panel; corrected image data remain uninspected. Supporting Evidence: |
| GO:0070131 positive regulation of mitochondrial translation | ISS GO_REF:0000024 | ACCEPT | Summary: C1QBP promotes mitochondrial protein synthesis through its RNA-associated role. Reason: Mouse loss/rescue and RNA-binding-mutant experiments connect C1QBP RNA engagement to mitochondrial translation. Human disease and the independent mouse-cell rescue study corroborate this conserved function. Retain participation in translation; do not infer catalytic translation-factor activity or ribosomal-subunit assembly solely from necessity. |
| GO:0090023 positive regulation of neutrophil chemotaxis | IDA PMID:9461517 C1q-mediated chemotaxis by human neutrophils: involvement of... | KEEP AS NON CORE | Summary: C1QBP promotes C1q-dependent human neutrophil chemotaxis. Reason: The accessible primary abstract reports enhanced C1q binding and increased C1q-mediated migration after gC1qR addition, with pharmacological pathway tests. This is genuine regulatory participation in the tested system, not an assertion that C1QBP itself is the chemoattractant receptor or G protein. Supporting Evidence: PMID:9461517 promoted C1q-mediated chemotaxis of neutrophils |
| GO:0097177 mitochondrial ribosome binding | ISS GO_REF:0000024 | ACCEPT | Summary: C1QBP associates with mitochondrial ribosomes. Reason: The primary study detects mitoribosomal proteins with human p32 in HeLa cells and confirms association with specific large- and small-subunit proteins in HeLa cells and mouse fibroblasts. This supports the existing mitochondrial-ribosome binding assertion without inventing a direct contact site or fixed stoichiometry. |
| GO:1900026 positive regulation of substrate adhesion-dependent cell spreading | IMP PMID:11859136 Cooperation of C1q receptors and integrins in C1q-mediated e... | KEEP AS NON CORE | Summary: C1QBP cooperates with integrins in C1q-dependent endothelial spreading. Reason: Human dermal microvascular endothelial-cell antibody inhibition supports gC1qR participation in adhesion/spreading. C1QBP does not need to span the membrane or independently transmit the entire signal; the cooperative role is retained as contextual. Supporting Evidence: |
| GO:1901165 positive regulation of trophoblast cell migration | IMP PMID:20810993 An alternative role of C1q in cell migration and tissue remo... | KEEP AS NON CORE | Summary: C1QBP contributes to C1q-dependent trophoblast migration. Reason: The human trophoblast antibody-blocking evidence supports a p33/integrin-dependent component of migration. Preserve that experiment separately from the paper’s C1q-deficient mouse placental phenotype; C1q loss is not C1QBP loss. Supporting Evidence: |
| GO:2000510 positive regulation of dendritic cell chemotaxis | IMP PMID:16140380 Chemotaxis of human monocyte-derived dendritic cells to comp... | KEEP AS NON CORE | Summary: C1QBP participates in C1q-induced migration of immature human dendritic cells. Reason: Anti-gC1qR/cC1qR antibodies abolish C1q-directed migration without abolishing the C5a control response. This supports source-specific receptor cooperation; the immature-cell context is not generalized to mature dendritic cells lacking the response. Supporting Evidence: |
| GO:0016020 membrane | IDA PMID:11290596 Expression and colocalization of cytokeratin 1 and urokinase... | MODIFY | Summary: C1QBP is exposed at the HUVEC cell surface in the contact-system study. Reason: The complete PMID:11290596 abstract reports flow-cytometric detection of gC1qR on HUVECs and inhibition of surface HK binding by anti-gC1qR. Refine generic membrane to the directly supported cell-surface location. CK1 and uPAR, but not gC1qR, colocalized in the reported microscopy; the surface finding therefore does not establish a constitutive three-protein complex. The full paper and images were not inspected in this follow-up. Proposed replacements: cell surface Supporting Evidence: |
| GO:0005886 plasma membrane | TAS PMID:8195709 Isolation, cDNA cloning, and overexpression of a 33-kD cell ... | ACCEPT | Summary: Cell-surface C1QBP is supported by the original human-protein study. Reason: Antibody recognition of surface molecules by flow/confocal analysis and the recombinant binding experiments support a plasma-membrane-associated pool. This is an extrinsic association, not a transmembrane topology claim. Supporting Evidence: |
| GO:0006955 immune response | TAS PMID:8195709 Isolation, cDNA cloning, and overexpression of a 33-kD cell ... | KEEP AS NON CORE | Summary: C1QBP participates in immune responses through ligand recognition and complement regulation. Reason: The original C1q-binding and hemolysis-inhibition evidence supports this broad process, while later ligand-dependent immune-cell studies add context. Retain the valid broad annotation as non-core rather than treating broadness alone as over-annotation. |
| GO:0005515 protein binding | IPI PMID:10831594 Protein kinase C [micro] is regulated by the multifunctional... | MODIFY | Summary: C1QBP associates with PRKD1, historically called PKC-mu. Reason: The PMID:10831594 abstract describes two-hybrid, fusion-protein precipitation and reciprocal co-immunoprecipitation for PKC-mu, whose source identifier Q15139 is PRKD1. Refine to serine/threonine kinase binding without classifying current PRKD1 as PRKCZ or assigning C1QBP the kinase reaction. The reported inhibition is substrate dependent and does not establish universal inhibition of all substrates. Proposed replacements: protein serine/threonine kinase binding |
| GO:0005515 protein binding | IPI PMID:16721827 CDC2L5, a Cdk-like kinase with RS domain, interacts with the... | MODIFY | Summary: C1QBP binds the serine/threonine kinase CDK13/CDC2L5. Reason: The complete PMID:16721827 abstract explicitly describes direct CDC2L5–p32 interaction and a splicing context. Refine to serine/threonine kinase binding. Preserve the original Q14004 versus Q14004-2 distinction; the latter exact product is independently represented in UniProt/IntAct, while the abstract does not resolve individual construct sequences. No kinase activity or isoform-exclusive function is assigned to C1QBP. Proposed replacements: protein serine/threonine kinase binding |
| GO:0005515 protein binding | IPI PMID:17486078 The autophagic inducer smARF interacts with and is stabilize... | KEEP AS NON CORE | Summary: C1QBP binds a short mitochondrial ARF product in the tested species. Reason: PMID:17486078 explicitly reports interaction with both human and murine smARF, mitochondrial colocalization and stabilization of the short form. Preserve human Q8N726. The abstract distinguishes short smARF from predominantly nucleolar full-length p19ARF. Do not generalize a short-product interaction to every ARF product or turn stabilization into C1QBP catalysis. |
| GO:0005515 protein binding | IPI PMID:28565870 C1QBP is upregulated in colon cancer and binds to apolipopro... | KEEP AS NON CORE | Summary: The exact C1QBP–LBR association is retained as a curated non-core edge. Reason: The source partner Q14739 is LBR, not APOA1 or YBX1. The original 28565870 target entry was not independently inspected; its accessible source describes C1QBP pulldown/MS with selected reverse-IP validation, prominently naming APOA1. The exact LBR pair is independently present in the UniProt/IntAct record and in the separate curated source row. Retain with curator deference without pretending APOA1 validation establishes the LBR experiment or assigning LBR enzymatic/chromatin activities to C1QBP. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The YBX1–C1QBP association is independently established and the curated source edge is retained. Reason: PMID:33961781 provides AP-MS co-complex networks in 293T/HCT116 cells; its exact C1QBP–YBX1 entry was not independently inspected. The original partner P67809 is retained with experimental curator deference. Independent targeted interaction evidence in PMID:23986595 and PMID:25497084 and the exact UniProt/IntAct edge support the claim. This does not pretend that the original target supplement or a direct binary interface was inspected, or assign YBX1’s RNA-binding/transcription activities to C1QBP. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The exact C1QBP–LBR association is retained as a curated non-core edge. Reason: The source partner Q14739 is LBR, not APOA1 or YBX1. The original 35271311 target entry was not independently inspected; its accessible source describes endogenous-tagging interaction profiling. The exact LBR pair is independently present in the UniProt/IntAct record and in the separate curated source row. Retain with curator deference without pretending APOA1 validation establishes the LBR experiment or assigning LBR enzymatic/chromatin activities to C1QBP. |
| GO:0005515 protein binding | IPI PMID:8710908 Identification of the zinc-dependent endothelial cell bindin... | MODIFY | Summary: C1QBP binds high-molecular-weight kininogen. Reason: The complete normal PMID:8710908 abstract explicitly reports zinc-dependent binding of high-molecular-weight kininogen to isolated and recombinant gC1qR. The official child term specifies this ligand class; preserve the P01042 source partner and do not assign kininogen cleavage. Proposed replacements: high molecular weight kininogen binding |
Loading supporting content…
Download this section (compressed HTML)Q: Which donor experiments support the rat-derived presynaptic active zone, glutamatergic synapse and GABA-ergic synapse assertions?
Q: Can the C1QBP–O00221 target records and validation experiments be inspected in the TNF/NF-kappaB and liver-interactome supplements?
Q: How are mitochondrial translation support and selective RNA clearance coordinated, and can purified C1QBP establish the affinity and structural basis of m5C-dependent RNA recognition independently of cellular partners?
Q: Which cell-surface partners couple extrinsic C1QBP ligand binding to intracellular signals in each physiological context?
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)