id: Q07021
gene_symbol: C1QBP
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  C1QBP (also known as p32, gC1qR, HABP1) is a multifunctional, multicompartmental
  acidic homotrimeric protein with a distinctive donut-shaped structure. It belongs
  to the MAM33 family and localizes predominantly to the mitochondrial matrix, with
  additional pools at the cell surface, cytoplasm, and nucleus. The two primary
  core functions are: (1) mitochondrial translation support through binding mitochondrial
  RNAs (including m5C-modified RNAs) and association with mitoribosomes, essential
  for OXPHOS and cellular metabolic fitness; and (2) cell-surface receptor function
  for complement C1q (gC1qR), binding the globular heads of C1q to modulate complement
  activation and immune signaling. Biallelic C1QBP mutations cause combined oxidative
  phosphorylation deficiency 33 (COXPD33), confirming its essential mitochondrial
  role.
existing_annotations:
# =====================
# IBA ANNOTATIONS (phylogenetically informed - generally reliable)
# =====================
  - term:
      id: GO:0005634
      label: nucleus
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        C1QBP has been documented in the nucleus in specific contexts, including
        nuclear localization with POLGARF (PMID:32958672), translocation during HCMV
        infection (deep research), and co-localization with CBF-B for transcriptional
        corepression (PMID:15243141).
      action: ACCEPT
      reason: >-
        Nuclear localization is well-documented though it represents a minor pool
        compared
        to mitochondria. The protein can function in the nucleus as a transcriptional
        corepressor and during viral infection.
      supported_by:
        - reference_id: PMID:15243141
          supporting_text: "Cellular localization by immunofluorescence staining revealed
            that p32 is present in the cell throughout the cytosol and nucleus, whereas
            CBF is present primarily in the nucleus. A portion of the p32 colocalizes
            with CBF-B in the nucleus."
        - reference_id: PMID:11083468
          supporting_text: "P32 (gClq-R) reactivity is also present... in nuclei of
            splenic lymphocytes"

        - reference_id: file:human/C1QBP/C1QBP-deep-research-falcon.md
          supporting_text: 'model: Edison Scientific Literature'
  - term:
      id: GO:0042256
      label: cytosolic ribosome assembly
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        C1QBP participates in ribosome biogenesis by regulating binding of Nop52
        and fibrillarin to preribosome particles (PMID:21536856). This involves
        the exchange of FBL for RRP1 in association with pre-ribosome particles.
      action: ACCEPT
      reason: >-
        Supported by direct experimental evidence showing C1QBP involvement in
        ribosome maturation processes, though this is likely a secondary function
        compared to mitochondrial roles.
      supported_by:
        - reference_id: PMID:21536856
          supporting_text: "Splicing factor 2-associated protein p32 participates
            in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin
            to preribosome particles."

  - term:
      id: GO:0001849
      label: complement component C1q complex binding
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        C1QBP was originally identified as the receptor for the globular heads of
        complement C1q (gC1qR). This is a core function supported by extensive
        literature (PMID:8195709, deep research from Ghebrehiwet 2024).
      action: ACCEPT
      reason: >-
        This is one of the two primary core functions of C1QBP. The protein binds
        specifically to the globular heads of C1q, modulating complement activation
        and immune signaling at the cell surface.
      supported_by:
        - reference_id: PMID:8195709
          supporting_text: "This protein designated gC1q-R, was first isolated from
            Raji cells and was found to bind to the globular \"heads\" of C1q molecules"

  - term:
      id: GO:0003714
      label: transcription corepressor activity
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        C1QBP interacts with NF-YB (CBF-B) and inhibits CBF-mediated transcription
        activation in vitro (PMID:15243141). This represents a non-core secondary
        function.
      action: KEEP_AS_NON_CORE
      reason: >-
        While experimentally supported, transcriptional corepression is not a
        core function of C1QBP. The primary functions are mitochondrial translation
        support and C1q receptor activity. This represents a secondary role
        when C1QBP is present in the nucleus.
      supported_by:
        - reference_id: PMID:15243141
          supporting_text: "p32 specifically inhibits CBF-mediated transcription activation.
            Altogether, our study identified p32 as a novel and specific corepressor
            of CBF-mediated transcription activation in vitro."

  - term:
      id: GO:0005886
      label: plasma membrane
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        C1QBP localizes to the plasma membrane as a peripheral membrane protein
        on the extracellular side, where it functions as the gC1qR receptor
        (PMID:8195709, PMID:8662673, PMID:12574814).
      action: ACCEPT
      reason: >-
        Cell surface localization is well-established and critical for the
        receptor function of C1QBP in binding C1q, kininogens, and other
        plasma proteins.
      supported_by:
        - reference_id: PMID:11083468
          supporting_text: "strong P32 (gClq-R) reactivity is also present... on the
            cell surface of microvascular endothelial cells in pancreas and kidney"

  - term:
      id: GO:0009986
      label: cell surface
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        C1QBP is present at the cell surface where it acts as a receptor for
        C1q and kininogens. Surface expression is enhanced upon platelet and
        monocyte activation (PMID:12574814).
      action: ACCEPT
      reason: >-
        Cell surface localization is essential for C1QBP's receptor functions
        in complement and kinin pathways.
      supported_by:
        - reference_id: PMID:11083468
          supporting_text: "strong P32 (gClq-R) reactivity is also present... on the
            cell surface of pancreatic acinar cells... on the cell surface of microvascular
            endothelial cells"

  - term:
      id: GO:0030449
      label: regulation of complement activation
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        C1QBP regulates complement activation by binding to the globular heads
        of C1q, thereby inhibiting C1 activation (PMID:8195709). This is a
        core function of the protein.
      action: ACCEPT
      reason: >-
        This is a well-established core function directly linked to C1QBP's
        role as the gC1qR receptor.
      supported_by:
        - reference_id: PMID:8195709
          supporting_text: "This protein designated gC1q-R, was first isolated from
            Raji cells and was found to bind to the globular \"heads\" of C1q molecules"

  - term:
      id: GO:0030984
      label: kininogen binding
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        C1QBP binds kininogen as part of its receptor function at the cell surface
        (PMID:8662673). In complex with KRT1, it serves as a high-affinity receptor
        for kininogen-1/HMWK.
      action: ACCEPT
      reason: >-
        Kininogen binding is a core receptor function of C1QBP, positioning it
        at the intersection of complement and kinin pathways.
      supported_by:
        - reference_id: PMID:8662673
          supporting_text: "Isolation and characterization of the kininogen-binding
            protein p33 from endothelial cells. Identity with the gC1q receptor."

  - term:
      id: GO:0048025
      label: negative regulation of mRNA splicing, via spliceosome
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        C1QBP (p32) regulates RNA splicing by inhibiting ASF/SF2 RNA binding
        and phosphorylation (PMID:10022843). This is a well-characterized
        secondary function.
      action: KEEP_AS_NON_CORE
      reason: >-
        While experimentally validated, splicing regulation is not a core function
        of C1QBP. The primary functions are mitochondrial translation support
        and complement receptor activity. C1QBP was originally co-purified with
        SF2 but its role is regulatory rather than essential.
      supported_by:
        - reference_id: PMID:10022843
          supporting_text: "p32 inhibits ASF/SF2 function as both a splicing enhancer
            and splicing repressor protein by preventing stable ASF/SF2 interaction
            with RNA... p32 functions as an ASF/SF2 inhibitory factor, regulating
            ASF/SF2 RNA binding and phosphorylation."

# =====================
# IEA ANNOTATIONS (keyword mappings - require careful review)
# =====================
  - term:
      id: GO:0002250
      label: adaptive immune response
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: >-
        Annotation based on UniProt keyword mapping (Adaptive immunity). C1QBP
        is involved in immune modulation through its C1q receptor function but
        is not directly part of adaptive immunity machinery.
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        C1QBP modulates immune responses through complement pathway but is not
        directly involved in adaptive immune response mechanisms. The annotation
        is too general and imprecise.

  - term:
      id: GO:0002376
      label: immune system process
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: >-
        Very broad term based on UniProt keyword. C1QBP participates in immune
        processes through complement modulation but this term is too general.
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        While technically accurate that C1QBP participates in immune processes
        through complement and kinin pathways, this annotation is too broad to
        be informative. More specific annotations (complement activation, C1q binding)
        better capture its function.

  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: IEA
    original_reference_id: GO_REF:0000044
    review:
      summary: >-
        C1QBP can be secreted by activated lymphocytes and released from tumor
        cells as a soluble form (deep research).
      action: ACCEPT
      reason: >-
        Secretion is documented in specific contexts (activated lymphocytes,
        tumor cells), supporting extracellular localization.

  - term:
      id: GO:0005634
      label: nucleus
    evidence_type: IEA
    original_reference_id: GO_REF:0000044
    review:
      summary: >-
        Duplicate of IBA annotation. Nuclear localization is documented.
      action: ACCEPT
      reason: >-
        Consistent with IBA annotation and experimental evidence. Nuclear pools
        exist under specific conditions.

  - term:
      id: GO:0005730
      label: nucleolus
    evidence_type: IEA
    original_reference_id: GO_REF:0000044
    review:
      summary: >-
        C1QBP localizes to the nucleolus when coexpressed with POLGARF (PMID:32958672).
        This is a conditional localization.
      action: ACCEPT
      reason: >-
        Nucleolar localization is supported by experimental evidence, though it
        requires interaction with POLGARF to prevent C1QBP maturation.

  - term:
      id: GO:0005737
      label: cytoplasm
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    review:
      summary: >-
        Cytoplasmic pools of C1QBP are documented (PMID:15243141, PMID:11083468).
      action: ACCEPT
      reason: >-
        Cytoplasmic localization is well-supported by immunostaining studies.
      supported_by:
        - reference_id: PMID:15243141
          supporting_text: "p32 is present in the cell throughout the cytosol and
            nucleus"

  - term:
      id: GO:0005759
      label: mitochondrial matrix
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    review:
      summary: >-
        C1QBP localizes predominantly to the mitochondrial matrix where it
        functions in mitochondrial translation (PMID:9305894, PMID:39019044).
      action: ACCEPT
      reason: >-
        Mitochondrial matrix localization is the primary location of C1QBP and
        is essential for its core function in supporting OXPHOS.

  - term:
      id: GO:0005886
      label: plasma membrane
    evidence_type: IEA
    original_reference_id: GO_REF:0000044
    review:
      summary: >-
        Duplicate annotation. Plasma membrane localization is well-documented.
      action: ACCEPT
      reason: >-
        Consistent with IBA annotation and receptor function.

  - term:
      id: GO:0006397
      label: mRNA processing
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: >-
        Based on UniProt mRNA processing keyword. C1QBP regulates splicing but
        this is a secondary function.
      action: KEEP_AS_NON_CORE
      reason: >-
        C1QBP regulates splicing through ASF/SF2 inhibition but this is not
        its core function. Acceptable but should be noted as non-core.

  - term:
      id: GO:0006915
      label: apoptotic process
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: >-
        This annotation is based on UniProt Apoptosis keyword. C1QBP interacts
        with HRK (PMID:15031724) and CDKN2A/smARF but it is NOT an evolved
        apoptotic factor. Its core functions are mitochondrial translation
        support and complement receptor activity.
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        C1QBP is over-annotated for apoptotic process. While it can interact
        with pro-apoptotic proteins like HRK (PMID:15031724), this represents
        a downstream/pleiotropic effect rather than a core evolved function.
        The protein's primary roles are mitochondrial RNA binding/translation
        support and C1q receptor function. Any effects on apoptosis are indirect.
      supported_by:
        - reference_id: PMID:15031724
          supporting_text: "small interfering RNA-mediated knockdown of p32 conferred
            protection against Hrk-induced apoptosis"
      additional_reference_ids:
        - deep-research

  - term:
      id: GO:0006958
      label: complement activation, classical pathway
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: >-
        C1QBP binds C1q and regulates complement activation. This is a core
        function.
      action: ACCEPT
      reason: >-
        Direct involvement in complement activation through C1q binding is a
        core function of C1QBP.

  - term:
      id: GO:0006974
      label: DNA damage response
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: >-
        C1QBP regulates homologous recombination by inhibiting MRE11 activity
        (PMID:31353207). In absence of DNA damage, it binds unphosphorylated
        MRE11 and RAD50, preventing MRN complex formation.
      action: KEEP_AS_NON_CORE
      reason: >-
        While C1QBP has a documented role in DNA damage response through MRE11
        regulation, this is not its primary evolved function. The mitochondrial
        and complement receptor roles are core.

  - term:
      id: GO:0008380
      label: RNA splicing
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: >-
        C1QBP regulates splicing through ASF/SF2 inhibition (PMID:10022843).
      action: KEEP_AS_NON_CORE
      reason: >-
        Splicing regulation is a secondary function. The protein was originally
        co-purified with SF2 but its primary roles are elsewhere.

  - term:
      id: GO:0042254
      label: ribosome biogenesis
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: >-
        C1QBP participates in ribosome biogenesis through regulation of
        nucleolar protein binding to pre-ribosome particles (PMID:21536856).
      action: KEEP_AS_NON_CORE
      reason: >-
        Ribosome biogenesis involvement is supported but is not the primary
        function. The mitochondrial translation role is more central.

  - term:
      id: GO:0045087
      label: innate immune response
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: >-
        C1QBP modulates innate immunity through complement C1q binding and
        regulation of RIG-I/MDA5 antiviral pathways (PMID:19164550).
      action: ACCEPT
      reason: >-
        Innate immune modulation is well-supported through complement pathway
        and antiviral response regulation.

# =====================
# IPI PROTEIN BINDING ANNOTATIONS
# =====================
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:10831594
    review:
      summary: >-
        Generic protein binding annotation from interaction with protein kinase C.
        The annotation is uninformative.
      action: REMOVE
      reason: >-
        'Protein binding' is too general and uninformative. More specific MF
        terms should be used when available (e.g., protein kinase C binding).

      supported_by:
        - reference_id: PMID:10831594
          supporting_text: >-
            is regulated by the multifunctional chaperon protein
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:11086025
    review:
      summary: >-
        Interaction with HCV core protein documented. Uninformative generic term.
      action: REMOVE
      reason: >-
        'Protein binding' is uninformative. The specific interaction with viral
        proteins could be captured with more specific terms.

      supported_by:
        - reference_id: PMID:11086025
          supporting_text: Interaction between complement receptor gC1qR and 
            hepatitis C virus core protein inhibits T-lymphocyte proliferation.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:12034482
    review:
      summary: >-
        Interaction with Rubella virus capsid protein.
      action: REMOVE
      reason: >-
        Generic protein binding annotation is uninformative.

      supported_by:
        - reference_id: PMID:12034482
          supporting_text: The N-terminal conserved domain of rubella virus 
            capsid interacts with the C-terminal region of cellular p32 and 
            overexpression of p32 enhances the viral infectivity.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:12220632
    review:
      summary: >-
        Interaction with MT1-MMP cytoplasmic tail.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:12220632
          supporting_text: The cytoplasmic tail peptide sequence of membrane 
            type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a
            compartment-specific chaperone-like regulatory protein.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:14743216
    review:
      summary: >-
        High-throughput mapping study.
      action: REMOVE
      reason: >-
        Generic protein binding from HTP study is uninformative.

      supported_by:
        - reference_id: PMID:14743216
          supporting_text: A physical and functional map of the human 
            TNF-alpha/NF-kappa B signal transduction pathway.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:15031724
    review:
      summary: >-
        Interaction with HRK (BH3-only protein).
      action: REMOVE
      reason: >-
        Generic protein binding. The interaction with HRK is documented but
        better captured by specific process terms.
      supported_by:
        - reference_id: PMID:15031724
          supporting_text: "verified specific interaction and colocalization of Hrk
            and p32, both of which depended on the presence of the highly conserved
            C-terminal region of p32"

  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:16721827
    review:
      summary: >-
        Interaction with CDK13 affecting splicing.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:16721827
          supporting_text: CDC2L5, a Cdk-like kinase with RS domain, interacts 
            with the ASF/SF2-associated protein p32 and affects splicing in 
            vivo.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:17486078
    review:
      summary: >-
        Interaction with CDKN2A/smARF.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:17486078
          supporting_text: May 7. The autophagic inducer smARF interacts with 
            and is stabilized by the mitochondrial p32 protein.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:18676636
    review:
      summary: >-
        Interaction with FOXC1.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:18676636
          supporting_text: Epub 2008 Aug 1. Human p32 is a novel 
            FOXC1-interacting protein that regulates FOXC1 transcriptional 
            activity in ocular cells.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:19164550
    review:
      summary: >-
        Interaction with MAVS for antiviral response regulation.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative. The functional consequence
        (RIG-I/MDA5 pathway inhibition) is better captured by specific BP terms.

      supported_by:
        - reference_id: PMID:19164550
          supporting_text: Inhibition of RIG-I and MDA5-dependent antiviral 
            response by gC1qR at mitochondria.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:21653829
    review:
      summary: >-
        HTP protein interaction study.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:21653829
          supporting_text: Protein interactome reveals converging molecular 
            pathways among autism disorders.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:21988832
    review:
      summary: >-
        HTP liver interactome study.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:21988832
          supporting_text: Toward an understanding of the protein interaction 
            network of the human liver.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:22118625
    review:
      summary: >-
        Interaction study with YB-1 and related proteins.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:22118625
          supporting_text: NONO and RALY proteins are required for YB-1 
            oxaliplatin induced resistance in colon adenocarcinoma cell lines.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:22238231
    review:
      summary: >-
        Interaction with Rubella virus P150 replicase.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:22238231
          supporting_text: Jan 13. Binding of cellular p32 protein to the 
            rubella virus P150 replicase protein via PxxPxR motifs.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:23986595
    review:
      summary: >-
        Interaction with YB-1 in HCV replication context.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:23986595
          supporting_text: A host YB-1 ribonucleoprotein complex is hijacked by 
            hepatitis C virus for the control of NS3-dependent particle 
            production.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:24955142
    review:
      summary: >-
        Panviral proteome interaction study.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:24955142
          supporting_text: 'Exploration of panviral proteome: high-throughput cloning
            and functional implications in virus-host interactions.'
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:25497084
    review:
      summary: >-
        Interaction with YBX1 in renal cell carcinoma.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:25497084
          supporting_text: C1QBP negatively regulates the activation of 
            oncoprotein YBX1 in the renal cell carcinoma as revealed by 
            interactomics analysis.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:25852190
    review:
      summary: >-
        TRAIL-induced apoptosis interactome study.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:25852190
          supporting_text: Integrative analysis of kinase networks in 
            TRAIL-induced apoptosis provides a source of potential targets for 
            combination therapy.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:26184334
    review:
      summary: >-
        RNA helicase interactome study.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:26184334
          supporting_text: 'Comprehensive Protein Interactome Analysis of a Key RNA
            Helicase: Detection of Novel Stress Granule Proteins.'
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:26816005
    review:
      summary: >-
        Interaction with DUX4.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:26816005
          supporting_text: eCollection 2016. Homologous Transcription Factors 
            DUX4 and DUX4c Associate with Cytoplasmic Proteins during Muscle 
            Differentiation.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:27499296
    review:
      summary: >-
        Mitochondrial protein interaction mapping.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:27499296
          supporting_text: 2016 Aug 4. Mitochondrial Protein Interaction Mapping
            Identifies Regulators of Respiratory Chain Function.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:28514442
    review:
      summary: >-
        Human interactome architecture study.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:28514442
          supporting_text: Architecture of the human interactome defines protein
            communities and disease networks.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:28565870
    review:
      summary: >-
        Interaction with apolipoprotein A-I in colon cancer.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:28565870
          supporting_text: Mar 21. C1QBP is upregulated in colon cancer and 
            binds to apolipoprotein A-I.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:31980649
    review:
      summary: >-
        EGFR network rewiring study.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:31980649
          supporting_text: Extensive rewiring of the EGFR network in colorectal 
            cancer cells expressing transforming levels of KRAS(G13D).
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:32296183
    review:
      summary: >-
        Human binary protein interactome reference map.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:32296183
          supporting_text: Apr 8. A reference map of the human binary protein 
            interactome.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:33961781
    review:
      summary: >-
        Dual proteome-scale network study.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:33961781
          supporting_text: 2021 May 6. Dual proteome-scale networks reveal 
            cell-specific remodeling of the human interactome.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:35271311
    review:
      summary: >-
        OpenCell endogenous tagging study.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:35271311
          supporting_text: '2022 Mar 11. OpenCell: Endogenous tagging for the cartography
            of human cellular organization.'
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:36882853
    review:
      summary: >-
        DUX4c interaction study in muscle regeneration.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:36882853
          supporting_text: The double homeodomain protein DUX4c is associated 
            with regenerating muscle fibers and RNA-binding proteins.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:8710908
    review:
      summary: >-
        Interaction with factor XII and kininogen.
      action: REMOVE
      reason: >-
        Generic protein binding. The kininogen binding is better captured by
        GO:0030984 (kininogen binding).

      supported_by:
        - reference_id: PMID:8710908
          supporting_text: 'Identification of the zinc-dependent endothelial cell
            binding protein for high molecular weight kininogen and factor XII: identity
            with the receptor that binds to the globular "heads" of C1q (gC1q-R).'
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:8900153
    review:
      summary: >-
        Interaction with vitronectin.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

# =====================
# IEA ENSEMBL COMPARA ANNOTATIONS
# =====================
      supported_by:
        - reference_id: PMID:8900153
          supporting_text: The binding protein for globular heads of complement 
            C1q, gC1qR.
  - term:
      id: GO:0001849
      label: complement component C1q complex binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000107
    review:
      summary: >-
        Duplicate of IBA annotation. C1q binding is a core function.
      action: ACCEPT
      reason: >-
        Core function supported by multiple evidence lines.

  - term:
      id: GO:0005080
      label: protein kinase C binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000107
    review:
      summary: >-
        C1QBP interacts with protein kinase C (PMID:10831594). This represents
        a specific interaction.
      action: ACCEPT
      reason: >-
        Specific binding annotation is more informative than generic protein binding.

  - term:
      id: GO:0005615
      label: extracellular space
    evidence_type: IEA
    original_reference_id: GO_REF:0000107
    review:
      summary: >-
        C1QBP can be secreted and found in extracellular space.
      action: ACCEPT
      reason: >-
        Secretion is documented for activated lymphocytes and tumor cells.

  - term:
      id: GO:0031690
      label: adrenergic receptor binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000107
    review:
      summary: >-
        C1QBP interacts with alpha-1B adrenergic receptor (ADRA1B) based on
        ortholog transfer from rat.
      action: UNDECIDED
      reason: >-
        This annotation is based on ortholog transfer. The functional significance
        of adrenergic receptor binding for C1QBP is unclear and not validated
        in human.

  - term:
      id: GO:0048786
      label: presynaptic active zone
    evidence_type: IEA
    original_reference_id: GO_REF:0000107
    review:
      summary: >-
        Localization to presynaptic active zone based on rat ortholog data.
      action: UNDECIDED
      reason: >-
        This neuronal localization is based on ortholog transfer and not
        validated in human. The functional relevance is unclear.

  - term:
      id: GO:0098978
      label: glutamatergic synapse
    evidence_type: IEA
    original_reference_id: GO_REF:0000107
    review:
      summary: >-
        Localization to glutamatergic synapse based on rat ortholog data.
      action: UNDECIDED
      reason: >-
        Synaptic localization based on ortholog transfer. Not validated in human.

  - term:
      id: GO:0098982
      label: GABA-ergic synapse
    evidence_type: IEA
    original_reference_id: GO_REF:0000107
    review:
      summary: >-
        Localization to GABAergic synapse based on rat ortholog data.
      action: UNDECIDED
      reason: >-
        Synaptic localization based on ortholog transfer. Not validated in human.

# =====================
# IDA EXPERIMENTAL ANNOTATIONS (HPA immunofluorescence)
# =====================
  - term:
      id: GO:0005739
      label: mitochondrion
    evidence_type: IDA
    original_reference_id: GO_REF:0000052
    review:
      summary: >-
        Mitochondrial localization confirmed by HPA immunofluorescence.
        This is the predominant localization of C1QBP.
      action: ACCEPT
      reason: >-
        Mitochondrial localization is the primary location and essential for
        the core mitochondrial translation support function.
      supported_by:
        - reference_id: PMID:11083468
          supporting_text: "Immunogold labeling of Raji lymphoma, CHO, human fibroblasts,
            HeLa and B-SC-1 cells shows reactivity primarily within mitochondria."

  - term:
      id: GO:0005886
      label: plasma membrane
    evidence_type: IDA
    original_reference_id: GO_REF:0000052
    review:
      summary: >-
        Plasma membrane localization confirmed by HPA immunofluorescence.
      action: ACCEPT
      reason: >-
        Consistent with receptor function at cell surface.

# =====================
# IDA EXPERIMENTAL ANNOTATIONS (from specific publications)
# =====================
  - term:
      id: GO:0000957
      label: mitochondrial RNA catabolic process
    evidence_type: IDA
    original_reference_id: PMID:39019044
    review:
      summary: >-
        C1QBP recognizes m5C-modified mitochondrial RNAs and promotes their
        degradation via recruitment of the mitochondrial degradosome complex.
        This is a recently discovered core function.
      action: ACCEPT
      reason: >-
        This 2024 study reveals a key mechanism by which C1QBP regulates
        mitochondrial RNA quality control, directly supporting its core
        mitochondrial function.

      supported_by:
        - reference_id: PMID:39019044
          supporting_text: Epub 2024 Jul 16. RNA 5-methylcytosine marks 
            mitochondrial double-stranded RNAs for degradation and cytosolic 
            release.
  - term:
      id: GO:0005759
      label: mitochondrial matrix
    evidence_type: IDA
    original_reference_id: PMID:39019044
    review:
      summary: >-
        Mitochondrial matrix localization confirmed in this 2024 study.
      action: ACCEPT
      reason: >-
        Consistent with other evidence for predominant mitochondrial matrix
        localization.

      supported_by:
        - reference_id: PMID:39019044
          supporting_text: Epub 2024 Jul 16. RNA 5-methylcytosine marks 
            mitochondrial double-stranded RNAs for degradation and cytosolic 
            release.
  - term:
      id: GO:0062153
      label: C5-methylcytidine-containing RNA reader activity
    evidence_type: IDA
    original_reference_id: PMID:39019044
    review:
      summary: >-
        C1QBP specifically recognizes and binds m5C-modified mitochondrial RNAs.
        This is a newly discovered molecular function that is central to its
        mitochondrial role.
      action: ACCEPT
      reason: >-
        This represents a specific and informative molecular function directly
        linked to C1QBP's core mitochondrial role.

      supported_by:
        - reference_id: PMID:39019044
          supporting_text: Epub 2024 Jul 16. RNA 5-methylcytosine marks 
            mitochondrial double-stranded RNAs for degradation and cytosolic 
            release.
  - term:
      id: GO:0005739
      label: mitochondrion
    evidence_type: HTP
    original_reference_id: PMID:34800366
    review:
      summary: >-
        High-throughput quantitative mitochondrial proteome study confirms
        C1QBP as a high-confidence mitochondrial protein.
      action: ACCEPT
      reason: >-
        Consistent with extensive evidence for mitochondrial localization.

      supported_by:
        - reference_id: PMID:34800366
          supporting_text: Epub 2021 Nov 19. Quantitative high-confidence human 
            mitochondrial proteome and its dynamics in cellular context.
  - term:
      id: GO:0004857
      label: enzyme inhibitor activity
    evidence_type: IDA
    original_reference_id: PMID:31353207
    review:
      summary: >-
        C1QBP inhibits MRE11 nuclease activity by binding unphosphorylated
        MRE11 and preventing MRN complex formation.
      action: KEEP_AS_NON_CORE
      reason: >-
        While experimentally demonstrated, this enzyme inhibitor activity
        related to DNA repair is not a core function of C1QBP.

      supported_by:
        - reference_id: PMID:31353207
          supporting_text: Epub 2019 Jul 25. C1QBP Promotes Homologous 
            Recombination by Stabilizing MRE11 and Controlling the Assembly and 
            Activation of MRE11/RAD50/NBS1 Complex.
  - term:
      id: GO:2000042
      label: negative regulation of double-strand break repair via homologous 
        recombination
    evidence_type: IDA
    original_reference_id: PMID:31353207
    review:
      summary: >-
        C1QBP negatively regulates HR by inhibiting MRN complex formation
        and MRE11 activity in the absence of DNA damage.
      action: KEEP_AS_NON_CORE
      reason: >-
        DNA repair regulation is not a core function of C1QBP. The mitochondrial
        and complement receptor roles are primary.

      supported_by:
        - reference_id: PMID:31353207
          supporting_text: Epub 2019 Jul 25. C1QBP Promotes Homologous 
            Recombination by Stabilizing MRE11 and Controlling the Assembly and 
            Activation of MRE11/RAD50/NBS1 Complex.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:32958672
    review:
      summary: >-
        Interaction with POLGARF leading to nucleolar localization.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

# =====================
# TAS REACTOME ANNOTATIONS
# =====================
      supported_by:
        - reference_id: PMID:32958672
          supporting_text: Unusually efficient CUG initiation of an overlapping 
            reading frame in POLG mRNA yields novel protein POLGARF.
  - term:
      id: GO:0005759
      label: mitochondrial matrix
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-9645692
    review:
      summary: >-
        Reactome annotation for C1QBP promoting p14ARF translocation to
        mitochondrial matrix.
      action: ACCEPT
      reason: >-
        Consistent with mitochondrial matrix localization.

  - term:
      id: GO:0005829
      label: cytosol
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-9645692
    review:
      summary: >-
        Reactome annotation for cytosolic pool of C1QBP involved in p14ARF
        pathway.
      action: ACCEPT
      reason: >-
        Cytosolic localization is documented.

  - term:
      id: GO:0005829
      label: cytosol
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-9645694
    review:
      summary: >-
        Duplicate cytosol annotation from Reactome.
      action: ACCEPT
      reason: >-
        Consistent with other evidence.

  - term:
      id: GO:0005829
      label: cytosol
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-9645766
    review:
      summary: >-
        Duplicate cytosol annotation from Reactome.
      action: ACCEPT
      reason: >-
        Consistent with other evidence.

  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:18191643
    review:
      summary: >-
        Interaction with PLEKHN1.
      action: REMOVE
      reason: >-
        Generic protein binding is uninformative.

      supported_by:
        - reference_id: PMID:18191643
          supporting_text: Novel tyrosine phosphorylated and cardiolipin-binding
            protein CLPABP functions as mitochondrial RNA granule.
  - term:
      id: GO:0005759
      label: mitochondrial matrix
    evidence_type: IDA
    original_reference_id: PMID:9305894
    review:
      summary: >-
        Original demonstration of C1QBP mitochondrial matrix localization
        and importance for OXPHOS maintenance.
      action: ACCEPT
      reason: >-
        This landmark study established the mitochondrial function of C1QBP.

      supported_by:
        - reference_id: PMID:9305894
          supporting_text: p32 protein, a splicing factor 2-associated protein, 
            is localized in mitochondrial matrix and is functionally important 
            in maintaining oxidative phosphorylation.
  - term:
      id: GO:0005739
      label: mitochondrion
    evidence_type: IDA
    original_reference_id: PMID:11083468
    review:
      summary: >-
        Immunogold electron microscopy confirming primary mitochondrial
        localization with specific extramitochondrial locations.
      action: ACCEPT
      reason: >-
        Strong experimental support for predominant mitochondrial localization.
      supported_by:
        - reference_id: PMID:11083468
          supporting_text: "Immunogold labeling of Raji lymphoma, CHO, human fibroblasts,
            HeLa and B-SC-1 cells shows reactivity primarily within mitochondria."

  - term:
      id: GO:0005886
      label: plasma membrane
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-158218
    review:
      summary: >-
        Reactome annotation for kinin pathway at plasma membrane.
      action: ACCEPT
      reason: >-
        Plasma membrane localization for receptor function is well-established.

  - term:
      id: GO:0005886
      label: plasma membrane
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-158251
    review:
      summary: >-
        Duplicate Reactome annotation for kinin pathway.
      action: ACCEPT
      reason: >-
        Consistent with other evidence.

  - term:
      id: GO:0005886
      label: plasma membrane
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-158311
    review:
      summary: >-
        Duplicate Reactome annotation for kinin pathway.
      action: ACCEPT
      reason: >-
        Consistent with other evidence.

  - term:
      id: GO:0005886
      label: plasma membrane
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-158313
    review:
      summary: >-
        Reactome annotation for factor XII activation.
      action: ACCEPT
      reason: >-
        Consistent with C1QBP role in kinin/complement pathways.

  - term:
      id: GO:0005886
      label: plasma membrane
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-158354
    review:
      summary: >-
        Reactome annotation for kininogen binding.
      action: ACCEPT
      reason: >-
        Consistent with receptor function.

# =====================
# IDA EXPERIMENTAL ANNOTATIONS (more publications)
# =====================
  - term:
      id: GO:0000122
      label: negative regulation of transcription by RNA polymerase II
    evidence_type: IDA
    original_reference_id: PMID:15243141
    review:
      summary: >-
        C1QBP inhibits CBF/NF-Y mediated transcription activation in vitro.
      action: KEEP_AS_NON_CORE
      reason: >-
        Transcriptional regulation is a secondary function when C1QBP is
        present in the nucleus. Not a core function.
      supported_by:
        - reference_id: PMID:15243141
          supporting_text: "p32 specifically inhibits CBF-mediated transcription activation"

  - term:
      id: GO:0003714
      label: transcription corepressor activity
    evidence_type: IDA
    original_reference_id: PMID:15243141
    review:
      summary: >-
        C1QBP acts as transcriptional corepressor for CBF/NF-Y.
      action: KEEP_AS_NON_CORE
      reason: >-
        Secondary function in nucleus. Not a core function.
      supported_by:
        - reference_id: PMID:15243141
          supporting_text: "our study identified p32 as a novel and specific corepressor
            of CBF-mediated transcription activation in vitro"

  - term:
      id: GO:0005634
      label: nucleus
    evidence_type: IDA
    original_reference_id: PMID:15243141
    review:
      summary: >-
        Nuclear localization demonstrated by immunofluorescence.
      action: ACCEPT
      reason: >-
        Consistent with other evidence for nuclear pools.
      supported_by:
        - reference_id: PMID:15243141
          supporting_text: "p32 is present in the cell throughout the cytosol and
            nucleus"

  - term:
      id: GO:0005829
      label: cytosol
    evidence_type: IDA
    original_reference_id: PMID:15243141
    review:
      summary: >-
        Cytosolic localization demonstrated by immunofluorescence.
      action: ACCEPT
      reason: >-
        Consistent with other evidence.

      supported_by:
        - reference_id: PMID:15243141
          supporting_text: Human p32, interacts with B subunit of the 
            CCAAT-binding factor, CBF/NF-Y, and inhibits CBF-mediated 
            transcription activation in vitro.
  - term:
      id: GO:0008134
      label: transcription factor binding
    evidence_type: IDA
    original_reference_id: PMID:15243141
    review:
      summary: >-
        C1QBP binds to NF-YB (CBF-B) transcription factor subunit.
      action: KEEP_AS_NON_CORE
      reason: >-
        Transcription factor binding is related to the secondary transcriptional
        corepressor function.

      supported_by:
        - reference_id: PMID:15243141
          supporting_text: Human p32, interacts with B subunit of the 
            CCAAT-binding factor, CBF/NF-Y, and inhibits CBF-mediated 
            transcription activation in vitro.
  - term:
      id: GO:0043065
      label: positive regulation of apoptotic process
    evidence_type: IMP
    original_reference_id: PMID:15031724
    review:
      summary: >-
        C1QBP interaction with HRK leads to positive regulation of apoptosis
        when HRK is expressed. However, p32 knockdown actually protected
        against Hrk-induced apoptosis, suggesting p32 facilitates HRK-mediated
        apoptosis rather than being a direct apoptotic factor.
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        This annotation overstates C1QBP's role in apoptosis. C1QBP is not
        an evolved apoptotic factor. It interacts with HRK and may facilitate
        HRK-induced apoptosis in specific contexts, but its core functions
        are mitochondrial translation support and complement receptor activity.
        Any apoptotic effects are downstream/pleiotropic.
      supported_by:
        - reference_id: PMID:15031724
          supporting_text: "small interfering RNA-mediated knockdown of p32 conferred
            protection against Hrk-induced apoptosis"

  - term:
      id: GO:0048025
      label: negative regulation of mRNA splicing, via spliceosome
    evidence_type: IDA
    original_reference_id: PMID:10022843
    review:
      summary: >-
        C1QBP inhibits ASF/SF2 RNA binding and phosphorylation, negatively
        regulating splicing.
      action: KEEP_AS_NON_CORE
      reason: >-
        Splicing regulation is a well-documented secondary function but not
        the core role of C1QBP.
      supported_by:
        - reference_id: PMID:10022843
          supporting_text: "p32 inhibits ASF/SF2 function as both a splicing enhancer
            and splicing repressor protein by preventing stable ASF/SF2 interaction
            with RNA"

  - term:
      id: GO:0001849
      label: complement component C1q complex binding
    evidence_type: IDA
    original_reference_id: PMID:8195709
    review:
      summary: >-
        Original identification of C1QBP as gC1qR, binding globular heads of C1q.
      action: ACCEPT
      reason: >-
        This is a core function established in the seminal paper.

      supported_by:
        - reference_id: PMID:8195709
          supporting_text: Isolation, cDNA cloning, and overexpression of a 
            33-kD cell surface glycoprotein that binds to the globular "heads" 
            of C1q.
  - term:
      id: GO:0003729
      label: mRNA binding
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        mRNA binding inferred from mouse ortholog. C1QBP binds mitochondrial
        RNAs to support translation.
      action: ACCEPT
      reason: >-
        RNA binding is part of the core mitochondrial translation support function.

  - term:
      id: GO:0005540
      label: hyaluronic acid binding
    evidence_type: IDA
    original_reference_id: PMID:8567680
    review:
      summary: >-
        C1QBP (HABP1) was identified as a hyaluronic acid-binding protein.
      action: KEEP_AS_NON_CORE
      reason: >-
        Hyaluronic acid binding is documented but not a core function.
        May be relevant in specific extracellular contexts.

      supported_by:
        - reference_id: PMID:8567680
          supporting_text: Molecular cloning of human fibroblast hyaluronic 
            acid-binding protein confirms its identity with P-32, a protein 
            co-purified with splicing factor SF2.
  - term:
      id: GO:0005737
      label: cytoplasm
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        Cytoplasmic localization from ortholog inference.
      action: ACCEPT
      reason: >-
        Consistent with experimental evidence for cytoplasmic pools.

  - term:
      id: GO:0005739
      label: mitochondrion
    evidence_type: IDA
    original_reference_id: PMID:19164550
    review:
      summary: >-
        Mitochondrial localization confirmed in context of antiviral response
        study (MAVS interaction).
      action: ACCEPT
      reason: >-
        Consistent with predominant mitochondrial localization.

      supported_by:
        - reference_id: PMID:19164550
          supporting_text: Inhibition of RIG-I and MDA5-dependent antiviral 
            response by gC1qR at mitochondria.
  - term:
      id: GO:0009986
      label: cell surface
    evidence_type: IDA
    original_reference_id: PMID:17881511
    review:
      summary: >-
        Cell surface localization in context of HCV core protein interaction
        study.
      action: ACCEPT
      reason: >-
        Cell surface localization is essential for receptor function.

      supported_by:
        - reference_id: PMID:17881511
          supporting_text: HCV core protein interaction with gC1q receptor 
            inhibits Th1 differentiation of CD4+ T cells via suppression of 
            dendritic cell IL-12 production.
  - term:
      id: GO:0016020
      label: membrane
    evidence_type: IDA
    original_reference_id: PMID:8662673
    review:
      summary: >-
        Membrane association documented in kininogen binding study.
      action: ACCEPT
      reason: >-
        Consistent with peripheral membrane protein localization.

      supported_by:
        - reference_id: PMID:8662673
          supporting_text: Isolation and characterization of the 
            kininogen-binding protein p33 from endothelial cells.
  - term:
      id: GO:0030449
      label: regulation of complement activation
    evidence_type: IDA
    original_reference_id: PMID:8195709
    review:
      summary: >-
        C1QBP regulates complement by binding C1q globular heads.
      action: ACCEPT
      reason: >-
        Core function established in seminal paper.

      supported_by:
        - reference_id: PMID:8195709
          supporting_text: Isolation, cDNA cloning, and overexpression of a 
            33-kD cell surface glycoprotein that binds to the globular "heads" 
            of C1q.
  - term:
      id: GO:0030984
      label: kininogen binding
    evidence_type: IDA
    original_reference_id: PMID:8662673
    review:
      summary: >-
        C1QBP/p33 identified as kininogen-binding protein on endothelial cells.
      action: ACCEPT
      reason: >-
        Kininogen binding is a core receptor function.

      supported_by:
        - reference_id: PMID:8662673
          supporting_text: Isolation and characterization of the 
            kininogen-binding protein p33 from endothelial cells.
  - term:
      id: GO:0031690
      label: adrenergic receptor binding
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        Adrenergic receptor binding from ortholog inference.
      action: UNDECIDED
      reason: >-
        Functional significance in human is unclear.

  - term:
      id: GO:0032689
      label: negative regulation of type II interferon production
    evidence_type: IDA
    original_reference_id: PMID:17881511
    review:
      summary: >-
        C1QBP (via HCV core protein interaction) suppresses IFN-gamma production.
      action: KEEP_AS_NON_CORE
      reason: >-
        Immune modulation is documented but represents downstream effect
        of C1QBP's receptor function rather than a core role.

      supported_by:
        - reference_id: PMID:17881511
          supporting_text: HCV core protein interaction with gC1q receptor 
            inhibits Th1 differentiation of CD4+ T cells via suppression of 
            dendritic cell IL-12 production.
  - term:
      id: GO:0032695
      label: negative regulation of interleukin-12 production
    evidence_type: IDA
    original_reference_id: PMID:16177118
    review:
      summary: >-
        gC1qR ligation downregulates IL-12 production through PI3K pathway.
      action: KEEP_AS_NON_CORE
      reason: >-
        IL-12 regulation is a downstream consequence of receptor function.

      supported_by:
        - reference_id: PMID:16177118
          supporting_text: gC1q receptor ligation selectively down-regulates 
            human IL-12 production through activation of the phosphoinositide 
            3-kinase pathway.
  - term:
      id: GO:0032695
      label: negative regulation of interleukin-12 production
    evidence_type: IDA
    original_reference_id: PMID:17881511
    review:
      summary: >-
        Duplicate annotation for IL-12 regulation.
      action: KEEP_AS_NON_CORE
      reason: >-
        Same as above - downstream effect of receptor function.

      supported_by:
        - reference_id: PMID:17881511
          supporting_text: HCV core protein interaction with gC1q receptor 
            inhibits Th1 differentiation of CD4+ T cells via suppression of 
            dendritic cell IL-12 production.
  - term:
      id: GO:0039534
      label: negative regulation of MDA-5 signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:19164550
    review:
      summary: >-
        C1QBP inhibits MDA5 (IFIH1) antiviral signaling through MAVS interaction.
      action: KEEP_AS_NON_CORE
      reason: >-
        Antiviral response modulation is a documented secondary function.

      supported_by:
        - reference_id: PMID:19164550
          supporting_text: Inhibition of RIG-I and MDA5-dependent antiviral 
            response by gC1qR at mitochondria.
  - term:
      id: GO:0039536
      label: negative regulation of RIG-I signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:19164550
    review:
      summary: >-
        C1QBP inhibits RIG-I antiviral signaling through MAVS interaction.
      action: KEEP_AS_NON_CORE
      reason: >-
        Antiviral response modulation is a documented secondary function.

      supported_by:
        - reference_id: PMID:19164550
          supporting_text: Inhibition of RIG-I and MDA5-dependent antiviral 
            response by gC1qR at mitochondria.
  - term:
      id: GO:0042256
      label: cytosolic ribosome assembly
    evidence_type: IMP
    original_reference_id: PMID:21536856
    review:
      summary: >-
        C1QBP participates in ribosome biogenesis by regulating nucleolar
        protein binding to pre-ribosome particles.
      action: KEEP_AS_NON_CORE
      reason: >-
        Ribosome biogenesis is a secondary function.

      supported_by:
        - reference_id: PMID:21536856
          supporting_text: Epub 2011 May 2. Splicing factor 2-associated protein
            p32 participates in ribosome biogenesis by regulating the binding of
            Nop52 and fibrillarin to preribosome particles.
  - term:
      id: GO:0043491
      label: phosphatidylinositol 3-kinase/protein kinase B signal transduction
    evidence_type: IMP
    original_reference_id: PMID:16177118
    review:
      summary: >-
        gC1qR ligation activates PI3K-AKT pathway.
      action: KEEP_AS_NON_CORE
      reason: >-
        PI3K signaling is a downstream consequence of receptor ligation.

      supported_by:
        - reference_id: PMID:16177118
          supporting_text: gC1q receptor ligation selectively down-regulates 
            human IL-12 production through activation of the phosphoinositide 
            3-kinase pathway.
  - term:
      id: GO:0045785
      label: positive regulation of cell adhesion
    evidence_type: IMP
    original_reference_id: PMID:20810993
    review:
      summary: >-
        C1q-C1QBP interaction promotes cell adhesion in trophoblast invasion.
      action: KEEP_AS_NON_CORE
      reason: >-
        Cell adhesion regulation is a downstream consequence of C1q binding.

      supported_by:
        - reference_id: PMID:20810993
          supporting_text: 'Sep 1. An alternative role of C1q in cell migration and
            tissue remodeling: contribution to trophoblast invasion and placental
            development.'
  - term:
      id: GO:0050687
      label: negative regulation of defense response to virus
    evidence_type: IMP
    original_reference_id: PMID:19164550
    review:
      summary: >-
        C1QBP inhibits RIG-I and MDA5 antiviral pathways.
      action: KEEP_AS_NON_CORE
      reason: >-
        Antiviral response modulation is a secondary function.

      supported_by:
        - reference_id: PMID:19164550
          supporting_text: Inhibition of RIG-I and MDA5-dependent antiviral 
            response by gC1qR at mitochondria.
  - term:
      id: GO:0051897
      label: positive regulation of phosphatidylinositol 3-kinase/protein kinase
        B signal transduction
    evidence_type: IMP
    original_reference_id: PMID:16177118
    review:
      summary: >-
        gC1qR ligation activates PI3K-AKT signaling.
      action: KEEP_AS_NON_CORE
      reason: >-
        Downstream signaling consequence of receptor function.

      supported_by:
        - reference_id: PMID:16177118
          supporting_text: gC1q receptor ligation selectively down-regulates 
            human IL-12 production through activation of the phosphoinositide 
            3-kinase pathway.
  - term:
      id: GO:0070131
      label: positive regulation of mitochondrial translation
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        C1QBP supports mitochondrial translation through RNA binding and
        mitoribosome association. This is a core function.
      action: ACCEPT
      reason: >-
        This is one of the two core functions of C1QBP - essential for
        OXPHOS and confirmed by disease mutations causing COXPD33.

  - term:
      id: GO:0090023
      label: positive regulation of neutrophil chemotaxis
    evidence_type: IDA
    original_reference_id: PMID:9461517
    review:
      summary: >-
        C1q-mediated chemotaxis of neutrophils involves gC1qR and G-protein
        signaling.
      action: KEEP_AS_NON_CORE
      reason: >-
        Chemotaxis regulation is a downstream consequence of C1q receptor
        function.

      supported_by:
        - reference_id: PMID:9461517
          supporting_text: 'C1q-mediated chemotaxis by human neutrophils: involvement
            of gClqR and G-protein signalling mechanisms.'
  - term:
      id: GO:0097177
      label: mitochondrial ribosome binding
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        C1QBP associates with mitoribosomes to support mitochondrial translation.
      action: ACCEPT
      reason: >-
        Mitoribosome binding is integral to the core mitochondrial translation
        support function.

  - term:
      id: GO:1900026
      label: positive regulation of substrate adhesion-dependent cell spreading
    evidence_type: IMP
    original_reference_id: PMID:11859136
    review:
      summary: >-
        C1q receptors including C1QBP cooperate with integrins in endothelial
        cell adhesion and spreading.
      action: KEEP_AS_NON_CORE
      reason: >-
        Cell spreading regulation is a downstream effect of C1q binding.

      supported_by:
        - reference_id: PMID:11859136
          supporting_text: Cooperation of C1q receptors and integrins in 
            C1q-mediated endothelial cell adhesion and spreading.
  - term:
      id: GO:1901165
      label: positive regulation of trophoblast cell migration
    evidence_type: IMP
    original_reference_id: PMID:20810993
    review:
      summary: >-
        C1q-C1QBP axis promotes trophoblast migration in placental development.
      action: KEEP_AS_NON_CORE
      reason: >-
        Trophoblast migration is a developmental context-specific consequence
        of C1q binding.

      supported_by:
        - reference_id: PMID:20810993
          supporting_text: 'Sep 1. An alternative role of C1q in cell migration and
            tissue remodeling: contribution to trophoblast invasion and placental
            development.'
  - term:
      id: GO:2000510
      label: positive regulation of dendritic cell chemotaxis
    evidence_type: IMP
    original_reference_id: PMID:16140380
    review:
      summary: >-
        C1q-mediated dendritic cell chemotaxis involves gC1qR.
      action: KEEP_AS_NON_CORE
      reason: >-
        Chemotaxis regulation is a downstream consequence of C1q receptor function.

      supported_by:
        - reference_id: PMID:16140380
          supporting_text: 2005 Sep 2. Chemotaxis of human monocyte-derived 
            dendritic cells to complement component C1q is mediated by the 
            receptors gC1qR and cC1qR.
  - term:
      id: GO:0016020
      label: membrane
    evidence_type: IDA
    original_reference_id: PMID:11290596
    review:
      summary: >-
        Membrane localization with cytokeratin 1 and urokinase receptor on
        endothelial cells.
      action: ACCEPT
      reason: >-
        Membrane association is consistent with cell surface receptor function.

      supported_by:
        - reference_id: PMID:11290596
          supporting_text: Expression and colocalization of cytokeratin 1 and 
            urokinase plasminogen activator receptor on endothelial cells.
  - term:
      id: GO:0005886
      label: plasma membrane
    evidence_type: TAS
    original_reference_id: PMID:8195709
    review:
      summary: >-
        Original description of C1QBP as cell surface glycoprotein.
      action: ACCEPT
      reason: >-
        Foundational evidence for cell surface localization.

      supported_by:
        - reference_id: PMID:8195709
          supporting_text: Isolation, cDNA cloning, and overexpression of a 
            33-kD cell surface glycoprotein that binds to the globular "heads" 
            of C1q.
  - term:
      id: GO:0006955
      label: immune response
    evidence_type: TAS
    original_reference_id: PMID:8195709
    review:
      summary: >-
        General immune response annotation from seminal paper.
      action: KEEP_AS_NON_CORE
      reason: >-
        Very broad term. More specific annotations (complement activation,
        C1q binding) better capture the function.

      supported_by:
        - reference_id: PMID:8195709
          supporting_text: Isolation, cDNA cloning, and overexpression of a 
            33-kD cell surface glycoprotein that binds to the globular "heads" 
            of C1q.
core_functions:
  - molecular_function:
      id: GO:0003729
      label: mRNA binding
    description: >-
      C1QBP is essential for mitochondrial protein synthesis. It binds
      mitochondrial RNAs (including m5C-modified RNAs), associates with
      mitoribosomes, and is required for OXPHOS maintenance. Biallelic
      mutations cause COXPD33, a severe mitochondrial disorder with
      respiratory chain deficiency.
    directly_involved_in:
      - id: GO:0070131
        label: positive regulation of mitochondrial translation
    locations:
      - id: GO:0005759
        label: mitochondrial matrix
    supported_by:
      - reference_id: PMID:28942965
        supporting_text: "Biallelic C1QBP mutations cause severe neonatal-, childhood-,
          or later-onset cardiomyopathy associated with combined respiratory-chain
          deficiencies."
      - reference_id: PMID:39019044
        supporting_text: "C1QBP recognizes m5C-modified mitochondrial RNAs and promotes
          their degradation via recruitment of the mitochondrial degradosome complex."
      - reference_id: PMID:9305894
        supporting_text: "p32 protein, a splicing factor 2-associated protein, is
          localized in mitochondrial matrix and is functionally important in maintaining
          oxidative phosphorylation."

  - molecular_function:
      id: GO:0001849
      label: complement component C1q complex binding
    description: >-
      C1QBP was originally identified as gC1qR, binding the globular heads
      of complement C1q. At the cell surface, it modulates complement
      activation, binds kininogens, and participates in immune signaling.
      It is proposed as a checkpoint-like immune modulator in the tumor
      microenvironment.
    directly_involved_in:
      - id: GO:0030449
        label: regulation of complement activation
    locations:
      - id: GO:0009986
        label: cell surface
    supported_by:
      - reference_id: PMID:8195709
        supporting_text: "This protein designated gC1q-R, was first isolated from
          Raji cells and was found to bind to the globular \"heads\" of C1q molecules"
      - reference_id: PMID:8662673
        supporting_text: "Isolation and characterization of the kininogen-binding
          protein p33 from endothelial cells. Identity with the gC1q receptor."

references:
  - id: GO_REF:0000024
    title: Manual transfer of experimentally-verified manual GO annotation data 
      to orthologs by curator judgment of sequence similarity
    findings: []
  - id: GO_REF:0000033
    title: Annotation inferences using phylogenetic trees
    findings: []
  - id: GO_REF:0000043
    title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword 
      mapping
    findings: []
  - id: GO_REF:0000044
    title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular 
      Location vocabulary mapping, accompanied by conservative changes to GO 
      terms applied by UniProt
    findings: []
  - id: GO_REF:0000052
    title: Gene Ontology annotation based on curation of immunofluorescence data
    findings: []
  - id: GO_REF:0000107
    title: Automatic transfer of experimentally verified manual GO annotation 
      data to orthologs using Ensembl Compara
    findings: []
  - id: GO_REF:0000120
    title: Combined Automated Annotation using Multiple IEA Methods
    findings: []
  - id: PMID:10022843
    title: The splicing factor-associated protein, p32, regulates RNA splicing 
      by inhibiting ASF/SF2 RNA binding and phosphorylation.
    findings:
      - statement: C1QBP inhibits ASF/SF2 RNA binding and phosphorylation
      - statement: Functions as ASF/SF2 inhibitory factor regulating splicing
  - id: PMID:10831594
    title: Protein kinase C [micro] is regulated by the multifunctional chaperon
      protein p32.
    findings: []
  - id: PMID:11083468
    title: Localization of P32 protein (gC1q-R) in mitochondria and at specific 
      extramitochondrial locations in normal tissues.
    findings:
      - statement: Primary localization is mitochondrial
      - statement: Cell surface localization in endothelial cells and acinar 
          cells
      - statement: Nuclear localization in splenic lymphocytes
  - id: PMID:11086025
    title: Interaction between complement receptor gC1qR and hepatitis C virus 
      core protein inhibits T-lymphocyte proliferation.
    findings: []
  - id: PMID:11290596
    title: Expression and colocalization of cytokeratin 1 and urokinase 
      plasminogen activator receptor on endothelial cells.
    findings: []
  - id: PMID:11859136
    title: Cooperation of C1q receptors and integrins in C1q-mediated 
      endothelial cell adhesion and spreading.
    findings: []
  - id: PMID:12034482
    title: The N-terminal conserved domain of rubella virus capsid interacts 
      with the C-terminal region of cellular p32 and overexpression of p32 
      enhances the viral infectivity.
    findings: []
  - id: PMID:12220632
    title: The cytoplasmic tail peptide sequence of membrane type-1 matrix 
      metalloproteinase (MT1-MMP) directly binds to gC1qR, a 
      compartment-specific chaperone-like regulatory protein.
    findings: []
  - id: PMID:14743216
    title: A physical and functional map of the human TNF-alpha/NF-kappa B 
      signal transduction pathway.
    findings: []
  - id: PMID:15031724
    title: Physical and functional interaction between BH3-only protein Hrk and 
      mitochondrial pore-forming protein p32.
    findings:
      - statement: C1QBP interacts with HRK in mitochondria
      - statement: p32 knockdown protects against Hrk-induced apoptosis
      - statement: C1QBP facilitates but is not directly apoptotic
  - id: PMID:15243141
    title: Human p32, interacts with B subunit of the CCAAT-binding factor, 
      CBF/NF-Y, and inhibits CBF-mediated transcription activation in vitro.
    findings:
      - statement: C1QBP interacts with NF-YB (CBF-B)
      - statement: Acts as transcriptional corepressor
      - statement: Present in cytosol and nucleus
  - id: PMID:16140380
    title: Chemotaxis of human monocyte-derived dendritic cells to complement 
      component C1q is mediated by the receptors gC1qR and cC1qR.
    findings: []
  - id: PMID:16177118
    title: gC1q receptor ligation selectively down-regulates human IL-12 
      production through activation of the phosphoinositide 3-kinase pathway.
    findings: []
  - id: PMID:16721827
    title: CDC2L5, a Cdk-like kinase with RS domain, interacts with the 
      ASF/SF2-associated protein p32 and affects splicing in vivo.
    findings: []
  - id: PMID:17486078
    title: The autophagic inducer smARF interacts with and is stabilized by the 
      mitochondrial p32 protein.
    findings: []
  - id: PMID:17881511
    title: HCV core protein interaction with gC1q receptor inhibits Th1 
      differentiation of CD4+ T cells via suppression of dendritic cell IL-12 
      production.
    findings: []
  - id: PMID:18191643
    title: Novel tyrosine phosphorylated and cardiolipin-binding protein CLPABP 
      functions as mitochondrial RNA granule.
    findings: []
  - id: PMID:18676636
    title: Human p32 is a novel FOXC1-interacting protein that regulates FOXC1 
      transcriptional activity in ocular cells.
    findings: []
  - id: PMID:19164550
    title: Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at
      mitochondria.
    findings: []
  - id: PMID:20810993
    title: 'An alternative role of C1q in cell migration and tissue remodeling: contribution
      to trophoblast invasion and placental development.'
    findings: []
  - id: PMID:21536856
    title: Splicing factor 2-associated protein p32 participates in ribosome 
      biogenesis by regulating the binding of Nop52 and fibrillarin to 
      preribosome particles.
    findings: []
  - id: PMID:21653829
    title: Protein interactome reveals converging molecular pathways among 
      autism disorders.
    findings: []
  - id: PMID:21988832
    title: Toward an understanding of the protein interaction network of the 
      human liver.
    findings: []
  - id: PMID:22118625
    title: NONO and RALY proteins are required for YB-1 oxaliplatin induced 
      resistance in colon adenocarcinoma cell lines.
    findings: []
  - id: PMID:22238231
    title: Binding of cellular p32 protein to the rubella virus P150 replicase 
      protein via PxxPxR motifs.
    findings: []
  - id: PMID:23986595
    title: A host YB-1 ribonucleoprotein complex is hijacked by hepatitis C 
      virus for the control of NS3-dependent particle production.
    findings: []
  - id: PMID:24955142
    title: 'Exploration of panviral proteome: high-throughput cloning and functional
      implications in virus-host interactions.'
    findings: []
  - id: PMID:25497084
    title: C1QBP negatively regulates the activation of oncoprotein YBX1 in the 
      renal cell carcinoma as revealed by interactomics analysis.
    findings: []
  - id: PMID:25852190
    title: Integrative analysis of kinase networks in TRAIL-induced apoptosis 
      provides a source of potential targets for combination therapy.
    findings: []
  - id: PMID:26184334
    title: 'Comprehensive Protein Interactome Analysis of a Key RNA Helicase: Detection
      of Novel Stress Granule Proteins.'
    findings: []
  - id: PMID:26816005
    title: Homologous Transcription Factors DUX4 and DUX4c Associate with 
      Cytoplasmic Proteins during Muscle Differentiation.
    findings: []
  - id: PMID:27499296
    title: Mitochondrial Protein Interaction Mapping Identifies Regulators of 
      Respiratory Chain Function.
    findings: []
  - id: PMID:28514442
    title: Architecture of the human interactome defines protein communities and
      disease networks.
    findings: []
  - id: PMID:28565870
    title: C1QBP is upregulated in colon cancer and binds to apolipoprotein A-I.
    findings: []
  - id: PMID:28942965
    title: Biallelic C1QBP mutations cause severe neonatal-, childhood-, or 
      later-onset cardiomyopathy associated with combined respiratory-chain 
      deficiencies.
    findings:
      - statement: C1QBP mutations cause COXPD33
      - statement: Essential for mitochondrial translation
      - statement: Required for OXPHOS
  - id: PMID:31353207
    title: C1QBP Promotes Homologous Recombination by Stabilizing MRE11 and 
      Controlling the Assembly and Activation of MRE11/RAD50/NBS1 Complex.
    findings: []
  - id: PMID:31980649
    title: Extensive rewiring of the EGFR network in colorectal cancer cells 
      expressing transforming levels of KRAS(G13D).
    findings: []
  - id: PMID:32296183
    title: A reference map of the human binary protein interactome.
    findings: []
  - id: PMID:32958672
    title: Unusually efficient CUG initiation of an overlapping reading frame in
      POLG mRNA yields novel protein POLGARF.
    findings: []
  - id: PMID:33961781
    title: Dual proteome-scale networks reveal cell-specific remodeling of the 
      human interactome.
    findings: []
  - id: PMID:34800366
    title: Quantitative high-confidence human mitochondrial proteome and its 
      dynamics in cellular context.
    findings: []
  - id: PMID:35271311
    title: 'OpenCell: Endogenous tagging for the cartography of human cellular organization.'
    findings: []
  - id: PMID:36882853
    title: The double homeodomain protein DUX4c is associated with regenerating 
      muscle fibers and RNA-binding proteins.
    findings: []
  - id: PMID:39019044
    title: RNA 5-methylcytosine marks mitochondrial double-stranded RNAs for 
      degradation and cytosolic release.
    findings:
      - statement: C1QBP recognizes m5C-modified mitochondrial RNAs
      - statement: Promotes recruitment of mitochondrial degradosome
      - statement: Key role in mitochondrial RNA quality control
  - id: PMID:8195709
    title: Isolation, cDNA cloning, and overexpression of a 33-kD cell surface 
      glycoprotein that binds to the globular "heads" of C1q.
    findings:
      - statement: Original identification of C1QBP as gC1qR
      - statement: Binds globular heads of C1q
      - statement: Cell surface glycoprotein
  - id: PMID:8567680
    title: Molecular cloning of human fibroblast hyaluronic acid-binding protein
      confirms its identity with P-32, a protein co-purified with splicing 
      factor SF2. Hyaluronic acid-binding protein as P-32 protein, co-purified 
      with splicing factor SF2.
    findings: []
  - id: PMID:8662673
    title: Isolation and characterization of the kininogen-binding protein p33 
      from endothelial cells. Identity with the gC1q receptor.
    findings:
      - statement: C1QBP/p33 is kininogen-binding protein
      - statement: Identical to gC1q receptor
  - id: PMID:8710908
    title: 'Identification of the zinc-dependent endothelial cell binding protein
      for high molecular weight kininogen and factor XII: identity with the receptor
      that binds to the globular "heads" of C1q (gC1q-R).'
    findings: []
  - id: PMID:8900153
    title: The binding protein for globular heads of complement C1q, gC1qR. 
      Functional expression and characterization as a novel vitronectin binding 
      factor.
    findings: []
  - id: PMID:9305894
    title: p32 protein, a splicing factor 2-associated protein, is localized in 
      mitochondrial matrix and is functionally important in maintaining 
      oxidative phosphorylation.
    findings:
      - statement: C1QBP localizes to mitochondrial matrix
      - statement: Important for OXPHOS maintenance
  - id: PMID:9461517
    title: 'C1q-mediated chemotaxis by human neutrophils: involvement of gClqR and
      G-protein signalling mechanisms.'
    findings: []
  - id: Reactome:R-HSA-158218
    title: prekallikrein + kininogen:C1q binding protein tetramer -> 
      prekallikrein:kininogen:C1q binding protein tetramer
    findings: []
  - id: Reactome:R-HSA-158251
    title: prekallikrein:kininogen:C1q binding protein tetramer -> 
      kallikrein:kininogen:C1q binding protein tetramer
    findings: []
  - id: Reactome:R-HSA-158311
    title: kallikrein:kininogen:C1q binding protein tetramer -> kallikrein + 
      activated kininogen:C1q binding protein tetramer + bradykinin
    findings: []
  - id: Reactome:R-HSA-158313
    title: factor XII -> factor XIIa
    findings: []
  - id: Reactome:R-HSA-158354
    title: kininogen + C1q binding protein tetramer -> kininogen:C1q binding 
      protein tetramer
    findings: []
  - id: Reactome:R-HSA-9645692
    title: C1QBP promotes translocation of p14ARF to the mitochondrial matrix
    findings: []
  - id: Reactome:R-HSA-9645694
    title: p14ARF binds C1QBP
    findings: []
  - id: Reactome:R-HSA-9645766
    title: p14ARF mutants do not bind C1QBP
    findings: []
  - id: deep-research
    title: C1QBP deep research summary (Falcon 2024)
    findings:
      - statement: Core functions are mitochondrial translation support and C1q 
          receptor
      - statement: Over-expressed in cancers
      - statement: Proposed as checkpoint-like immune modulator
      - statement: Biallelic mutations cause COXPD33 with cardiomyopathy
  - id: file:human/C1QBP/C1QBP-deep-research-falcon.md
    title: Deep research report on C1QBP
    findings: []