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."
    full_text_unavailable: true
  - 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: []