id: Q5U5X0
gene_symbol: LYRM7
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  LYRM7 (LYR motif-containing protein 7; also MZM1L/C5orf31) is a small mitochondrial-matrix
  LYR-family assembly chaperone for respiratory Complex III (cytochrome bc1 / ubiquinol-cytochrome
  c reductase). It acts as a dedicated chaperone for the Rieske iron-sulfur protein UQCRFS1,
  binding and stabilising UQCRFS1 in the mitochondrial matrix prior to insertion of its
  [2Fe-2S] cluster and the subunit's translocation and incorporation into the late Complex III
  dimeric intermediate in the inner membrane. Its LYR motif recruits the Fe-S transfer cochaperone
  HSC20 (HSCB), coupling the UQCRFS1-LYRM7 intermediate to the ISCU-HSPA9-HSC20 cluster-delivery
  machinery. LYRM7 is non-catalytic and is the human ortholog of yeast Mzm1. Loss-of-function
  variants cause mitochondrial complex III deficiency, nuclear type 8 (a leukoencephalopathy).
existing_annotations:
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: >-
      Phylogenetic (IBA) propagation placing LYRM7 in the mitochondrial matrix, where it acts
      as a chaperone. This is directly confirmed experimentally: LYRM7 binds and stabilises
      UQCRFS1 within the mitochondrial matrix.
    action: ACCEPT
    reason: >-
      The matrix location is the site of LYRM7's chaperone activity and is supported by direct
      experimental evidence (IDA, PMID:23168492) and the UniProt subcellular location, in
      addition to this phylogenetic inference. is_active_in is appropriate for the compartment
      where it chaperones UQCRFS1.
    supported_by:
    - reference_id: PMID:23168492
      supporting_text: >-
        binding to this subunit within the
    - reference_id: file:human/LYRM7/LYRM7-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion matrix"
- term:
    id: GO:0034551
    label: mitochondrial respiratory chain complex III assembly
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: >-
      Phylogenetic (IBA) inference that LYRM7 is involved in Complex III assembly. This is the
      core biological process of the gene and is strongly supported experimentally.
    action: ACCEPT
    reason: >-
      LYRM7 is a bona fide Complex III assembly factor mediating the UQCRFS1/Rieske Fe-S protein
      incorporation step. This is the precise, well-evidenced core BP and is consistent across
      IBA, IDA (PMID:23168492), IEA and Reactome TAS annotations.
    supported_by:
    - reference_id: PMID:23168492
      supporting_text: >-
        LYRM7/MZM1L is a novel human CIII assembly factor involved in the UQCRFS1
- term:
    id: GO:0044183
    label: protein folding chaperone
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: >-
      Phylogenetic (IBA) assignment of a protein folding chaperone molecular function. LYRM7
      is a non-catalytic chaperone that binds and stabilises (holds) its client UQCRFS1, so a
      chaperone MF is the correct, most informative non-catalytic molecular function.
    action: ACCEPT
    reason: >-
      The chaperone MF is directly supported: LYRM7 works as a UQCRFS1 chaperone, binding and
      stabilising the Rieske Fe-S protein prior to its incorporation into Complex III
      (PMID:23168492). This is the appropriate MF for this non-enzymatic assembly factor and is
      retained as the core molecular function; no catalytic activity should be assigned.
    supported_by:
    - reference_id: PMID:23168492
      supporting_text: >-
        works as a human Rieske
    - reference_id: file:human/LYRM7/LYRM7-uniprot.txt
      supporting_text: >-
        Assembly factor required for Rieske Fe-S protein UQCRFS1
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: located_in
  review:
    summary: >-
      InterPro2GO electronic annotation to the mitochondrion, based on the Complex1_LYR domain
      family. Correct but less specific than the matrix localisation.
    action: ACCEPT
    reason: >-
      Mitochondrial localisation is correct and well supported; this is simply a broader (parent)
      location than the experimentally established mitochondrial matrix. Retained as a valid,
      if general, CC annotation.
    supported_by:
    - reference_id: file:human/LYRM7/LYRM7-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion matrix"
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: >-
      Electronic annotation to the mitochondrial matrix from the UniProt Swiss-Prot subcellular
      location vocabulary mapping. Matches the curated UniProt location and experimental evidence.
    action: ACCEPT
    reason: >-
      Consistent with the experimentally determined (IDA, PMID:23168492) and curated UniProt
      matrix location where LYRM7 chaperones UQCRFS1.
    supported_by:
    - reference_id: file:human/LYRM7/LYRM7-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion matrix"
- term:
    id: GO:0006457
    label: protein folding
  evidence_type: IEA
  original_reference_id: GO_REF:0000108
  qualifier: involved_in
  review:
    summary: >-
      Inter-ontology (logical) inference of a protein folding BP from the protein folding
      chaperone MF (GO:0044183). Consistent with LYRM7's role in stabilising/holding UQCRFS1.
    action: ACCEPT
    reason: >-
      This is a sound, if general, logical consequence of the chaperone MF. LYRM7 stabilises its
      unfolded/apo client UQCRFS1, which falls under protein folding. It is broader than the
      specific Complex III assembly BP but not incorrect. Kept as non-core context; the precise
      core BP is mitochondrial respiratory chain complex III assembly.
    supported_by:
    - reference_id: file:human/LYRM7/LYRM7-uniprot.txt
      supporting_text: >-
        stabilizing it prior to its translocation and insertion into the late
- term:
    id: GO:0034551
    label: mitochondrial respiratory chain complex III assembly
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: >-
      InterPro2GO electronic annotation to Complex III assembly, based on the LYRM7-specific
      InterPro family (IPR045298). Correct and matches experimental evidence.
    action: ACCEPT
    reason: >-
      The LYRM7/MZM1-LYRM7 family signature reliably predicts a Complex III assembly-factor role,
      which is experimentally confirmed. This is the core BP.
    supported_by:
    - reference_id: PMID:23168492
      supporting_text: >-
        LYRM7/MZM1L is a novel human CIII assembly factor involved in the UQCRFS1
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:24606901
  qualifier: enables
  review:
    summary: >-
      IPI (IntAct) capturing a physical interaction between LYRM7 and HSC20/HSCB (UniProt Q8IWL3),
      the Fe-S cluster transfer cochaperone. This is a real and functionally meaningful interaction
      (LYRM7's LYR motif is an HSC20 binding site), but the GO term "protein binding" is
      uninformative.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Bare protein binding (GO:0005515) conveys no specific molecular function. The underlying
      LYRM7-HSC20 interaction is genuine and biologically important (it couples the UQCRFS1-LYRM7
      intermediate to the Fe-S transfer machinery), so this is not removed; but the term is
      retained only as an uninformative over-annotation. The informative MF is the chaperone
      activity (GO:0044183).
    supported_by:
    - reference_id: PMID:24606901
      supporting_text: >-
        SDHAF1 and LYRM7, respectively, are HSC20 binding partners
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:27499296
  qualifier: enables
  review:
    summary: >-
      IPI (IntAct) capturing a physical interaction between LYRM7 and UQCRFS1 (P47985) reported in
      a large-scale mitochondrial protein interaction map. UQCRFS1 is the physiological client of
      LYRM7, so the interaction is correct, but "protein binding" is uninformative.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      The LYRM7-UQCRFS1 interaction is the core, well-established relationship of this gene, but
      bare GO:0005515 does not capture the chaperone function. Retained as an uninformative
      over-annotation rather than removed.
    supported_by:
    - reference_id: PMID:27499296
      supporting_text: Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:28380382
  qualifier: enables
  review:
    summary: >-
      IPI (IntAct) capturing physical interactions of LYRM7 with UQCRFS1 (P47985) and with
      HSC20/HSCB (Q8IWL3). Both are physiologically central: the UQCRFS1-LYRM7 intermediate
      recruits HSC20 via LYRM7's LYR motif to deliver the [2Fe-2S] cluster to UQCRFS1.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      The interactions are real and mechanistically important, but bare protein binding is
      uninformative and does not capture the chaperone/assembly-factor MF. Retained as an
      over-annotation rather than removed.
    supported_by:
    - reference_id: PMID:28380382
      supporting_text: >-
        direct binding of the co-chaperone HSC20 to the LYR (Leucine, Tyrosine, Arginine)
        consensus sequence of LYRM7 was required for recruitment of the Fe-S transfer complex to
        the LYRM7-UQCRFS1 assembly intermediate
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32296183
  qualifier: enables
  review:
    summary: >-
      IPI from the HuRI binary (yeast two-hybrid) reference interactome mapping LYRM7 to SAT1
      (P21673, spermidine/spermine N1-acetyltransferase). SAT1 has no known mitochondrial or
      Complex III role; this is most likely a non-physiological binary-screen hit.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Bare protein binding is uninformative, and this particular partner (SAT1) is not a plausible
      physiological interactor of a mitochondrial-matrix CIII assembly chaperone. Per curation
      policy, an experimental IPI is not removed on the basis of an incomplete assessment; it is
      marked as an uninformative (and here likely non-physiological) over-annotation.
    supported_by:
    - reference_id: PMID:32296183
      supporting_text: A reference map of the human binary protein interactome
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33961781
  qualifier: enables
  review:
    summary: >-
      IPI (BioPlex) capturing a physical interaction between LYRM7 and UQCRFS1 (P47985) in a
      proteome-scale affinity-purification interactome. Consistent with the core LYRM7-UQCRFS1
      client relationship.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Correct interaction with the physiological client UQCRFS1, but bare GO:0005515 is
      uninformative. Retained as an over-annotation rather than removed; the chaperone MF
      (GO:0044183) captures the function.
    supported_by:
    - reference_id: PMID:33961781
      supporting_text: Dual proteome-scale networks reveal cell-specific remodeling of the human
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:40205054
  qualifier: enables
  review:
    summary: >-
      IPI capturing a physical interaction between LYRM7 and UQCRFS1 (P47985) in a large-scale
      cell-map / structural-functional genomics interactome. Consistent with the core client
      relationship.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Correct interaction with UQCRFS1 but bare protein binding is uninformative. Retained as an
      over-annotation; the informative MF is the chaperone activity.
    supported_by:
    - reference_id: PMID:40205054
      supporting_text: Multimodal cell maps as a foundation for structural and functional genomics
- term:
    id: GO:0034551
    label: mitochondrial respiratory chain complex III assembly
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9865881
  qualifier: involved_in
  review:
    summary: >-
      Reactome (TAS) annotation placing LYRM7 in the Complex III assembly pathway. Matches the
      core, experimentally supported BP.
    action: ACCEPT
    reason: >-
      Reactome curates LYRM7 as a Complex III assembly factor (the UQCRFS1/Rieske protein binds
      and is stabilised by LYRM7). This is the correct core BP.
    supported_by:
    - reference_id: PMID:23168492
      supporting_text: >-
        LYRM7/MZM1L is a novel human CIII assembly factor involved in the UQCRFS1
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: HTP
  original_reference_id: PMID:34800366
  qualifier: located_in
  review:
    summary: >-
      High-throughput annotation of LYRM7 to the mitochondrion from a quantitative high-confidence
      human mitochondrial proteome. Consistent with the curated matrix localisation.
    action: ACCEPT
    reason: >-
      Independent proteomic support for mitochondrial localisation; broader than the specific
      matrix location but correct.
    supported_by:
    - reference_id: file:human/LYRM7/LYRM7-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion matrix"
- term:
    id: GO:0044183
    label: protein folding chaperone
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9866253
  qualifier: enables
  review:
    summary: >-
      Reactome (TAS) assignment of the protein folding chaperone MF, corresponding to the reaction
      in which apo-UQCRFS1 binds and is stabilised by LYRM7. Matches the core chaperone function.
    action: ACCEPT
    reason: >-
      Reactome curates LYRM7 as the chaperone that binds and stabilises apo-UQCRFS1 in the matrix,
      the correct non-catalytic MF for this assembly factor. Core molecular function.
    supported_by:
    - reference_id: PMID:23168492
      supporting_text: >-
        works as a human Rieske
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9866253
  qualifier: located_in
  review:
    summary: >-
      Reactome (TAS) localisation of LYRM7 to the mitochondrial matrix, the compartment where
      apo-UQCRFS1 binds LYRM7. Matches experimental and curated localisation.
    action: ACCEPT
    reason: >-
      Consistent with the experimentally established matrix location where LYRM7 chaperones
      UQCRFS1.
    supported_by:
    - reference_id: file:human/LYRM7/LYRM7-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion matrix"
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9866272
  qualifier: located_in
  review:
    summary: >-
      Reactome (TAS) localisation of LYRM7 to the mitochondrial matrix, associated with the
      reaction inserting the [2Fe-2S] cluster into UQCRFS1 as part of the UQCRFS1:LYRM7 complex.
    action: ACCEPT
    reason: >-
      Consistent with the matrix location where the LYRM7-UQCRFS1 intermediate recruits the Fe-S
      transfer machinery for cluster insertion.
    supported_by:
    - reference_id: file:human/LYRM7/LYRM7-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion matrix"
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:23168492
  qualifier: enables
  review:
    summary: >-
      IPI (UniProt) capturing the physical interaction between LYRM7 and UQCRFS1 (P47985) from the
      primary characterisation paper, in which LYRM7 was shown to bind and stabilise the Rieske
      Fe-S protein. This is the defining, physiological interaction of LYRM7.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      The LYRM7-UQCRFS1 interaction is the core relationship establishing LYRM7 as the UQCRFS1
      chaperone, so it is not removed; however, bare protein binding (GO:0005515) is uninformative
      and does not capture the chaperone MF. The chaperone activity (GO:0044183) is the informative
      MF that should represent this function.
    supported_by:
    - reference_id: PMID:23168492
      supporting_text: >-
        works as a human Rieske
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: IDA
  original_reference_id: PMID:23168492
  qualifier: located_in
  review:
    summary: >-
      Direct experimental (IDA) localisation of LYRM7 to the mitochondrial matrix from the primary
      characterisation study. This is the strongest evidence for the core localisation.
    action: ACCEPT
    reason: >-
      LYRM7 was experimentally shown to reside in and act within the mitochondrial matrix, where it
      binds and stabilises UQCRFS1. Core CC annotation.
    supported_by:
    - reference_id: PMID:23168492
      supporting_text: >-
        binding to this subunit within the
    - reference_id: file:human/LYRM7/LYRM7-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion matrix"
- term:
    id: GO:0031966
    label: mitochondrial membrane
  evidence_type: IDA
  original_reference_id: PMID:23168492
  qualifier: located_in
  review:
    summary: >-
      Direct experimental (IDA) detection of a pool of LYRM7 associated with the mitochondrial
      membrane, consistent with its transient association with the membrane-embedded late Complex
      III dimeric intermediate during UQCRFS1 insertion.
    action: KEEP_AS_NON_CORE
    reason: >-
      Membrane association is a real but secondary/transient aspect of LYRM7 function: its primary
      site of action is the matrix, where it chaperones UQCRFS1; the membrane pool reflects delivery
      of UQCRFS1 to the inner-membrane CIII intermediate. Kept but marked non-core relative to the
      matrix localisation.
    supported_by:
    - reference_id: file:human/LYRM7/LYRM7-uniprot.txt
      supporting_text: >-
        stabilizing it prior to its translocation and insertion into the late
- term:
    id: GO:0034551
    label: mitochondrial respiratory chain complex III assembly
  evidence_type: IDA
  original_reference_id: PMID:23168492
  qualifier: involved_in
  review:
    summary: >-
      Direct experimental (IDA) evidence that LYRM7 is required for the UQCRFS1 insertion step of
      Complex III assembly. This is the definitive experimental support for the core BP.
    action: ACCEPT
    reason: >-
      The primary study established LYRM7 as a Complex III assembly factor acting at the UQCRFS1
      incorporation step; this is the core, best-supported biological process.
    supported_by:
    - reference_id: PMID:23168492
      supporting_text: >-
        LYRM7/MZM1L is a novel human CIII assembly factor involved in the UQCRFS1
- term:
    id: GO:0045333
    label: cellular respiration
  evidence_type: IDA
  original_reference_id: PMID:23168492
  qualifier: involved_in
  review:
    summary: >-
      IDA annotation to cellular respiration, based on the observation that loss of LYRM7 impairs
      Complex III activity and hence respiration. LYRM7 is an assembly factor, not itself a
      respiratory-chain component; its effect on respiration is indirect (via enabling functional
      Complex III).
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      LYRM7 does not itself carry out or directly participate in respiration; it enables assembly
      of Complex III, whose activity is required for respiration. The precise, mechanistically
      accurate BP is mitochondrial respiratory chain complex III assembly (GO:0034551). Cellular
      respiration is an over-annotation capturing a downstream consequence rather than LYRM7's
      direct role. Not removed (experimental annotation) but flagged as over-annotated.
    supported_by:
    - reference_id: PMID:23168492
      supporting_text: >-
        which enables formation of the mature and functional CIII
core_functions:
- description: >-
    Non-catalytic protein-folding chaperone that binds and stabilises the Rieske iron-sulfur
    protein UQCRFS1 in the mitochondrial matrix, holding it prior to [2Fe-2S] cluster insertion
    and its incorporation into respiratory Complex III (cytochrome bc1). LYRM7's LYR motif also
    recruits the Fe-S transfer cochaperone HSC20, coupling the UQCRFS1-LYRM7 intermediate to the
    cluster-delivery machinery.
  molecular_function:
    id: GO:0044183
    label: protein folding chaperone
  directly_involved_in:
  - id: GO:0034551
    label: mitochondrial respiratory chain complex III assembly
  locations:
  - id: GO:0005759
    label: mitochondrial matrix
  supported_by:
  - reference_id: PMID:23168492
    supporting_text: >-
      works as a human Rieske
  - reference_id: PMID:23168492
    supporting_text: >-
      LYRM7/MZM1L is a novel human CIII assembly factor involved in the UQCRFS1
  - reference_id: PMID:28380382
    supporting_text: >-
      direct binding of the co-chaperone HSC20 to the LYR (Leucine, Tyrosine, Arginine)
      consensus sequence of LYRM7 was required for recruitment of the Fe-S transfer complex to
      the LYRM7-UQCRFS1 assembly intermediate
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  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:0000108
  title: Automatic assignment of GO terms using logical inference, based on on inter-ontology
    links
  findings: []
- id: PMID:23168492
  title: LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of mitochondrial
    Complex III assembly in human cells.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Primary characterisation of human LYRM7/MZM1L. Establishes it as a mitochondrial-matrix
      UQCRFS1 (Rieske Fe-S) chaperone and Complex III assembly factor. Supports the core MF, BP,
      and matrix localisation.
- id: PMID:24606901
  title: Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster
    delivery.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Full text explicitly names LYRM7 as an HSC20 (HSC20/HSCB) binding partner among the LYR-motif
      family that assist Complex II/III assembly, supporting the LYRM7-HSC20 interaction.
- id: PMID:27499296
  title: Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory
    Chain Function.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      Large-scale mitochondrial interaction map; source of an IntAct LYRM7-UQCRFS1 interaction.
      Supports the physiological client relationship but not gene-specific mechanism.
- id: PMID:28380382
  title: A Single Adaptable Cochaperone-Scaffold Complex Delivers Nascent Iron-Sulfur
    Clusters to Mammalian Respiratory Chain Complexes I-III.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Full text details the UQCRFS1-LYRM7 intermediate recruiting HSC20 via LYRM7's LYR motif to
      deliver the [2Fe-2S] cluster to UQCRFS1. Strong mechanistic support for the core function.
- id: PMID:32296183
  title: A reference map of the human binary protein interactome.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      HuRI binary (Y2H) interactome; source of an IntAct LYRM7-SAT1 hit. SAT1 has no known
      mitochondrial/CIII role, so this is likely a non-physiological binary-screen interaction.
- id: PMID:33961781
  title: Dual proteome-scale networks reveal cell-specific remodeling of the human
    interactome.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      BioPlex proteome-scale interactome; source of an IntAct LYRM7-UQCRFS1 interaction consistent
      with the core client relationship.
- id: PMID:34800366
  title: Quantitative high-confidence human mitochondrial proteome and its dynamics
    in cellular context.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      High-confidence mitochondrial proteome; supports mitochondrial localisation of LYRM7 (HTP).
- id: PMID:40205054
  title: Multimodal cell maps as a foundation for structural and functional genomics.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      Large-scale cell-map interactome; source of an IntAct LYRM7-UQCRFS1 interaction consistent
      with the core client relationship.
- id: Reactome:R-HSA-9865881
  title: Complex III assembly
  findings: []
- id: Reactome:R-HSA-9866253
  title: apo-UQCRFS1 binds LYRM7
  findings: []
- id: Reactome:R-HSA-9866272
  title: 2Fe-2S is inserted in UQCRFS1
  findings: []
- id: file:human/LYRM7/LYRM7-uniprot.txt
  title: UniProtKB entry Q5U5X0 (LYRM7_HUMAN)
  findings: []
suggested_questions:
- question: >-
    Does LYRM7 act purely as a holdase that stabilises apo-UQCRFS1, or does it also
    actively template/position UQCRFS1 for [2Fe-2S] cluster receipt and membrane insertion?
suggested_experiments:
- description: >-
    Reconstitute the UQCRFS1-LYRM7 intermediate with the HSC20-HSPA9-ISCU Fe-S transfer complex
    in vitro to determine the minimal components and the order of cluster insertion versus
    membrane insertion of UQCRFS1.