id: Q86XE5
gene_symbol: HOGA1
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: HOGA1 (4-hydroxy-2-oxoglutarate aldolase, mitochondrial; EC 4.1.3.16;
  formerly DHDPSL/C10orf65) is a mitochondrial matrix enzyme that catalyzes the final
  step of the hydroxyproline (4-hydroxyproline) degradation pathway, performing the
  retro-aldol cleavage of 4-hydroxy-2-oxoglutarate (HOG) into glyoxylate and pyruvate.
  It belongs to the dihydrodipicolinate synthase (DapA/DHDPS) family and functions
  as a Schiff-base (type I) aldolase, using an active-site lysine (Lys196) as the
  catalytic nucleophile; the enzyme is active against both the (4R) and (4S) enantiomers
  of HOG. The mature protein, produced after cleavage of an N-terminal mitochondrial
  transit peptide, assembles into a homotetramer (dimer of dimers). HOGA1 is expressed
  most highly in kidney and liver, the principal sites of hydroxyproline turnover.
  Loss-of-function variants cause primary hyperoxaluria type 3 (PH3/HP3), an autosomal-recessive
  disorder of endogenous oxalate synthesis characterized by calcium oxalate urolithiasis.
existing_annotations:
- term:
    id: GO:0008700
    label: (R,S)-4-hydroxy-2-oxoglutarate aldolase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: Phylogenetically-inferred core molecular function. This is the enzyme's
      defining activity, directly confirmed for the human protein by structural and
      kinetic study.
    action: ACCEPT
    reason: This is the precise, correct molecular function of HOGA1, supported by
      direct biochemical characterization of the recombinant human enzyme and matching
      the IDA annotation from PMID:21998747. The IBA call is at the right level of
      specificity and represents the core function.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: The activity of recombinant hHOGA proves that it is indeed
        the aldolase identified in the genomic analysis of PH3 patients.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: Phylogenetically-inferred mitochondrial localization, consistent with
      the N-terminal mitochondrial transit peptide and the ortholog-based subcellular
      location.
    action: ACCEPT
    reason: HOGA1 carries an N-terminal mitochondrial transit peptide (residues 1-25)
      and is a mitochondrial-matrix enzyme; the IBA is-active-in mitochondrion annotation
      is correct.
    supported_by:
    - reference_id: file:human/HOGA1/HOGA1-uniprot.txt
      supporting_text: Mitochondrion {ECO:0000250|UniProtKB:Q0P5I5}
- term:
    id: GO:0009436
    label: glyoxylate catabolic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Phylogenetically-inferred participation in glyoxylate metabolism. HOGA1
      is a mitochondrial glyoxylate-generating enzyme in the hydroxyproline degradation
      pathway.
    action: KEEP_AS_NON_CORE
    reason: HOGA1 participates in mitochondrial glyoxylate metabolism, producing glyoxylate
      as a product of HOG cleavage. Note that HOGA1 generates rather than degrades
      glyoxylate, so "glyoxylate catabolic process" is a somewhat imperfect descriptor
      of its direct role; however it is the standard consortium call for the hydroxyproline/glyoxylate
      pathway and is not wrong at the pathway level. The core BP is hydroxyproline
      catabolism; retain this as a non-core pathway-participation annotation.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: In the terminal reaction, HOG is cleaved by HOGA to produce
        pyruvate and glyoxylate.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: Electronic mitochondrial localization from UniProt SubCell/ARBA, consistent
      with the transit peptide and experimental data.
    action: ACCEPT
    reason: Correct localization supported by the mitochondrial targeting sequence
      and multiple experimental/orthology-based annotations.
    supported_by:
    - reference_id: file:human/HOGA1/HOGA1-uniprot.txt
      supporting_text: Mitochondrion {ECO:0000250|UniProtKB:Q0P5I5}
- term:
    id: GO:0008700
    label: (R,S)-4-hydroxy-2-oxoglutarate aldolase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: Electronic annotation of the core aldolase activity from the ARBA/RHEA/EC
      mapping (EC 4.1.3.16, RHEA:30687).
    action: ACCEPT
    reason: Correct core molecular function, redundant with and consistent with the
      IBA and IDA annotations to the same term. EC 4.1.3.16 is the enzyme's assigned
      EC number.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: hHOGA performs a retro-aldol cleavage reaction reminiscent of
        the trimeric 2-keto-3-deoxy-6-phosphogluconate aldolases.
- term:
    id: GO:0009436
    label: glyoxylate catabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: involved_in
  review:
    summary: Electronic (ARBA) annotation to glyoxylate catabolic process, duplicating
      the IBA/IMP calls to the same term.
    action: KEEP_AS_NON_CORE
    reason: Same reasoning as the IBA glyoxylate catabolic process annotation - a
      valid pathway-participation term but not the core BP (which is hydroxyproline
      catabolism). Keep as non-core.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: In the terminal reaction, HOG is cleaved by HOGA to produce
        pyruvate and glyoxylate.
- term:
    id: GO:0016829
    label: lyase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: InterPro2GO electronic annotation to the broad parent term lyase activity,
      based on the DapA-like domain.
    action: MARK_AS_OVER_ANNOTATED
    reason: "\"lyase activity\" is a correct but uninformatively general ancestor of\
      \ the specific molecular function (GO:0008700, an aldolase, which is a carbon-carbon\
      \ lyase). It is subsumed by the more precise aldolase-activity annotations and\
      \ adds no information; mark as over-annotated rather than removed since it is\
      \ not wrong."
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: hHOGA performs a retro-aldol cleavage reaction reminiscent of
        the trimeric 2-keto-3-deoxy-6-phosphogluconate aldolases.
- term:
    id: GO:0106009
    label: (4S)-4-hydroxy-2-oxoglutarate aldolase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000116
  qualifier: enables
  review:
    summary: RHEA-based electronic annotation of the (4S)-stereospecific aldolase
      activity (RHEA:35639).
    action: ACCEPT
    reason: HOGA1 cleaves the (4S) enantiomer of HOG (RHEA:35639), so this stereospecific
      child term is correct. The enzyme also acts on the (4R) form, hence the broader
      (R,S) term GO:0008700 is retained as the primary MF; both are legitimate.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: Previous studies have shown that the bovine kidney, bovine liver,
        and rat liver enzymes have equal activity against the R- and S-forms of HOG
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:27499296
  qualifier: enables
  review:
    summary: High-throughput mitochondrial protein-interaction screen; captured interaction
      with STARD7 (Q9NQZ5). Uninformative bare "protein binding" term.
    action: MARK_AS_OVER_ANNOTATED
    reason: "\"protein binding\" (GO:0005515) is an uninformative molecular-function\
      \ term that does not describe HOGA1's activity. This IPI derives from a large-scale\
      \ mitochondrial protein-interaction mapping study, with no evidence that the\
      \ interaction is functionally relevant to the aldolase. Per curation policy,\
      \ bare protein-binding IPIs are marked as over-annotated rather than removed."
    supported_by:
    - reference_id: PMID:27499296
      supporting_text: 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
  qualifier: enables
  review:
    summary: High-throughput affinity-purification interactome screen (BioPlex); captured
      interaction with USP47 (Q96K76). Uninformative bare "protein binding" term.
    action: MARK_AS_OVER_ANNOTATED
    reason: Uninformative "protein binding" term from a proteome-scale interactome
      dataset, with no evidence of functional relevance to HOGA1's catalytic role.
      Marked as over-annotated per policy on bare protein-binding IPIs.
    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:32296183
  qualifier: enables
  review:
    summary: High-throughput binary (Y2H) interactome screen (HuRI); captured interaction
      with CIMAP1A (Q96PU9). Uninformative bare "protein binding" term.
    action: MARK_AS_OVER_ANNOTATED
    reason: Uninformative "protein binding" term from a systematic binary-interactome
      map, with no evidence of functional relevance to the aldolase activity. Marked
      as over-annotated per policy on bare protein-binding IPIs.
    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: High-throughput affinity-purification interactome screen (BioPlex 3.0);
      captured interaction with USP47 (Q96K76). Uninformative bare "protein binding"
      term.
    action: MARK_AS_OVER_ANNOTATED
    reason: Uninformative "protein binding" term from a proteome-scale interactome
      dataset, duplicating the other HT interaction annotations. Marked as over-annotated
      per policy on bare protein-binding IPIs.
    supported_by:
    - reference_id: PMID:33961781
      supporting_text: Dual proteome-scale networks reveal cell-specific remodeling
        of the human interactome.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: HTP
  original_reference_id: PMID:34800366
  qualifier: located_in
  review:
    summary: High-throughput identification of HOGA1 in the high-confidence human
      mitochondrial proteome.
    action: ACCEPT
    reason: Independent proteomic evidence for mitochondrial localization, consistent
      with the transit peptide and all other localization annotations.
    supported_by:
    - reference_id: PMID:34800366
      supporting_text: Quantitative high-confidence human mitochondrial proteome and
        its dynamics in cellular context.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: located_in
  review:
    summary: Sequence-similarity transfer of mitochondrial localization from the bovine
      ortholog (Q0P5I5).
    action: ACCEPT
    reason: Correct localization; the bovine ortholog was purified from kidney mitochondria
      and human HOGA1 has the corresponding transit peptide.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: mitochondrial enzyme purified from bovine kidney
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6784423
  qualifier: located_in
  review:
    summary: Reactome-curated localization of the HOGA1-catalyzed HOG cleavage reaction
      to the mitochondrial matrix.
    action: ACCEPT
    reason: Mitochondrial matrix is the precise sub-compartment for this soluble matrix
      aldolase; more specific than "mitochondrion" and consistent with the pathway
      context. This is the best cellular-component term.
    supported_by:
    - reference_id: Reactome:R-HSA-6784423
      supporting_text: aldol-cleaves 4-OH-2-oxoglutarate (HOG) to glyoxylate and pyruvate
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: ISS
  original_reference_id: PMID:21998747
  qualifier: located_in
  review:
    summary: Sequence-similarity-based mitochondrial localization annotation (BHF-UCL),
      referencing the structural/biochemical paper and bovine ortholog.
    action: ACCEPT
    reason: Correct mitochondrial localization; the human enzyme was characterized
      from the mitochondrial hydroxyproline pathway and the bovine ortholog was purified
      from kidney mitochondria.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: mitochondrial enzyme purified from bovine kidney
- term:
    id: GO:0008700
    label: (R,S)-4-hydroxy-2-oxoglutarate aldolase activity
  evidence_type: IDA
  original_reference_id: PMID:21998747
  qualifier: enables
  review:
    summary: Direct assay of recombinant human HOGA1 aldolase activity, including
      crystal structure, catalytic-residue mutagenesis (Lys196, Tyr168), and kinetics.
    action: ACCEPT
    reason: This is the definitive experimental demonstration of HOGA1's core molecular
      function. Recombinant human enzyme performs retro-aldol cleavage of HOG; catalytic
      mutants (K196A, Y168F) abolish activity, establishing the mechanism. Core function.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: The Y168F and K196A hHOGA variants exhibited no enzymatic activity
    - reference_id: PMID:21998747
      supporting_text: The activity of recombinant hHOGA proves that it is indeed
        the aldolase identified in the genomic analysis of PH3 patients.
- term:
    id: GO:0019470
    label: trans-4-hydroxy-L-proline catabolic process
  evidence_type: IDA
  original_reference_id: PMID:21998747
  qualifier: involved_in
  review:
    summary: HOGA1 catalyzes the terminal (final) step of the four-enzyme mitochondrial
      hydroxyproline degradation pathway.
    action: ACCEPT
    reason: This is the core biological process for HOGA1. The enzyme catalyzes the
      terminal step of 4-hydroxyproline catabolism, and UniProt describes its function
      as catalyzing the final step in the metabolic pathway of hydroxyproline.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: The degradation pathway for 4-Hyp (Figure 1) involves the step-wise
        action of four mitochondrial enzymes
    - reference_id: file:human/HOGA1/HOGA1-uniprot.txt
      supporting_text: Catalyzes the final step in the metabolic pathway of
- term:
    id: GO:0033609
    label: oxalate metabolic process
  evidence_type: IMP
  original_reference_id: PMID:21896830
  qualifier: involved_in
  review:
    summary: HOGA1 variants influence urinary oxalate; loss-of-function mutations
      cause primary hyperoxaluria type 3, linking HOGA1 function to oxalate homeostasis.
    action: KEEP_AS_NON_CORE
    reason: The connection to oxalate metabolism is real but indirect - HOGA1 does
      not act on oxalate directly; rather, its dysfunction perturbs glyoxylate/oxalate
      handling and causes hyperoxaluria (PH3). This is a disease-level/physiological
      link rather than the enzyme's direct catalytic role, so keep as non-core.
    supported_by:
    - reference_id: PMID:21896830
      supporting_text: hypothesized to cause a gain of mitochondrial 4-hydroxy-2-oxoglutarate
        aldolase
    - reference_id: PMID:21896830
      supporting_text: HOGA1 may be a predisposing factor for this
- term:
    id: GO:0042803
    label: protein homodimerization activity
  evidence_type: IDA
  original_reference_id: PMID:21998747
  qualifier: enables
  review:
    summary: Structural study shows HOGA1 assembles via a "tight" dimer interface
      into a homotetramer (dimer of dimers); the active site lies at the dimer interface.
    action: ACCEPT
    reason: The crystal structure directly demonstrates self-association. The biological
      assembly is a homotetramer, but it is built as a dimer of dimers, and the active
      site is formed at the tight dimer interface (a residue from the adjacent monomer,
      Tyr140', contributes to the active site), so homodimerization is a genuine,
      structurally-supported self-association activity. UniProt records the assembly
      as a homotetramer.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: reveal a tetrameric structure composed of a dimer of dimers
    - reference_id: file:human/HOGA1/HOGA1-uniprot.txt
      supporting_text: 'SUBUNIT: Homotetramer'
- term:
    id: GO:0042866
    label: pyruvate biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:21998747
  qualifier: involved_in
  review:
    summary: Pyruvate is a co-product of the HOGA1-catalyzed cleavage of HOG (HOG
      -> glyoxylate + pyruvate).
    action: KEEP_AS_NON_CORE
    reason: Pyruvate is genuinely produced by the HOGA1 reaction, so this annotation
      is factually correct. However, pyruvate is a minor co-product of hydroxyproline
      catabolism and HOGA1 is not a dedicated pyruvate-biosynthetic enzyme; keep as
      a non-core annotation rather than a core function.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: In the terminal reaction, HOG is cleaved by HOGA to produce
        pyruvate and glyoxylate.
- term:
    id: GO:0046487
    label: glyoxylate metabolic process
  evidence_type: IDA
  original_reference_id: PMID:21998747
  qualifier: involved_in
  review:
    summary: HOGA1 produces glyoxylate as a product of HOG cleavage, participating
      in mitochondrial glyoxylate metabolism.
    action: KEEP_AS_NON_CORE
    reason: Correct - HOGA1 generates glyoxylate, so it participates in glyoxylate
      metabolic process. This is a more accurate parent than "glyoxylate catabolic
      process" (since HOGA1 makes, not degrades, glyoxylate), but it is a downstream/pathway
      annotation rather than the core hydroxyproline-catabolic function; keep as non-core.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: In the terminal reaction, HOG is cleaved by HOGA to produce
        pyruvate and glyoxylate.
- term:
    id: GO:0009436
    label: glyoxylate catabolic process
  evidence_type: IMP
  original_reference_id: PMID:20797690
  qualifier: involved_in
  review:
    summary: Mutations in HOGA1 (DHDPSL) cause primary hyperoxaluria type 3, establishing
      HOGA1's role in the glyoxylate/hydroxyproline pathway by loss of function.
    action: KEEP_AS_NON_CORE
    reason: The disease-based IMP correctly places HOGA1 in the glyoxylate pathway,
      but "glyoxylate catabolic process" is an imperfect descriptor since HOGA1 produces
      rather than degrades glyoxylate; the core BP is hydroxyproline catabolism. Retain
      as a non-core pathway-participation annotation.
    supported_by:
    - reference_id: PMID:20797690
      supporting_text: cause a third type of PH (PH III)
    - reference_id: PMID:20797690
      supporting_text: the gene encoding 4-hydroxy-2-oxoglutarate
- term:
    id: GO:0008700
    label: (R,S)-4-hydroxy-2-oxoglutarate aldolase activity
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: enables
  review:
    summary: Sequence-similarity transfer of the core aldolase activity from the bovine
      ortholog (Q0P5I5), which shares ~90% identity with human HOGA1.
    action: ACCEPT
    reason: Correct core molecular function, redundant with the direct experimental
      (IDA) annotation to the same term. The bovine ortholog is 90.2% identical and
      functionally characterized.
    supported_by:
    - reference_id: PMID:21998747
      supporting_text: Sequence comparison of human HOGA with bovine HOGA (90.2% identity)
core_functions:
- description: Catalyzes the terminal step of the mitochondrial 4-hydroxyproline degradation
    pathway, the retro-aldol cleavage of 4-hydroxy-2-oxoglutarate (HOG) into glyoxylate
    and pyruvate, via a Schiff-base (type I aldolase) mechanism using Lys196 as the
    catalytic nucleophile.
  molecular_function:
    id: GO:0008700
    label: (R,S)-4-hydroxy-2-oxoglutarate aldolase activity
  directly_involved_in:
  - id: GO:0019470
    label: trans-4-hydroxy-L-proline catabolic process
  locations:
  - id: GO:0005759
    label: mitochondrial matrix
  supported_by:
  - reference_id: PMID:21998747
    supporting_text: In the terminal reaction, HOG is cleaved by HOGA to produce pyruvate
      and glyoxylate.
  - reference_id: PMID:21998747
    supporting_text: The Y168F and K196A hHOGA variants exhibited no enzymatic activity
  - reference_id: file:human/HOGA1/HOGA1-uniprot.txt
    supporting_text: Catalyzes the final step in the metabolic pathway of
proposed_new_terms: []
suggested_questions:
- question: Given that HOGA1 produces glyoxylate (an oxalate precursor), what is the
    precise mechanism by which HOGA1 loss-of-function causes hyperoxaluria in PH3 -
    accumulation of HOG or upstream intermediates, dominant-negative effects, or dysregulation
    of glyoxylate detoxification?
suggested_experiments:
- description: Metabolomic quantification of HOG, glyoxylate, and oxalate in HOGA1-deficient
    versus wild-type hepatocyte/renal models to test whether HOG accumulation (rather
    than loss of glyoxylate production) drives the hyperoxaluric phenotype.
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- 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:0000116
  title: Automatic Gene Ontology annotation based on Rhea mapping
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:20797690
  title: Mutations in DHDPSL are responsible for primary hyperoxaluria type III.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified. Identifies DHDPSL/HOGA1 mutations as the cause of
      primary hyperoxaluria type 3 and proposes HOGA1 as the gene encoding 4-hydroxy-2-oxoglutarate
      aldolase.
- id: PMID:21896830
  title: Primary hyperoxaluria type III gene HOGA1 (formerly DHDPSL) as a possible
    risk factor for idiopathic calcium oxalate urolithiasis.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified. Supports a loss-of-function mechanism for HOGA1
      and links HOGA1 variants to oxalate/urolithiasis risk.
- id: PMID:21998747
  title: 'Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase:
    implications for hydroxyproline metabolism in primary hyperoxaluria.'
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified full text. Definitive structural and enzymatic characterization
      of human HOGA1 - retro-aldol cleavage of HOG to pyruvate and glyoxylate, homotetramer
      (dimer of dimers), catalytic residues Lys196/Tyr168, terminal step of hydroxyproline
      degradation.
- id: PMID:27499296
  title: Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory
    Chain Function.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: High-throughput mitochondrial protein-interaction mapping; source
      of a bare "protein binding" IPI (STARD7). Not informative for HOGA1's molecular
      function.
- id: PMID:28514442
  title: Architecture of the human interactome defines protein communities and disease
    networks.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Proteome-scale interactome (BioPlex); source of a bare "protein binding"
      IPI (USP47). Not informative for molecular function.
- id: PMID:32296183
  title: A reference map of the human binary protein interactome.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Binary interactome map (HuRI); source of a bare "protein binding"
      IPI (CIMAP1A). Not informative for molecular function.
- id: PMID:33961781
  title: Dual proteome-scale networks reveal cell-specific remodeling of the human
    interactome.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Proteome-scale interactome (BioPlex 3.0); source of a bare "protein
      binding" IPI (USP47). Not informative for molecular function.
- 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; independent proteomic support
      for mitochondrial localization of HOGA1.
- id: Reactome:R-HSA-6784423
  title: HOGA1 tetramer aldol-cleaves 4-OH-2-oxoglutarate (HOG) to glyoxylate and
    pyruvate
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Reactome reaction curating the HOGA1-catalyzed HOG cleavage in the
      mitochondrial matrix.
- id: file:human/HOGA1/HOGA1-uniprot.txt
  title: UniProt entry Q86XE5 (HOGA1_HUMAN)
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: UniProt/Swiss-Prot record; source of function, subunit, subcellular
      location, transit peptide, active-site, and disease annotations.