id: Q9H2F3
gene_symbol: HSD3B7
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: HSD3B7 (3 beta-hydroxysteroid dehydrogenase type 7; 3-beta-hydroxy-Delta(5)-C27-steroid
  oxidoreductase, EC 1.1.1.181) catalyzes the second committed step of bile-acid biosynthesis.
  Acting on the 7-alpha-hydroxylated sterols generated by CYP7A1/CYP7B1, it oxidizes the
  3-beta-hydroxyl group and isomerizes the Delta5 double bond, converting 7-alpha-hydroxycholesterol
  (and related 7-alpha-hydroxy-oxysterols such as 7-alpha,25-, 7-alpha,26- and 7-alpha,24-triols)
  to the corresponding 3-oxo-Delta4 intermediates, e.g. 7-alpha-hydroxy-4-cholesten-3-one.
  A single such enzyme feeds all known pathways of bile-acid synthesis. It is specific for
  C27 bile-acid-precursor sterols and does not metabolize the C19/C21 steroids handled by
  the steroidogenic paralogs HSD3B1/HSD3B2 (with which it shares only ~34% identity). HSD3B7
  is a multi-pass endoplasmic-reticulum-membrane (microsomal) enzyme expressed predominantly
  in liver. Loss-of-function mutations cause congenital bile acid synthesis defect type 1
  (CBAS1), presenting as neonatal cholestasis, progressive liver disease and fat-soluble-vitamin
  malabsorption. By acting on the oxysterol 7-alpha,25-dihydroxycholesterol, the enzyme also
  contributes to turnover of the EBI2/GPR183 ligand that positions lymphocytes in lymphoid
  tissue.
alternative_products:
- name: '1'
  id: Q9H2F3-1
- name: '2'
  id: Q9H2F3-2
  sequence_note: VSP_042658
existing_annotations:
- term:
    id: GO:0016616
    label: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP
      as acceptor
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: Broad phylogenetically-inferred molecular-function term correctly placing
      HSD3B7 as an NAD(P)-dependent dehydrogenase acting on a CH-OH group. This is
      accurate but general; the specific activity is the 3-beta-hydroxy-Delta5-steroid
      dehydrogenase reaction on 7-alpha-hydroxylated C27 sterols.
    action: MODIFY
    reason: The IBA term is correct at the family level but too general for a gene
      with a demonstrated specific catalytic activity. Retain the parent but propose
      the specific dehydrogenase terms already supported by experiment (GO:0003854,
      GO:0047016) as the core molecular function.
    proposed_replacement_terms:
    - id: GO:0003854
      label: 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity
    - id: GO:0047016
      label: cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity
    propagation_review:
      root_cause: TERM_SCOPING_PROBLEM
      failure_modes:
      - GRANULARITY_MISMATCH
      source_entities:
      - source_id: PANTHER:PTN000041225
        source_label: 3-beta-HSD family node (GO_Central IBA)
        source_status: SUPPORTS_TRANSFER
        comment: Family-level IBA correctly assigns the general NAD(P)-dependent CH-OH
          dehydrogenase activity, but HSD3B7 has a demonstrated more specific
          3-beta-hydroxy-Delta5-C27-steroid dehydrogenase activity (PMID:11067870).
    supported_by:
    - reference_id: file:human/HSD3B7/HSD3B7-uniprot.txt
      supporting_text: HSD VII is active
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: HSD3B7 is a multi-pass endoplasmic reticulum membrane (microsomal) protein;
      this UniProt SubCellular-mapping IEA correctly captures the primary localization.
    action: ACCEPT
    reason: The ER membrane localization is directly stated in UniProt (SUBCELLULAR
      LOCATION) and consistent with the microsomal enzyme described in PMID:11067870
      and with the two predicted transmembrane helices. This is a core aspect of the
      annotation.
    supported_by:
    - reference_id: file:human/HSD3B7/HSD3B7-uniprot.txt
      supporting_text: 'Endoplasmic reticulum membrane; Multi-pass'
- term:
    id: GO:0006694
    label: steroid biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: involved_in
  review:
    summary: Broad biosynthetic-process term. HSD3B7 participates in steroid (sterol/bile-acid)
      biosynthesis, so the term is not wrong, but the specific and better-supported
      process is bile acid biosynthesis (GO:0006699).
    action: MODIFY
    reason: Bile-acid precursors are C27 sterols and the enzyme is specific for the
      bile-acid pathway; the more informative process term GO:0006699 is preferred.
      The broad steroid-biosynthesis term is retained conceptually but should be specialized.
    proposed_replacement_terms:
    - id: GO:0006699
      label: bile acid biosynthetic process
    supported_by:
    - reference_id: file:human/HSD3B7/HSD3B7-uniprot.txt
      supporting_text: 'Lipid metabolism; steroid biosynthesis'
- term:
    id: GO:0016616
    label: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP
      as acceptor
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: Same broad dehydrogenase molecular-function term as the IBA annotation,
      here from InterPro/ARBA. Correct but general.
    action: MODIFY
    reason: Correct family-level assignment (NAD(P)-dependent CH-OH oxidoreductase),
      but a more specific term is warranted given the demonstrated 3-beta-hydroxy-Delta5-steroid
      dehydrogenase activity. Propose the specific MF terms.
    proposed_replacement_terms:
    - id: GO:0003854
      label: 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity
    - id: GO:0047016
      label: cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity
    supported_by:
    - reference_id: file:human/HSD3B7/HSD3B7-uniprot.txt
      supporting_text: HSD VII is active
- term:
    id: GO:0047016
    label: cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: Specific molecular-function term (EC 1.1.1.181) for the 3-beta-dehydrogenation
      of the 7-alpha-hydroxylated sterol cholest-5-ene-3-beta,7-alpha-diol (7-alpha-hydroxycholesterol).
      This is the demonstrated activity of HSD3B7 and is the core function; here inferred
      electronically but corroborated by experiment (PMID:11067870).
    action: ACCEPT
    reason: This is exactly the biochemically characterized activity of HSD3B7 acting
      on 7-alpha-hydroxycholesterol, matching the UniProt catalytic-activity entry (Rhea:11896,
      EC 1.1.1.181). Accept as a core molecular function.
    supported_by:
    - reference_id: PMID:11067870
      supporting_text: active against four 7alpha-hydroxylated sterols
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25416956
  qualifier: enables
  review:
    summary: Generic protein-binding annotation from a proteome-scale (HuRI/CCSB) binary
      interactome screen. The partner (SPRY2, O43597) is not part of a functionally
      characterized HSD3B7 complex, and the bare protein-binding term is uninformative
      about the enzyme's molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: High-throughput interactome hits assigned only the uninformative GO:0005515
      term. Per curation guidance, bare protein binding does not describe HSD3B7's
      catalytic function; this is retained as an over-annotation rather than removed,
      since the interaction data itself is experimental.
    supported_by:
    - reference_id: PMID:25416956
      supporting_text: A proteome-scale map of the human interactome network
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32296183
  qualifier: enables
  review:
    summary: Generic protein-binding annotations from the HuRI binary interactome map,
      covering many heterogeneous partners (keratin-associated proteins, transcription
      factors, etc.). None represent a defined functional HSD3B7 complex, and the term
      is uninformative about molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: These are large-scale yeast-two-hybrid/binary-screen hits annotated only
      to the bare GO:0005515 term. Not informative for HSD3B7's dehydrogenase function;
      marked as over-annotated per policy rather than removed.
    supported_by:
    - reference_id: PMID:32296183
      supporting_text: A reference map of the human binary protein interactome
- term:
    id: GO:0035754
    label: B cell chemotaxis
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Biological-process annotation transferred by Ensembl Compara from the
      mouse ortholog (Q9EQC1), reflecting HSD3B7's role in degrading the oxysterol
      7-alpha,25-dihydroxycholesterol, an EBI2/GPR183 ligand that positions B cells
      in lymphoid tissue.
    action: KEEP_AS_NON_CORE
    reason: This is a genuine but downstream/physiological consequence inferred from
      the mouse ortholog, not HSD3B7's core catalytic role in bile-acid synthesis.
      The human enzyme does act on 7-alpha,25-OHC in vitro (UniProt catalytic activity
      Rhea:47156), supporting relevance, but the process is peripheral and evidence
      is by-similarity; keep as non-core.
    supported_by:
    - reference_id: file:human/HSD3B7/HSD3B7-uniprot.txt
      supporting_text: Plays a key role in cell positioning and
- term:
    id: GO:0006699
    label: bile acid biosynthetic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-193368
  qualifier: involved_in
  review:
    summary: HSD3B7 catalyzes the second step of the classic (neutral) bile-acid pathway
      via 7-alpha-hydroxycholesterol; Reactome annotates its participation in bile
      acid biosynthesis. This is a core biological process for HSD3B7.
    action: ACCEPT
    reason: Bile acid biosynthesis is the central, disease-defining role of HSD3B7,
      established biochemically and genetically (PMID:11067870). Accept as core.
    supported_by:
    - reference_id: PMID:11067870
      supporting_text: a single C(27) 3beta-HSD enzyme can
        participate in all known pathways of bile acid synthesis
- term:
    id: GO:0006699
    label: bile acid biosynthetic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-193775
  qualifier: involved_in
  review:
    summary: Participation in bile-acid/bile-salt synthesis via the 24-hydroxycholesterol
      (acidic/alternative) branch; HSD3B7 performs the 3-beta-dehydrogenation/isomerization
      step on the 7-alpha-hydroxylated 24-hydroxy sterol. Core bile-acid process annotation.
    action: ACCEPT
    reason: Duplicate of the core bile-acid biosynthetic process annotation, from a
      different Reactome pathway branch. Correct and core; the enzyme acts across all
      bile-acid pathway branches.
    supported_by:
    - reference_id: PMID:11067870
      supporting_text: a single C(27) 3beta-HSD enzyme can
        participate in all known pathways of bile acid synthesis
- term:
    id: GO:0006699
    label: bile acid biosynthetic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-193807
  qualifier: involved_in
  review:
    summary: Participation in bile-acid/bile-salt synthesis via the 27-hydroxycholesterol
      branch. HSD3B7 acts on the 7-alpha-hydroxylated 27-hydroxy sterol. Core bile-acid
      process annotation.
    action: ACCEPT
    reason: Duplicate of the core bile-acid biosynthetic process annotation from another
      Reactome branch. Consistent with the enzyme's broad substrate range across
      bile-acid pathways.
    supported_by:
    - reference_id: PMID:11067870
      supporting_text: a single C(27) 3beta-HSD enzyme can
        participate in all known pathways of bile acid synthesis
- term:
    id: GO:0003854
    label: 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-192097
  qualifier: enables
  review:
    summary: Core molecular function - NAD+-dependent 3-beta-hydroxy-Delta5-steroid
      dehydrogenase (with associated isomerase activity). Reactome R-HSA-192097 describes
      HSD3B7 oxidizing/isomerizing 7-alpha-hydroxycholesterol to 4-cholesten-7-alpha-ol-3-one.
    action: ACCEPT
    reason: This is the defining catalytic activity of HSD3B7, supported by biochemistry
      (PMID:11067870) and by the Reactome reaction. Accept as a core molecular function.
    supported_by:
    - reference_id: Reactome:R-HSA-192097
      supporting_text: catalyzed by HSD3B7 (3 beta-hydroxysteroid
        dehydrogenase type 7) in the endoplasmic reticulum membrane
- term:
    id: GO:0003854
    label: 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-193789
  qualifier: enables
  review:
    summary: Same core 3-beta-hydroxy-Delta5-steroid dehydrogenase activity, annotated
      from the Reactome reaction on cholest-5-ene-3beta,7alpha,24(S)-triol (the 24-hydroxy
      branch substrate).
    action: ACCEPT
    reason: Duplicate core molecular-function annotation from another Reactome reaction;
      correct and central to HSD3B7 function.
    supported_by:
    - reference_id: Reactome:R-HSA-193789
      supporting_text: catalyzed by HSD3B7 (3 beta-hydroxysteroid dehydrogenase type 7)
        in the endoplasmic reticulum membrane
- term:
    id: GO:0003854
    label: 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-193816
  qualifier: enables
  review:
    summary: Same core 3-beta-hydroxy-Delta5-steroid dehydrogenase activity, annotated
      from the Reactome reaction on cholest-5-ene-3beta,7alpha,27-triol (the 27-hydroxy
      branch substrate).
    action: ACCEPT
    reason: Duplicate core molecular-function annotation from another Reactome reaction;
      correct and central to HSD3B7 function.
    supported_by:
    - reference_id: Reactome:R-HSA-193816
      supporting_text: in a reaction catalyzed by HSD3B7 (3 beta-hydroxysteroid
        dehydrogenase type 7) in the endoplasmic reticulum membrane
- term:
    id: GO:0005811
    label: lipid droplet
  evidence_type: IDA
  original_reference_id: GO_REF:0000052
  qualifier: located_in
  review:
    summary: Immunofluorescence-based (HPA) localization to lipid droplets. HSD3B7's
      mechanistically-supported and primary compartment is the ER membrane; a lipid-droplet
      signal is plausible for an ER-associated lipid-metabolizing enzyme but is secondary.
    action: KEEP_AS_NON_CORE
    reason: The IDA/HPA lipid-droplet signal is a real immunolocalization observation
      but is not the primary functional compartment (ER membrane, multi-pass). Lipid
      droplets are ER-derived and this may reflect ER continuity; retain as non-core
      rather than treat as a core localization.
    supported_by:
    - reference_id: file:human/HSD3B7/HSD3B7-uniprot.txt
      supporting_text: 'Endoplasmic reticulum membrane; Multi-pass'
- term:
    id: GO:0047016
    label: cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity
  evidence_type: EXP
  original_reference_id: PMID:11067870
  qualifier: enables
  review:
    summary: Experimentally demonstrated activity - the expression-cloned C27 3beta-HSD
      acts on 7-alpha-hydroxylated sterols (cholest-5-ene-3-beta,7-alpha-diol, i.e.
      7-alpha-hydroxycholesterol), catalyzing the 3-beta-dehydrogenation (EC 1.1.1.181).
      This is the specific, disease-relevant core molecular function.
    action: ACCEPT
    reason: Direct experimental evidence (transfection/activity assay) for this exact
      specific activity in the defining paper. Core molecular function.
    supported_by:
    - reference_id: PMID:11067870
      supporting_text: active against four 7alpha-hydroxylated sterols
- term:
    id: GO:0035754
    label: B cell chemotaxis
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: Sequence-similarity transfer from the mouse ortholog (Q9EQC1) of the role
      in lymphocyte positioning via degradation of the EBI2/GPR183 ligand 7-alpha,25-dihydroxycholesterol.
    action: KEEP_AS_NON_CORE
    reason: Same physiological role as the Ensembl IEA annotation, here as manual ISS
      from mouse. Genuine but peripheral relative to HSD3B7's core bile-acid catalytic
      function, and inferred by similarity; keep as non-core.
    supported_by:
    - reference_id: file:human/HSD3B7/HSD3B7-uniprot.txt
      supporting_text: Plays a key role in cell positioning and
- term:
    id: GO:0047016
    label: cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: enables
  review:
    summary: Sequence-similarity transfer (from mouse Q9EQC1) of the specific 3-beta-dehydrogenase
      activity on 7-alpha-hydroxycholesterol. Corroborates the experimentally-established
      human activity.
    action: ACCEPT
    reason: The specific MF is independently demonstrated experimentally for the human
      enzyme (PMID:11067870); the ISS transfer is consistent and correct. Accept as
      core molecular function.
    supported_by:
    - reference_id: PMID:11067870
      supporting_text: active against four 7alpha-hydroxylated sterols
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-192097
  qualifier: located_in
  review:
    summary: ER-membrane localization asserted by Reactome for the HSD3B7-catalyzed
      reaction. Consistent with UniProt (multi-pass ER membrane) and the microsomal
      enzyme described in PMID:11067870. Core localization.
    action: ACCEPT
    reason: Correct and core; matches the authoritative UniProt subcellular location
      and the biochemistry (microsomal fraction).
    supported_by:
    - reference_id: Reactome:R-HSA-192097
      supporting_text: catalyzed by HSD3B7 (3 beta-hydroxysteroid
        dehydrogenase type 7) in the endoplasmic reticulum membrane
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-193789
  qualifier: located_in
  review:
    summary: Duplicate ER-membrane localization from another Reactome reaction for
      HSD3B7. Core localization.
    action: ACCEPT
    reason: Correct and core; consistent with UniProt subcellular location.
    supported_by:
    - reference_id: Reactome:R-HSA-193789
      supporting_text: catalyzed by HSD3B7 (3 beta-hydroxysteroid dehydrogenase type 7)
        in the endoplasmic reticulum membrane
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-193816
  qualifier: located_in
  review:
    summary: Duplicate ER-membrane localization from another Reactome reaction for
      HSD3B7. Core localization.
    action: ACCEPT
    reason: Correct and core; consistent with UniProt subcellular location.
    supported_by:
    - reference_id: Reactome:R-HSA-193816
      supporting_text: in a reaction catalyzed by HSD3B7 (3 beta-hydroxysteroid dehydrogenase type 7)
        in the endoplasmic reticulum membrane
- term:
    id: GO:0003854
    label: 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity
  evidence_type: NAS
  original_reference_id: PMID:11067870
  qualifier: enables
  review:
    summary: Non-traceable-author-statement assignment of the general 3-beta-hydroxy-Delta5-steroid
      dehydrogenase (NAD+) activity, sourced to the defining paper. Consistent with
      the experimentally-established specific activity.
    action: ACCEPT
    reason: The core dehydrogenase molecular function is well supported by the same
      paper's experiments (PMID:11067870). Accept.
    supported_by:
    - reference_id: PMID:11067870
      supporting_text: active against four 7alpha-hydroxylated sterols
- term:
    id: GO:0006699
    label: bile acid biosynthetic process
  evidence_type: TAS
  original_reference_id: PMID:11067870
  qualifier: involved_in
  review:
    summary: The defining paper establishes HSD3B7's central role in bile-acid biosynthesis;
      TAS annotation of the core biological process. Loss of activity causes a bile-acid
      synthesis defect (CBAS1).
    action: ACCEPT
    reason: Central, disease-defining biological process supported directly by PMID:11067870.
      Accept as core.
    supported_by:
    - reference_id: PMID:11067870
      supporting_text: establish the central role of C(27) 3beta-HSD in the
        biosynthesis of bile acids
core_functions:
- description: NAD+-dependent 3-beta-hydroxy-Delta5-steroid dehydrogenase/isomerase that
    oxidizes the 3-beta-hydroxyl and isomerizes the Delta5 double bond of 7-alpha-hydroxylated
    C27 sterols (e.g. 7-alpha-hydroxycholesterol -> 7-alpha-hydroxy-4-cholesten-3-one),
    the second step of bile-acid biosynthesis.
  molecular_function:
    id: GO:0003854
    label: 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity
  directly_involved_in:
  - id: GO:0006699
    label: bile acid biosynthetic process
  locations:
  - id: GO:0005789
    label: endoplasmic reticulum membrane
  supported_by:
  - reference_id: PMID:11067870
    supporting_text: active against four 7alpha-hydroxylated sterols
- description: Specific 3-beta-dehydrogenation of the 7-alpha-hydroxylated sterol
    cholest-5-ene-3-beta,7-alpha-diol (7-alpha-hydroxycholesterol), EC 1.1.1.181,
    the biochemically demonstrated bile-acid-precursor-specific activity of HSD3B7.
  molecular_function:
    id: GO:0047016
    label: cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity
  directly_involved_in:
  - id: GO:0006699
    label: bile acid biosynthetic process
  locations:
  - id: GO:0005789
    label: endoplasmic reticulum membrane
  supported_by:
  - reference_id: PMID:11067870
    supporting_text: active against four 7alpha-hydroxylated sterols
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: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: file:human/HSD3B7/HSD3B7-uniprot.txt
  title: UniProtKB Q9H2F3 (3BHS7_HUMAN) - 3 beta-hydroxysteroid dehydrogenase type 7
  findings: []
- id: PMID:11067870
  title: The bile acid synthetic gene 3beta-hydroxy-Delta(5)-C(27)-steroid oxidoreductase
    is mutated in progressive intrahepatic cholestasis.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified defining paper; expression cloning shows the C27
      3beta-HSD acts on four 7-alpha-hydroxylated sterols, does not metabolize C19/21
      steroids, and that loss of activity causes neonatal cholestasis. Abstract-only
      in cache (full_text_available false); quotes taken verbatim from the abstract.
- id: PMID:25416956
  title: A proteome-scale map of the human interactome network.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: High-throughput interactome map (HuRI/CCSB); source of bare protein-binding
      IPI. Correctly cited but uninformative for HSD3B7's molecular 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 interactome map; source of numerous bare protein-binding
      IPIs. Correctly cited but uninformative for HSD3B7's molecular function.
- id: Reactome:R-HSA-192097
  title: 7alpha-hydroxycholesterol is oxidized and isomerized to 4-cholesten-7alpha-ol-3-one
  findings: []
- id: Reactome:R-HSA-193368
  title: Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
  findings: []
- id: Reactome:R-HSA-193775
  title: Synthesis of bile acids and bile salts via 24-hydroxycholesterol
  findings: []
- id: Reactome:R-HSA-193789
  title: Cholest-5-ene-3beta,7alpha,24(S)-triol is oxidized and isomerized to 4-cholesten-7alpha,24(S)-diol-3-one
  findings: []
- id: Reactome:R-HSA-193807
  title: Synthesis of bile acids and bile salts via 27-hydroxycholesterol
  findings: []
- id: Reactome:R-HSA-193816
  title: Cholest-5-ene-3beta,7alpha,27-triol is oxidized and isomerized to 4-cholesten-7alpha,27-diol-3-one
  findings: []