id: pn_mapping_set:chaperone_systems
label: Chaperone-system PN mappings
references:
- proteostasis-workbook-2024
- proteostasis-ms1
notes: >-
  Cross-branch chaperone-system mappings where the PN source is a family, system, or complex
  role.
subject_curations:
- subject_code: Cytonuclear proteostasis
  subject_level: branch
  curation_status: no_mapping
  rationale: Reviewed as a top-level PN branch. This is a systems/taxonomy umbrella, not a
    direct GO assertion; narrower child curations carry any propagating GO mappings.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone
  subject_level: class
  curation_status: no_mapping
  rationale: Reviewed as a broad PN category rather than a specific GO class. The member
    genes span multiple activities, complexes, or contexts, so propagation from this node
    would overstate the shared biology; use narrower child or gene-level curations.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Folding enzyme
  subject_level: class
  curation_status: no_mapping
  rationale: Reviewed as a broad PN category rather than a specific GO class. The member
    genes span multiple activities, complexes, or contexts, so propagation from this node
    would overstate the shared biology; use narrower child or gene-level curations.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|CCT/TRiC system
  subject_level: group
  curation_status: no_mapping
  rationale: Reviewed as a broad PN category rather than a specific GO class. The member
    genes span multiple activities, complexes, or contexts, so propagation from this node
    would overstate the shared biology; use narrower child or gene-level curations.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|Chaperone for alpha-actinin in myofibril
    assembly
  subject_level: group
  curation_status: no_mapping
  rationale: Reviewed as a contextual PN bucket. The label is useful for curator triage, but
    no direct GO mapping is appropriate because propagation would add a process, activity,
    or localization not shared cleanly by all members.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70 system
  subject_level: group
  curation_status: no_mapping
  rationale: Reviewed as a broad PN category rather than a specific GO class. The member
    genes span multiple activities, complexes, or contexts, so propagation from this node
    would overstate the shared biology; use narrower child or gene-level curations.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system integration
  subject_level: group
  curation_status: no_mapping
  rationale: Reviewed as a broad PN category rather than a specific GO class. The member
    genes span multiple activities, complexes, or contexts, so propagation from this node
    would overstate the shared biology; use narrower child or gene-level curations.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP90 system
  subject_level: group
  curation_status: no_mapping
  rationale: Reviewed as a broad PN category rather than a specific GO class. The member
    genes span multiple activities, complexes, or contexts, so propagation from this node
    would overstate the shared biology; use narrower child or gene-level curations.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|small HSP system
  subject_level: group
  curation_status: no_mapping
  rationale: Reviewed as a narrower taxonomy bucket that is already covered by a curated
    parent mapping or by gene-level annotations. No additional direct GO mapping is
    appropriate from this node.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Folding enzyme|Peptidyl-prolyl isomerases
  subject_level: group
  curation_status: mapped
  target_term:
    id: GO:0003755
    label: peptidyl-prolyl cis-trans isomerase activity
  mapping_scope: ok_for_propagation_to_go
  rationale: This PN group is the cytonuclear peptidyl-prolyl isomerase branch. The matching
    GO molecular-function term is appropriate for propagation.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
  - file:human/CWC27/CWC27-ai-review.yaml
  - PMID:20676357
  excluded_subjects:
  - condition_level: gene_symbol
    condition_code: CWC27
  notes: >-
    CWC27 is excluded after gene-level review. Although it carries a
    cyclophilin domain, structural and biochemical work shows it is a
    catalytically dead pseudo-isomerase (active-site substitutions, no
    cyclosporin binding, no detectable PPIase activity); the gene review
    records GO:0003755 as a NOT annotation. CWC27 acts as a spliceosomal
    scaffold rather than a folding enzyme, so the PPIase-activity term must not
    propagate to it.
- subject_code: Cytonuclear proteostasis|Chaperone|CCT/TRiC system|CCT/TRiC cochaperone
  subject_level: type
  curation_status: no_mapping
  rationale: Reviewed as a broad PN category rather than a specific GO class. The member
    genes span multiple activities, complexes, or contexts, so propagation from this node
    would overstate the shared biology; use narrower child or gene-level curations.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: >-
    Cytonuclear proteostasis|Chaperone|CCT/TRiC system|CCT/TRiC subunit
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0005832
    label: chaperonin-containing T-complex
  mapping_scope: ok_for_propagation_to_go
  rationale: >-
    This PN path denotes subunits of the cytosolic CCT/TRiC chaperonin
    complex. Propagation to the GO cellular-component term for the
    chaperonin-containing T-complex is appropriate, although the PN source is
    specifically the subunit role class.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|CCT/TRiC system|sequence similar
    non-CCT/TRiC subunit
  subject_level: type
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70 system|HSP70
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0140662
    label: ATP-dependent protein folding chaperone
  mapping_scope: ok_for_propagation_to_go
  rationale: >-
    In the PN hierarchy, the type label HSP70 within the chaperone/HSP70-system
    context denotes canonical HSP70 chaperones. Propagation to the GO
    molecular function ATP-dependent protein folding chaperone is appropriate
    for curation, but the PN family label is not itself a strict
    GO-equivalent class.
  references:
  - proteostasis-workbook-2024
  - file:human/HSPA12A/HSPA12A-notes.md
  - file:human/HSPA12B/HSPA12B-notes.md
  - PMID:12552099
  - file:human/HSPA14/HSPA14-ai-review.yaml
  excluded_subjects:
  - condition_level: gene_symbol
    condition_code: HSPA12A
  - condition_level: gene_symbol
    condition_code: HSPA12B
  notes: >-
    Conditional mapping. The source string HSP70 occurs in multiple PN
    branches, so the chaperone and HSP70-system context is required for this
    mapping. HSPA12A and HSPA12B are excluded after gene-level review because
    they are atypical/distant HSP70-family proteins without direct evidence for
    canonical ATP-dependent protein-folding chaperone activity. By contrast,
    proteostasis-batch-5 review of HSPA14/HSP70L1 supports the mapping: it has
    ATP hydrolysis activity and acts in co-translational nascent-chain folding
    as the HSP70 subunit of the ribosome-associated complex (RAC, with
    DNAJC2/MPP11), so it is retained.
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70 system|HSP70 nucleotide exchange
    factor
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0000774
    label: adenyl-nucleotide exchange factor activity
  mapping_scope: ok_for_propagation_to_go
  representative_genes:
  - GRPEL1
  - GRPEL2
  - BAG1
  - HSPBP1
  rationale: >-
    These PN entries denote nucleotide exchange factors that reset HSP70
    chaperones by promoting ADP release. The current validated GO cache does
    not expose a more HSP70-specific exchange-factor term, so
    adenyl-nucleotide exchange factor activity is the best supported target.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70 system|HSP70 nucleotide exchange
    inhibitor
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0030544
    label: Hsp70 protein binding
  mapping_scope: ok_for_propagation_to_go
  rationale: This PN type is represented by ST13/HIP, an HSP70 nucleotide-exchange
    inhibitor. The shared mechanistic assertion is Hsp70 protein binding.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70 system|J-domain containing HSP70
    cochaperone
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0030544
    label: Hsp70 protein binding
  mapping_scope: ok_for_propagation_to_go
  representative_genes:
  - DNAJA3
  - HSCB
  - DNAJB1
  - DNAJB6
  rationale: >-
    In the PN hierarchy, this type denotes J-domain cochaperones assigned to
    the HSP70 system. Their shared mechanistic role is direct interaction
    with HSP70-family chaperones, making Hsp70 protein binding the most
    defensible GO target in the current cache.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
  - file:human/DNAJB4/DNAJB4-ai-review.yaml
  - file:human/DNAJC7/DNAJC7-ai-review.yaml
  - file:human/DNAJC12/DNAJC12-ai-review.yaml
  excluded_subjects:
  - condition_level: gene_symbol
    condition_code: DNAJC27
  notes: >-
    Confirmed for canonical cytosolic/nuclear J-proteins by gene-level review
    (proteostasis batch 5): DNAJB4, DNAJB5, DNAJC7, DNAJC9, DNAJC12, DNAJC13,
    DNAJC16, DNAJC17, DNAJC21, DNAJC24 all act as HSP70/HSC70 cochaperones that
    bind HSP70-family chaperones. For HPD-motif members with direct biochemical
    data the more specific MF GO:0001671 (ATPase activator activity) is also
    supported (e.g. DNAJB4, DNAJC24 carry IDA-grade ATPase-stimulation
    evidence); GO:0030544 Hsp70 protein binding is retained as the safe
    family-level propagation target. DNAJC27 (RBJ) is EXCLUDED: despite a
    degenerate J-domain it is a chimeric Rab/J GTP-binding protein that acts as
    a MEK-ERK scaffold and has no demonstrated HSP70-cochaperone function.
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0031072
    label: heat shock protein binding
  mapping_scope: ok_for_propagation_to_go
  rationale: This PN type groups joint HSP70/HSP90 cochaperones. The shared mechanistic
    assertion is binding heat-shock-protein chaperones, while narrower domain labels remain
    non-mapping unless they carry an independent activity.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP90 system|HSP90
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0140662
    label: ATP-dependent protein folding chaperone
  mapping_scope: ok_for_propagation_to_go
  rationale: >-
    In the PN hierarchy, HSP90 within the chaperone/HSP90-system context
    denotes canonical HSP90 chaperones across multiple proteostasis branches.
    Propagation to ATP-dependent protein folding chaperone is appropriate,
    while strict equivalence would overstate the family label as a GO class.
  references:
  - proteostasis-workbook-2024
  notes: >-
    This mirrors the HSP70 mapping strategy and intentionally covers the
    cytonuclear, ER, and mitochondrial HSP90-system contexts.
- subject_code: Cytonuclear proteostasis|Chaperone|HSP90 system|HSP90 cochaperone
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0051879
    label: Hsp90 protein binding
  mapping_scope: ok_for_propagation_to_go
  rationale: This PN type groups HSP90 cochaperones. Hsp90 protein binding is the most
    defensible shared GO molecular-function target for propagation.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
  - file:human/CDC37L1/CDC37L1-ai-review.yaml
  - file:human/AARSD1/AARSD1-ai-review.yaml
  - file:human/AARSD1/AARSD1-notes.md
  - PMID:26884463
  - file:human/TTC28/TTC28-ai-review.yaml
  - file:human/TTC28/TTC28-notes.md
  - PMID:23036704
  - PMID:39630868
  - file:human/FKBP4/FKBP4-ai-review.yaml
  - file:human/FKBP5/FKBP5-ai-review.yaml
  - file:human/FKBP8/FKBP8-ai-review.yaml
  - file:human/FKBPL/FKBPL-ai-review.yaml
  excluded_subjects:
  - condition_level: gene_symbol
    condition_code: AARSD1
  - condition_level: gene_symbol
    condition_code: TTC28
  notes: >-
    AARSD1 is excluded after gene-level review because the HSP90 cochaperone
    evidence appears to apply to muscle/readthrough-derived Aarsd1L or
    PTGES3L-AARSD1-like fusion products rather than canonical AARSD1. Keep this
    as contextual/isoform-associated biology, not a general gene-level
    Hsp90-binding propagation. TTC28 is excluded because the supported
    chaperone-related evidence is HSPA8-mediated CMA/microautophagy substrate
    biology, while its stronger core role is mitotic scaffold/AURKB-associated
    cell-division biology; the evidence does not support HSP90 cochaperone
    propagation. By contrast, gene-level review of CDC37L1 (Cdc37-like-1)
    confirmed this propagation: it is a bona fide HSP90/HSP70 cochaperone with
    accepted Hsp90 protein binding (GO:0051879). Proteostasis batch 5 added the
    FKBP immunophilin cochaperones FKBP4/FKBP52, FKBP5/FKBP51, FKBP8/FKBP38 and
    FKBPL, all confirmed as HSP90 cochaperones that bind Hsp90 (GO:0051879). This
    also supports keeping the child subtype "CC-TPR and PPIase domain containing"
    as no_mapping: FKBP4/5/8 carry PPIase activity but FKBPL has no catalytic
    PPIase domain, so a subtype-level PPIase-activity mapping would over-annotate
    that member while the shared Hsp90-binding role propagates correctly here.
- subject_code: Cytonuclear proteostasis|Chaperone|small HSP system|small HSP
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0044183
    label: protein folding chaperone
  mapping_scope: ok_for_propagation_to_go
  rationale: This PN type denotes small heat-shock chaperones. Protein folding chaperone is
    the appropriate shared molecular-function term.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
  - file:human/HSPB2/HSPB2-ai-review.yaml
  - file:human/HSPB3/HSPB3-ai-review.yaml
  - file:human/HSPB7/HSPB7-ai-review.yaml
  - file:human/HSPB8/HSPB8-ai-review.yaml
  - file:human/HSPB9/HSPB9-ai-review.yaml
  notes: >-
    Confirmed and refined by gene-level review (proteostasis batch 5). HSPB2,
    HSPB3, HSPB7 and HSPB8 are ATP-independent holdases whose gene-level core
    molecular function is GO:0051082 (unfolded protein binding) - a more specific
    holdase term than the family-level GO:0044183 used here for propagation;
    GO:0044183 is retained as the conservative shared target. Note two member
    caveats surfaced by review: HSPB7 acts predominantly as an aggregate
    sequestrase rather than a refolding chaperone, and HSPB9 is a testis-
    restricted small HSP whose best-supported MF is dynein light chain binding
    (GO:0045503) rather than general holdase activity, so the holdase mapping is
    weakest for HSPB9.
- subject_code: Cytonuclear proteostasis|Folding enzyme|Peptidyl-prolyl
    isomerases|Cyclophilin type
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0003755
    label: peptidyl-prolyl cis-trans isomerase activity
  mapping_scope: ok_for_propagation_to_go
  rationale: This PN type denotes cyclophilin-family peptidyl-prolyl isomerases. The
    matching GO molecular-function term is appropriate for propagation.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
  - file:human/CWC27/CWC27-ai-review.yaml
  - PMID:20676357
  excluded_subjects:
  - condition_level: gene_symbol
    condition_code: CWC27
  notes: >-
    CWC27 is excluded after gene-level review: it is a catalytically dead
    cyclophilin-domain pseudo-isomerase (the gene review records GO:0003755 as
    a NOT annotation), so the cyclophilin PPIase-activity term must not
    propagate to it. Genuine catalytic cyclophilins in this type retain the
    mapping.
- subject_code: Cytonuclear proteostasis|Folding enzyme|Peptidyl-prolyl isomerases|FKBP type
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0003755
    label: peptidyl-prolyl cis-trans isomerase activity
  mapping_scope: ok_for_propagation_to_go
  rationale: This PN type denotes FKBP-family peptidyl-prolyl isomerases. The matching GO
    molecular-function term is appropriate for propagation.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: ER proteostasis|Chaperone|HSP70 system|HSP70
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0140662
    label: ATP-dependent protein folding chaperone
  mapping_scope: ok_for_propagation_to_go
  rationale: >-
    In the PN hierarchy, the type label HSP70 within the chaperone/HSP70-system
    context denotes canonical HSP70 chaperones. Propagation to the GO
    molecular function ATP-dependent protein folding chaperone is appropriate
    for curation, but the PN family label is not itself a strict
    GO-equivalent class.
  references:
  - proteostasis-workbook-2024
  - file:human/HSPA13/HSPA13-ai-review.yaml
  excluded_subjects:
  - condition_level: gene_symbol
    condition_code: HSPA13
  notes: >-
    Conditional mapping. The source string HSP70 occurs in multiple PN
    branches, so the chaperone and HSP70-system context is required for this
    mapping. HSPA13/STCH is excluded after gene-level review (proteostasis
    batch 5): it is an atypical microsomal/ER HSP70 with a truncated
    substrate-binding domain and a peptide-stimulation-independent ATPase, and
    its review marks the canonical refolding/foldase terms as over-annotations.
    Its supported activities are ATP hydrolysis (GO:0016887) and ubiquitin-like
    protein binding, not canonical ATP-dependent protein-folding chaperone
    activity, so it should not inherit GO:0140662 from this node. Canonical ER
    HSP70s (e.g. HSPA5/BiP) retain the mapping.
- subject_code: ER proteostasis|Chaperone|HSP70 system|HSP70 nucleotide exchange factor
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0000774
    label: adenyl-nucleotide exchange factor activity
  mapping_scope: ok_for_propagation_to_go
  representative_genes:
  - GRPEL1
  - GRPEL2
  - BAG1
  - HSPBP1
  rationale: >-
    These PN entries denote nucleotide exchange factors that reset HSP70
    chaperones by promoting ADP release. The current validated GO cache does
    not expose a more HSP70-specific exchange-factor term, so
    adenyl-nucleotide exchange factor activity is the best supported target.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: ER proteostasis|Chaperone|HSP70 system|J-domain containing HSP70 cochaperone
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0030544
    label: Hsp70 protein binding
  mapping_scope: ok_for_propagation_to_go
  representative_genes:
  - DNAJA3
  - HSCB
  - DNAJB1
  - DNAJB6
  rationale: >-
    In the PN hierarchy, this type denotes J-domain cochaperones assigned to
    the HSP70 system. Their shared mechanistic role is direct interaction
    with HSP70-family chaperones, making Hsp70 protein binding the most
    defensible GO target in the current cache.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: ER proteostasis|Chaperone|HSP90 system|HSP90
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0140662
    label: ATP-dependent protein folding chaperone
  mapping_scope: ok_for_propagation_to_go
  rationale: >-
    In the PN hierarchy, HSP90 within the chaperone/HSP90-system context
    denotes canonical HSP90 chaperones across multiple proteostasis branches.
    Propagation to ATP-dependent protein folding chaperone is appropriate,
    while strict equivalence would overstate the family label as a GO class.
  references:
  - proteostasis-workbook-2024
  notes: >-
    This mirrors the HSP70 mapping strategy and intentionally covers the
    cytonuclear, ER, and mitochondrial HSP90-system contexts.
- subject_code: Mitochondrial proteostasis|Chaperone|HSP70 system|HSP70
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0140662
    label: ATP-dependent protein folding chaperone
  mapping_scope: ok_for_propagation_to_go
  rationale: >-
    In the PN hierarchy, the type label HSP70 within the chaperone/HSP70-system
    context denotes canonical HSP70 chaperones. Propagation to the GO
    molecular function ATP-dependent protein folding chaperone is appropriate
    for curation, but the PN family label is not itself a strict
    GO-equivalent class.
  references:
  - proteostasis-workbook-2024
  notes: >-
    Conditional mapping. The source string HSP70 occurs in multiple PN
    branches, so the chaperone and HSP70-system context is required for this
    mapping.
- subject_code: Mitochondrial proteostasis|Chaperone|HSP70 system|HSP70 nucleotide exchange
    factor
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0000774
    label: adenyl-nucleotide exchange factor activity
  mapping_scope: ok_for_propagation_to_go
  representative_genes:
  - GRPEL1
  - GRPEL2
  - BAG1
  - HSPBP1
  rationale: >-
    These PN entries denote nucleotide exchange factors that reset HSP70
    chaperones by promoting ADP release. The current validated GO cache does
    not expose a more HSP70-specific exchange-factor term, so
    adenyl-nucleotide exchange factor activity is the best supported target.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Mitochondrial proteostasis|Chaperone|HSP70 system|J-domain containing HSP70
    cochaperone
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0030544
    label: Hsp70 protein binding
  mapping_scope: ok_for_propagation_to_go
  representative_genes:
  - DNAJA3
  - HSCB
  - DNAJB1
  - DNAJB6
  rationale: >-
    In the PN hierarchy, this type denotes J-domain cochaperones assigned to
    the HSP70 system. Their shared mechanistic role is direct interaction
    with HSP70-family chaperones, making Hsp70 protein binding the most
    defensible GO target in the current cache.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
  - file:human/DNAJC19/DNAJC19-ai-review.yaml
  - file:human/DNAJC15/DNAJC15-ai-review.yaml
  - file:human/DNAJC11/DNAJC11-ai-review.yaml
  excluded_subjects:
  - condition_level: gene_symbol
    condition_code: DNAJC11
  notes: >-
    Confirmed for genuine mitochondrial import-motor J-proteins by gene-level
    review (proteostasis batch 5): DNAJC19/TIM14 and DNAJC15/MCJ are
    inner-membrane PAM/TIM23-motor J-proteins that stimulate the mortalin
    (HSPA9/mtHSP70) ATPase, so for these the more specific MF GO:0001671
    (ATPase activator activity) also applies; GO:0030544 Hsp70 protein binding
    is retained as the family-level propagation target. DNAJC11 is EXCLUDED:
    although it carries a J-domain, the human protein is a structural component
    of the mitochondrial intermembrane-bridging (MIB)/MICOS complex required
    for cristae organization, with no demonstrated HSP70-cochaperone activity,
    so it should not inherit the Hsp70-binding MF from this node.
- subject_code: Mitochondrial proteostasis|Chaperone|HSP90 system|HSP90
  subject_level: type
  curation_status: mapped
  target_term:
    id: GO:0140662
    label: ATP-dependent protein folding chaperone
  mapping_scope: ok_for_propagation_to_go
  rationale: >-
    In the PN hierarchy, HSP90 within the chaperone/HSP90-system context
    denotes canonical HSP90 chaperones across multiple proteostasis branches.
    Propagation to ATP-dependent protein folding chaperone is appropriate,
    while strict equivalence would overstate the family label as a GO class.
  references:
  - proteostasis-workbook-2024
  notes: >-
    This mirrors the HSP70 mapping strategy and intentionally covers the
    cytonuclear, ER, and mitochondrial HSP90-system contexts.
- subject_code: Cytonuclear proteostasis|Chaperone|CCT/TRiC system|CCT/TRiC cochaperone|Open
    state cofactor
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|CCT/TRiC system|CCT/TRiC
    cochaperone|Phosducin-like proteins
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|CCT/TRiC system|CCT/TRiC
    cochaperone|Tubulin folding
  subject_level: subtype
  curation_status: mapped
  target_term:
    id: GO:0007023
    label: post-chaperonin tubulin folding pathway
  mapping_scope: ok_for_propagation_to_go
  rationale: This PN subtype is the tubulin-folding cofactor branch downstream of CCT/TRiC.
    The GO post-chaperonin tubulin folding pathway term captures the shared pathway role.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|CCT/TRiC system|CCT/TRiC
    cochaperone|prefoldin subunit
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a mixed canonical-prefoldin and prefoldin-like subtype. Canonical
    PFDN/VBP1 members map cleanly to GO:0016272 prefoldin complex, but UXT/URI1-like members
    should not inherit canonical prefoldin-complex membership from this source node; use
    gene-level curation for those distinctions.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70 system|HSP70 nucleotide exchange
    factor|BAG domain subtype
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a narrower taxonomy bucket that is already covered by a curated
    parent mapping or by gene-level annotations. No additional direct GO mapping is
    appropriate from this node.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70 system|HSP70 nucleotide exchange
    factor|HSP110/GRP170 subtype
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a narrower taxonomy bucket that is already covered by a curated
    parent mapping or by gene-level annotations. No additional direct GO mapping is
    appropriate from this node.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70 system|HSP70 nucleotide exchange
    factor|HSPBP1 subtype
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a narrower taxonomy bucket that is already covered by a curated
    parent mapping or by gene-level annotations. No additional direct GO mapping is
    appropriate from this node.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70 system|HSP70 nucleotide exchange
    inhibitor|TPR domain subtype
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a narrower taxonomy bucket that is already covered by a curated
    parent mapping or by gene-level annotations. No additional direct GO mapping is
    appropriate from this node.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR and Armadillo domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR and CS domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR and Cns1/TTC4 wheel domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR and J domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR and PPIase domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a mixed TPR/PPIase-domain subtype. Although several members are
    active peptidyl-prolyl isomerases, the bucket also contains PPIase-like cochaperones, so
    subtype-level PPIase propagation would overstate the shared activity.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR and RPAP3-like C-terminal domain
    containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR and SGTA dimerization domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR and STI/HOP domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR and methyltransferase domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR and phosphatase domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR domain and Ub ligase
  subject_level: subtype
  curation_status: mapped
  target_term:
    id: GO:0061630
    label: ubiquitin protein ligase activity
  mapping_scope: ok_for_propagation_to_go
  rationale: This PN subtype explicitly denotes TPR-containing ubiquitin ligases in the
    HSP70/HSP90 co-chaperone branch. The shared catalytic assertion is ubiquitin protein
    ligase activity.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system
    integration|HSP70-HSP90 joint cochaperone|CC-TPR domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP90 system|HSP90 cochaperone|CC-TPR and
    Armadillo domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP90 system|HSP90 cochaperone|CC-TPR and
    PPIase domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a mixed HSP90 cochaperone subtype with FKBP/PPIase-like members.
    The parent HSP90-cochaperone mapping captures the shared HSP90-binding role; a
    subtype-level PPIase mapping would overstate the activity for all members.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP90 system|HSP90 cochaperone|CC-TPR and
    RPAP3-like C-terminal domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP90 system|HSP90 cochaperone|CS domain
    containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP90 system|HSP90 cochaperone|TPR and CS
    domain containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP90 system|HSP90 cochaperone|TPR domain
    containing
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a family/domain/subtype label. It classifies PN members but is not
    itself a GO annotation target; any functional assertion should come from a parent role
    mapping or gene-specific review.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
- subject_code: Cytonuclear proteostasis|Chaperone|HSP90 system|HSP90 cochaperone|no
    characteristic domain
  subject_level: subtype
  curation_status: no_mapping
  rationale: Reviewed as a narrower taxonomy bucket that is already covered by a curated
    parent mapping or by gene-level annotations. No additional direct GO mapping is
    appropriate from this node.
  references:
  - proteostasis-workbook-2024
  - proteostasis-ms1
