UQCRB

UniProt ID: P14927
Organism: Homo sapiens
Review Status: INITIALIZED
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Gene Description

UQCRB (ubiquinol-cytochrome c reductase binding protein; also QP-C / cytochrome b-c1 complex subunit 7 / QCR7) is a small (~13.5 kDa, 111 aa) nuclear-encoded, non-catalytic structural subunit of mitochondrial respiratory Complex III (the cytochrome b-c1 complex / ubiquinol-cytochrome c oxidoreductase). It is one of the low-molecular-weight subunits of the 11-subunit complex; the redox catalysis of Complex III is carried out by the catalytic subunits cytochrome b, the Rieske iron-sulfur protein (UQCRFS1) and cytochrome c1, whereas UQCRB contributes to assembly and structural integrity of the complex rather than to catalysis. Complex III is an obligate dimer embedded as a peripheral protein on the matrix side of the mitochondrial inner membrane, and it associates with Complex I and Complex IV to form respiratory supercomplexes and megacomplexes. Within the electron transport chain, Complex III transfers electrons from ubiquinol to cytochrome c, coupling this redox reaction to proton translocation across the inner membrane (the Q cycle) and thereby contributing to oxidative phosphorylation and aerobic respiration. UQCRB was originally proposed to be the ubiquinone-binding protein, but this ubiquinone-binding role is no longer considered established. Loss-of-function variants in UQCRB cause mitochondrial complex III deficiency (nuclear type 3), a mitochondrial disorder that can present with hypoglycemia and lactic acidosis.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0045275 respiratory chain complex III
IBA
GO_REF:0000033
ACCEPT
Summary: Phylogenetic (IBA) annotation placing UQCRB as part of respiratory chain complex III. This is the defining, well-established localization/membership of this subunit and is supported by cryo-EM structures of human Complex III and by UniProt.
Reason: UQCRB is a bona fide low-molecular-weight subunit of the cytochrome b-c1 complex (Complex III). This is confirmed structurally and by the family definition, and the complex membership is a core aspect of the gene's function.
Supporting Evidence:
file:human/UQCRB/UQCRB-uniprot.txt
Component of the ubiquinol-cytochrome c oxidoreductase, a
GO:0006122 mitochondrial electron transport, ubiquinol to cytochrome c
IBA
GO_REF:0000033
ACCEPT
Summary: Phylogenetic (IBA) annotation to the specific Complex III process, transfer of electrons from ubiquinol to cytochrome c. As a structural subunit of Complex III, UQCRB participates in this process.
Reason: This is the core biological process of Complex III and the most appropriate specific BP term for a CIII subunit. Well supported by the complex's catalytic role.
Supporting Evidence:
file:human/UQCRB/UQCRB-uniprot.txt
transfer from ubiquinol to cytochrome c, linking this redox reaction to
GO:0005743 mitochondrial inner membrane
IEA
GO_REF:0000044
ACCEPT
Summary: Electronic annotation from UniProt Subcellular Location mapping placing UQCRB in the mitochondrial inner membrane. Consistent with its role as a peripheral inner-membrane Complex III subunit.
Reason: Complex III, and hence UQCRB, resides in the mitochondrial inner membrane. This is the correct, specific location and matches the UniProt subcellular location.
Supporting Evidence:
file:human/UQCRB/UQCRB-uniprot.txt
SUBCELLULAR LOCATION: Mitochondrion inner membrane
GO:0006122 mitochondrial electron transport, ubiquinol to cytochrome c
IEA
GO_REF:0000002
ACCEPT
Summary: InterPro2GO electronic annotation to the Complex III electron transport process, based on the QCR7 family signatures (IPR003197, IPR036544). Duplicates the IBA/NAS annotations to the same specific BP.
Reason: The InterPro-to-GO mapping is appropriate for this family and points to the correct, specific Complex III process. Consistent with the experimental and phylogenetic evidence.
Supporting Evidence:
file:human/UQCRB/UQCRB-uniprot.txt
transfer from ubiquinol to cytochrome c, linking this redox reaction to
GO:0016020 membrane
IEA
GO_REF:0000117
MARK AS OVER ANNOTATED
Summary: Generic ARBA machine-learning electronic annotation to "membrane". This is correct but far less informative than the specific mitochondrial inner membrane location that is also annotated.
Reason: "membrane" is a high-level parent of the specific and better-supported term mitochondrial inner membrane (GO:0005743). It is not wrong, but it is uninformatively general given more precise annotations exist.
Supporting Evidence:
file:human/UQCRB/UQCRB-uniprot.txt
SUBCELLULAR LOCATION: Mitochondrion inner membrane
GO:0045275 respiratory chain complex III
IEA
GO_REF:0000002
ACCEPT
Summary: InterPro2GO electronic annotation for complex III membership based on the QCR7 family superfamily signature (IPR036544). Duplicates the IBA and experimental (ComplexPortal IPI) annotations to the same term.
Reason: Correct complex membership for a QCR7-family protein; consistent with structural and phylogenetic evidence.
Supporting Evidence:
file:human/UQCRB/UQCRB-uniprot.txt
Component of the ubiquinol-cytochrome c oxidoreductase, a
GO:0005515 protein binding
IPI
PMID:16189514
Towards a proteome-scale map of the human protein-protein in...
MARK AS OVER ANNOTATED
Summary: Large-scale protein-protein interaction (IntAct/IPI) annotation to the uninformative term "protein binding". From a high-throughput human interactome screen.
Reason: "protein binding" (GO:0005515) is an uninformative molecular function term that does not capture the actual, specific function of UQCRB. This is an experimental IntAct record, so it is retained rather than removed, but flagged as over-annotated per curation policy that discourages bare "protein binding".
GO:0005515 protein binding
IPI
PMID:25416956
A proteome-scale map of the human interactome network.
MARK AS OVER ANNOTATED
Summary: Large-scale interactome (HuRI / IPI) annotation to the uninformative term "protein binding".
Reason: Uninformative "protein binding" from a high-throughput interactome map. Retained as an experimental IntAct record but flagged as over-annotated; it does not describe UQCRB's specific structural function within Complex III.
GO:0005515 protein binding
IPI
PMID:28514442
Architecture of the human interactome defines protein commun...
MARK AS OVER ANNOTATED
Summary: Large-scale interactome (BioPlex / IPI) annotation to the uninformative term "protein binding".
Reason: Uninformative "protein binding" from a high-throughput interactome study. Retained as an experimental IntAct record but flagged as over-annotated.
GO:0005515 protein binding
IPI
PMID:32296183
A reference map of the human binary protein interactome.
MARK AS OVER ANNOTATED
Summary: Large-scale binary interactome (HuRI reference map / IPI) annotation to the uninformative term "protein binding".
Reason: Uninformative "protein binding" from a high-throughput binary interactome map. Retained as an experimental IntAct record but flagged as over-annotated.
GO:0005515 protein binding
IPI
PMID:32814053
Interactome Mapping Provides a Network of Neurodegenerative ...
MARK AS OVER ANNOTATED
Summary: Large-scale interactome (neurodegenerative-disease interactome / IPI) annotation to the uninformative term "protein binding".
Reason: Uninformative "protein binding" from a high-throughput interactome study. Retained as an experimental IntAct record but flagged as over-annotated.
GO:0005515 protein binding
IPI
PMID:33961781
Dual proteome-scale networks reveal cell-specific remodeling...
MARK AS OVER ANNOTATED
Summary: Large-scale interactome (BioPlex 3.0 dual-cell networks / IPI) annotation to the uninformative term "protein binding".
Reason: Uninformative "protein binding" from a high-throughput interactome study. Retained as an experimental IntAct record but flagged as over-annotated.
GO:0005515 protein binding
IPI
PMID:40205054
Multimodal cell maps as a foundation for structural and func...
MARK AS OVER ANNOTATED
Summary: Large-scale multimodal cell-map interactome (IPI) annotation to the uninformative term "protein binding".
Reason: Uninformative "protein binding" from a high-throughput interactome/cell-map study. Retained as an experimental IntAct record but flagged as over-annotated.
GO:0005743 mitochondrial inner membrane
ISS
GO_REF:0000024
ACCEPT
Summary: Curator-judged sequence-similarity (ISS) transfer of the mitochondrial inner membrane location from the bovine ortholog (UniProtKB:P00128). Consistent with all other location evidence.
Reason: The inner-membrane localization is well established for Complex III subunits across species; the ISS transfer from the bovine QCR7 ortholog is appropriate and matches the specific, correct location.
Supporting Evidence:
file:human/UQCRB/UQCRB-uniprot.txt
SUBCELLULAR LOCATION: Mitochondrion inner membrane
GO:0005743 mitochondrial inner membrane
IDA
PMID:28844695
Architecture of Human Mitochondrial Respiratory Megacomplex ...
ACCEPT
Summary: Direct experimental (IDA, ComplexPortal) assignment of UQCRB to the mitochondrial inner membrane, based on the cryo-EM structure of the human respiratory megacomplex in which Complex III is resolved in the inner membrane.
Reason: Strong experimental support: the cryo-EM structure of the human MCI2III2IV2 megacomplex places the dimeric Complex III (and thus its UQCRB subunit) in the mitochondrial inner membrane. This is the core, specific location.
Supporting Evidence:
PMID:28844695
The MCI2III2IV2 forms a circular structure with the dimeric CIII located in the center, where it is surrounded by two copies each of CI and CIV.
GO:0006122 mitochondrial electron transport, ubiquinol to cytochrome c
NAS
PMID:28844695
Architecture of Human Mitochondrial Respiratory Megacomplex ...
ACCEPT
Summary: Non-traceable author statement (NAS, ComplexPortal) that UQCRB, as a Complex III subunit, is involved in mitochondrial electron transport from ubiquinol to cytochrome c.
Reason: This is the core, specific process of Complex III and is consistent with the IBA/InterPro annotations to the same term and with the structural characterization of the electron transport chain in this study.
Supporting Evidence:
PMID:28844695
Two cytochrome c (Cyt.c) molecules are positioned to accept electrons on the surface of the c1 state CIII dimer.
GO:0045275 respiratory chain complex III
IPI
PMID:28844695
Architecture of Human Mitochondrial Respiratory Megacomplex ...
ACCEPT
Summary: Experimental (IPI, ComplexPortal) assignment of UQCRB as part of respiratory chain complex III, based on the cryo-EM structure that resolves the individual subunits of human Complex III.
Reason: Direct structural evidence for UQCRB being a component of Complex III. Core complex membership annotation.
Supporting Evidence:
PMID:28844695
The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:0045333 cellular respiration
NAS
PMID:28844695
Architecture of Human Mitochondrial Respiratory Megacomplex ...
KEEP AS NON CORE
Summary: Non-traceable author statement (NAS, ComplexPortal) annotating UQCRB to the broad process "cellular respiration".
Reason: Correct but general: cellular respiration is a broad parent process. The more specific and informative BP is mitochondrial electron transport, ubiquinol to cytochrome c (GO:0006122), which is separately annotated and represents the core function. Retained as valid but non-core.
Supporting Evidence:
file:human/UQCRB/UQCRB-uniprot.txt
electron transport chain which drives oxidative phosphorylation
GO:0005739 mitochondrion
HTP
PMID:34800366
Quantitative high-confidence human mitochondrial proteome an...
ACCEPT
Summary: High-throughput (HTP) proteomic identification of UQCRB in the mitochondrion, from a quantitative high-confidence human mitochondrial proteome (MitoCoP). Correct but less specific than the mitochondrial inner membrane location.
Reason: Reliable high-throughput evidence for mitochondrial localization. It is a general parent of the more specific inner-membrane location, but it is correct and independently corroborates the organellar assignment.
Supporting Evidence:
PMID:34800366
mitochondrial high-confidence proteome of >1,100 proteins (MitoCoP)
GO:0005743 mitochondrial inner membrane
TAS
Reactome:R-HSA-164651
ACCEPT
Summary: Traceable author statement (Reactome) placing UQCRB in the mitochondrial inner membrane, associated with the reaction "Electron transfer from ubiquinol to cytochrome c of complex III".
Reason: Correct, specific location consistent with all other evidence. Reactome pathway context matches the Complex III role.
Supporting Evidence:
Reactome:R-HSA-164651
The protonmotive Q cycle is the mechanism by which complex III transfers electrons from ubiquinol to cytochrome c, linking this process to translocation of protons across the membrane.
GO:0005743 mitochondrial inner membrane
TAS
Reactome:R-HSA-9906017
ACCEPT
Summary: Traceable author statement (Reactome) placing UQCRB in the mitochondrial inner membrane, in the context of Complex III assembly (proteolytic processing of the UQCRFS1 subunit).
Reason: Correct, specific location. The Reactome reaction concerns Complex III assembly in the inner membrane, consistent with UQCRB's structural/assembly role.
Supporting Evidence:
Reactome:R-HSA-9906017
Proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer.
GO:0005743 mitochondrial inner membrane
TAS
Reactome:R-HSA-9906042
ACCEPT
Summary: Traceable author statement (Reactome) placing UQCRB in the mitochondrial inner membrane, in the context of Complex III maturation (TTC19 clearance of UQCRFS1 fragments).
Reason: Correct, specific location consistent with the Complex III assembly/maturation pathway context.
Supporting Evidence:
Reactome:R-HSA-9906042
N-terminal cleavage fragments of UQCRFS1 are cleared by TTC19, stabilizing the final complex.
GO:0006119 oxidative phosphorylation
TAS
PMID:3056408
Cloning and sequencing of a cDNA for human mitochondrial ubi...
ACCEPT
Summary: Traceable author statement (from the original human QP-C/UQCRB cDNA cloning paper) annotating involvement in oxidative phosphorylation, reflecting Complex III's role in driving OXPHOS via the electron transport chain.
Reason: Complex III is a core component of the electron transport chain that drives oxidative phosphorylation, so this is a valid process annotation for UQCRB. It is broader than the specific electron-transport step (GO:0006122) but correctly captures the downstream energetic role.
Supporting Evidence:
file:human/UQCRB/UQCRB-uniprot.txt
electron transport chain which drives oxidative phosphorylation
GO:0009060 aerobic respiration
TAS
PMID:3056408
Cloning and sequencing of a cDNA for human mitochondrial ubi...
KEEP AS NON CORE
Summary: Traceable author statement (original QP-C cDNA cloning paper) annotating involvement in aerobic respiration.
Reason: Correct but broad. Aerobic respiration is a high-level process; the core, specific function is captured by mitochondrial electron transport, ubiquinol to cytochrome c (GO:0006122). Retained as valid but non-core.
Supporting Evidence:
PMID:3056408
The ubiquinone-binding protein (QP-C) is a nuclear-encoded component of ubiquinol-cytochrome c oxidoreductase in the mitochondrial respiratory chain and plays an important role in electron transfer
GO:0098803 respiratory chain complex
TAS
PMID:3056408
Cloning and sequencing of a cDNA for human mitochondrial ubi...
MARK AS OVER ANNOTATED
Summary: Traceable author statement placing UQCRB in a respiratory chain complex, based on the original cDNA cloning paper identifying QP-C as a component of ubiquinol-cytochrome c oxidoreductase.
Reason: Correct but general: respiratory chain complex (GO:0098803) is a parent of the specific and better-supported term respiratory chain complex III (GO:0045275), which is annotated by IBA, InterPro and experimental (ComplexPortal IPI) evidence. Retained but flagged as over-general.
Supporting Evidence:
PMID:3056408
The ubiquinone-binding protein (QP-C) is a nuclear-encoded component of ubiquinol-cytochrome c oxidoreductase in the mitochondrial respiratory chain
GO:0005198 structural molecule activity
ISS
file:human/UQCRB/UQCRB-uniprot.txt
NEW
Summary: Proposed molecular function annotation. UQCRB has no informative molecular function in GOA (only the uninformative "protein binding" IPIs). As a non-catalytic subunit of Complex III, its molecular function is best captured as structural molecule activity, contributing to the structural integrity of the cytochrome b-c1 complex.
Reason: The catalytic activity of Complex III (electron transfer from ubiquinol to cytochrome c) is carried by cytochrome b, the Rieske iron-sulfur protein and cytochrome c1; UQCRB is a low-molecular-weight, non-catalytic structural subunit. Structural molecule activity (GO:0005198) is the appropriate subunit-specific molecular function, and it is not currently represented in GOA. No catalytic activity is asserted for UQCRB.
Supporting Evidence:
file:human/UQCRB/UQCRB-uniprot.txt
Component of the ubiquinol-cytochrome c oxidoreductase, a

Core Functions

Non-catalytic structural subunit of mitochondrial respiratory Complex III (cytochrome b-c1 complex / ubiquinol-cytochrome c oxidoreductase). UQCRB contributes to the structural integrity and assembly of the complex; the complex as a whole transfers electrons from ubiquinol to cytochrome c in the mitochondrial inner membrane during aerobic respiration and oxidative phosphorylation.

Supporting Evidence:
  • file:human/UQCRB/UQCRB-uniprot.txt
    Component of the ubiquinol-cytochrome c oxidoreductase, a
  • PMID:28844695
    The structure not only reveals the precise assignment of individual subunits of human CI and CIII

References

Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Towards a proteome-scale map of the human protein-protein interaction network.
A proteome-scale map of the human interactome network.
Architecture of the human interactome defines protein communities and disease networks.
Architecture of Human Mitochondrial Respiratory Megacomplex I(2)III(2)IV(2).
Cloning and sequencing of a cDNA for human mitochondrial ubiquinone-binding protein of complex III.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Multimodal cell maps as a foundation for structural and functional genomics.
Reactome:R-HSA-164651
Electron transfer from ubiquinol to cytochrome c of complex III
Reactome:R-HSA-9906017
Unknown peptidase cleaves UQCRFS1 subunit
Reactome:R-HSA-9906042
TTC19 clears UQCRFS1 fragments from Complex III
file:human/UQCRB/UQCRB-uniprot.txt
UniProtKB P14927 (QCR7_HUMAN) Cytochrome b-c1 complex subunit 7

📚 Additional Documentation

Notes

(UQCRB-notes.md)

UQCRB (P14927) review notes

Gene: UQCRB / UQBP; "Cytochrome b-c1 complex subunit 7" (QCR7); AltNames: Complex III subunit 7 / VII, QP-C,
"Ubiquinol-cytochrome c reductase complex 14 kDa protein". Human, taxon 9606. 111 aa, ~13.5 kDa.

Deep research status

Falcon deep research is OUT OF CREDITS (HTTP 402) — no -deep-research-falcon.md. Review grounded in the cached
UniProt record (UQCRB-uniprot.txt), the seeded GOA (UQCRB-goa.tsv), cached publications/PMID_*.md, cached
Reactome entries, and OLS term lookups.

Core biology (verified)

  • UQCRB is a small, non-catalytic structural subunit of mitochondrial respiratory Complex III (cytochrome
    b-c1 complex / ubiquinol-cytochrome c oxidoreductase; CIII). The redox catalysis is carried by cytochrome b, the
    Rieske Fe-S protein (UQCRFS1) and cytochrome c1; UQCRB is one of the six low-molecular-weight subunits
    [UniProt SUBUNIT: "6 low-molecular weight protein subunits UQCRH/QCR6, UQCRB/QCR7, ..."].
  • Complex III is an obligate dimer embedded in the mitochondrial inner membrane; it is a peripheral inner-membrane
    protein on the matrix side [UniProt SUBCELLULAR LOCATION]. It forms supercomplexes/megacomplexes with CI and CIV
    PMID:28844695.
  • CIII catalyzes transfer of electrons from ubiquinol to cytochrome c coupled to proton translocation (Q cycle)
    [Reactome R-HSA-164651; UniProt FUNCTION]. UQCRB participates in this process as a structural component.
  • UQCRB was originally thought to be the ubiquinone-binding protein (QP-C) [PMID:3056408 title/abstract], but
    UniProt now flags this as CAUTION: "Was originally thought to be the ubiquinone-binding protein (QP-C)." So do
    NOT assert a ubiquinone-binding molecular function.
  • Nuclear-encoded; imported without a cleavable presequence PMID:3056408.

Disease

  • Biallelic/deletion variants cause Mitochondrial complex III deficiency, nuclear type 3 (MC3DN3; MIM:615158);
    a QP-C gene deletion caused CIII deficiency with hypoglycaemia and lactic acidosis [PMID:12709789, cited in
    UniProt DISEASE + reference 8]. (PMID_12709789 is not cached, so not used as supporting_text.)

MF decision (important)

GOA carries NO informative MF for UQCRB — the only MF term is GO:0005515 "protein binding" (IPI, from large-scale
interactome screens). Per project policy protein binding is uninformative and these IPIs are marked
MARK_AS_OVER_ANNOTATED (not REMOVE — they are experimental IntAct records whose full text I cannot verify).

For core_functions, the appropriate subunit-specific MF is structural molecule activity (GO:0005198) — this is
the schema-prescribed MF for a non-catalytic structural subunit ("contributes to the structural integrity of a
complex"), NOT an invented catalytic activity. It contributes_to the complex-level MF quinol-cytochrome-c
reductase activity (GO:0008121)
enabled by the whole CIII.

Complex CC term

Task prompt mentioned GO:0005750 for Complex III, but OLS confirms GO:0005750 is OBSOLETE ("obsolete
mitochondrial respiratory chain complex III"). The current, GOA-present complex term is GO:0045275 "respiratory
chain complex III"
— used for in_complex. (GOA does not carry GO:0005750.)

GOA annotation inventory (41 data lines -> 25 unique annotation rows after collapsing duplicate PMID IPIs)

  • CC:
  • GO:0045275 respiratory chain complex III — IBA (GO_REF:0000033), IEA (InterPro), IPI (PMID:28844695
    ComplexPortal) -> ACCEPT (core; complex membership)
  • GO:0005743 mitochondrial inner membrane — IEA(SubCell), ISS(P00128), IDA(PMID:28844695 ComplexPortal),
    TAS x3 (Reactome) -> ACCEPT (core location)
  • GO:0016020 membrane — IEA(ARBA) -> MARK_AS_OVER_ANNOTATED (too general; inner membrane is the specific term)
  • GO:0005739 mitochondrion — HTP(PMID:34800366) -> ACCEPT (correct but less specific than inner membrane;
    keep, high-throughput mito proteome)
  • GO:0098803 respiratory chain complex — TAS(PMID:3056408) -> ACCEPT (correct but parent of GO:0045275)
  • BP:
  • GO:0006122 mitochondrial electron transport, ubiquinol to cytochrome c — IBA, IEA(InterPro), NAS(ComplexPortal)
    -> ACCEPT (core process)
  • GO:0045333 cellular respiration — NAS(ComplexPortal) -> ACCEPT (broader; keep non-core)
  • GO:0006119 oxidative phosphorylation — TAS(PMID:3056408) -> ACCEPT (CIII drives OXPHOS)
  • GO:0009060 aerobic respiration — TAS(PMID:3056408) -> KEEP_AS_NON_CORE (broad)
  • MF:
  • GO:0005515 protein binding — IPI x many (interactome screens) -> MARK_AS_OVER_ANNOTATED

📄 View Raw YAML

id: P14927
gene_symbol: UQCRB
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  UQCRB (ubiquinol-cytochrome c reductase binding protein; also QP-C / cytochrome b-c1
  complex subunit 7 / QCR7) is a small (~13.5 kDa, 111 aa) nuclear-encoded, non-catalytic
  structural subunit of mitochondrial respiratory Complex III (the cytochrome b-c1 complex /
  ubiquinol-cytochrome c oxidoreductase). It is one of the low-molecular-weight subunits of
  the 11-subunit complex; the redox catalysis of Complex III is carried out by the catalytic
  subunits cytochrome b, the Rieske iron-sulfur protein (UQCRFS1) and cytochrome c1, whereas
  UQCRB contributes to assembly and structural integrity of the complex rather than to
  catalysis. Complex III is an obligate dimer embedded as a peripheral protein on the matrix
  side of the mitochondrial inner membrane, and it associates with Complex I and Complex IV to
  form respiratory supercomplexes and megacomplexes. Within the electron transport chain,
  Complex III transfers electrons from ubiquinol to cytochrome c, coupling this redox reaction
  to proton translocation across the inner membrane (the Q cycle) and thereby contributing to
  oxidative phosphorylation and aerobic respiration. UQCRB was originally proposed to be the
  ubiquinone-binding protein, but this ubiquinone-binding role is no longer considered
  established. Loss-of-function variants in UQCRB cause mitochondrial complex III deficiency
  (nuclear type 3), a mitochondrial disorder that can present with hypoglycemia and lactic
  acidosis.
alternative_products:
- name: '1'
  id: P14927-1
- name: '2'
  id: P14927-2
  sequence_note: VSP_045601
existing_annotations:
- term:
    id: GO:0045275
    label: respiratory chain complex III
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  review:
    summary: >-
      Phylogenetic (IBA) annotation placing UQCRB as part of respiratory chain complex III.
      This is the defining, well-established localization/membership of this subunit and is
      supported by cryo-EM structures of human Complex III and by UniProt.
    action: ACCEPT
    reason: >-
      UQCRB is a bona fide low-molecular-weight subunit of the cytochrome b-c1 complex
      (Complex III). This is confirmed structurally and by the family definition, and the
      complex membership is a core aspect of the gene's function.
    supported_by:
    - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
      supporting_text: "Component of the ubiquinol-cytochrome c oxidoreductase, a"
- term:
    id: GO:0006122
    label: mitochondrial electron transport, ubiquinol to cytochrome c
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: >-
      Phylogenetic (IBA) annotation to the specific Complex III process, transfer of
      electrons from ubiquinol to cytochrome c. As a structural subunit of Complex III,
      UQCRB participates in this process.
    action: ACCEPT
    reason: >-
      This is the core biological process of Complex III and the most appropriate specific
      BP term for a CIII subunit. Well supported by the complex's catalytic role.
    supported_by:
    - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
      supporting_text: "transfer from ubiquinol to cytochrome c, linking this redox reaction to"
- term:
    id: GO:0005743
    label: mitochondrial inner membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: >-
      Electronic annotation from UniProt Subcellular Location mapping placing UQCRB in the
      mitochondrial inner membrane. Consistent with its role as a peripheral inner-membrane
      Complex III subunit.
    action: ACCEPT
    reason: >-
      Complex III, and hence UQCRB, resides in the mitochondrial inner membrane. This is the
      correct, specific location and matches the UniProt subcellular location.
    supported_by:
    - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
      supporting_text: >-
        SUBCELLULAR LOCATION: Mitochondrion inner membrane
- term:
    id: GO:0006122
    label: mitochondrial electron transport, ubiquinol to cytochrome c
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: >-
      InterPro2GO electronic annotation to the Complex III electron transport process, based
      on the QCR7 family signatures (IPR003197, IPR036544). Duplicates the IBA/NAS annotations
      to the same specific BP.
    action: ACCEPT
    reason: >-
      The InterPro-to-GO mapping is appropriate for this family and points to the correct,
      specific Complex III process. Consistent with the experimental and phylogenetic evidence.
    supported_by:
    - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
      supporting_text: "transfer from ubiquinol to cytochrome c, linking this redox reaction to"
- term:
    id: GO:0016020
    label: membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: located_in
  review:
    summary: >-
      Generic ARBA machine-learning electronic annotation to "membrane". This is correct but
      far less informative than the specific mitochondrial inner membrane location that is
      also annotated.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      "membrane" is a high-level parent of the specific and better-supported term
      mitochondrial inner membrane (GO:0005743). It is not wrong, but it is uninformatively
      general given more precise annotations exist.
    supported_by:
    - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
      supporting_text: >-
        SUBCELLULAR LOCATION: Mitochondrion inner membrane
- term:
    id: GO:0045275
    label: respiratory chain complex III
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: part_of
  review:
    summary: >-
      InterPro2GO electronic annotation for complex III membership based on the QCR7 family
      superfamily signature (IPR036544). Duplicates the IBA and experimental (ComplexPortal
      IPI) annotations to the same term.
    action: ACCEPT
    reason: >-
      Correct complex membership for a QCR7-family protein; consistent with structural and
      phylogenetic evidence.
    supported_by:
    - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
      supporting_text: "Component of the ubiquinol-cytochrome c oxidoreductase, a"
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16189514
  qualifier: enables
  review:
    summary: >-
      Large-scale protein-protein interaction (IntAct/IPI) annotation to the uninformative
      term "protein binding". From a high-throughput human interactome screen.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      "protein binding" (GO:0005515) is an uninformative molecular function term that does not
      capture the actual, specific function of UQCRB. This is an experimental IntAct record,
      so it is retained rather than removed, but flagged as over-annotated per curation policy
      that discourages bare "protein binding".
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25416956
  qualifier: enables
  review:
    summary: >-
      Large-scale interactome (HuRI / IPI) annotation to the uninformative term
      "protein binding".
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" from a high-throughput interactome map. Retained as an
      experimental IntAct record but flagged as over-annotated; it does not describe UQCRB's
      specific structural function within Complex III.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:28514442
  qualifier: enables
  review:
    summary: >-
      Large-scale interactome (BioPlex / IPI) annotation to the uninformative term
      "protein binding".
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" from a high-throughput interactome study. Retained as an
      experimental IntAct record but flagged as over-annotated.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32296183
  qualifier: enables
  review:
    summary: >-
      Large-scale binary interactome (HuRI reference map / IPI) annotation to the
      uninformative term "protein binding".
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" from a high-throughput binary interactome map. Retained
      as an experimental IntAct record but flagged as over-annotated.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32814053
  qualifier: enables
  review:
    summary: >-
      Large-scale interactome (neurodegenerative-disease interactome / IPI) annotation to the
      uninformative term "protein binding".
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" from a high-throughput interactome study. Retained as an
      experimental IntAct record but flagged as over-annotated.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33961781
  qualifier: enables
  review:
    summary: >-
      Large-scale interactome (BioPlex 3.0 dual-cell networks / IPI) annotation to the
      uninformative term "protein binding".
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" from a high-throughput interactome study. Retained as an
      experimental IntAct record but flagged as over-annotated.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:40205054
  qualifier: enables
  review:
    summary: >-
      Large-scale multimodal cell-map interactome (IPI) annotation to the uninformative term
      "protein binding".
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" from a high-throughput interactome/cell-map study.
      Retained as an experimental IntAct record but flagged as over-annotated.
- term:
    id: GO:0005743
    label: mitochondrial inner membrane
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: located_in
  review:
    summary: >-
      Curator-judged sequence-similarity (ISS) transfer of the mitochondrial inner membrane
      location from the bovine ortholog (UniProtKB:P00128). Consistent with all other location
      evidence.
    action: ACCEPT
    reason: >-
      The inner-membrane localization is well established for Complex III subunits across
      species; the ISS transfer from the bovine QCR7 ortholog is appropriate and matches the
      specific, correct location.
    supported_by:
    - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
      supporting_text: >-
        SUBCELLULAR LOCATION: Mitochondrion inner membrane
- term:
    id: GO:0005743
    label: mitochondrial inner membrane
  evidence_type: IDA
  original_reference_id: PMID:28844695
  qualifier: located_in
  review:
    summary: >-
      Direct experimental (IDA, ComplexPortal) assignment of UQCRB to the mitochondrial inner
      membrane, based on the cryo-EM structure of the human respiratory megacomplex in which
      Complex III is resolved in the inner membrane.
    action: ACCEPT
    reason: >-
      Strong experimental support: the cryo-EM structure of the human MCI2III2IV2 megacomplex
      places the dimeric Complex III (and thus its UQCRB subunit) in the mitochondrial inner
      membrane. This is the core, specific location.
    supported_by:
    - reference_id: PMID:28844695
      supporting_text: >-
        The MCI2III2IV2 forms a circular structure with the dimeric CIII located in the
        center, where it is surrounded by two copies each of CI and CIV.
- term:
    id: GO:0006122
    label: mitochondrial electron transport, ubiquinol to cytochrome c
  evidence_type: NAS
  original_reference_id: PMID:28844695
  qualifier: involved_in
  review:
    summary: >-
      Non-traceable author statement (NAS, ComplexPortal) that UQCRB, as a Complex III subunit,
      is involved in mitochondrial electron transport from ubiquinol to cytochrome c.
    action: ACCEPT
    reason: >-
      This is the core, specific process of Complex III and is consistent with the
      IBA/InterPro annotations to the same term and with the structural characterization of
      the electron transport chain in this study.
    supported_by:
    - reference_id: PMID:28844695
      supporting_text: >-
        Two cytochrome c (Cyt.c) molecules are positioned to accept electrons on the surface
        of the c1 state CIII dimer.
- term:
    id: GO:0045275
    label: respiratory chain complex III
  evidence_type: IPI
  original_reference_id: PMID:28844695
  qualifier: part_of
  review:
    summary: >-
      Experimental (IPI, ComplexPortal) assignment of UQCRB as part of respiratory chain
      complex III, based on the cryo-EM structure that resolves the individual subunits of
      human Complex III.
    action: ACCEPT
    reason: >-
      Direct structural evidence for UQCRB being a component of Complex III. Core complex
      membership annotation.
    supported_by:
    - reference_id: PMID:28844695
      supporting_text: >-
        The structure not only reveals the precise assignment of individual subunits of human
        CI and CIII
- term:
    id: GO:0045333
    label: cellular respiration
  evidence_type: NAS
  original_reference_id: PMID:28844695
  qualifier: involved_in
  review:
    summary: >-
      Non-traceable author statement (NAS, ComplexPortal) annotating UQCRB to the broad process
      "cellular respiration".
    action: KEEP_AS_NON_CORE
    reason: >-
      Correct but general: cellular respiration is a broad parent process. The more specific
      and informative BP is mitochondrial electron transport, ubiquinol to cytochrome c
      (GO:0006122), which is separately annotated and represents the core function. Retained
      as valid but non-core.
    supported_by:
    - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
      supporting_text: "electron transport chain which drives oxidative phosphorylation"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: HTP
  original_reference_id: PMID:34800366
  qualifier: located_in
  review:
    summary: >-
      High-throughput (HTP) proteomic identification of UQCRB in the mitochondrion, from a
      quantitative high-confidence human mitochondrial proteome (MitoCoP). Correct but less
      specific than the mitochondrial inner membrane location.
    action: ACCEPT
    reason: >-
      Reliable high-throughput evidence for mitochondrial localization. It is a general parent
      of the more specific inner-membrane location, but it is correct and independently
      corroborates the organellar assignment.
    supported_by:
    - reference_id: PMID:34800366
      supporting_text: mitochondrial high-confidence proteome of >1,100 proteins (MitoCoP)
- term:
    id: GO:0005743
    label: mitochondrial inner membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-164651
  qualifier: located_in
  review:
    summary: >-
      Traceable author statement (Reactome) placing UQCRB in the mitochondrial inner membrane,
      associated with the reaction "Electron transfer from ubiquinol to cytochrome c of complex
      III".
    action: ACCEPT
    reason: >-
      Correct, specific location consistent with all other evidence. Reactome pathway context
      matches the Complex III role.
    supported_by:
    - reference_id: Reactome:R-HSA-164651
      supporting_text: >-
        The protonmotive Q cycle is the mechanism by which complex III transfers electrons
        from ubiquinol to cytochrome c, linking this process to translocation of protons across
        the membrane.
- term:
    id: GO:0005743
    label: mitochondrial inner membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9906017
  qualifier: located_in
  review:
    summary: >-
      Traceable author statement (Reactome) placing UQCRB in the mitochondrial inner membrane,
      in the context of Complex III assembly (proteolytic processing of the UQCRFS1 subunit).
    action: ACCEPT
    reason: >-
      Correct, specific location. The Reactome reaction concerns Complex III assembly in the
      inner membrane, consistent with UQCRB's structural/assembly role.
    supported_by:
    - reference_id: Reactome:R-HSA-9906017
      supporting_text: >-
        Proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex
        III dimer.
- term:
    id: GO:0005743
    label: mitochondrial inner membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9906042
  qualifier: located_in
  review:
    summary: >-
      Traceable author statement (Reactome) placing UQCRB in the mitochondrial inner membrane,
      in the context of Complex III maturation (TTC19 clearance of UQCRFS1 fragments).
    action: ACCEPT
    reason: >-
      Correct, specific location consistent with the Complex III assembly/maturation pathway
      context.
    supported_by:
    - reference_id: Reactome:R-HSA-9906042
      supporting_text: >-
        N-terminal cleavage fragments of UQCRFS1 are cleared by TTC19, stabilizing the final
        complex.
- term:
    id: GO:0006119
    label: oxidative phosphorylation
  evidence_type: TAS
  original_reference_id: PMID:3056408
  qualifier: involved_in
  review:
    summary: >-
      Traceable author statement (from the original human QP-C/UQCRB cDNA cloning paper)
      annotating involvement in oxidative phosphorylation, reflecting Complex III's role in
      driving OXPHOS via the electron transport chain.
    action: ACCEPT
    reason: >-
      Complex III is a core component of the electron transport chain that drives oxidative
      phosphorylation, so this is a valid process annotation for UQCRB. It is broader than the
      specific electron-transport step (GO:0006122) but correctly captures the downstream
      energetic role.
    supported_by:
    - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
      supporting_text: "electron transport chain which drives oxidative phosphorylation"
- term:
    id: GO:0009060
    label: aerobic respiration
  evidence_type: TAS
  original_reference_id: PMID:3056408
  qualifier: involved_in
  review:
    summary: >-
      Traceable author statement (original QP-C cDNA cloning paper) annotating involvement in
      aerobic respiration.
    action: KEEP_AS_NON_CORE
    reason: >-
      Correct but broad. Aerobic respiration is a high-level process; the core, specific
      function is captured by mitochondrial electron transport, ubiquinol to cytochrome c
      (GO:0006122). Retained as valid but non-core.
    supported_by:
    - reference_id: PMID:3056408
      supporting_text: >-
        The ubiquinone-binding protein (QP-C) is a nuclear-encoded component of
        ubiquinol-cytochrome c oxidoreductase in the mitochondrial respiratory chain and plays
        an important role in electron transfer
- term:
    id: GO:0098803
    label: respiratory chain complex
  evidence_type: TAS
  original_reference_id: PMID:3056408
  qualifier: located_in
  review:
    summary: >-
      Traceable author statement placing UQCRB in a respiratory chain complex, based on the
      original cDNA cloning paper identifying QP-C as a component of ubiquinol-cytochrome c
      oxidoreductase.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Correct but general: respiratory chain complex (GO:0098803) is a parent of the specific
      and better-supported term respiratory chain complex III (GO:0045275), which is annotated
      by IBA, InterPro and experimental (ComplexPortal IPI) evidence. Retained but flagged as
      over-general.
    supported_by:
    - reference_id: PMID:3056408
      supporting_text: >-
        The ubiquinone-binding protein (QP-C) is a nuclear-encoded component of
        ubiquinol-cytochrome c oxidoreductase in the mitochondrial respiratory chain
- term:
    id: GO:0005198
    label: structural molecule activity
  evidence_type: ISS
  original_reference_id: file:human/UQCRB/UQCRB-uniprot.txt
  qualifier: enables
  review:
    summary: >-
      Proposed molecular function annotation. UQCRB has no informative molecular function in
      GOA (only the uninformative "protein binding" IPIs). As a non-catalytic subunit of
      Complex III, its molecular function is best captured as structural molecule activity,
      contributing to the structural integrity of the cytochrome b-c1 complex.
    action: NEW
    reason: >-
      The catalytic activity of Complex III (electron transfer from ubiquinol to cytochrome c)
      is carried by cytochrome b, the Rieske iron-sulfur protein and cytochrome c1; UQCRB is a
      low-molecular-weight, non-catalytic structural subunit. Structural molecule activity
      (GO:0005198) is the appropriate subunit-specific molecular function, and it is not
      currently represented in GOA. No catalytic activity is asserted for UQCRB.
    supported_by:
    - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
      supporting_text: "Component of the ubiquinol-cytochrome c oxidoreductase, a"
core_functions:
- description: >-
    Non-catalytic structural subunit of mitochondrial respiratory Complex III (cytochrome
    b-c1 complex / ubiquinol-cytochrome c oxidoreductase). UQCRB contributes to the structural
    integrity and assembly of the complex; the complex as a whole transfers electrons from
    ubiquinol to cytochrome c in the mitochondrial inner membrane during aerobic respiration
    and oxidative phosphorylation.
  molecular_function:
    id: GO:0005198
    label: structural molecule activity
  contributes_to_molecular_function:
    id: GO:0008121
    label: quinol-cytochrome-c reductase activity
  directly_involved_in:
  - id: GO:0006122
    label: mitochondrial electron transport, ubiquinol to cytochrome c
  locations:
  - id: GO:0005743
    label: mitochondrial inner membrane
  in_complex:
    id: GO:0045275
    label: respiratory chain complex III
  supported_by:
  - reference_id: file:human/UQCRB/UQCRB-uniprot.txt
    supporting_text: "Component of the ubiquinol-cytochrome c oxidoreductase, a"
  - reference_id: PMID:28844695
    supporting_text: >-
      The structure not only reveals the precise assignment of individual subunits of human CI
      and CIII
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: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:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: PMID:16189514
  title: Towards a proteome-scale map of the human protein-protein interaction network.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      High-throughput interactome screen; source of a bare "protein binding" IPI. Does not
      inform UQCRB's specific function.
- id: PMID:25416956
  title: A proteome-scale map of the human interactome network.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      Large-scale interactome map; source of a bare "protein binding" IPI. Contextual only.
- id: PMID:28514442
  title: Architecture of the human interactome defines protein communities and disease
    networks.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      BioPlex interactome; source of a bare "protein binding" IPI. Contextual only.
- id: PMID:28844695
  title: Architecture of Human Mitochondrial Respiratory Megacomplex I(2)III(2)IV(2).
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Cryo-EM structure of the human respiratory megacomplex; directly resolves Complex III
      (including UQCRB) in the inner membrane and its role in electron transfer to cytochrome c.
- id: PMID:3056408
  title: Cloning and sequencing of a cDNA for human mitochondrial ubiquinone-binding
    protein of complex III.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Original cloning of human UQCRB/QP-C cDNA; establishes it as a nuclear-encoded component
      of ubiquinol-cytochrome c oxidoreductase (Complex III). Note the historical
      "ubiquinone-binding protein" attribution is now flagged CAUTION by UniProt.
- 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; source of bare "protein binding" IPIs. Contextual only.
- id: PMID:32814053
  title: Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins
    and Uncovers Widespread Protein Aggregation in Affected Brains.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      Neurodegenerative-disease interactome; source of bare "protein binding" IPIs. Contextual
      only.
- 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: >-
      BioPlex 3.0 interactome; source of bare "protein binding" IPIs. Contextual only.
- 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: >-
      MitoCoP high-confidence mitochondrial proteome; independently supports mitochondrial
      localization of UQCRB.
- id: PMID:40205054
  title: Multimodal cell maps as a foundation for structural and functional genomics.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      Multimodal cell-map interactome; source of a bare "protein binding" IPI. Contextual only.
- id: Reactome:R-HSA-164651
  title: Electron transfer from ubiquinol to cytochrome c of complex III
  findings: []
- id: Reactome:R-HSA-9906017
  title: Unknown peptidase cleaves UQCRFS1 subunit
  findings: []
- id: Reactome:R-HSA-9906042
  title: TTC19 clears UQCRFS1 fragments from Complex III
  findings: []
- id: file:human/UQCRB/UQCRB-uniprot.txt
  title: UniProtKB P14927 (QCR7_HUMAN) Cytochrome b-c1 complex subunit 7
  findings: []