Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Ensembl Compara ortholog transfer from rodent UQCRC1 (UniProtKB:Q68FY0, Q9CZ13) propagates response-to-activity, response-to-alkaloid, and protein-containing complex binding annotations to human UQCRC1.
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Complete coding sequence, intron/exon organization, and chromosomal location of the gene for the core I protein of human ubiquinol-cytochrome c reductase.
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Reports the complete coding sequence of human UQCRC1, showing 480 amino acids with a 34-residue mitochondrial leader peptide. Shows highest homology with rat beta-MPP (74% similarity, 55% identity) and N. crassa processing enhancing protein (64% similarity).
"Core I protein is a nuclear-encoded component of the ubiquinol-cytochrome c reductase complex of the mitochondrial respiratory chain."
Large-scale mapping of human protein-protein interactions by mass spectrometry.
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Large-scale IP-MS interactome mapping of 338 bait proteins; detected UQCRC1-UQCRC2 interaction.
"Large-scale immunoprecipitation of Flag-tagged versions of these proteins followed by LC-ESI-MS/MS analysis resulted in the identification of 24,540 potential protein interactions."
LC-MS/MS as an alternative for SDS-PAGE in blue native analysis of protein complexes.
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BN-PAGE/LC-MS/MS analysis of OXPHOS complexes confirming UQCRC1 as part of Complex III and its co-migration with UQCRC2.
"We demonstrate the feasibility of this approach by considering the oxidative phosphorylation complexes I-V in the native human embryonic kidney 293 mitochondrial fraction"
Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function.
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Identified UQCRC1 as one of 14 Parkin interactants by tandem affinity purification/MS, linking Parkin E3 ligase to mitochondrial OXPHOS components.
"Tandem affinity purification/MS revealed 14 potential interactants of Parkin; CKB, DBT, HSPD1, HSPA9, LRPPRC, NDUFS2, PRDX6, SLC25A5, TPI1, UCHL1, UQCRC1, VCL, YWHAZ, YWHAE."
Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes.
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Identified UQCRC1 in mitochondria purified from human skeletal muscle biopsies by phosphoproteomics.
"We performed a phosphoproteomics study of functional mitochondria isolated from human muscle biopsies"
Architecture of Human Mitochondrial Respiratory Megacomplex I(2)III(2)IV(2).
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Cryo-EM structure of the human respiratory megacomplex at 3.4 Angstrom resolution directly resolves UQCRC1 (chains L/Y) within the CIII2 dimer at the center of the megacomplex I2III2IV2.
"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."
Mitochondrial peptide BRAWNIN is essential for vertebrate respiratory complex III assembly.
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Identified UQCC6/BRAWNIN as a mitochondrial peptide essential for CIII2 assembly that interacts with UQCRC1.
"Mitochondrial peptide BRAWNIN is essential for vertebrate respiratory complex III assembly."
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
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Large-scale Y2H interactome mapping of neurodegenerative disease proteins identified numerous UQCRC1 interaction partners, most from high-throughput screening without targeted validation.
"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.
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BioPlex 3.0 proteome-scale interactome detected UQCRC1-UQCRC2 interaction in 293T cells.
"Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks."
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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Identified UQCRC1 as a high-confidence mitochondrial protein in the quantitative human mitochondrial proteome.
"Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context."
The cardiac-enriched microprotein mitolamban regulates mitochondrial respiratory complex assembly and function in mice.
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Identified mitolamban (Mtlbn/STMP1) as a microprotein that interacts with Complex III subunits including UQCRC1 and regulates complex assembly.
"Mtlbn localizes specifically to the inner mitochondrial membrane where it interacts with subunits of complex III of the electron transport chain and with mitochondrial respiratory supercomplexes."
Mitochondrial UQCRC1 mutations cause autosomal dominant parkinsonism with polyneuropathy.
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Identified UQCRC1 mutations (I311L, Y314S) as causing autosomal dominant parkinsonism with polyneuropathy (PKNPY). UQCRC1 plays an important role in maintenance of proper mitochondrial function in nigral dopaminergic neurons.
"Mitochondrial UQCRC1 mutations cause autosomal dominant parkinsonism with polyneuropathy."
Electron transfer from ubiquinol to cytochrome c of complex III
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Reactome pathway describing the Q-cycle mechanism by which Complex III transfers electrons from ubiquinol to cytochrome c with concomitant proton translocation.
"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."
Unknown peptidase cleaves UQCRFS1 subunit
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Reactome notes that the peptidase that cleaves UQCRFS1 in humans is unknown, with UQCRC1 and UQCRC2 listed as possible candidates based on the cattle model.
"Possible candidates for the peptidase are the UQCRC1 and UQCRC2 subunits (as hinted at in the cattle model) or the SPY complex"
TTC19 clears UQCRFS1 fragments from Complex III
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TTC19 clears N-terminal cleavage fragments of UQCRFS1 from Complex III to stabilize the final complex.
"N-terminal cleavage fragments of UQCRFS1 are cleared by TTC19, stabilizing the final complex."
Deep research review of UQCRC1 (Falcon/Edison)
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Comprehensive review confirms UQCRC1 as a non-catalytic structural core subunit of CIII2 with no intrinsic enzymatic activity. It stabilizes the CIII2 dimer and mediates matrix-side contacts with Complex I in supercomplexes via interactions with NDUFB4 and NDUFB9.
"UQCRC1 has no demonstrated enzymatic activity within Complex III. It is a structural core protein; catalytic chemistry (Q cycle) is executed by cytochrome b, Rieske (UQCRFS1), and cytochrome c1 (CYC1). Thus, there is no substrate specificity attributable to UQCRC1; its contribution is architectural and organizational."