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
CLIC, a tool for expanding biological pathways based on co-expression across thousands of datasets.
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Endogenous C7orf55/FMC1 localizes to mitochondria in HeLa cells (immunofluorescence).
"First, we confirmed mitochondrial localization (Fig 6A) by immunostaining with antibodies to endogenous C7orf55"
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FMC1 knockout specifically destabilizes complex V (reduced F1 subunits, assembled complex and ATPase activity), and all defects are rescued by re-expression.
"All the defects in complex V were entirely rescued by the reintroduction of a CRISPR-resistant version of C7orf55 (Fig 6B and 6C, fourth column)."
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FMC1 co-immunoprecipitates with the F1 assembly factor ATPAF2.
"To confirm this binding association, we also tagged ATPAF2 with a V5 tag and showed that immunoprecipitation of ATPAF2-V5 binds C7orf55-FLAG (Fig 6E)."
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Human FMC1 and yeast Fmc1p share an LYR domain but have no BLASTP-detectable sequence homology.
"however these short human and yeast proteins have no sequence homology detectable via BLASTP"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions.
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Yeast Fmc1p is a soluble mitochondrial matrix protein needed at 37 C for F1 formation/stability, and its loss is compensated by overexpressing Atp12p.
"soluble protein located in the mitochondrial matrix"
Eukaryotic LYR Proteins Interact with Mitochondrial Protein Complexes.
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Review placing FMC1 among LYR-motif-related assembly factors of OXPHOS complexes, and noting that Pfam did not then recognize human FMC1 as a LYRM.
"Human formation of mitochondrial complexes protein 1 (FMC1, Table 1) is not recognized as LYRM by the Pfam search tool"
Human mitochondrial protein complexes revealed by large-scale coevolution analysis and deep learning-based structure modeling.
RPL27 Promotes Gastric Cancer Progression by Enhancing Oxidative Phosphorylation Via FMC1.
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In gastric cancer cells, FMC1 acts downstream of RPL27 and affects mitochondrial function, including ATP5A expression.
"including alterations in membrane potential,"
UniProtKB entry Q96HJ9 (FMC1_HUMAN)