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 keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Falcon deep research synthesis for human SDHC
Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of iron sulfur (Ip) subunit of liver mitochondria.
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Established Complex II as a mitochondrial enzyme involved in the TCA cycle and aerobic respiratory chain. Cloned the iron-sulfur (Ip/SDHB) subunit.
"Complex II (succinate-ubiquinone oxidoreductase) is an important enzyme complex of both the tricarboxylic acid cycle and of the aerobic respiratory chains of mitochondria in eukaryotic cell and prokaryotic organisms"
Cytochrome b in human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the components in liver mitochondria and chromosome assignment of the genes for the large (SDHC) and small (SDHD) subunits to 1q21 and 11q23.
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Original cDNA cloning of SDHC (cybL, 140 mature amino acids) and SDHD (cybS, 103 amino acids) from human liver. Predicted three transmembrane segments for each subunit. Identified histidine residues as potential heme axial ligands. Mapped SDHC to chromosome 1q21 and SDHD to 11q23.
"the amino acid sequences of the large (cybL) and small (cybS) subunits of cytochrome b in human liver complex II were deduced from cDNAs isolated by homology probing with mixed primers for the polymerase chain reaction. The mature cybL and cybS contain 140 and 103 amino acids, respectively"
Assembly of mammalian oxidative phosphorylation complexes I-V and supercomplexes.
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Review of OXPHOS complex assembly. Complex II assembly involves the SDHA:SDHB catalytic subcomplex associating with the SDHC:SDHD membrane anchor in the inner mitochondrial membrane.
"The assembly of the five oxidative phosphorylation system (OXPHOS) complexes in the inner mitochondrial membrane is an intricate process"
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 for neurodegenerative disease. Detected interactions between SDHC and several nuclear/cytoplasmic proteins (PRKCA, YWHAG, KAT5, SETDB1, LMO3) of uncertain biological significance for a mitochondrial membrane protein.
"we report on an interactome map that focuses on neurodegenerative disease (ND), connects"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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Quantitative proteomics confirmed SDHC as a component of the high-confidence human mitochondrial proteome.
"Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context [SDHC identified by quantitative mass spectrometry]"
Structure of the human respiratory complex II.
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Determined cryo-EM structure of human Complex II at 2.86 angstroms. SDHC resolved with three transmembrane helices, one heme b group (shared with SDHD), and ubiquinone bound at the pocket formed by transmembrane helix I of SDHC, helix II of SDHD, and the C-terminal segment of SDHB. SDHC residues Ile56, Trp61, Met65, Ile69 directly contact ubiquinone. His127 of SDHC provides an axial ligand to heme b iron. The heme b is proposed to serve as an electron sink during the two-electron reduction of ubiquinone.
"The two membrane-anchored proteins (SDHC and SDHD) in human CII, each with three transmembrane helices, contain only one heme b group"
SDH complex dehydrogenates succinate
SDHA:SDHB binds to SDHC:SDHD