Gene Ontology annotation through association of InterPro records with GO terms
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
Mutation of C20orf7 disrupts complex I assembly and causes lethal neonatal mitochondrial disease.
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C20orf7 (NDUFAF5) is peripherally associated with the matrix face of the mitochondrial inner membrane, and silencing it decreases Complex I activity; patient fibroblasts show near-complete loss of Complex I holoenzyme with an early assembly defect.
"peripherally associated with the matrix face of the"
NDUFAF5 Hydroxylates NDUFS7 at an Early Stage in the Assembly of Human Complex I.
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NDUFAF5 is a 7-beta-strand SAM-dependent methyltransferase-fold enzyme that, like RdmB, catalyzes hydroxylation (SAM as cofactor) of Arg-73 of NDUFS7 early in Complex I assembly.
"RdmB has no methyltransferase activity, and SAM acts as a cofactor in the process of hydroxylation"
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Suppression of NDUFAF5 reduces NDUFS7 Arg-73 hydroxylation and impairs Complex I biogenesis at an early stage, affecting both arms of the complex.
"The suppression of NDUFAF5 affected the biogenesis of complex I at an early stage of assembly"
Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function.
Architecture of the human interactome defines protein communities and disease networks.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Defining mitochondrial protein functions through deep multiomic profiling.
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PYURF is a SAM-dependent methyltransferase chaperone that supports Complex I assembly and CoQ biosynthesis; it directly binds and stabilizes NDUFAF5.
"methyltransferase chaperone that supports both complex I assembly"
Peripheral arm subunits bind the 815kDa complex to form a 980kDa complex
Intermediate 2 binds MT-ND1:NDUFAF5:NDUFAF6 to form a 315kDa subcomplex
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NDUFAF5 is part of the MT-ND1:NDUFAF5:NDUFAF6 assembly intermediate anchoring the IP subcomplex to the inner membrane; NDUFAF8 and PYURF stabilize NDUFAF5.
"The IP subcomplex is anchored to the inner mitochondrial membrane by NADH-ubiquinone oxidoreductase chain 1 (MT-ND1)"
The MCIA complex, NDUFAF2-7 all dissociate from the 980kDa complex, resulting in Complex I
ND4, ND5 bind the 550kDa complex to form the 815kDa complex
The 315kDa subcomplex binds the 370kDa subcomplex to form the 550kDa complex