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
Gene Ontology annotation based on curation of immunofluorescence data
TMEM70 mutations cause isolated ATP synthase deficiency and neonatal mitochondrial encephalocardiomyopathy.
Mitochondrial membrane assembly of TMEM70 protein.
TMEM70 facilitates biogenesis of mammalian ATP synthase by promoting subunit c incorporation into the rotor structure of the enzyme.
TMEM70 functions in the assembly of complexes I and V.
A reference map of the human binary protein interactome.
TMEM70 forms oligomeric scaffolds within mitochondrial cristae promoting in situ assembly of mammalian ATP synthase proton channel.
TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase and interact with assembly factors for complex I.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Deep research report on TMEM70
Cyberian deep research on TMEM70 function
OpenScientist hypothesis run: TMEM70 c-ring versus complex-I boundary
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TMEM70 is strongly supported as the oligomeric scaffold for mitochondrial ATP synthase c-ring assembly, with TMEM242 acting downstream in Fo completion.
"TMEM70 functions as a dedicated oligomeric scaffold for mitochondrial ATP synthase c-ring (proton channel rotor) assembly"
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The reported contribution of TMEM70 to respiratory-chain complex-I biogenesis remains unresolved because specific complexome changes coexist with secondary cristae and complex-V explanations.
"The evidence is genuinely mixed, and the current data do not permit a definitive conclusion."