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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Knockdown of DAPIT (diabetes-associated protein in insulin-sensitive tissue) results in loss of ATP synthase in mitochondria.
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DAPIT knockdown in HeLa cells reduces the population of ATP synthase in mitochondria and lowers mitochondrial ATP synthesis activity, indicating that DAPIT is required to maintain the ATP synthase complex.
"DAPIT-knockdown cells show smaller mitochondrial ATP synthesis activity"
Assembly of human mitochondrial ATP synthase through two separate intermediates, F1-c-ring and b-e-g complex.
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Human mitochondrial ATP synthase assembles from separately formed rotor and stator modules; the abstract foregrounds d-subunit knockdown, but ComplexPortal uses this study as the reference for ATP5MD complex membership, PMF-driven ATP synthesis, and inner-membrane localization.
"human cells could not form ATP synthase holocomplex"
USMG5 Ashkenazi Jewish founder mutation impairs mitochondrial complex V dimerization and ATP synthesis.
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A homozygous USMG5 (ATP5MD/ATP5MK) splice mutation abolishes the protein and selectively reduces Complex V dimer expression and ATP synthesis without affecting monomeric CV; wild-type cDNA rescue restores dimerization and ATP production, defining USMG5 as a Complex V subunit required for dimerization.
"reduced both CV dimer expression and ATP synthesis rate"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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ATP5MD is identified as part of the high-confidence human mitochondrial proteome, corroborating its mitochondrial localization.
"high-confidence human mitochondrial proteome"
Enzyme-bound ATP is released
ADP and Pi bind to ATPase
F1Fo ATP synthase dimerizes
UniProtKB Q96IX5 (ATPMK_HUMAN) - ATP synthase F(0) complex subunit k, mitochondrial
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UniProt curates ATP5MD as subunit k of the mitochondrial membrane ATP synthase complex (Complex V), part of the F(o) domain, required for dimerization of the complex and localized to the mitochondrion membrane as a single-pass membrane protein.
"Subunit k, of the mitochondrial membrane ATP synthase complex"