protein
ATP synthase F(0) complex subunit e, mitochondrial
aka ATPase subunit e
Gene
ATP5ME
Organism
Homo sapiens(9606)
Length
69 aa
Mass
7,933 Da
ATP synthase F(0) complex subunit e (ATP5ME) is a small structural subunit of the mitochondrial ATP synthase complex (Complex V), which catalyzes ATP synthesis coupled to proton translocation across the inner mitochondrial membrane during oxidative phosphorylation (UniProt: P56385). The protein is part of the membrane-embedded F(0) domain and participates in the rotary mechanism that links proton gradient-driven conformational changes to ATP production in the catalytic F(1) head.
ATP5ME is localized to the inner mitochondrial membrane as a component of the respiratory electron transport chain machinery. UniProt records no primary disease associations for this protein, though ATP synthase dysfunction is implicated broadly in mitochondrial and metabolic disorders.
Quantitative proteomics data from human post-mortem Alzheimer's disease brain tissue show ambiguous directionality for ATP5ME across subcellular fractions (mean log2 fold-change: 0.83), indicating variable changes depending on the subcellular compartment analyzed (Chaparral AD proteomics). This ambiguous pattern may reflect differential subcellular redistribution or fraction-specific alterations in ATP synthase assembly or stability in AD pathology, warranting further investigation of mitochondrial energetics in neurodegeneration.
Generated from the curated entity record below. May contain errors — verify against source links.
Proteomics Evidence · AD
⚠ Ambiguous — detected in AD samples, direction unclear across fractionsP3
-0.228
P2
not detected
S2
+1.889
S3
not detected
Mean log₂FC across detected fractions: +0.8307 (2 of 4 fractions detected)
Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.
Related Publications
Browse all →Tau molecular diversity contributes to clinical heterogeneity in Alzheimer's disease.
Dujardin Simon et al.Nature medicine2020PMID 32572268Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer's Disease Progression.
Bai Bing et al.Neuron2020PMID 31926610A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer's Disease.
Seyfried Nicholas T et al.Cell systems2017PMID 27989508Large-scale deep multi-layer analysis of Alzheimer's disease brain reveals strong proteomic disease-related changes not observed at the RNA level.
Johnson Erik C B et al.Nature neuroscience2022PMID 35115731Organization and regulation of gene transcription.
Cramer PatrickNature2019PMID 31462772
Function
Subunit e, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (PubMed:37244256)
Sources
Last updated 5/8/2026, 6:27:21 AM