protein
ATP synthase peripheral stalk subunit b, mitochondrial
Gene
ATP5PB
Organism
Homo sapiens(9606)
Length
256 aa
Mass
28,909 Da
ATP synthase peripheral stalk subunit b (ATP5PB) is a component of the mitochondrial F₀F₁-ATP synthase complex (Complex V), which catalyzes ATP synthesis from ADP using the proton gradient generated by the electron transport chain (UniProt: P24539). The protein functions as part of the peripheral stalk that acts as a stator, holding the catalytic core stationary relative to rotating central stalk elements during the rotary mechanism of ATP production.
ATP5PB localizes to the inner mitochondrial membrane within the F₀ domain and peripheral stalk structure (UniProt: P24539). No primary disease associations are documented in UniProt for this protein.
ATP5PB has been identified as relevant to Alzheimer's Disease through proteomic profiling of post-mortem AD brain tissue. However, the direction of dysregulation is ambiguous across subcellular fractions examined (Chaparral AD proteomics). The mean log₂ fold-change was 0.56, indicating modest overall elevation, though this masks heterogeneous changes across the four fractions (P2, P3, S2, S3) analyzed in the TMT-labeled discovery proteomics study.
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
-0.651
P2
not detected
S2
+1.762
S3
not detected
Mean log₂FC across detected fractions: +0.5558 (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 b, 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). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity)
Sources
Last updated 5/8/2026, 6:27:18 AM