ATP5F1B

ATP5F1B is a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked mul

ATP Synthase F1 Subunit Beta

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

Angiogenesis Source: UniProtKB
ATP biosynthetic process Source: UniProtKB
Cellular response to interleukin-7 Source: Ensembl
Cristae formation Source: Reactome
Generation of precursor metabolites and energy Source: UniProtKB
Lipid metabolic process Source: Ensembl
Mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
Mitochondrion organization Source: Reactome
Negative regulation of cell adhesion involved in substrate-bound cell migration Source: Ensembl
Osteoblast differentiation Source: UniProtKB
Positive regulation of blood vessel endothelial cell migration Source: CAFA
Proton transmembrane transport Source: UniProtKB
Regulation of intracellular pH Source: UniProtKB

Mitochondrion inner membrane