Anti-RIOK2 Antibody Picoband® Fluoro647 Conjugated

RIO kinase 2 (RIOK2) is a member of the RIO family of atypical serine protein kinases first characterized in yeast. There are three RIO kinase subfamilies: RIO1, RIO2, and RIO3. RIOK1 and RIOK2 proteins are present in organisms from Archaea to humans. Studies of RIO kinases in yeast indicate that they play a role in ribosome biogenesis. Human RIOK2 has been shown to be a part of a late 40S pre-ribosomal particle and have influence on 40S maturation.

ATP synthase F (0) complex subunit C1,2,3, mitochondrial; ATP synthase lipid-binding protein; ATP synthase membrane subunit c locus 1,2,3; ATP synthase proteolipid P1; ATP synthase proton-transporting mitochondrial F (0) complex subunit C1,2,3; ATPase protein 9; ATPase subunit c; ATP5MC1,2,3; ATP5G1,2,3

Highly expressed in thymus, uterus and testis. Detected at lower levels in brain, mammary gland, prostate, salivary gland and fetal spleen. In brain, highest expression in thalamus, hippocampus and amygdala. .

Amino Acid Metabolism, Amino Acids, Cancer, Channels, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Plasma Membrane, Signal Transduction

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. Part of the complex F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

1. Ameismeier, M., Cheng, J., Berninghausen, O., Beckmann, R. Visualizing late states of human 40S ribosomal subunit maturation. Nature 558: 249-253, 2018. 2. Guderian, G., Peter, C., Wiesner, J., Sickmann, A., Schulze-Osthoff, K., Fischer, U., Grimmler, M. RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity. J. Biol. Chem. 286: 1976-1986, 2011. 3. Hartz, P. A. Personal Communication. Baltimore, Md. 10/31/2017.