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The protein encoded by this gene localizes to the primary cilium and to the plasma membrane. The gene functions in centriole migration to the apical membrane and formation of the primary cilium. Multiple transcript variants encoding different isoforms have been found for this gene. Defects in this gene are a cause of Meckel syndrome type 3 (MKS3) and Joubert syndrome type 6 (JBTS6). [provided by RefSeq, Nov 2008]

GNAQ belong to the family of heterotrimeric Guanine nucleotide-binding proteins proteins that couple cell surface, 7-transmembrane domain receptors to intracellular signaling pathways. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. GNAQ is the alpha subunit of one of the heterotrimeric GTP-binding proteins that mediates stimulation of phospholipase C-beta. in recent st

Known to be prominent in bacteria, D amino acids were generally thought to be absent in mammals. D-serine has since been found in high levels in the mammalian brain and in various mammalian fluids. D-serine activates N-methyl-D-aspartate (NMDA) receptors--molecules with important roles in learning, brain growth and brain cell death. Serine racemase is the enzyme catalyzing the formation of D-serine from L-serine. Serine racemase is a member of the family of pyridoxal-5’ phosphate-dependent

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S8E family of ribosomal proteins. It is located in the cytoplasm. Increased expression of this gene in colorectal tumors and colon polyps compared to matched normal colo

Calcium signaling in mitochondria is important in order for it to function in response to a variety of extracellular stimuli. Signaling begins with Ca(2+) entry in mitochondria via the Ca(2+) uniporter followed by Ca(2+) activation of three dehydrogenases in the mitochondrial matrix. ARALAR, the neuronal Ca(2+)-binding mitochondrial aspartate-glutamate carrier, has Ca(2+) binding domains facing the extramitochondrial space and functions in the malate-aspartate NADH shuttle (MAS). ARALAR is enc