RGS14

Regulator of G-protein signaling 14 (RGS14) is a protein that in humans is encoded by the RGS14 gene.^[5]

RGS14
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2JNU, 2OM2, 2XNS, 3ONW, 3QI2
Identifiers
Aliases	RGS14, regulator of G protein signaling 14
External IDs	OMIM: 602513; MGI: 1859709; HomoloGene: 4735; GeneCards: RGS14; OMA:RGS14 - orthologs
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q35.3 Start 177,357,924 bp[1] End 177,372,596 bp[1]
Gene location (Mouse) Chr. Chromosome 13 (mouse)[2] Band 13 B1|13 29.8 cM Start 55,517,545 bp[2] End 55,532,500 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte caudate nucleus putamen nucleus accumbens right lobe of liver blood monocyte spleen right uterine tube lymph node Top expressed in granulocyte CA3 field entorhinal cortex perirhinal cortex thymus nucleus accumbens hippocampus proper tibiofemoral joint olfactory tubercle dentate gyrus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function GTPase activating protein binding GTPase activator activity GTPase regulator activity microtubule binding protein binding GDP-dissociation inhibitor activity G-protein alpha-subunit binding signaling receptor complex adaptor activity protein kinase binding GTPase activity Cellular component cytoplasm PML body centrosome postsynaptic membrane cell projection spindle pole nuclear body membrane postsynaptic density plasma membrane spindle dendritic spine synapse microtubule organizing center cell junction dendrite microtubule cytoskeleton nucleus glutamatergic synapse Biological process visual learning intracellular signal transduction regulation of G protein-coupled receptor signaling pathway chromosome segregation learning response to oxidative stress cell division positive regulation of neurogenesis positive regulation of GTPase activity spindle organization long-term memory negative regulation of MAP kinase activity nucleocytoplasmic transport zygote asymmetric cell division negative regulation of ERK1 and ERK2 cascade cell cycle platelet-derived growth factor receptor signaling pathway negative regulation of signal transduction regulation of DNA-templated transcription in response to stress negative regulation of synaptic plasticity signal transduction long-term potentiation mitotic cell cycle negative regulation of G protein-coupled receptor signaling pathway modulation of chemical synaptic transmission G protein-coupled receptor signaling pathway positive regulation of signal transduction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10636 51791 Ensembl ENSG00000169220 ENSMUSG00000052087 UniProt O43566 P97492 RefSeq (mRNA) NM_006480 NM_001366617 NM_001366618 NM_016758 NM_001360714 RefSeq (protein) NP_006471 NP_001353546 NP_001353547 NP_058038 NP_001347643 Location (UCSC) Chr 5: 177.36 – 177.37 Mb Chr 13: 55.52 – 55.53 Mb PubMed search [3] [4]
Wikidata
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Function

RGS14 is a member of the regulator of G protein signalling family. This protein contains one RGS domain, two Raf-like Ras-binding domains (RBDs), and one GoLoco motif. The protein attenuates the signaling activity of G-proteins by binding, through its GoLoco domain, to specific types of activated, GTP-bound G alpha subunits. Acting as a GTPase activating protein (GAP), the protein increases the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.^[5]

Increasing the expression of the RGS14 protein in the V2 secondary visual cortex of mice promotes the conversion of short-term to long-term object-recognition memory.^[6] Conversely RGS14 is enriched in CA2 pyramidal neurons and suppresses synaptic plasticity of these synapses and hippocampal-based learning and memory.^[7]

Interactions

RGS14 has been shown to interact with:

• GNAI1^{[8][9][10][11]} and
• GNAI3.^[8]