RGS16

Regulator of G-protein signalling 16
File:PBB Protein RGS16 image.jpg PDB rendering based on 2ik8.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 2ik8​
Identifiers
Symbols	RGS16 ; A28-RGS14; A28-RGS14P; RGS-R
External IDs	Template:OMIM5 Template:MGI HomoloGene: 2196
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE RGS16 209324 s at tn.png
File:PBB GE RGS16 209325 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Regulator of G-protein signalling 16, also known as RGS16, is a human gene.

The protein encoded by this gene belongs to the 'regulator of G protein signaling' family. It inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits. It also may play a role in regulating the kinetics of signaling in the phototransduction cascade.

Further reading

• De Vries L, Zheng B, Fischer T; et al. (2000). "The regulator of G protein signaling family". Annu. Rev. Pharmacol. Toxicol. 40: 235–71. doi:10.1146/annurev.pharmtox.40.1.235. PMID 10836135.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chen CK, Wieland T, Simon MI (1996). "RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling". Proc. Natl. Acad. Sci. U.S.A. 93 (23): 12885–9. PMID 8917514.CS1 maint: Multiple names: authors list (link)
• Chen C, Zheng B, Han J, Lin SC (1997). "Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast". J. Biol. Chem. 272 (13): 8679–85. PMID 9079700.CS1 maint: Multiple names: authors list (link)
• Buckbinder L, Velasco-Miguel S, Chen Y; et al. (1997). "The p53 tumor suppressor targets a novel regulator of G protein signaling". Proc. Natl. Acad. Sci. U.S.A. 94 (15): 7868–72. PMID 9223279.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Natochin M, Lipkin VM, Artemyev NO (1997). "Interaction of human retinal RGS with G-protein alpha-subunits". FEBS Lett. 411 (2–3): 179–82. PMID 9271201.CS1 maint: Multiple names: authors list (link)
• Snow BE, Antonio L, Suggs S, Siderovski DP (1998). "Cloning of a retinally abundant regulator of G-protein signaling (RGS-r/RGS16): genomic structure and chromosomal localization of the human gene". Gene. 206 (2): 247–53. PMID 9469939.CS1 maint: Multiple names: authors list (link)
• Beadling C, Druey KM, Richter G; et al. (1999). "Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes". J. Immunol. 162 (5): 2677–82. PMID 10072511.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Druey KM, Ugur O, Caron JM; et al. (1999). "Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling". J. Biol. Chem. 274 (26): 18836–42. PMID 10373502.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Popov SG, Krishna UM, Falck JR, Wilkie TM (2000). "Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity". J. Biol. Chem. 275 (25): 18962–8. doi:10.1074/jbc.M001128200. PMID 10747990.CS1 maint: Multiple names: authors list (link)
• Zheng B, Chen D, Farquhar MG (2000). "MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16". Proc. Natl. Acad. Sci. U.S.A. 97 (8): 3999–4004. PMID 10760272.CS1 maint: Multiple names: authors list (link)
• Chatterjee TK, Fisher RA (2000). "Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs". J. Biol. Chem. 275 (31): 24013–21. doi:10.1074/jbc.M002082200. PMID 10791963.
• Wieland T, Bahtijari N, Zhou XB; et al. (2000). "Polarity exchange at the interface of regulators of G protein signaling with G protein alpha-subunits". J. Biol. Chem. 275 (37): 28500–6. doi:10.1074/jbc.M004187200. PMID 10878019.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chen C, Wang H, Fong CW, Lin SC (2001). "Multiple phosphorylation sites in RGS16 differentially modulate its GAP activity". FEBS Lett. 504 (1–2): 16–22. PMID 11522288.CS1 maint: Multiple names: authors list (link)
• Derrien A, Druey KM (2002). "RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation". J. Biol. Chem. 276 (51): 48532–8. doi:10.1074/jbc.M108862200. PMID 11602604.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Derrien A, Zheng B, Osterhout JL; et al. (2003). "Src-mediated RGS16 tyrosine phosphorylation promotes RGS16 stability". J. Biol. Chem. 278 (18): 16107–16. doi:10.1074/jbc.M210371200. PMID 12588871.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Osterhout JL, Waheed AA, Hiol A; et al. (2003). "Palmitoylation regulates regulator of G-protein signaling (RGS) 16 function. II. Palmitoylation of a cysteine residue in the RGS box is critical for RGS16 GTPase accelerating activity and regulation of Gi-coupled signalling". J. Biol. Chem. 278 (21): 19309–16. doi:10.1074/jbc.M210124200. PMID 12642592.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hiol A, Davey PC, Osterhout JL; et al. (2003). "Palmitoylation regulates regulators of G-protein signaling (RGS) 16 function. I. Mutation of amino-terminal cysteine residues on RGS16 prevents its targeting to lipid rafts and palmitoylation of an internal cysteine residue". J. Biol. Chem. 278 (21): 19301–8. doi:10.1074/jbc.M210123200. PMID 12642593.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Johnson EN, Seasholtz TM, Waheed AA; et al. (2004). "RGS16 inhibits signalling through the G alpha 13-Rho axis". Nat. Cell Biol. 5 (12): 1095–103. doi:10.1038/ncb1065. PMID 14634662.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)