RGS16

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2BT2, 2IK8

Identifiers

Aliases

RGS16, A28-RGS14, A28-RGS14P, RGS-R, regulator of G-protein signaling 16, regulator of G protein signaling 16

External IDs

OMIM: 602514 MGI: 108407 HomoloGene: 2196 GeneCards: RGS16

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1q25.3	Start	182,598,623 bp^[1]
Band	1q25.3	End	182,604,389 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 1 (mouse)^[2]

Band	1 G3\|1 65.43 cM	Start	153,616,095 bp^[2]
Band	1 G3\|1 65.43 cM	End	153,621,214 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

vena cava

oocyte

left lobe of thyroid gland

right lobe of thyroid gland

anterior pituitary

saphenous vein

gastric mucosa

secondary oocyte

gallbladder

lymph node

Top expressed in

medial geniculate nucleus

suprachiasmatic nucleus

medial dorsal nucleus

lateral geniculate nucleus

internal carotid artery

external carotid artery

islet of Langerhans

inferior colliculus

entorhinal cortex

Paneth cell

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding GTPase activator activity calmodulin binding GTPase activity
Cellular component	cytoplasm plasma membrane membrane intrinsic component of membrane
Biological process	negative regulation of signal transduction regulation of G protein-coupled receptor signaling pathway visual perception positive regulation of GTPase activity G protein-coupled receptor signaling pathway
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


6004


19734

Ensembl


ENSG00000143333


ENSMUSG00000026475

UniProt


O15492


P97428

RefSeq (mRNA)


NM_002928


NM_011267

RefSeq (protein)


NP_002919


NP_035397

Location (UCSC)

Chr 1: 182.6 – 182.6 Mb

Chr 1: 153.62 – 153.62 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Regulator of G-protein signaling 16 is a protein that in humans is encoded by the RGS16 gene.^[5]^[6]

Function

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.^[6]

Interactions

RGS16 has been shown to interact with GNAQ^[7] and GNAI3.^[8]^[9]

References

Berman DM, Wilkie TM, Gilman AG (Aug 1996). "GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits". Cell. 86 (3): 445–52. doi:10.1016/S0092-8674(00)80117-8. PMID 8756726. S2CID 12427406.
De Vries L, Zheng B, Fischer T, Elenko E, Farquhar MG (2000). "The regulator of G protein signaling family". Annual Review of Pharmacology and Toxicology. 40: 235–71. doi:10.1146/annurev.pharmtox.40.1.235. PMID 10836135.
Chen CK, Wieland T, Simon MI (Nov 1996). "RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling". Proceedings of the National Academy of Sciences of the United States of America. 93 (23): 12885–9. Bibcode:1996PNAS...9312885C. doi:10.1073/pnas.93.23.12885. PMC 24015. PMID 8917514.
Chen C, Zheng B, Han J, Lin SC (Mar 1997). "Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast". The Journal of Biological Chemistry. 272 (13): 8679–85. doi:10.1074/jbc.272.13.8679. PMID 9079700.
Buckbinder L, Velasco-Miguel S, Chen Y, Xu N, Talbott R, Gelbert L, Gao J, Seizinger BR, Gutkind JS, Kley N (Jul 1997). "The p53 tumor suppressor targets a novel regulator of G protein signaling". Proceedings of the National Academy of Sciences of the United States of America. 94 (15): 7868–72. Bibcode:1997PNAS...94.7868B. doi:10.1073/pnas.94.15.7868. PMC 21521. PMID 9223279.
Luo X, Popov S, Bera AK, Wilkie TM, Muallem S (Mar 2001). "RGS proteins provide biochemical control of agonist-evoked [Ca2+]i oscillations". Molecular Cell. 7 (3): 651–60. doi:10.1016/S1097-2765(01)00211-8. PMID 11463389.
Natochin M, Lipkin VM, Artemyev NO (Jul 1997). "Interaction of human retinal RGS with G-protein alpha-subunits". FEBS Letters. 411 (2–3): 179–82. doi:10.1016/S0014-5793(97)00687-X. PMID 9271201. S2CID 84269212.
Beadling C, Druey KM, Richter G, Kehrl JH, Smith KA (Mar 1999). "Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes". Journal of Immunology. 162 (5): 2677–82. PMID 10072511.
Druey KM, Ugur O, Caron JM, Chen CK, Backlund PS, Jones TL (Jun 1999). "Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling". The Journal of Biological Chemistry. 274 (26): 18836–42. doi:10.1074/jbc.274.26.18836. PMID 10373502.
Pashkov V, Huang J, Parameswara VK, Kedzierski W, Kurrasch DM, Tall GG, Esser V, Gerard RD, Uyeda K, Towle HC, Wilkie TM (Apr 2011). "Regulator of G protein signaling (RGS16) inhibits hepatic fatty acid oxidation in a carbohydrate response element-binding protein (ChREBP)-dependent manner". The Journal of Biological Chemistry. 286 (17): 15116–25. doi:10.1074/jbc.M110.216234. PMC 3083217. PMID 21357625.
Popov S, Yu K, Kozasa T, Wilkie TM (Jul 1997). "The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro". Proceedings of the National Academy of Sciences of the United States of America. 94 (14): 7216–20. Bibcode:1997PNAS...94.7216P. doi:10.1073/pnas.94.14.7216. PMC 23796. PMID 9207071.
Popov SG, Krishna UM, Falck JR, Wilkie TM (Jun 2000). "Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity". The Journal of Biological Chemistry. 275 (25): 18962–8. doi:10.1074/jbc.M001128200. PMID 10747990.
Zheng B, Chen D, Farquhar MG (Apr 2000). "MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16". Proceedings of the National Academy of Sciences of the United States of America. 97 (8): 3999–4004. Bibcode:2000PNAS...97.3999Z. doi:10.1073/pnas.97.8.3999. PMC 18131. PMID 10760272.
Chatterjee TK, Fisher RA (Aug 2000). "Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs". The Journal of Biological Chemistry. 275 (31): 24013–21. doi:10.1074/jbc.M002082200. PMID 10791963.
Wieland T, Bahtijari N, Zhou XB, Kleuss C, Simon MI (Sep 2000). "Polarity exchange at the interface of regulators of G protein signaling with G protein alpha-subunits". The Journal of Biological Chemistry. 275 (37): 28500–6. doi:10.1074/jbc.M004187200. PMID 10878019.
Chen C, Wang H, Fong CW, Lin SC (Aug 2001). "Multiple phosphorylation sites in RGS16 differentially modulate its GAP activity". FEBS Letters. 504 (1–2): 16–22. doi:10.1016/S0014-5793(01)02757-0. PMID 11522288.
Derrien A, Druey KM (Dec 2001). "RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation". The Journal of Biological Chemistry. 276 (51): 48532–8. doi:10.1074/jbc.M108862200. PMID 11602604.
Derrien A, Zheng B, Osterhout JL, Ma YC, Milligan G, Farquhar MG, Druey KM (May 2003). "Src-mediated RGS16 tyrosine phosphorylation promotes RGS16 stability". The Journal of Biological Chemistry. 278 (18): 16107–16. doi:10.1074/jbc.M210371200. PMID 12588871.
Osterhout JL, Waheed AA, Hiol A, Ward RJ, Davey PC, Nini L, Wang J, Milligan G, Jones TL, Druey KM (May 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". The Journal of Biological Chemistry. 278 (21): 19309–16. doi:10.1074/jbc.M210124200. PMID 12642592.
Hiol A, Davey PC, Osterhout JL, Waheed AA, Fischer ER, Chen CK, Milligan G, Druey KM, Jones TL (May 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". The Journal of Biological Chemistry. 278 (21): 19301–8. doi:10.1074/jbc.M210123200. PMID 12642593.
Johnson EN, Seasholtz TM, Waheed AA, Kreutz B, Suzuki N, Kozasa T, Jones TL, Brown JH, Druey KM (Dec 2003). "RGS16 inhibits signalling through the G alpha 13-Rho axis". Nature Cell Biology. 5 (12): 1095–103. doi:10.1038/ncb1065. PMID 14634662. S2CID 6798899.
Ross EM, Wilkie TM (2000). "GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins". Annual Review of Biochemistry. 69: 795–827. doi:10.1146/annurev.biochem.69.1.795. PMID 10966476. S2CID 11637673.
Sierra DA, Gilbert DJ, Householder D, Grishin NV, Yu K, Ukidwe P, Barker SA, He W, Wensel TG, Otero G, Brown G, Copeland NG, Jenkins NA, Wilkie TM (Feb 2002). "Evolution of the regulators of G-protein signaling multigene family in mouse and human". Genomics. 79 (2): 177–85. doi:10.1006/geno.2002.6693. PMID 11829488. S2CID 16065132.
Villasenor A, Wang ZV, Rivera LB, Ocal O, Asterholm IW, Scherer PE, Brekken RA, Cleaver O, Wilkie TM (2010). "Rgs16 and Rgs8 in embryonic endocrine pancreas and mouse models of diabetes". Disease Models & Mechanisms. 3 (9–10): 567–80. doi:10.1242/dmm.003210. PMC 2931535. PMID 20616094.
Wilkie TM, Kinch L (Oct 2005). "New roles for Galpha and RGS proteins: communication continues despite pulling sisters apart". Current Biology. 15 (20): R843-54. doi:10.1016/j.cub.2005.10.008. PMID 16243026. S2CID 18174795.

v t e PDB gallery
2ik8: Crystal structure of the heterodimeric complex of human RGS16 and activated Gi alpha 1

Function

Interactions

References

Further reading