RGS18

Regulator of G-protein signaling 18 is a protein that in humans is encoded by the RGS18 gene.[5][6]

RGS18
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2DLV, 2JM5, 2OWI
Identifiers
Aliases	RGS18, RGS13, regulator of G-protein signaling 18, regulator of G protein signaling 18
External IDs	OMIM: 607192 MGI: 1927498 HomoloGene: 11281 GeneCards: RGS18
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q31.2 Start 192,158,462 bp[1] End 192,185,815 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 F|1 62.99 cM Start 144,752,683 bp[2] End 144,775,435 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity • GO:0001948 protein binding • GTPase activity Cellular component • cytoplasm • cell membrane Biological process • G-protein coupled receptor signaling pathway • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity • negative regulation of signal transduction • regulation of G-protein coupled receptor protein signaling pathway Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	64407	64214
Ensembl	ENSG00000150681	ENSMUSG00000026357
UniProt	Q9NS28	Q99PG4
RefSeq (mRNA)	NM_130782	NM_022881
RefSeq (protein)	NP_570138	NP_075019
Location (UCSC)	Chr 1: 192.16 – 192.19 Mb	Chr 1: 144.75 – 144.78 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the regulator of G-protein signaling family. This protein contains a conserved 120 amino acid motif called the RGS domain. The protein attenuates the signaling activity of G-proteins by binding to activated, GTP-bound G alpha subunits and acting as a GTPase activating protein (GAP), increasing 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.[6]

Interactions

RGS18 has been shown to interact with GNAI3.[7][8]

References

1. GRCh38: Ensembl release 89: ENSG00000150681 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026357 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Park IK, Klug CA, Li K, Jerabek L, Li L, Nanamori M, Neubig RR, Hood L, Weissman IL, Clarke MF (Jan 2001). "Molecular cloning and characterization of a novel regulator of G-protein signaling from mouse hematopoietic stem cells". The Journal of Biological Chemistry. 276 (2): 915–23. doi:10.1074/jbc.M005947200. PMID 11042171.
6. "Entrez Gene: RGS18 regulator of G-protein signalling 18".
7. Yowe D, Weich N, Prabhudas M, Poisson L, Errada P, Kapeller R, Yu K, Faron L, Shen M, Cleary J, Wilkie TM, Gutierrez-Ramos C, Hodge MR (Oct 2001). "RGS18 is a myeloerythroid lineage-specific regulator of G-protein-signalling molecule highly expressed in megakaryocytes". The Biochemical Journal. 359 (Pt 1): 109–18. doi:10.1042/bj3590109. PMC 1222126. PMID 11563974.
8. Gagnon AW, Murray DL, Leadley RJ (Jul 2002). "Cloning and characterization of a novel regulator of G protein signalling in human platelets". Cellular Signalling. 14 (7): 595–606. doi:10.1016/S0898-6568(02)00012-8. PMID 11955952.

Further reading

• Nagata Y, Oda M, Nakata H, Shozaki Y, Kozasa T, Todokoro K (May 2001). "A novel regulator of G-protein signaling bearing GAP activity for Galphai and Galphaq in megakaryocytes". Blood. 97 (10): 3051–60. doi:10.1182/blood.V97.10.3051. PMID 11342430.
• Yowe D, Weich N, Prabhudas M, Poisson L, Errada P, Kapeller R, Yu K, Faron L, Shen M, Cleary J, Wilkie TM, Gutierrez-Ramos C, Hodge MR (Oct 2001). "RGS18 is a myeloerythroid lineage-specific regulator of G-protein-signalling molecule highly expressed in megakaryocytes". The Biochemical Journal. 359 (Pt 1): 109–18. doi:10.1042/bj3590109. PMC 1222126. PMID 11563974.
• 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.
• Gagnon AW, Murray DL, Leadley RJ (Jul 2002). "Cloning and characterization of a novel regulator of G protein signalling in human platelets". Cellular Signalling. 14 (7): 595–606. doi:10.1016/S0898-6568(02)00012-8. PMID 11955952.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
• Larminie C, Murdock P, Walhin JP, Duckworth M, Blumer KJ, Scheideler MA, Garnier M (Mar 2004). "Selective expression of regulators of G-protein signaling (RGS) in the human central nervous system". Brain Research. Molecular Brain Research. 122 (1): 24–34. doi:10.1016/j.molbrainres.2003.11.014. PMID 14992813.
• Aldenhoven J, Chen Y, Moran C (2006). "Assignment of UCK2, ATF3 and RGS18 from human chromosome 1 to porcine chromosomes 4, 9 and 10 with somatic and radiation hybrid panels". Cytogenetic and Genome Research. 112 (3–4): 341F. doi:10.1159/000089896. PMID 16484797.