RGS19

From Wikipedia, the free encyclopedia

Regulator of G-protein signalling 19

PDB rendering based on 1cmz.

Available structures: 1cmz

Identifiers

Symbol(s)

RGS19; GAIP; RGSGAIP

External IDs

OMIM: 605071 MGI: 1915153 HomoloGene: 23320

Gene ontology
Molecular Function:	• signal transducer activity • GTPase activator activity • protein binding
Cellular Component:	• membrane fraction • Golgi apparatus • heterotrimeric G-protein complex • membrane
Biological Process:	• autophagy • G-protein coupled receptor protein signaling pathway • small GTPase mediated signal transduction • negative regulation of signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001039467 (mRNA)
NP_001034556 (protein)

XM_990290 (mRNA)
XP_995384 (protein)

Location

Chr 20: 62.17 - 62.18 Mb

Chr 2: 181.62 - 181.62 Mb

Pubmed search

[1]

[2]

Regulator of G-protein signalling 19, also known as RGS19, is a human gene.^[1]

G proteins mediate a number of cellular processes. The protein encoded by this gene belongs to the RGS (regulators of G-protein signaling) family and specifically interacts with G protein, GAI3. This protein is a guanosine triphosphatase-activating protein that functions to down-regulate Galpha i/Galpha q-linked signaling.^[1]

[edit] References

^ ^a ^b Entrez Gene: RGS19 regulator of G-protein signalling 19.

[edit] Further reading

De Vries L, Mousli M, Wurmser A, Farquhar MG (1996). "GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain.". Proc. Natl. Acad. Sci. U.S.A. 92 (25): 11916–20. PMID 8524874.
De Vries L, Elenko E, Hubler L, et al. (1997). "GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits.". Proc. Natl. Acad. Sci. U.S.A. 93 (26): 15203–8. PMID 8986788.
Ogier-Denis E, Petiot A, Bauvy C, Codogno P (1997). "Control of the expression and activity of the Galpha-interacting protein (GAIP) in human intestinal cells.". J. Biol. Chem. 272 (39): 24599–603. PMID 9305927.
De Vries L, Elenko E, McCaffery JM, et al. (1998). "RGS-GAIP, a GTPase-activating protein for Galphai heterotrimeric G proteins, is located on clathrin-coated vesicles.". Mol. Biol. Cell 9 (5): 1123–34. PMID 9571244.
Wang J, Ducret A, Tu Y, et al. (1998). "RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane association, regulation by Galphaz phosphorylation, and relationship to a Gz gtpase-activating protein subfamily.". J. Biol. Chem. 273 (40): 26014–25. PMID 9748280.
De Vries L, Lou X, Zhao G, et al. (1998). "GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP.". Proc. Natl. Acad. Sci. U.S.A. 95 (21): 12340–5. PMID 9770488.
Fischer T, Elenko E, McCaffery JM, et al. (1999). "Clathrin-coated vesicles bearing GAIP possess GTPase-activating protein activity in vitro.". Proc. Natl. Acad. Sci. U.S.A. 96 (12): 6722–7. PMID 10359779.
Woulfe DS, Stadel JM (1999). "Structural basis for the selectivity of the RGS protein, GAIP, for Galphai family members. Identification of a single amino acid determinant for selective interaction of Galphai subunits with GAIP.". J. Biol. Chem. 274 (25): 17718–24. PMID 10364213.
de Alba E, De Vries L, Farquhar MG, Tjandra N (1999). "Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling.". J. Mol. Biol. 291 (4): 927–39. doi:10.1006/jmbi.1999.2989. PMID 10452897.
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.
Fischer T, Elenko E, Wan L, et al. (2000). "Membrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesicles.". Proc. Natl. Acad. Sci. U.S.A. 97 (8): 4040–5. PMID 10760275.
Ogier-Denis E, Pattingre S, El Benna J, Codogno P (2001). "Erk1/2-dependent phosphorylation of Galpha-interacting protein stimulates its GTPase accelerating activity and autophagy in human colon cancer cells.". J. Biol. Chem. 275 (50): 39090–5. doi:10.1074/jbc.M006198200. PMID 10993892.
Ito E, Xie G, Maruyama K, Palmer PP (2000). "A core-promoter region functions bi-directionally for human opioid-receptor-like gene ORL1 and its 5'-adjacent gene GAIP.". J. Mol. Biol. 304 (3): 259–70. doi:10.1006/jmbi.2000.4212. PMID 11090272.
Lou X, Yano H, Lee F, et al. (2001). "GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways.". Mol. Biol. Cell 12 (3): 615–27. PMID 11251075.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
Sierra DA, Gilbert DJ, Householder D, et al. (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.
Kirikoshi H, Katoh M (2002). "Expression of human GIPC1 in normal tissues, cancer cell lines, and primary tumors.". Int. J. Mol. Med. 9 (5): 509–13. PMID 11956658.
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.
Xie GX, Han X, Ito E, et al. (2003). "Gene structure, dual-promoters and mRNA alternative splicing of the human and mouse regulator of G protein signaling GAIP/RGS19.". J. Mol. Biol. 325 (4): 721–32. PMID 12507475.
Fischer T, De Vries L, Meerloo T, Farquhar MG (2003). "Promotion of G alpha i3 subunit down-regulation by GIPN, a putative E3 ubiquitin ligase that interacts with RGS-GAIP.". Proc. Natl. Acad. Sci. U.S.A. 100 (14): 8270–5. doi:10.1073/pnas.1432965100. PMID 12826607.