RGS19

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Regulator of G-protein signaling 19

PDB rendering based on 1cmz.

Available structures

PDB

Ortholog search: PDBe, RCSB

List of PDB id codes
1CMZ

Identifiers

Symbols

RGS19; GAIP; RGSGAIP

External IDs

OMIM: 605071 MGI: 1915153 HomoloGene: 23320 GeneCards: RGS19 Gene

Gene Ontology
Molecular function	• G-protein alpha-subunit binding • GTPase activator activity • protein binding
Cellular component	• cytoplasm • Golgi apparatus • heterotrimeric G-protein complex • plasma membrane • brush border • membrane • clathrin-coated vesicle • cytosolic part
Biological process	• autophagy • G-protein coupled receptor signaling pathway • small GTPase mediated signal transduction • termination of G-protein coupled receptor signaling pathway • positive regulation of GTPase activity
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 20:
62.7 – 62.71 Mb

Chr 2:
181.69 – 181.69 Mb

PubMed search

[1]

[2]

Regulator of G-protein signaling 19 is a protein that in humans is encoded by the RGS19 gene.^[1]^[2]

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.^[2]

1 Interactions
2 References
3 Further reading
4 External links

Interactions

RGS19 has been shown to interact with GNAO1,^[3]^[4] GIPC1,^[5] OSTM1,^[6] GNAI1,^[3]^[4] GNAI3^[1]^[3]^[4] and GNAZ.^[3]^[7]

References

^ ^a ^b De Vries L, Mousli M, Wurmser A, Farquhar MG (January 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. doi:10.1073/pnas.92.25.11916. PMC 40514. PMID 8524874.
^ ^a ^b "Entrez Gene: RGS19 regulator of G-protein signalling 19".
^ ^a ^b ^c ^d De Vries, L; Elenko E, Hubler L, Jones T L, Farquhar M G (Dec. 1996). "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. (UNITED STATES) 93 (26): 15203–8. doi:10.1073/pnas.93.26.15203. ISSN 0027-8424. PMC 26381. PMID 8986788.
^ ^a ^b ^c Woulfe, D S; Stadel J M (June 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. (UNITED STATES) 274 (25): 17718–24. doi:10.1074/jbc.274.25.17718. ISSN 0021-9258. PMID 10364213.
^ Lou, X; Yano H, Lee F, Chao M V, Farquhar M G (March 2001). "GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways". Mol. Biol. Cell (United States) 12 (3): 615–27. ISSN 1059-1524. PMC 30968. PMID 11251075.
^ Fischer, Thierry; De Vries Luc, Meerloo Timo, Farquhar Marilyn Gist (July 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. (United States) 100 (14): 8270–5. doi:10.1073/pnas.1432965100. ISSN 0027-8424. PMC 166218. PMID 12826607.
^ Fan, X; Brass L F, Poncz M, Spitz F, Maire P, Manning D R (October 2000). "The alpha subunits of Gz and Gi interact with the eyes absent transcription cofactor Eya2, preventing its interaction with the six class of homeodomain-containing proteins". J. Biol. Chem. (UNITED STATES) 275 (41): 32129–34. doi:10.1074/jbc.M004577200. ISSN 0021-9258. PMID 10906137.

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. doi:10.1073/pnas.93.26.15203. PMC 26381. 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. doi:10.1074/jbc.272.39.24599. 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. PMC 25334. 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. doi:10.1074/jbc.273.40.26014. 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. doi:10.1073/pnas.95.21.12340. PMC 22833. 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. doi:10.1073/pnas.96.12.6722. PMC 21982. 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. doi:10.1074/jbc.274.25.17718. 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. doi:10.1073/pnas.97.8.3999. PMC 18131. 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. doi:10.1073/pnas.97.8.4040. PMC 18141. 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. PMC 30968. 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. PMC 139241. 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. doi:10.1016/S0022-2836(02)01283-4. 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. PMC 166218. PMID 12826607.

External links

RGS19 human gene location in the UCSC Genome Browser.
RGS19 human gene details in the UCSC Genome Browser.

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RGS19

Contents

Interactions

References

Further reading

External links