TRIO (gene)

Triple functional domain (PTPRF interacting)
File:PBB Protein TRIO image.jpg PDB rendering based on 1nty.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1nty​, 2nz8​
Identifiers
Symbols	TRIO ; tgat
External IDs	Template:OMIM5 Template:MGI HomoloGene: 20847
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE TRIO 209012 at tn.png
File:PBB GE TRIO 208178 x at tn.png
File:PBB GE TRIO 209010 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

Triple functional domain (PTPRF interacting), also known as TRIO, is a human gene.

Further reading

• Debant A, Serra-Pagès C, Seipel K; et al. (1996). "The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains". Proc. Natl. Acad. Sci. U.S.A. 93 (11): 5466–71. PMID 8643598.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Taviaux S, Diriong S, Bellanger JM; et al. (1997). "Assignment of TRIO, the Trio gene (PTPRF interacting) to human chromosome bands 5p 15.1-->p 14 by in situ hybridization". Cytogenet. Cell Genet. 76 (1–2): 107–8. PMID 9154137.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Liu X, Wang H, Eberstadt M; et al. (1998). "NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio". Cell. 95 (2): 269–77. PMID 9790533.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Seipel K, Medley QG, Kedersha NL; et al. (1999). "Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth". J. Cell. Sci. 112 ( Pt 12): 1825–34. PMID 10341202.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Medley QG, Serra-Pagès C, Iannotti E; et al. (2000). "The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain". J. Biol. Chem. 275 (46): 36116–23. doi:10.1074/jbc.M003775200. PMID 10948190.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bellanger JM, Astier C, Sardet C; et al. (2001). "The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin". Nat. Cell Biol. 2 (12): 888–92. doi:10.1038/35046533. PMID 11146652.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gao Y, Xing J, Streuli M; et al. (2002). "Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors". J. Biol. Chem. 276 (50): 47530–41. doi:10.1074/jbc.M108865200. PMID 11595749.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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)
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Skowronek KR, Guo F, Zheng Y, Nassar N (2004). "The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids". J. Biol. Chem. 279 (36): 37895–907. doi:10.1074/jbc.M312677200. PMID 15199069.CS1 maint: Multiple names: authors list (link)
• Zheng M, Simon R, Mirlacher M; et al. (2004). "TRIO amplification and abundant mRNA expression is associated with invasive tumor growth and rapid tumor cell proliferation in urinary bladder cancer". Am. J. Pathol. 165 (1): 63–9. PMID 15215162.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yoshizuka N, Moriuchi R, Mori T; et al. (2004). "An alternative transcript derived from the trio locus encodes a guanosine nucleotide exchange factor with mouse cell-transforming potential". J. Biol. Chem. 279 (42): 43998–4004. doi:10.1074/jbc.M406082200. PMID 15308664.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Portales-Casamar E, Briançon-Marjollet A, Fromont S; et al. (2006). "Identification of novel neuronal isoforms of the Rho-GEF Trio". Biol. Cell. 98 (3): 183–93. doi:10.1042/BC20050009. PMID 16033331.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tao WA, Wollscheid B, O'Brien R; et al. (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nat. Methods. 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Adamowicz M, Radlwimmer B, Rieker RJ; et al. (2006). "Frequent amplifications and abundant expression of TRIO, NKD2, and IRX2 in soft tissue sarcomas". Genes Chromosomes Cancer. 45 (9): 829–38. doi:10.1002/gcc.20343. PMID 16752383.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chhatriwala MK, Betts L, Worthylake DK, Sondek J (2007). "The DH and PH domains of Trio coordinately engage Rho GTPases for their efficient activation". J. Mol. Biol. 368 (5): 1307–20. doi:10.1016/j.jmb.2007.02.060. PMID 17391702.CS1 maint: Multiple names: authors list (link)
• Rojas RJ, Yohe ME, Gershburg S; et al. (2007). "Galphaq directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain". J. Biol. Chem. 282 (40): 29201–10. doi:10.1074/jbc.M703458200. PMID 17606614.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)