TRIO (gene): Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Triple functional domain protein''' is a [[protein]] that in humans is encoded by the ''TRIO'' [[gene]].<ref name="pmid8643598">{{cite journal | vauthors = Debant A, Serra-Pagès C, Seipel K, O'Brien S, Tang M, Park SH, Streuli M | title = 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 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 11 | pages = 5466–71 | date = May 1996 | pmid = 8643598 | pmc = 39269 | doi = 10.1073/pnas.93.11.5466 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TRIO triple functional domain (PTPRF interacting)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7204| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image = PBB_Protein_TRIO_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nty.
| PDB = {{PDB2|1nty}}, {{PDB2|2nz8}}
| Name = Triple functional domain (PTPRF interacting)
| HGNCid = 12303
| Symbol = TRIO
| AltSymbols =; tgat
| OMIM = 601893
| ECnumber = 
| Homologene = 20847
| MGIid = 1927230
| GeneAtlas_image1 = PBB_GE_TRIO_209012_at_tn.png
| GeneAtlas_image2 = PBB_GE_TRIO_208178_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_TRIO_209010_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005085 |text = guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005089 |text = Rho guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007185 |text = transmembrane receptor protein tyrosine phosphatase signaling pathway}} {{GNF_GO|id=GO:0035023 |text = regulation of Rho protein signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7204
    | Hs_Ensembl = ENSG00000038382
    | Hs_RefseqProtein = NP_009049
    | Hs_RefseqmRNA = NM_007118
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 14196829
    | Hs_GenLoc_end = 14563312
    | Hs_Uniprot = O75962
    | Mm_EntrezGene = 223435
    | Mm_Ensembl = ENSMUSG00000022263
    | Mm_RefseqmRNA = XM_888341
    | Mm_RefseqProtein = XP_893434
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 15
    | Mm_GenLoc_start = 27677210
    | Mm_GenLoc_end = 27863884
    | Mm_Uniprot = 
  }}
}}
'''Triple functional domain (PTPRF interacting)''', also known as '''TRIO''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TRIO triple functional domain (PTPRF interacting)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7204| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
TRIO (gene) has been shown to [[Protein-protein interaction|interact]] with [[Filamin]]<ref name=pmid11146652>{{cite journal | vauthors = Bellanger JM, Astier C, Sardet C, Ohta Y, Stossel TP, Debant A | title = The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin | journal = Nature Cell Biology | volume = 2 | issue = 12 | pages = 888–92 | date = Dec 2000 | pmid = 11146652 | doi = 10.1038/35046533 }}</ref> and [[RHOA]].<ref name=pmid10948190>{{cite journal | vauthors = Medley QG, Serra-Pagès C, Iannotti E, Seipel K, Tang M, O'Brien SP, Streuli M | title = The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain | journal = The Journal of Biological Chemistry | volume = 275 | issue = 46 | pages = 36116–23 | date = Nov 2000 | pmid = 10948190 | doi = 10.1074/jbc.M003775200 }}</ref>
{{PBB_Summary
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| summary_text =  
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Taviaux S, Diriong S, Bellanger JM, Streuli M, Debant A | title = Assignment of TRIO, the Trio gene (PTPRF interacting) to human chromosome bands 5p 15.1-->p 14 by in situ hybridization | journal = Cytogenetics and Cell Genetics | volume = 76 | issue = 1-2 | pages = 107–8 | year = 1997 | pmid = 9154137 | doi = 10.1159/000134524 }}
| citations =
* {{cite journal | vauthors = Liu X, Wang H, Eberstadt M, Schnuchel A, Olejniczak ET, Meadows RP, Schkeryantz JM, Janowick DA, Harlan JE, Harris EA, Staunton DE, Fesik SW | title = NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio | journal = Cell | volume = 95 | issue = 2 | pages = 269–77 | date = Oct 1998 | pmid = 9790533 | doi = 10.1016/S0092-8674(00)81757-2 }}
*{{cite journal | author=Debant A, Serra-Pagès C, Seipel K, ''et al.'' |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 11 |pages= 5466-71 |year= 1996 |pmid= 8643598 |doi=  }}
* {{cite journal | vauthors = Seipel K, Medley QG, Kedersha NL, Zhang XA, O'Brien SP, Serra-Pages C, Hemler ME, Streuli M | title = Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth | journal = Journal of Cell Science | volume = 112 ( Pt 12) | issue = 12 | pages = 1825–34 | date = Jun 1999 | pmid = 10341202 | doi =  }}
*{{cite journal  | author=Taviaux S, Diriong S, Bellanger JM, ''et al.'' |title=Assignment of TRIO, the Trio gene (PTPRF interacting) to human chromosome bands 5p 15.1-->p 14 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=76 |issue= 1-2 |pages= 107-8 |year= 1997 |pmid= 9154137 |doi= }}
* {{cite journal | vauthors = Medley QG, Serra-Pagès C, Iannotti E, Seipel K, Tang M, O'Brien SP, Streuli M | title = The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain | journal = The Journal of Biological Chemistry | volume = 275 | issue = 46 | pages = 36116–23 | date = Nov 2000 | pmid = 10948190 | doi = 10.1074/jbc.M003775200 }}
*{{cite journal | author=Liu X, Wang H, Eberstadt M, ''et al.'' |title=NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio. |journal=Cell |volume=95 |issue= 2 |pages= 269-77 |year= 1998 |pmid= 9790533 |doi= }}
* {{cite journal | vauthors = Bellanger JM, Astier C, Sardet C, Ohta Y, Stossel TP, Debant A | title = The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin | journal = Nature Cell Biology | volume = 2 | issue = 12 | pages = 888–92 | date = Dec 2000 | pmid = 11146652 | doi = 10.1038/35046533 }}
*{{cite journal | author=Seipel K, Medley QG, Kedersha NL, ''et al.'' |title=Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth. |journal=J. Cell. Sci. |volume=112 ( Pt 12) |issue= |pages= 1825-34 |year= 1999 |pmid= 10341202 |doi=  }}
* {{cite journal | vauthors = Gao Y, Xing J, Streuli M, Leto TL, Zheng Y | title = Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors | journal = The Journal of Biological Chemistry | volume = 276 | issue = 50 | pages = 47530–41 | date = Dec 2001 | pmid = 11595749 | doi = 10.1074/jbc.M108865200 }}
*{{cite journal | author=Medley QG, Serra-Pagès C, Iannotti E, ''et al.'' |title=The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36116-23 |year= 2000 |pmid= 10948190 |doi= 10.1074/jbc.M003775200 }}
* {{cite journal | vauthors = Skowronek KR, Guo F, Zheng Y, Nassar N | title = The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids | journal = The Journal of Biological Chemistry | volume = 279 | issue = 36 | pages = 37895–907 | date = Sep 2004 | pmid = 15199069 | doi = 10.1074/jbc.M312677200 }}
*{{cite journal | author=Bellanger JM, Astier C, Sardet C, ''et al.'' |title=The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin. |journal=Nat. Cell Biol. |volume=2 |issue= 12 |pages= 888-92 |year= 2001 |pmid= 11146652 |doi= 10.1038/35046533 }}
* {{cite journal | vauthors = Zheng M, Simon R, Mirlacher M, Maurer R, Gasser T, Forster T, Diener PA, Mihatsch MJ, Sauter G, Schraml P | title = TRIO amplification and abundant mRNA expression is associated with invasive tumor growth and rapid tumor cell proliferation in urinary bladder cancer | journal = The American Journal of Pathology | volume = 165 | issue = 1 | pages = 63–9 | date = Jul 2004 | pmid = 15215162 | pmc = 1618551 | doi = 10.1016/S0002-9440(10)63275-0 }}
*{{cite journal | author=Gao Y, Xing J, Streuli M, ''et al.'' |title=Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors. |journal=J. Biol. Chem. |volume=276 |issue= 50 |pages= 47530-41 |year= 2002 |pmid= 11595749 |doi= 10.1074/jbc.M108865200 }}
* {{cite journal | vauthors = Yoshizuka N, Moriuchi R, Mori T, Yamada K, Hasegawa S, Maeda T, Shimada T, Yamada Y, Kamihira S, Tomonaga M, Katamine S | title = An alternative transcript derived from the trio locus encodes a guanosine nucleotide exchange factor with mouse cell-transforming potential | journal = The Journal of Biological Chemistry | volume = 279 | issue = 42 | pages = 43998–4004 | date = Oct 2004 | pmid = 15308664 | doi = 10.1074/jbc.M406082200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Portales-Casamar E, Briançon-Marjollet A, Fromont S, Triboulet R, Debant A | title = Identification of novel neuronal isoforms of the Rho-GEF Trio | journal = Biology of the Cell / Under the Auspices of the European Cell Biology Organization | volume = 98 | issue = 3 | pages = 183–93 | date = Mar 2006 | pmid = 16033331 | doi = 10.1042/BC20050009 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{cite journal | vauthors = Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R | title = Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry | journal = Nature Methods | volume = 2 | issue = 8 | pages = 591–8 | date = Aug 2005 | pmid = 16094384 | doi = 10.1038/nmeth776 }}
*{{cite journal  | author=Skowronek KR, Guo F, Zheng Y, Nassar N |title=The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids. |journal=J. Biol. Chem. |volume=279 |issue= 36 |pages= 37895-907 |year= 2004 |pmid= 15199069 |doi= 10.1074/jbc.M312677200 }}
* {{cite journal | vauthors = Adamowicz M, Radlwimmer B, Rieker RJ, Mertens D, Schwarzbach M, Schraml P, Benner A, Lichter P, Mechtersheimer G, Joos S | title = Frequent amplifications and abundant expression of TRIO, NKD2, and IRX2 in soft tissue sarcomas | journal = Genes, Chromosomes & Cancer | volume = 45 | issue = 9 | pages = 829–38 | date = Sep 2006 | pmid = 16752383 | doi = 10.1002/gcc.20343 }}
*{{cite journal | author=Zheng M, Simon R, Mirlacher M, ''et al.'' |title=TRIO amplification and abundant mRNA expression is associated with invasive tumor growth and rapid tumor cell proliferation in urinary bladder cancer. |journal=Am. J. Pathol. |volume=165 |issue= 1 |pages= 63-9 |year= 2004 |pmid= 15215162 |doi= }}
* {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = Nov 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 }}
*{{cite journal | author=Yoshizuka N, Moriuchi R, Mori T, ''et al.'' |title=An alternative transcript derived from the trio locus encodes a guanosine nucleotide exchange factor with mouse cell-transforming potential. |journal=J. Biol. Chem. |volume=279 |issue= 42 |pages= 43998-4004 |year= 2004 |pmid= 15308664 |doi= 10.1074/jbc.M406082200 }}
* {{cite journal | vauthors = Chhatriwala MK, Betts L, Worthylake DK, Sondek J | title = The DH and PH domains of Trio coordinately engage Rho GTPases for their efficient activation | journal = Journal of Molecular Biology | volume = 368 | issue = 5 | pages = 1307–20 | date = May 2007 | pmid = 17391702 | pmc = 1890047 | doi = 10.1016/j.jmb.2007.02.060 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
* {{cite journal | vauthors = Rojas RJ, Yohe ME, Gershburg S, Kawano T, Kozasa T, Sondek J | title = Galphaq directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain | journal = The Journal of Biological Chemistry | volume = 282 | issue = 40 | pages = 29201–10 | date = Oct 2007 | pmid = 17606614 | pmc = 2655113 | doi = 10.1074/jbc.M703458200 }}
*{{cite journal  | author=Portales-Casamar E, Briançon-Marjollet A, Fromont S, ''et al.'' |title=Identification of novel neuronal isoforms of the Rho-GEF Trio. |journal=Biol. Cell |volume=98 |issue= 3 |pages= 183-93 |year= 2006 |pmid= 16033331 |doi= 10.1042/BC20050009 }}
*{{cite journal | author=Tao WA, Wollscheid B, O'Brien R, ''et al.'' |title=Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. |journal=Nat. Methods |volume=2 |issue= 8 |pages= 591-8 |year= 2005 |pmid= 16094384 |doi= 10.1038/nmeth776 }}
*{{cite journal | author=Adamowicz M, Radlwimmer B, Rieker RJ, ''et al.'' |title=Frequent amplifications and abundant expression of TRIO, NKD2, and IRX2 in soft tissue sarcomas. |journal=Genes Chromosomes Cancer |volume=45 |issue= 9 |pages= 829-38 |year= 2006 |pmid= 16752383 |doi= 10.1002/gcc.20343 }}
*{{cite journal | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
*{{cite journal | author=Chhatriwala MK, Betts L, Worthylake DK, Sondek J |title=The DH and PH domains of Trio coordinately engage Rho GTPases for their efficient activation. |journal=J. Mol. Biol. |volume=368 |issue= 5 |pages= 1307-20 |year= 2007 |pmid= 17391702 |doi= 10.1016/j.jmb.2007.02.060 }}
*{{cite journal | author=Rojas RJ, Yohe ME, Gershburg S, ''et al.'' |title=Galphaq directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain. |journal=J. Biol. Chem. |volume=282 |issue= 40 |pages= 29201-10 |year= 2007 |pmid= 17606614 |doi= 10.1074/jbc.M703458200 }}
}}
{{refend}}
{{refend}}


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[[Category:EC 2.7.11]]

Latest revision as of 02:12, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Triple functional domain protein is a protein that in humans is encoded by the TRIO gene.[1][2]

Interactions

TRIO (gene) has been shown to interact with Filamin[3] and RHOA.[4]

References

  1. Debant A, Serra-Pagès C, Seipel K, O'Brien S, Tang M, Park SH, Streuli M (May 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". Proceedings of the National Academy of Sciences of the United States of America. 93 (11): 5466–71. doi:10.1073/pnas.93.11.5466. PMC 39269. PMID 8643598.
  2. "Entrez Gene: TRIO triple functional domain (PTPRF interacting)".
  3. Bellanger JM, Astier C, Sardet C, Ohta Y, Stossel TP, Debant A (Dec 2000). "The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin". Nature Cell Biology. 2 (12): 888–92. doi:10.1038/35046533. PMID 11146652.
  4. Medley QG, Serra-Pagès C, Iannotti E, Seipel K, Tang M, O'Brien SP, Streuli M (Nov 2000). "The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain". The Journal of Biological Chemistry. 275 (46): 36116–23. doi:10.1074/jbc.M003775200. PMID 10948190.

Further reading