TRIO

  • Official Full Name

    TrioB6
  • Overview

    Triple functional domain protein is a protein that in humans is encoded by the TRIO gene. TRIO (gene) has been shown to interact with Filamin and RHOA.
  • Synonyms

    trio;0368/10;0959/14;1372/03;1386/06;BEST:LD36950;CG18214;CG9208;Dmel\CG18214;DTrio;l(3)036810;l(3)6D104;l(3)S036810;l(3)S095914;l(3)S137203;l(3)S138606;l(3)S[1372/3];l(3)S[1386/06];l(3)trio;M89;UNC-73/Trio;CG18214 gene product from transcript CG18214-RA;CG18214-PA;CG18214-PB;CG18214-PC;CG18214-PD;CG18214-PE;CG18214-PF;trio-PA;trio-PB;trio-PC;trio-PD;trio-PE;trio-PF
Cat.# Product name Source (Host) Species Tag Protein Length Price
TRIO-17404M Recombinant Mouse TRIO Protein Mammalian Cells Mouse His
TRIO-9628M Recombinant Mouse TRIO Protein, His (Fc)-Avi-tagged HEK293 Mouse Avi&Fc&His
TRIO-9628M-B Recombinant Mouse TRIO Protein Pre-coupled Magnetic Beads HEK293 Mouse

    Involved Pathway

    TRIO involved in several pathways and played different roles in them. We selected most pathways TRIO participated on our site, such as Axon guidance,Cell death signalling via NRAGE, NRIF and NADE,DCC mediated attractive signaling, which may be useful for your reference. Also, other proteins which involved in the same pathway with TRIO were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Developmental Biology CLTB,ACTR2B,EFNA3B,GDF1,DPYSL4,CACNG2,CNTN6,MED22,MED23,DNM2
    DCC mediated attractive signaling DOCK1,NTN1B,NTN1A,DCC
    Cell death signalling via NRAGE, NRIF and NADE ITGB3BP,ARHGEF1A,CASP2,KALRN,KALRNB,ARHGEF18,DCLRE1B,FGD4A,ARHGAP4,ABR
    G alpha (q) signalling events GPR65,ANXA1,EDN1,OXTRL,GPRC6A,GPR132,MLN,CASR,GCGA,EDNRA
    G alpha (12/13) signalling events AKAP13,ARHGEF1A,KALRNB,ARHGEF9,FGD4A,FGD2,ARHGEF18,PLEKHG2,ARHGEF18A,TIAM2
    Axon guidance EFNA1,PLXNA1,RAC3,CDK5R1B,NETO2,PAK3,FRS2B,MARK3,NTN1A,ST8SIA2
    GPCR downstream signaling OPN4A,CCR6,EDNRAB,CALCRL,FGD4,OPN5,ARHGEF18A,CNR2,EDNRA,GPR132
    Gastrin-CREB signalling pathway via PKC and MAPK TAC3,TRPC6A,MGLL,GPR68,PROKR2,OPN4B,LPAR1,CASR,QRFP,UTS2

    Protein Function

    TRIO has several biochemical functions, for example, ATP binding,Rho guanyl-nucleotide exchange factor activity,enzyme binding. Some of the functions are cooperated with other proteins, some of the functions could acted by TRIO itself. We selected most functions TRIO had, and list some proteins which have the same functions with TRIO. You can find most of the proteins on our site.

    Function Related Protein
    protein serine/threonine kinase activity SNRKA,GSK3A,CAMK2G1,KALRN,IRAK4,ROCK2A,CHEK2,PAK4,RPS6KA2,TSSK1
    enzyme binding SPDL1,LDB1,HDAC1,NKX2-1,PRKCE,FOXO4,APBA3,MTA1,ZFHX3,UGT1A4
    Rho guanyl-nucleotide exchange factor activity FGD6,PREX1,FGD4,ARHGEF25,ARHGEF10,BCR,ITSN2,ARHGEF9,ARHGEF37,SOS1
    kinase activity KALRN,GM4922,MIBP,SPS2,BMPR1BA,INSRA,NEK1,HIPK2,MKNK2A,HYKK.2
    nucleotide binding SRPK1A,ABCG2D,MAP3K12,HNRNPL,SRSF9,RPS6KB1B,MAPK14B,HNRNPR,ENOX1,NCBP2
    ATP binding ALDH18A1,KIF3CB,PRPS2,PDK1,ACSL3,STK35L,UCK1,PIKFYVE,PMS2,UBE2S
    protein kinase activity GRK7A,RAF1A,NRBP1,MYO3A,BMPR1BB,PKN1,CAMK1DB,PDPK1B,STK35L,EEF2K
    transferase activity BST1,PDXKB,CKMT1,PFKMA,B3GNT9-PS,WBP7,ZDHHC23B,ZDHHC20A,SBK1,HECTD1
    guanyl-nucleotide exchange factor activity RASGEF1BA,ARHGEF1B,GDPGP1,TBXA2R,SH2D3A,RASGRP3,RALGDS,VAV2,DENND1C,TBC1D10A

    Interacting Protein

    TRIO has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with TRIO here. Most of them are supplied by our site. Hope this information will be useful for your research of TRIO.

    Resources

    References

    • Bradshaw, NJ; Bader, V; et al. Aggregation of the Protein TRIOBP-1 and Its Potential Relevance to Schizophrenia. PLOS ONE 9:-(2014).
    • Marie, A; Holzmuller, P; et al. Anopheles gambiae salivary protein expression modulated by wild Plasmodium falciparum infection: highlighting of new antigenic peptides as candidates of An. gambiae bites. PARASITES & VECTORS 7:-(2014).

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