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FLASH GENE
Symbol TRIOBP contributors: mct - updated : 08-09-2010
HGNC name TRIO and F-actin binding protein
HGNC id 17009
DNA
TYPE functioning gene
STRUCTURE 79.69 kb     23 Exon(s)
MAPPING cloned Y linked N status provisional
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
23 splicing 4753 72 652 ubiquitous Seipel, Yu (2008), Kitajiri (2010)
  • TARA
  • Exon 11 includes the 5prime UTR and translation start codon
  • - splicing 1743 - 431 - Seipel, Yu (2008)
    utilizing an alternate 3'-terminal exon
    24 - 10159 261.4 2367 only expressed in fetal brain, retina, and cochlea Shahin, Yu (2008)
    TRIOBP6, responsible of DFNB28
    11 - - 107 - expressed predominantly in the eye and inner ear Kitajiri (2010)
  • organizes actin filaments into uniquely dense bundles reminiscent of rootlets but distinct from bundles formed by espin, an actin crosslinker in stereocilia
  • has a translation stop codon and 3prime untranslated region (UTR) in exon 6
  • 24 - - 218 - expressed predominantly in the eye and inner ear Kitajiri (2010)
    EXPRESSION
    Type widely
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    blood / hematopoieticspleen   highly
    Cardiovascularheart   highly
    Digestiveliver   highly
    Endocrinepancreas   highly
    Hearing/Equilibriumearinnercochlea  
    Nervousbrain    
    Reproductivemale systemprostate  highly
    Respiratorylung   highly
    Urinarykidney   highly
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Epithelialsecretoryglandularendocrine 
    Epithelialsecretoryglandularexocrine 
    Lymphoid    
    Muscularstriatumskeletal  
    cells
    SystemCellPubmedSpeciesStageRna symbol
    Hearing / Equilibriumstereocilia
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    physiological period pregnancy
    Text placenta highly
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • a pleckstrin homology (PH) domain
  • a coiled-coil region (at least two actin-binding sites per coiled-coil dimer)
  • HOMOLOGY
    interspecies ortholog to murine Triobp
    Homologene
    FAMILY
    CATEGORY regulatory
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,cytoskeleton,microfilament
    text
  • localized to F-actin in a periodic pattern
  • cytoskeleton-associated protein localized to rootlets (Kitajiri 2010)
  • basic FUNCTION
  • regulating actin cytoskeletal organisation, cell spreading and cell contraction by directly binding
  • stabilizing filamentous (F)-actin
  • involved in many important fundamental cellular processes, ranging from actin remodeling, directed cell movement, to cell cycle regulation
  • serving as a linker protein to recruit proteins required for F-actin formation and turnover
  • may be involved in mitotic regulation through interacting with TRF1
  • actin-bundling protein that is critical for rootlet formation (Kitajiri 2010)
  • implication in the bundling of actin filaments that is essential for the biogenesis of rootlets providing durable flexibility at the taper and mechanical rigidity to the stereocilia bundle (Kitajiri 2010)
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • binding to F-actin, TRIO and myosin II
  • interacting partner of guanine nucleotide exchange factor Trio and TRF1 (TRF1 interacting protein)
  • interacting with HECTD3 (HECTD3 may facilitate cell cycle progression via regulating ubiquitination and degradation of TRIOBP) (Yu 2008)
  • purified TRIOBP interacted with TERF1, suggesting that the purified protein is functional and biologically active (Li 2007)
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s) DFNB28
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS