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FLASH GENE
Symbol TRAP1 contributors: mct - updated : 26-01-2022
HGNC name TNF receptor-associated protein 1
HGNC id 16264
Location 16p13.3      Physical location : 3.708.038 - 3.767.598
Synonym name
  • tumor necrosis factor type 1, receptor associated protein
  • heat shock protein 75
  • Synonym symbol(s) HSP75, HSP90L, HSP 75, TRAP-1
    DNA
    TYPE functioning gene
    STRUCTURE 59.49 kb     18 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    MAPPING cloned Y linked N status provisional
    Map pter - D16S521 - MPG - HAGH - RPL3 - D16S3024 - CLCN7 - UBE2I - ZNF174 - D16S3070 - ABCA3 - CD63 - TSC2 TSC2 - D16S510 - cen
    Authors Gene Map (98)
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    17 - 2064 - 651 - 2005 16269234
    15 - 2248 62 547 testis 2005 16269234
    15 exons
    19 - 2189 76 669 trachea 2005 16269234
    19 exons
    13 - 2309 54 469 - 2005 16269234
    13 exons
    18 - 2265 76 672 brain 2005 16269234
    18 exons
    18 - 2208 76 672 placenta 2005 16269234
    18 exons
    18 - 2310 79 704 - 2005 16269234
    EXPRESSION
    Type ubiquitous
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularheart    
    Digestiveliver    
     mouthtongue  highly
    Endocrinepancreas    
    Nervousbrain    
    Reproductivefemale systemuteruscervix highly
     female systemplacenta   
    Respiratorylung    
    Urinarykidney    
    Visualeye   highly
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Muscularstriatumskeletal  
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    physiological period pregnancy
    Text amnion cells
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
    mitochondrial localization sequence in the N terminus
    conjugated PhosphoP
    HOMOLOGY
    interspecies homolog to murine Trap1 (88.5pc)
    homolog to rattus Trap1 (88.5pc)
    Homologene
    FAMILY heat shock protein 90 (HSP90) chaperone family
    CATEGORY chaperone/stress
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,mitochondria,inner
    intracellular,cytoplasm,organelle,mitochondria,interspace
    intracellular,cytoplasm,organelle,mitochondria,matrix
    intracellular,cytoplasm,organelle,membrane
    intracellular,nucleus,nucleoplasm
    basic FUNCTION
  • exhibiting ATPase activity
  • might play a role in protecting mitochondria against damaging stimuli via decrease of reactive oxygen species generation
  • protecting cells from oxidative stress and apoptosis
  • mitochondrial survival factor differentially expressed in localized and metastatic prostate cancer compared with normal prostate
  • acts as a molecular chaperone to retinoblastoma protein (Rb) during cellular stress
  • controls cell cycle activity through the tumor necrosis factor pathways
  • mitochondrial chaperone with antioxidant and antiapoptotic functions, involved in multidrug resistance in colorectal carcinoma cells
  • likely reduces the hypertrophy and fibrosis induced by pressure overload through blocking TAK/P38, JNK, and AKT signaling pathways
  • is involved in the translational control of cancer cells through an attenuation of global protein synthesis
  • controls cell migration of cancer cells in metabolic stress conditions
  • TRAP1 is relevant in the control of the complex machinery that governs cell cycle progression and mitotic entry
  • molecular chaperone involved in the regulation of energetic metabolism in cancer cells
  • role of TRAP1 is to enhance or suppress oxidative phosphorylation
  • potential TRAP1 role in triggering the alternate energy metabolism in cancer cells
  • TRAP1 role in tumor metastasis, which is in addition to altered energy metabolism
  • it is involved in the assembly of the electron transport chain, and it favours the switch from oxidative phosphorylation to glycolysis
  • supports protein folding and contributes to the maintenance of mitochondrial integrity even under cellular stress
  • cellular regulator of mitochondrial bioenergetics, redox homeostasis, oxidative stress-induced cell death, apoptosis, and unfolded protein response (UPR) in the endoplasmic reticulum (ER)
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule nucleotide,
  • ATP binding
  • protein
  • binding to the intracellular domain of tumor necrosis factor type 1 receptor
  • binding to RB1
  • interacting with cyclophilin D and negatively regulating mitochondrial cell death
  • Sorcin (SI) is a new TRAP1 interactor
  • a functional role of TRAP1 in maintaining mitochondrial integrity downstream of PINK1 and complex I deficits but parallel to or upstream of Parkin
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --over  
    prevented cardiac hypertrophy and fibrosis
    tumoral     --over  
    in several cancers, such as glioblastoma, colon, breast, prostate and lung cancers, often associated with drug resistance
    tumoral     --low  
    in specific tumors, such as ovarian, bladder and renal cancers, correlated with the worst prognoses and chemoresistance
    constitutional germinal mutation      
    autoinflammatory disease might be enhanced by bi-allelic mutations
    Susceptibility
    Variant & Polymorphism
    Candidate gene
  • potential of TRAP1 inhibitors as neuroprotective drugs
  • Marker
    Therapy target
    SystemTypeDisorderPubmed
    cancerreproductiveprostate
    targeting the TRAP1 pathway with Gamitrinibs could be explored as novel molecular therapy in patients with advanced prostate cancer
    cancer  
    targeting TRAP1 constitutes likely a new antitumor approach
    cancerendocrinethyroid
    TRAP1 inhibition may be regarded as potential strategy to target specific features of thyroid carcinoma (TC), cell proliferation and resistance to apoptosis
    ANIMAL & CELL MODELS