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FLASH GENE
Symbol CASP10 contributors: mct - updated : 18-04-2015
HGNC name caspase 10, apoptosis-related cysteine protease
HGNC id 1500
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • two N terminal FADD-like DEATH effector domains
  • a conserved QACXG pentapeptide active site motif
  • mono polymer heteromer , dimer
    isoforms Precursor
    HOMOLOGY
    interspecies homolog to C.elegans Ced-3
    Homologene
    FAMILY peptidase C14 family
    CATEGORY enzyme
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,cytosolic
    text stored in the mitochondrial intermembrane space and released into cytosol after appropriate apoptotic stimuli
    basic FUNCTION
  • recruited to the CD99 and p55 tumor necrosis factor receptor signaling complexes and promoting CD95 (APO1/Fas) apoptosis
  • CASP8 and CASP10 may be involved in the pathogenesis of rectal cancer
  • involved in the extrinsic death receptor pathway
  • prodeath role for both cleaved and uncleaved CASP10
  • may play a critical role in PTK7-knockdown-induced apoptosis, downstream of mitochondria
  • concerted endoproteolytic activity of CASP5 and CASP10
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    text
  • can serve as an initiator caspase in Fas signaling leading to Bid processing, caspase cascade activation, and apoptosis
  • PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • activating CASP3 and CASP7
  • ABCF1, AKAP1, CPE, DOPEY1 and GOPC may be targeted specifically by the initiator CASP8 and CASP10 during the early stages of apoptosis
  • RIOK3 interacted with caspase-10 (interaction was mediated by the RIO domain of RIOK3 and each death effector domain of CASP10)
  • CASP10 negatively regulates CASP8-mediated cell death
  • CASP8 is required upstream of both CFLAR and CASP10 and death-inducing signaling complex (DISC) formation critically depends on the scaffold function of CASP8
  • cell & other
    REGULATION
    activated by CASP9
    CASP8 which cleaved caspase-10 directly
    ASSOCIATED DISORDERS
    corresponding disease(s) ALPS2
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --over  
    in term placentas from women with pregnancies complicated by preeclampsia
    tumoral somatic mutation      
    CASP10 mutation might contribute to the pathogenesis of some colon carcinomas together with other CASP gene mutations (CASP3, CASP7, CASP8)
    tumoral somatic mutation      
    CASP10 mutation might contribute to the pathogenesis of factions of T-ALL and multiple myelomas
    Susceptibility
  • to breast cancer
  • Variant & Polymorphism other polymorphisms significantly associated with a highly decreased familial breast cancer risk
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS