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FLASH GENE
Symbol COX20 contributors: mct - updated : 30-04-2013
HGNC name Cox2 chaperone homolog (S. cerevisiae)
HGNC id 26970
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • hydrophilic domains located in the intermembrane space
  • C-terminus is substantially protected from proteinase K by the outer mitochondrial membrane
  • HOMOLOGY
    interspecies ortholog to rattus Fam36a_predicted
    ortholog to fungal complex IV assembly factor COX20
    Homologene
    FAMILY
  • FAM36 family
  • CATEGORY chaperone/stress , enzyme
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,mitochondria,inner
    intracellular,cytoplasm,organelle,membrane
    text integral inner membrane protein
    basic FUNCTION
  • acts as a membrane-bound chaperone necessary for cleavage of COX2 and for interaction of the mature protein with other subunits of cytochrome oxidase in a later step of the assembly process
  • control the coordinate assembly process to prevent potentially harmful redox reactions of unassembled or misassembled subunits
  • serves as a substrate-specific cofactor during proteolysis and modulates the initial interaction of nonassembled COX2 with the protease
  • required for efficient export of the COX2 C-tail
  • COX20 chaperone has important roles in leader peptide processing, C-tail export, and stabilization of COX2
  • involvement of FAM36A in complex IV function
  • function in complex IV assembly
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • interacts by co-immune precipitation with COX18, and this interaction requires the presence of COX2
  • COX20 cooperates with SCO1 and SCO2 to mature COX2 and promote the assembly of cytochrome c oxidase
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s) AHMU
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS