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FLASH GENE
Symbol TMX1 contributors: npt/mct - updated : 04-11-2015
HGNC name thioredoxin domain containing 1
HGNC id 15487
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
8 - 4119 31 280 - Matsuo (2009)
EXPRESSION
Type widely
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
blood / hematopoieticspleen   highly
Digestiveliver   moderately
Endocrinepancreas   highly
Nervousbrain   moderately
Reproductivemale systemprostate  highly
Respiratorylung   moderately
Urinarykidney   highly
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Blood / Hematopoieticbone marrow   
Connectivebone   
Epithelialsecretoryglandularendocrine 
Epithelialsecretoryglandularexocrine 
Lymphoid    
Muscularstriatumskeletal  
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • N terminal signal peptide containing the Trx-like domain present with a catalytic CXXC motif in the ER lumen, where protein disulfide isomerase (PDI) was found to assist protein folding
  • a thioredoxin (TRX)-like domain with a unique active site sequence Cys-Pro-Ala-Cys, with oxidoreductase activity
  • ER-targeting signal sequence
  • one transmembrane domain (Sugiura 2010)
  • HOMOLOGY
    interspecies homolog to C.elegans F54d8.3
    Homologene
    FAMILY
  • thioredoxin family
  • CATEGORY enzyme
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    text
  • as CANX, shuttles between the rough ER and the shuttles between the rough ER and the mitochondria-associated membrane (MAM) depending on its palmitoylation status
  • basic FUNCTION
  • can modify certain molecules with its oxidoreductase activity and be involved in the redox regulation in the ER
  • specific role for TMX1 and its mechanism of action in redox-based ER quality control (Matsuo 2009)
  • prevents an overexpressed major histocompatibility complex class I heavy chain from being degraded (Sugiura 2010)
  • cooperate with calnexin in protein retention in the ER, followed by refolding of misfolded proteins (Sugiura 2010)
  • thought to be an isomerase in the ER (Sugiura 2010)
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism energetic
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein associates with the molecular chaperon calnexin, which can mediate substrate binding (Matsuo 2009)
    cell & other
    REGULATION
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS