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FLASH GENE
Symbol RARA contributors: mct/ - updated : 13-06-2014
HGNC name retinoic acid receptor, alpha
HGNC id 9864
EXPRESSION
Type widely
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Reproductivefemale systembreastmammary gland  
cells
SystemCellPubmedSpeciesStageRna symbol
Skin/Tegumentkeratinocyte
cell lineage
cell lines
fluid/secretion blood
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • a N terminal modulator domain, an activation function domain (AF-1)
  • a central DNA-binding domain (DBD) followed by a short hinge/D region
  • a central bipartite (class II) zinc finger DNA binding domain
  • a C terminal ligand domain, a ligand-binding and ligand-dependent transactivation function domain (LBD/AF-2)
  • HOMOLOGY
    Homologene
    FAMILY
  • steroid/thyroid hormone receptor superfamily
  • NR1 subfamily
  • CATEGORY transcription factor , receptor
    SUBCELLULAR LOCALIZATION extracellular
        plasma membrane
        intracellular
    intracellular,cytoplasm
    intracellular,nucleus,nucleoplasm
    intracellular,nucleus,chromatin/chromosome
    basic FUNCTION
  • negatively regulating growth plate chondrocyte proliferation and matrix synthesis
  • role for RAR-alpha engagement in the regulation of genes and proteins involved with human T cell activation and type 2 cytokine production
  • requirement of RARalpha-mediated retinoid signaling specifically in germ cells
  • CELLULAR PROCESS cell life, differentiation
    nucleotide, transcription
    cell organization/biogenesis
    PHYSIOLOGICAL PROCESS
    text adipocyte differentiation
    PATHWAY
    metabolism
    signaling signal transduction
    a component
  • component with PML, RXRA,TIF1 of a transcription complex, retinoic acid dependent
  • receptor RXRA : RARA (RXRalpha:RARalpha) are repressor of ABCC3 activation by transcription factor Sp1
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • retinoic acid receptor binding
  • interacting with BNIP1 (repressed by TNIP1)
  • is a novel negative regulator of the IFN/STAT pathway, suggesting that this repression through RARA inhibition may prevent liver cancer
  • PML/RARA binds to FAS and blocks FAS-mediated apoptosis in acute promyelocytic leukemia (APL) by forming an apoptotic inhibitory complex with CFLAR
  • TRIM32 interacts with RARA and enhances its transcriptional activity in the presence of RA
  • CACUL1 is a novel type of RARA coregulator that interacts with RARA and inhibits its transcriptional activity
  • USP37 interacted with ZBTB16/RARA through the PLZF moiety and sustained ZBTB16/RARA steady state levels
  • RARA-ZBTB16 acts as a modifier oncogene that subverts differentiation in the granulocytic lineage by associating with CEBPA and inhibiting its activity
  • UCP1 expression is differently affected by RARA in mouse and human adipocytes (PMUID: 24059847)
  • cell & other
    REGULATION
    activated by both all-trans (T-RA) and its 9-cis isomer (9-cis-RA) retinoic acids
    Other regulated by TADA3 which regulates retinoic acid receptor RARA-mediated transactivation
    ASSOCIATED DISORDERS
    corresponding disease(s) RARA
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral fusion      
    PML-RARalpha fusion alone can confer properties of self-renewal to committed hematopoietic progenitors before the onset of acute promyelocytic leukemia
    tumoral fusion      
    STAT5B-RARA fusion transcript in acute promyelocytic leukemia with the normal chromosome 17 on G-banding
    tumoral fusion      
    fusion partner of BCOR in a t(X;17)(p11;q12) variant of acute promyelocytic leukemia
    Susceptibility
  • to obesity
  • to meningomyelocele (MM)
  • Variant & Polymorphism SNP
  • rs12051734 conferred a protective effect for MM susceptibility (MID: 21254357)
  • Candidate gene for isolated cleft lip/palate
    Marker
    Therapy target PML-RARA degradation or therapy-triggered degradation of oncoproteins could be a general strategy to eradicate cancer stem cells
    ANIMAL & CELL MODELS