Gene content    
RARA ( by HUGO)
Retinoic Acid Receptor, Alpha
Oncogene
Retinoic Acid Receptor
Alpha
Nuclear Receptor Subfamily 1 Group B Member 1
NR1B1
RAR-alpha
RAR
Nucleophosmin-Retinoic Acid Receptor Alpha Fusion Protein NPM-RAR Long Form
Retinoic Acid Nuclear Receptor Alpha Variant 1
Retinoic Acid Nuclear Receptor Alpha Variant 2
Retinoic Acid Receptor Alpha
Retinoic Acid Receptor
Alpha Polypeptide
NCBI: 17q21    Ensembl: 17q21.2
RARA_HUMANSize: 462 amino acidsMass: 50771 Da

  • Subunit: Heterodimer; with RXRA. Binds DNA preferentially as a heterodimer. Interacts with CDK7 (By similarity). Interacts with coactivators NCOA3 and NCOA6. Interacts with NCOA7; the interaction requires ligand-binding. Interacts with KMT2E/MLL5. Interacts (via the ligand-binding domain) with PRAME; the interaction is ligand (retinoic acid)-dependent. Interacts with AKT1; the interaction phosphorylates RARA and represses transactivation. Interacts with PRKAR1A; the interaction negatively regulates RARA transcriptional activity. Interacts with NCOR1 and NCOR2. Interacts with PRMT2. Interacts with LRIF1. Interacts with ASXL1 and NCOA1 Sequence caution: Sequence=AAB00112.1; Type=Erroneous initiation; Sequence=AAB00113.1; Type=Erroneous initiation; Sequence=BAB62809.1; Type=Erroneous initiation; 6 PDB 3D structures from [IMAGE] and Proteopedia [IMAGE] for RARA: 1DKF (3D) [IMAGE] 1DSZ (3D) [IMAGE] 3A9E (3D) [IMAGE] 3KMR (3D) [IMAGE] 3KMZ (3D) [IMAGE] 4DQM (3D) [IMAGE]
  • Function:
    UniProtKB/Swiss-Prot Summary: RARA_HUMAN, P10276 Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). Regulates expression of target genes in a ligand-dependent manner by recruiting chromatin complexes containing KMT2E/MLL5. Mediates retinoic acid-induced granulopoiesis
  • Similarity:
    Belongs to the nuclear hormone receptor family. NR1 subfamily
                          
    Contains 1 nuclear receptor DNA-binding domain [IMAGE]
  • Protein Domain/Family    
    Source ID Domain Name Type
    InterProIPR000536Nucl_hrmn_rcpt_lig-bd_coreNuclear hormone receptor, ligand-bindingDomain
    IPR001628Znf_hrmn_rcptNuclear hormone receptor, DNA-bindingDomain
    IPR001723Str_hrmn_rcptSteroid hormone receptorFamily
    IPR003078Retinoic_acid_rcptRetinoic acid receptorFamily
    IPR008946Nucl_hormone_rcpt_ligand-bdSteroid nuclear receptor, ligand-bindingDomain
    BlocksIPB001723Steroid hormone receptor signatureSteroid hormone receptor signature
    IPB003078Retinoic acid receptor (1B nuclear receptor) signatureRetinoic acid receptor (1B nuclear receptor) signature

    Gene Ontology    
    Type Term Evidence Source Pub
    Biological Process apoptotic cell clearance IMP GOA 19628791
    cellular response to retinoic acid IDA GOA 19917671
    intracellular estrogen receptor signaling pathway IDA GOA 15831516
    negative regulation of granulocyte differentiation IDA GOA 19917671
    negative regulation of interferon-gamma production IDA GOA 18416830
    negative regulation of tumor necrosis factor production IDA GOA 18416830
    positive regulation of interleukin-13 production IDA GOA 18416830
    positive regulation of interleukin-4 production IDA GOA 18416830
    positive regulation of interleukin-5 production IDA GOA 18416830
    positive regulation of T-helper 2 cell differentiation IDA GOA 18416830
    positive regulation of transcription from RNA polymerase II promoter IDA GOA 19850744
    positive regulation of transcription, DNA-templated IMP GOA 19628791
    positive regulation of transcription, DNA-templated IDA GOA 18845237
    protein phosphorylation IMP GOA 16456540
    response to estradiol IDA GOA 15831516
    response to retinoic acid IMP GOA 17538076
    retinoic acid receptor signaling pathway IMP GOA 17538076
    signal transduction IDA GOA 2825025
    Cellular Component cell surface IC GOA 2825025
    cytoplasm IDA GOA 19850744
    nuclear chromatin IDA GOA 17363140
    nucleus IDA GOA 18845237
    Molecular Function chromatin DNA binding IDA GOA 19917671
    enzyme binding IPI GOA 12039952
    protein binding IPI GOA 16189514
    protein heterodimerization activity IDA GOA 19917671
    protein kinase B binding IPI GOA 16417524
    receptor binding IDA GOA 19628791
    retinoic acid binding IDA GOA 2825025
    retinoic acid receptor activity IDA GOA 2825025
    retinoic acid-responsive element binding IDA GOA 19917671
    sequence-specific DNA binding transcription factor activity IDA GOA 18922886
    transcription coactivator activity IMP GOA 19917671
    transcription factor binding IPI GOA 17641689

    Disorder & Mutation    
    Source Disease
    Genatlasacute promyelocytic leukemia or myeloid leukemia (APL),common breakpoints in translocation t (15;17) clustered in RARA second intron (see PML),in translocation t(11;17) (see ZNF145),in translocation t(5;17),and others
    SWISS-PROTNote=Chromosomal aberrations involving RARA are commonly found in acute promyelocytic leukemia. Translocation t(11;17)(q32;q21) with ZBTB16/PLZF; translocation t(15;17)(q21;q21) with PML; translocation t(5;17)(q32;q11) with NPM. The PML-RARA oncoprotein requires both the PML ring structure and coiled-coil domain for both interaction with UBE2I, nuclear microspeckle location and sumoylation. In addition, the coiled-coil domain functions in blocking RA-mediated transactivation and cell differentiation

    RARA cross reference    
    PubMed OMIM Entrez Gene NCKU SNP Nucleotide UniProt Genome Data Viewer HomoloGene