Retinoic acid receptor alpha (Protein name
), RARA_HUMAN from NCBI database.
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Gene name:
RARA(NR1B1);
Protein name:
Retinoic acid receptor alpha(RAR-alpha);
Alternative:
Nuclear receptor subfamily 1 group B member 1;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
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 MLL5. Interacts (via the ligand-binding domain) with PRAME; the interaction is ligand (retinoic acid)-dependent. Interacts with AKT1; the interaction phosphorylates RARA and repressses transactivation. Interacts with PRKAR1A; the interaction negatively regulates RARA transcriptional activity. Interacts with NCOR1 and NCOR2. Interacts with PRMT2. Interacts with LRIF1.
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 MLL5. Mediates retinoic acid-induced granulopoiesis.
Subcellular Location:
Nucleus
Cytoplasm
Nuclear localization depends on ligand binding, phosphorylation and sumoylation. Transloaction to the nucleus in the absence of ligand is dependent on activation of PKC and the downstream MAPK phosphorylation.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1);CHROMOSOMAL TRANSLOCATION WITH PML
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-1)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1-DELTABC)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2)
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-80 (ISOFORM ALPHA-1)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 61-462;CHROMOSOMAL TRANSLOCATION WITH NPM
"Homo sapiens retinoic acid receptor alpha (RAR-alpha) gene, promoter and 5' region of RAR-alpha 2 isoform." Chen A.
,
Petrie K.
,
Waxman S.
,
Zelent A.
Submitted (2000-06) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54 (ISOFORM ALPHA-2)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 61-68;CHROMOSOMAL TRANSLOCATION WITH PML
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Cited for: INTERACTION OF THE PML-RARALPHA ONCOPROTEIN WITH UBE2I;SUMOYLATION;SUBCELLULAR LOCATION
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Cited for: PHOSPHORYLATION AT SER-96;FUNCTION;INTERACTION WITH AKT1;MUTAGENESIS OF SER-95; SER-96; SER-154 AND SER-157
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Cited for: INTERACTION WITH ASXL1 AND NCOA1;MUTAGENESIS OF 409-ILE-LEU-410; GLU-412; 413-MET-LEU-414 AND GLU-415
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Cited for: SUMOYLATION AT LYS-166; LYS-171 AND LYS-399;FUNCTION;SUBCELLULAR LOCATION;MUTAGENESIS OF LYS-147; LYS-166; LYS-171 AND LYS-399
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Cited for: PHOSPHORYLATION AT SER-219 AND SER-369;INTERACTION WITH RXRA AND PRKAR1A;FUNCTION;MUTAGENESIS OF SER-219 AND SER-369
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Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 82-167 IN COMPLEX WITH RXRA AND DNA
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Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 182-416 IN COMPLEX WITH M.MUSCULUS RXRA
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Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 176-421 IN COMPLEXES WITH AGONIST AM580 AND NCOA1 AND WITH INVERSE AGONIST BMS493 AND NCOR1;INTERACTION WITH NCOR1 AND NCOR2;MUTAGENESIS OF ILE-396
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Vaild Sequence:
