The N-terminal domain of the human androgen receptor is encoded by one, large exon.
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Faber PW, Kuiper GG, van Rooij HC, van der Korput JA, Brinkmann AO, Trapman J
The N-terminal domain of the human androgen receptor is encoded by one, large exon.
Mol Cell Endocrinol. 1989 Feb;61(2):257-62.
- PubMed ID
- 2917688 [ View in PubMed]
- Abstract
Using specific cDNA hybridization probes, the first coding exon of the human androgen receptor gene was isolated from a genomic library. The exon contained an open reading frame of 1586 bp, encoding an androgen receptor amino-terminal region of 529 amino acids. The deduced amino acid sequence was characterized by the presence of several poly-amino acid stretches of which the long poly-glycine stretch (16 residues) and the poly-glutamine stretch (20 residues) were most prominent. Androgen receptor cDNAs from different sources contained information for poly-glycine stretches of variable size (23 and 27 residues, respectively). The androgen receptor amino-terminal domain was found to be hydrophilic and have a net negative charge. Combined with the previously described, partially overlapping cDNA clone 7A2M27 (Trapman et al. (1988) Biochem. Biophys. Res. Commun. 153, 241-248), the complete human androgen receptor was deduced to have a size of 910 amino acids.