Converts testosterone (T) into 5-alpha-dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.

This gene encodes a multifunctional Ser/Thr protein kinase that is implicated in the control of several regulatory proteins including glycogen synthase, and transcription factors, such as JUN. It also plays a role in the WNT and PI3K signaling pathways, as well as regulates the production of beta-amyloid peptides associated with Alzheimer's disease. [provided by RefSeq, Oct 2011]

TMEFF2 is a growth factor implicated in the progression of prostate cancer. It is highly expressed in the brain and may act as a survival factor for mesencephalic and hippocampal neurons.

Fos and Jun dimerize to form Activator Protein 1 (AP1), a transcriptional factor that binds to the 12-O-tetradecanoylphorbol 13 acetate (TPA) response element (TRE) of several cellular and viral genes including human collagenase, metallothionein IIa, stromelysin, interleukin 2, SV40 and polyoma. Fos and Jun contain the 'leucine-zipper' motif that allows for dimerization and an adjacent basic domain required for biological activity. The functionally active form of Fos is in a heterodimer

The protein encoded by this gene shares similarity with Saccharomyces cerevisiae Rad52, a protein important for DNA double-strand break repair and homologous recombination. This gene product was shown to bind single-stranded DNA ends, and mediate the DNA-DNA interaction necessary for the annealing of complementary DNA strands. It was also found to interact with DNA recombination protein RAD51, which suggested its role in RAD51 related DNA recombination and repair. [provided by RefSeq, Jul 20

The protein encoded by this gene is an atypical member of the family of growth factor receptor protein tyrosine kinases, differing from other members at a number of conserved residues in the activation and nucleotide binding domains. This gene product belongs to a subfamily whose members do not appear to be regulated by phosphorylation in the activation segment. It has been suggested that mediation of biological activity by recruitment of a signaling-competent auxiliary protein may occur throu