Androgen receptor (AR) transcriptional activity depends on interactions between the AR NH-terminal region and transcriptional coregulators. A yeast two-hybrid screen of a human testis library using predicted α-helical NH-terminal fragment AR-(370-420) as bait identified suppressor of variegation 3-9 homolog 2 (SUV39H2) histone methyltransferase as an AR interacting protein. SUV39H2 interaction with AR and the AR coregulator, melanoma antigen-A11 (MAGE-A11), was verified in two-hybrid, in vitro glutathione S-transferase affinity matrix and coimmunoprecipitation assays.