E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (Probable). Plays a negative role in drought stress tolerance through transcriptional and post-translational regulation of diverse stress-related genes. Interacts with the serine/threonine-protein kinase NEK6 and promotes its degradation via the 26S proteasome-dependent pathway (PubMed:21719639). S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Protein modification; protein ubiquitination. Homodimer (Probable). Interacts with NEK6 (PubMed:21719639). Interacts with SKIPA (PubMed:22067990). Predominantly nuclear. Partially cytoplasmic. Induced by drought stress. The RING-type zinc finger domain is essential for ubiquitin ligase activity. The SBD domain (substrate-binding domain) mediates the homodimerization and the interaction with substrate proteins. It is related to the TRAF family. Plants overexpressing DIS1 exhibit reduced drought tolerance. Plants silencing DIS1 show enhanced drought tolerance. Belongs to the SINA (Seven in absentia) family.