E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. CRLs complexes and arih1 collaborate in tandem to mediate ubiquitination of target proteins, arih1 mediating addition of the first ubiquitin on CRLs targets. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. Protein modification; protein ubiquitination. Part of SCF complexes, which consist of skp1, cul1, rbx1 and a F-box protein. Interacts with ube2m (By similarity). Expressed in heart and kidney. During hyperosmotic stress and thermal stress. The RING-type zinc finger domain is essential for ubiquitin ligase activity. It coordinates an additional third zinc ion. Belongs to the RING-box family.