COP1: 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. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Homodimer. Homodimerization is mediated by the coiled coil domain. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Isoform 2 does not interact with CUL4A but still binds to RBX1, suggesting that the interaction may be mediated by another culllin protein. Isoform 1 and isoform 2 interact with CUL5 but not with CUL1, CUL2 not CUL3. Interacts with bZIP transcription factors JUN, JUNB and JUND but not with FOS, ATF2 nor XBP1. Interacts with p53 (TP53). By p53/TP53. Ubiquitously expressed at low level. Expressed at higher level in testis, placenta, skeletal muscle and heart. Belongs to the COP1 family. 3 isoforms of the human protein are produced by alternative splicing.
Protein type: EC 6.3.2.-; Ubiquitin conjugating system; Ligase; EC 6.3.2.19; Ubiquitin ligase
Chromosomal Location of Human Ortholog: 1q25.1-q25.2
Cellular Component: Golgi membrane; nucleoplasm; centrosome; focal adhesion; cytoplasm; nuclear speck; cytosol
Molecular Function: protein binding; zinc ion binding; ligase activity
Biological Process: positive regulation of proteasomal ubiquitin-dependent protein catabolic process; protein ubiquitination; response to ionizing radiation; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
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