Large tegument protein that plays multiple roles in the viral cycle. During viral entry, remains associated with the capsid while most of the tegument is detached and participates in the capsid transport toward the host nucleus. Plays a role in the routing of the capsid at the nuclear pore complex and subsequent uncoating. Within the host nucleus, acts as a deneddylase and promotes the degradation of nuclear CRLs (cullin-RING ubiquitin ligases) and thereby stabilizes nuclear CRL substrates, while cytoplasmic CRLs remain unaffected. These modifications prevent host cell cycle S-phase progression and create a favorable environment allowing efficient viral genome replication. Participates later in the secondary envelopment of capsids. Indeed, plays a linker role for the association of the outer viral tegument to the capsids together with the inner tegument protein. Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Interacts with host CUL1 and CUL4A; these interactions inhibit the E3 ligase activity of cullins. Interacts with inner tegument protein. Interacts with capsid vertex specific component CVC2. Interacts with the major capsid protein/MCP. Tightly associated with the capsid. Proteolytically processed, possibly into several polypeptides. Enzymatic activity is only detectable following cleavage of the UL36 protein, which occurs late during viral replication (By similarity). Belongs to the herpesviridae large tegument protein family.