Component of the nuclear pore complex. Acts as a docking site for activities required for desumoylation and mRNA export. Required for the proper expression or localization of a subset of miRNAs. Plays a role in meristematic cell division by interacting with spindle assembly checkpoint proteins. Part of the nuclear pore complex (NPC). The NPC has an eight-fold symmetrical structure comprising a central transport channel and two rings, the cytoplasmic and nuclear rings, to which eight filaments are attached. The cytoplasmic filaments have loose ends, while the nuclear filaments are joined in a distal ring, forming a nuclear basket. NPCs are highly dynamic in configuration and composition, and can be devided in 3 subcomplexes, the NUP62 subcomplex, the NUP107-160 subcomplex and the NUP93 subcomplex, containing approximately 30 different nucleoporin proteins. Interacts with MAD1 and (via N-terminus) with ESD4. Located at the inner surface of the nuclear envelope during interphase and in the vicinity of the spindle during prometaphase. Ubiquitous. Highest expression in the shoot apical region. Not induced by vernalization. The N-terminal domain is involved in RNA and SUMO homeostasis while the C-terminal part is required for nuclear pore association. Early flowering under both long and short days and pleiotropic alterations in shoot development and auxin signaling. Stunted primary root development in the absence of sucrose. Accumulation of nuclear poly(A)+ RNA and high-molecular weight SUMO conjugates.