Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. Binds to NUP1 and NUP2 forming the nuclear basket and the distal ring. The interaction with NUP2 is GSP1-GTP-dependent. Interacts through its FG repeats with karyopherins, such as KAP123 and KAP95-SRP1 (KAP60). Also interacts with GSP1-GTP and SRM1 (PRP20), where NUP60 reduces SRM1 activity, thus inhibiting GSP1 guanine nucleotide dissociation. Nuclear basket. Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side. Phosphorylated by CDC28. Present with 4590 molecules/cell in log phase SD medium.