NUP159 FG-nucleoporin NUP159 [Saccharomyces cerevisiae S288C] - Gene

Summary

Official Symbol: NUP159
Official Full Name: FG-nucleoporin NUP159
Primary source: SGD:S000001377
Locus tag: YIL115C
See related: AllianceGenome:SGD:S000001377; FungiDB:YIL115C; VEuPathDB:YIL115C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: NUP158; RAT7
Summary: Enables adenyl-nucleotide exchange factor activity. A structural constituent of nuclear pore. Involved in nuclear pore localization and nucleocytoplasmic transport. Part of nuclear pore central transport channel and nuclear pore cytoplasmic filaments. [provided by Alliance of Genome Resources, Jul 2025]
Orthologs: all
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Chromosome IX - NC_001141.2 Genomic Context describing neighboring genes

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Biophysical characterization of the interaction of Atg8 with a disordered region of Nup159 involved in selective autophagy of the nuclear pore complex.
Title: Biophysical characterization of the interaction of Atg8 with a disordered region of Nup159 involved in selective autophagy of the nuclear pore complex.
TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes.
Title: TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes.
Nup159 is an Atg8-interacting motif-dependent Atg8 receptor.
Title: Selective autophagy degrades nuclear pore complexes.
Multiple recognition motifs in nucleoporin Nup159 provide a stable and rigid Nup159-Dyn2 assembly
Title: Multiple recognition motifs in nucleoporin Nup159 provide a stable and rigid Nup159-Dyn2 assembly.
Data indicate that the comparative binding of Dyn2 to two Nup159 target sites shows similar affinities (18 and 13 muM), but divergent thermal binding modes.
Title: Structure of a yeast Dyn2-Nup159 complex and molecular basis for dynein light chain-nuclear pore interaction.
the Nup159 NTD functions in mRNA export as a binding platform, tethering shuttling Dbp5 molecules at the nuclear periphery
Title: The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore.

Submit: New GeneRIF Correction

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

Function	Evidence Code	Pubs
enables adenyl-nucleotide exchange factor activity	IDA Inferred from Direct Assay more info	PubMed
enables adenyl-nucleotide exchange factor activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables structural constituent of nuclear pore	IPI Inferred from Physical Interaction more info	PubMed
enables transcription corepressor activity	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in NLS-bearing protein import into nucleus	IGI Inferred from Genetic Interaction more info	PubMed
involved_in RNA export from nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mRNA transport	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of DNA-templated transcription	IEA Inferred from Electronic Annotation more info
involved_in nuclear pore localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in nucleocytoplasmic transport	NAS Non-traceable Author Statement more info	PubMed
involved_in poly(A)+ mRNA export from nucleus	IGI Inferred from Genetic Interaction more info	PubMed
involved_in poly(A)+ mRNA export from nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein export from nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info
involved_in ribosomal large subunit export from nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in ribosomal small subunit export from nucleus	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in nuclear envelope	NAS Non-traceable Author Statement more info	PubMed
located_in nuclear membrane	IEA Inferred from Electronic Annotation more info
part_of nuclear pore	IDA Inferred from Direct Assay more info	PubMed
part_of nuclear pore	IEA Inferred from Electronic Annotation more info
part_of nuclear pore central transport channel	IDA Inferred from Direct Assay more info	PubMed
part_of nuclear pore cytoplasmic filaments	IDA Inferred from Direct Assay more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info

NP_012151.1

FG-nucleoporin component of central core of the nuclear pore complex; also part of the nuclear pore complex (NPC) cytoplasmic filaments; contributes directly to nucleocytoplasmic transport; regulates ADP release from the ATP-dependent RNA helicase Dbp5p; forms a stable association with Nup82p, Gle2p and two other FG-nucleoporins (Nsp1p and Nup116p)

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