POM152 Pom152p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: POM152
Official Full Name: Pom152p
Primary source: SGD:S000004736
Locus tag: YMR129W
See related: AllianceGenome:SGD:S000004736; FungiDB:YMR129W; VEuPathDB:YMR129W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables protein-membrane adaptor activity. A structural constituent of nuclear pore. Involved in nuclear pore organization; protein import into nucleus; and spindle pole body duplication. Located in nuclear envelope lumen. Part of nuclear pore transmembrane ring. [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See POM152 in Genome Data Viewer

Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (527804..531817)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Study presents the integrative molecular architecture of Pom152, the major component of the nuclear pore complex (NPC) membrane ring. Pom152 is formed by a flexible string-of-pearls arrangement of nine repetitive cadherin-like Ig-like domains, indicating an evolutionary connection between NPCs and the cell adhesion machinery.
Title: Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex.
Sec66-mediated regulation of Pom152 plays an nuclear pore complex-independent role in the control of spindle-pole body duplication
Title: Sec66-Dependent Regulation of Yeast Spindle-Pole Body Duplication Through Pom152.
Data shsow that loss of Ncs2, Nup60, or Pom152 led to an impaired ability to increase SPB size during metaphase arrest, implicating these proteins in SPB component assembly.
Title: Identification of Saccharomyces cerevisiae spindle pole body remodeling factors.
Truncations of the N-glycosylated, lumenal domain of Pom152p and pom152 mutants lacking N-linked glycosylation sites are viable in combination with nup1Delta, and partially suppress the nuclear protein import defects associated with the deletion of NUP1.
Title: Nuclear pore complex function in Saccharomyces cerevisiae is influenced by glycosylation of the transmembrane nucleoporin Pom152p.
The absence of Pom152p results in aberrant nuclear pores that have enlarged diameters and lack proteinaceous material, leading to an increased diffusion between the cytoplasm and the nucleus.
Title: The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables protein-membrane adaptor activity	IDA Inferred from Direct Assay more info	PubMed
enables structural constituent of nuclear pore	IEA Inferred from Electronic Annotation more info
enables structural constituent of nuclear pore	IGI Inferred from Genetic Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in mRNA transport	IEA Inferred from Electronic Annotation more info
involved_in nuclear pore organization	IBA Inferred from Biological aspect of Ancestor more info
involved_in nuclear pore organization	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein import into nucleus	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein import into nucleus	IDA Inferred from Direct Assay more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info
involved_in spindle pole body duplication	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in cell periphery	HDA more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in nuclear envelope lumen	IDA Inferred from Direct Assay more info	PubMed
located_in nuclear membrane	IEA Inferred from Electronic Annotation more info
located_in nuclear periphery	HDA more info	PubMed
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 transmembrane ring	IBA Inferred from Biological aspect of Ancestor more info
part_of nuclear pore transmembrane ring	IDA Inferred from Direct Assay more info	PubMed
part_of nuclear pore transmembrane ring	IPI Inferred from Physical Interaction more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Pom152p

NP_013848.1

Glycoprotein subunit of transmembrane ring of nuclear pore complex; contributes to nucleocytoplasmic transport, nuclear pore complex (NPC) biogenesis and spindle pole body duplication; type II transmembrane protein composed of N-terminal cytosolic and C-terminal nuclear envelope lumenal domains; homologous to human NUP210