NUP98

UniProt ID: P52948
Organism: Homo sapiens
Review Status: DRAFT
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Gene Description

NUP98 encodes a precursor protein that cleaves itself autoproteolytically, via its C-terminal domain, into two distinct nucleoporins of the nuclear pore complex (NPC): Nup98 and Nup96 (alternatively spliced Nup98-only transcripts give Nup98 alone). Nup98 has a long, intrinsically disordered N-terminal domain of FG and GLFG repeats that forms a cohesive, phase-separating meshwork. Within the NPC central channel this meshwork is a major part of the selective permeability barrier: it excludes inert macromolecules while providing binding sites that let nuclear transport receptors (importins, exportins, NXF1) and their cargoes cross the pore. Through its GLEBS motif Nup98 binds the mRNA export factor RAE1, and the RAE1-Nup98 complex contacts mRNPs during mRNA export. Nup98 sits mainly at the nucleoplasmic side of the NPC and in the pore core, and it is dynamic. A mobile pool in the nucleoplasm and in intranuclear GLFG bodies binds chromatin and transcripts and acts as a cofactor of the RNA helicase DHX9, stimulating its ATPase activity and supporting transcription and splicing of target genes. Nup96 is a stable scaffold subunit of the Nup107-160 (Y) complex that forms the NPC outer rings. It is essential for NPC assembly, and the complex is recruited to kinetochores in mitosis. Several viral proteins, including SARS-CoV-2 ORF6 and vesicular stomatitis virus M, target the RAE1-Nup98 complex to block host mRNA export and STAT nuclear import. Fusions of the NUP98 FG-repeat region to many partner genes drive acute leukemias.

Functional Isoforms

Curated functional classes representing distinct biological activities. These may be splice variants, cleavage products, or other forms with different functions.

Nup98 (N-terminal autoproteolytic product, FG-repeat nucleoporin) CLEAVAGE PRODUCT
ID: NUP98_NUP98
UNIPROT CHAIN:PRO_0000019929 (residues 1-880)
N-terminal product of autoproteolysis of the Nup98-Nup96 precursor (isoforms 1/2), and the sole product of the Nup98-specific isoforms 3/4. Carries the FG/GLFG-repeat domain that forms the selective permeability barrier and binds transport receptors, the GLEBS motif that binds RAE1, and the C-terminal autoproteolytic (peptidase S59) domain that also anchors Nup98 to the NPC. Responsible for the FG-barrier, mRNA export, intranuclear GLFG-body and DHX9-cofactor functions.
Isoform-specific terms: molecular condensate scaffold activity protein autoprocessing nuclear body
Nup96 (C-terminal autoproteolytic product, scaffold nucleoporin) CLEAVAGE PRODUCT
ID: NUP98_NUP96
UNIPROT CHAIN:PRO_0000019930 (residues 881-1817)
C-terminal product of the Nup98-Nup96 precursor (isoforms 1/2 only). A structured scaffold nucleoporin and stable subunit of the Nup107-160 (Y) complex that forms the NPC outer rings, essential for NPC assembly; the complex is recruited to kinetochores in mitosis. Lacks FG repeats.
Isoform-specific terms: nuclear pore outer ring kinetochore

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000776 kinetochore
IDA
PMID:15146057
The entire Nup107-160 complex, including three new members, ...
KEEP AS NON CORE
Summary: Nup96, the C-terminal autoproteolytic product of the NUP98 precursor, is a stable Nup107-160 complex subunit that the whole complex targets to kinetochores from prophase to anaphase. Nup98 itself was not detected at kinetochores in this study.
Reason: Supported for the Nup96 chain encoded by NUP98 (colocalizes_with). Kinetochore association of the Nup107-160 complex is a mitotic moonlighting role, not the core NPC function.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:15146057
indicating that most, if not all, Nup96 is stably associated with the Nup107-160 complex during the entire cell cycle
GO:0000973 post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery
IBA
GO_REF:0000033
KEEP AS NON CORE
Summary: IBA from a PANTHER node seeded by yeast GLFG nucleoporins (Nup100/Nup145) that maintain transcriptional memory by tethering recently repressed genes at the nuclear periphery.
Reason: Human Nup98 binds promoters of inducible genes and is required for transcriptional memory of interferon-gamma-induced genes (reviewed in the introduction of PMID:28221134), consistent with conserved inheritance of a gene-tethering/memory role. However, metazoan Nup98 acts largely in the nucleoplasm off the pore, so the peripheral tethering aspect is not directly shown in human cells. Retained as non-core.
Supporting Evidence:
PMID:28221134
One such nucleoporin, Nup98, binds chromatin and regulates gene expression.
GO:0003713 transcription coactivator activity
IMP
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
KEEP AS NON CORE
Summary: Capitanio et al. show Nup98 binds DHX9, stimulates its ATPase activity and supports DHX9-stimulated transcription in a reporter assay.
Reason: Nup98 acts as a cofactor of the DHX9 helicase rather than as a classical coactivator bridging a DNA-bound transcription factor; the curator-assigned IMP is accepted as a non-core off-pore regulatory role. A more mechanistic MF (ATPase activator activity) is proposed under the DHX9 protein binding row.
Supporting Evidence:
PMID:28221134
Nup98 functions as a co-factor that regulates DHX9 and, potentially, other RNA helicases
PMID:28221134
Importantly, binding of Nup98 stimulates the ATPase activity of DHX9, and a transcriptional reporter assay suggests Nup98 supports DHX9-stimulated transcription.
GO:0003723 RNA binding
IBA
GO_REF:0000033
KEEP AS NON CORE
Summary: IBA for RNA binding at the GLFG nucleoporin node. Human Nup98 associates with transcripts in an RNA-facilitated manner and, in complex with RAE1, binds single-stranded RNA.
Reason: RNA association is supported (RAE1-Nup98 complex ssRNA binding; Nup98-DHX9 binding to transcripts), but the predicted nucleoporin RNA-binding motif in the C-terminal domain is structurally unlikely to bind RNA, and much of the RNA contact may be contributed by partners. Non-core.
Supporting Evidence:
PMID:20498086
we demonstrate that the complex possesses single-stranded RNA-binding capability
PMID:28221134
Nup98 and DHX9 bind interdependently to similar gene loci and their transcripts
PMID:12191480
The structure further reveals that the suggested nucleoporin RNA binding motif is unlikely to bind to RNA.
GO:0003729 mRNA binding
IMP
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
KEEP AS NON CORE
Summary: Nup98 and DHX9 bind interdependently to the same gene loci and their transcripts (RNA immunoprecipitation).
Reason: Supported experimentally for intranuclear Nup98; this is part of its off-pore gene-regulatory role rather than its core transport function.
Supporting Evidence:
PMID:28221134
Nup98 and DHX9 bind interdependently to similar gene loci and their transcripts
GO:0005515 protein binding
IPI
PMID:15146057
The entire Nup107-160 complex, including three new members, ...
REMOVE
Summary: IPI from the Nup107-160 complex study; the interactions reported involve Nup96 (the C-terminal NUP98 precursor product) with other Nup107-160 complex members.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. The Nup96 scaffold role is captured by nuclear pore outer ring and structural constituent of nuclear pore annotations.
Supporting Evidence:
PMID:15146057
indicating that most, if not all, Nup96 is stably associated with the Nup107-160 complex during the entire cell cycle
GO:0005515 protein binding
IPI
PMID:15146057
The entire Nup107-160 complex, including three new members, ...
REMOVE
Summary: IPI from the Nup107-160 complex study; the interactions reported involve Nup96 (the C-terminal NUP98 precursor product) with other Nup107-160 complex members.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. The Nup96 scaffold role is captured by nuclear pore outer ring and structural constituent of nuclear pore annotations.
Supporting Evidence:
PMID:15146057
indicating that most, if not all, Nup96 is stably associated with the Nup107-160 complex during the entire cell cycle
GO:0005515 protein binding
IPI
PMID:15146057
The entire Nup107-160 complex, including three new members, ...
REMOVE
Summary: IPI from the Nup107-160 complex study; the interactions reported involve Nup96 (the C-terminal NUP98 precursor product) with other Nup107-160 complex members.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. The Nup96 scaffold role is captured by nuclear pore outer ring and structural constituent of nuclear pore annotations.
Supporting Evidence:
PMID:15146057
indicating that most, if not all, Nup96 is stably associated with the Nup107-160 complex during the entire cell cycle
GO:0005515 protein binding
IPI
PMID:17172455
Rae1 interaction with NuMA is required for bipolar spindle f...
REMOVE
Summary: Rae1 co-immunoprecipitates NuMA together with Nup98 and dynein in mitotic cells.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms.
Supporting Evidence:
PMID:17172455
By immunoblotting of anti-Rae1 immunoprecipitates, we detected coprecipitating NuMA along with Nup98 and dynein
GO:0005515 protein binding
IPI
PMID:18832153
Cohesin subunit SMC1 associates with mitotic microtubules at...
REMOVE
Summary: IPI from a study of cohesin SMC1 binding to Rae1 at the spindle pole; the cached abstract does not describe the NUP98 interaction itself.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms.
GO:0005515 protein binding
IPI
PMID:20498086
Structural and functional analysis of the interaction betwee...
REMOVE
Summary: Crystal structure of human RAE1 bound to the Nup98 GLEBS motif; the complex binds ssRNA and functions in mRNA export.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. The biological meaning of the RAE1 interaction (mRNA export) is captured by the RNA export and mRNA export process terms.
Supporting Evidence:
PMID:20498086
Rae1 and Nup98 are evolutionarily conserved mRNA export factors
GO:0005515 protein binding
IPI
PMID:25562883
Nup98 FG domains from diverse species spontaneously phase-se...
REMOVE
Summary: Nup98 FG domains phase-separate into permselective FG particles that bind nuclear transport receptors.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. The informative activity from this paper is captured by molecular condensate scaffold activity and structural constituent of nuclear pore.
Supporting Evidence:
PMID:25562883
All Nup98 FG phases rejected inert macromolecules and yet allowed far larger NTR cargo complexes to rapidly enter.
GO:0005515 protein binding
IPI
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
MODIFY
Summary: Capitanio et al. show that the Nup98 FG/GLFG region binds DHX9 directly and that this binding stimulates DHX9 ATPase activity.
Reason: The paper supports a specific activity beyond binding: Nup98 binding increases the ATP hydrolysis activity of DHX9. ATPase activator activity (GO:0001671, "Binds to and increases the activity of an ATP hydrolysis activity") captures this better than protein binding.
Proposed replacements: ATPase activator activity
Supporting Evidence:
PMID:28221134
Importantly, binding of Nup98 stimulates the ATPase activity of DHX9, and a transcriptional reporter assay suggests Nup98 supports DHX9-stimulated transcription.
PMID:28221134
We demonstrate that Nup98 binds DHX9 in the nucleoplasm, regulates the nuclear distribution of DHX9, and influences DHX9 RNA-binding and ATPase activity.
GO:0005515 protein binding
IPI
PMID:30543681
Biallelic mutations in nucleoporin NUP88 cause lethal fetal ...
REMOVE
Summary: IPI from a NUP88 disease study; the cached abstract does not describe the NUP98 interaction (UniProt records NUP98-NUP88 interaction from this paper).
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms.
GO:0005515 protein binding
IPI
PMID:32353859
A SARS-CoV-2 protein interaction map reveals targets for dru...
REMOVE
Summary: High-throughput SARS-CoV-2-human affinity-purification mass spectrometry screen in which ORF6 copurified with NUP98-RAE1.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. Host-virus interaction screen; no informative host MF.
GO:0005515 protein binding
IPI
PMID:33060197
Comparative host-coronavirus protein interaction networks re...
REMOVE
Summary: Comparative coronavirus-host AP-MS interaction network (SARS-CoV, SARS-CoV-2, MERS) including ORF6-NUP98.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. Host-virus interaction screen; no informative host MF.
GO:0005515 protein binding
IPI
PMID:33060197
Comparative host-coronavirus protein interaction networks re...
REMOVE
Summary: Comparative coronavirus-host AP-MS interaction network (SARS-CoV, SARS-CoV-2, MERS) including ORF6-NUP98.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. Host-virus interaction screen; no informative host MF.
GO:0005515 protein binding
IPI
PMID:33097660
SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import a...
REMOVE
Summary: SARS-CoV-2 Orf6 directly binds the Nup98-Rae1 complex and thereby blocks STAT1/2 nuclear import; Nup98 overexpression rescues import.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. The physiologically relevant host role revealed (Nup98-dependent protein import) is captured by protein import into nucleus.
Supporting Evidence:
PMID:33097660
This result demonstrates that the C-terminal region of Orf6 directly binds the Nup98-Rae1 complex with an estimated dissociation constant in the submicromolar range.
PMID:33097660
strongly suggesting that Orf6 specifically targets Nup98 to block STAT nuclear import
GO:0005515 protein binding
IPI
PMID:33097660
SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import a...
REMOVE
Summary: SARS-CoV-2 Orf6 directly binds the Nup98-Rae1 complex and thereby blocks STAT1/2 nuclear import; Nup98 overexpression rescues import.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. The physiologically relevant host role revealed (Nup98-dependent protein import) is captured by protein import into nucleus.
Supporting Evidence:
PMID:33097660
This result demonstrates that the C-terminal region of Orf6 directly binds the Nup98-Rae1 complex with an estimated dissociation constant in the submicromolar range.
PMID:33097660
strongly suggesting that Orf6 specifically targets Nup98 to block STAT nuclear import
GO:0005515 protein binding
IPI
PMID:33097660
SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import a...
REMOVE
Summary: SARS-CoV-2 Orf6 directly binds the Nup98-Rae1 complex and thereby blocks STAT1/2 nuclear import; Nup98 overexpression rescues import.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. The physiologically relevant host role revealed (Nup98-dependent protein import) is captured by protein import into nucleus.
Supporting Evidence:
PMID:33097660
This result demonstrates that the C-terminal region of Orf6 directly binds the Nup98-Rae1 complex with an estimated dissociation constant in the submicromolar range.
PMID:33097660
strongly suggesting that Orf6 specifically targets Nup98 to block STAT nuclear import
GO:0005515 protein binding
IPI
PMID:33765414
Sarbecovirus ORF6 proteins hamper induction of interferon si...
REMOVE
Summary: Sarbecovirus ORF6 proteins interact with RAE1 and NUP98 in co-immunoprecipitation assays.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. Viral interaction; no informative host MF.
Supporting Evidence:
PMID:33765414
HEK293T cells were transfected with a SARS-CoV-2 ORF6 expression plasmid with or without the expression plasmids for FLAG-RAE1 and HA-NUP98
GO:0005515 protein binding
IPI
PMID:33765414
Sarbecovirus ORF6 proteins hamper induction of interferon si...
REMOVE
Summary: Sarbecovirus ORF6 proteins interact with RAE1 and NUP98 in co-immunoprecipitation assays.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. Viral interaction; no informative host MF.
Supporting Evidence:
PMID:33765414
HEK293T cells were transfected with a SARS-CoV-2 ORF6 expression plasmid with or without the expression plasmids for FLAG-RAE1 and HA-NUP98
GO:0005515 protein binding
IPI
PMID:33849972
SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Tra...
REMOVE
Summary: SARS-CoV-2 ORF6 copurifies with the mRNA export factors Rae1 and Nup98 and traps host mRNA in the nucleus.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. The relevant host function (mRNA export) is captured by process terms.
Supporting Evidence:
PMID:33849972
ORF6's nuclear entrapment of host mRNA is associated with its ability to copurify with the mRNA export factors, Rae1 and Nup98.
GO:0005515 protein binding
IPI
PMID:33849972
SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Tra...
REMOVE
Summary: SARS-CoV-2 ORF6 copurifies with the mRNA export factors Rae1 and Nup98 and traps host mRNA in the nucleus.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. The relevant host function (mRNA export) is captured by process terms.
Supporting Evidence:
PMID:33849972
ORF6's nuclear entrapment of host mRNA is associated with its ability to copurify with the mRNA export factors, Rae1 and Nup98.
GO:0005515 protein binding
IPI
PMID:33961781
Dual proteome-scale networks reveal cell-specific remodeling...
REMOVE
Summary: Proteome-scale yeast two-hybrid/interactome mapping (HuRI-type) study; the cached text does not describe the specific NUP98 interaction.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms.
GO:0005515 protein binding
IPI
PMID:35096974
Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1-Nup...
REMOVE
Summary: Crystal structures of SARS-CoV and SARS-CoV-2 Orf6 C-termini bound to the Rae1-Nup98 heterodimer, occupying its mRNA-binding groove.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. Viral interaction; host mRNA-export role captured elsewhere.
Supporting Evidence:
PMID:35096974
SARS-CoV Orf6 occupies the same potential mRNA-binding groove of the Rae1-Nup98 complex
GO:0005515 protein binding
IPI
PMID:35096974
Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1-Nup...
REMOVE
Summary: Crystal structures of SARS-CoV and SARS-CoV-2 Orf6 C-termini bound to the Rae1-Nup98 heterodimer, occupying its mRNA-binding groove.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. Viral interaction; host mRNA-export role captured elsewhere.
Supporting Evidence:
PMID:35096974
SARS-CoV Orf6 occupies the same potential mRNA-binding groove of the Rae1-Nup98 complex
GO:0005515 protein binding
IPI
PMID:35096974
Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1-Nup...
REMOVE
Summary: Crystal structures of SARS-CoV and SARS-CoV-2 Orf6 C-termini bound to the Rae1-Nup98 heterodimer, occupying its mRNA-binding groove.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms. Viral interaction; host mRNA-export role captured elsewhere.
Supporting Evidence:
PMID:35096974
SARS-CoV Orf6 occupies the same potential mRNA-binding groove of the Rae1-Nup98 complex
GO:0005515 protein binding
IPI
PMID:9348540
Nup93, a vertebrate homologue of yeast Nic96p, forms a compl...
REMOVE
Summary: Nup93 complex study (Xenopus/human); Nup98 is mentioned as a basket-side nucleoporin, not as an interactor characterized in this paper.
Reason: GO:0005515 protein binding is uninformative about molecular function. Removal does not dispute the reported interaction; the functionally meaningful roles of NUP98 (FG-repeat structural constituent of the pore, mRNA export with RAE1, Nup107-160 scaffold via Nup96) are captured by other terms.
Supporting Evidence:
PMID:9348540
Two proteins have been localized to the nuclear side of the pore on or near the nuclear basket, Nup153 and Nup98.
GO:0005634 nucleus
IEA
GO_REF:0000117
ACCEPT
Summary: ARBA-predicted nuclear localization.
Reason: Correct though general; Nup98 and Nup96 are NPC components and Nup98 also has an intranuclear pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
PMID:28221134
Immunofluorescence analysis revealed that Nup98 is visible throughout the nucleoplasm, but can accumulate at intranuclear structures termed GLFG bodies
GO:0005635 nuclear envelope
IDA
PMID:15146057
The entire Nup107-160 complex, including three new members, ...
ACCEPT
Summary: Nup96 labeled at the nuclear envelope (prophase) in the Nup107-160 study.
Reason: NPC components reside in the nuclear envelope; directly observed.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
GO:0005635 nuclear envelope
IDA
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
ACCEPT
Summary: GFP-Nup98 and endogenous Nup98 at the nuclear envelope (NPCs) as well as in the nucleoplasm.
Reason: Correct; Nup98 is a nuclear pore component of the nuclear envelope.
Supporting Evidence:
PMID:28221134
Immunofluorescence analysis revealed that Nup98 is visible throughout the nucleoplasm, but can accumulate at intranuclear structures termed GLFG bodies
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-1176059
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-165043
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-165047
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-170796
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-180622
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-1855161
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-1855168
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-1855173
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-1855188
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-1855190
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-1855201
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-1855203
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-1855212
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-1855220
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-192627
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-192925
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-2990880
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-2990882
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-3000348
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-3000399
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-3000411
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-4551649
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-4551679
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-4570493
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-4615872
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-4615987
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-4655355
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-5228508
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-5228523
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-5252041
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-5661474
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-6783483
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-75096
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-75097
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-75098
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-9614367
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-9614369
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005635 nuclear envelope
TAS
Reactome:R-HSA-9708889
ACCEPT
Summary: Reactome places NUP98 (as part of the NPC) in the nuclear envelope for this reaction.
Reason: Consistent with NUP98 being an NPC constituent embedded in the nuclear envelope; general but correct.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005643 nuclear pore
IDA
PMID:12802065
Direct interaction with nup153 mediates binding of Tpr to th...
ACCEPT
Summary: Nup98 recruited to NPCs during anaphase/telophase NPC reassembly and dissociates in prophase (immunofluorescence, HeLa).
Reason: Both NUP98 products are bona fide nucleoporins; nuclear pore is the core location.
Supporting Evidence:
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005643 nuclear pore
IDA
PMID:15229283
Nucleoporins as components of the nuclear pore complex core ...
ACCEPT
Summary: Immunogold EM localizes Nup98 to NPC core regions and Nup96 is a core NPC element.
Reason: Both NUP98 products are bona fide nucleoporins; nuclear pore is the core location.
Supporting Evidence:
PMID:15229283
Immunogold-labeling for Nup98 also results in preferential labeling of NPC core regions
PMID:15229283
We show that Nup96 and Nup107 are core elements of the NPC proper that are essential for NPC assembly and docking of Nup153 and Tpr to the NPC.
GO:0005643 nuclear pore
IDA
PMID:9348540
Nup93, a vertebrate homologue of yeast Nic96p, forms a compl...
ACCEPT
Summary: Nup98 listed as a nuclear-basket-side nucleoporin in the Nup93 complex study.
Reason: Both NUP98 products are bona fide nucleoporins; nuclear pore is the core location.
Supporting Evidence:
PMID:9348540
Two proteins have been localized to the nuclear side of the pore on or near the nuclear basket, Nup153 and Nup98.
GO:0005643 nuclear pore
IEA
GO_REF:0000120
ACCEPT
Summary: Combined automated annotation of nuclear pore localization.
Reason: Both NUP98 products are bona fide nucleoporins; nuclear pore is the core location.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus, nuclear pore complex
GO:0005643 nuclear pore
NAS
PMID:10087256
A conserved biogenesis pathway for nucleoporins: proteolytic...
ACCEPT
Summary: Nup98 and Nup96 are nucleoporins generated from a common precursor; both target to the NPC.
Reason: Both NUP98 products are bona fide nucleoporins; nuclear pore is the core location.
Supporting Evidence:
PMID:10087256
Proteolytic cleavage of the precursor yields two nucleoporins: Nup98, a previously characterized GLFG-repeat containing nucleoporin, and Nup96.
PMID:10087256
Using immunoelectron microscopy, Nup96 was localized to the nucleoplasmic side of the NPC, at or near the nucleoplasmic basket.
GO:0005654 nucleoplasm
IDA
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
ACCEPT
Summary: Nup98 visible throughout the nucleoplasm and in GLFG bodies.
Reason: Intranuclear (off-pore) Nup98 pool is well established.
Supporting Evidence:
PMID:28221134
Immunofluorescence analysis revealed that Nup98 is visible throughout the nucleoplasm, but can accumulate at intranuclear structures termed GLFG bodies
GO:0005654 nucleoplasm
IDA
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
ACCEPT
Summary: Same observation as the located_in nucleoplasm row (curated with part_of relation).
Reason: Nup98 has a dynamic nucleoplasmic pool; location is correct.
Supporting Evidence:
PMID:28221134
Immunofluorescence analysis revealed that Nup98 is visible throughout the nucleoplasm, but can accumulate at intranuclear structures termed GLFG bodies
GO:0005654 nucleoplasm
IEA
GO_REF:0000120
ACCEPT
Summary: Combined automated annotation of nucleoplasm.
Reason: Consistent with experimental data.
Supporting Evidence:
PMID:28221134
Immunofluorescence analysis revealed that Nup98 is visible throughout the nucleoplasm, but can accumulate at intranuclear structures termed GLFG bodies
GO:0005654 nucleoplasm
TAS
PMID:7736573
The peptide repeat domain of nucleoporin Nup98 functions as ...
ACCEPT
Summary: Rat Nup98 cloning paper; Nup98 localizes to the nucleoplasmic side of the NPC.
Reason: Nucleoplasmic-side localization supported; intranuclear pool documented in human cells.
Supporting Evidence:
PMID:7736573
Immunoelectron microscopy showed Nup98 to be asymmetrically located at the nucleoplasmic side of the NPC.
GO:0005654 nucleoplasm
TAS
Reactome:R-HSA-2990880
ACCEPT
Summary: Reactome: NEK6/NEK7 phosphorylate NUP98 during mitotic NPC disassembly (nucleoplasm compartment).
Reason: Nucleoplasmic Nup98 is correct.
Supporting Evidence:
PMID:28221134
Immunofluorescence analysis revealed that Nup98 is visible throughout the nucleoplasm, but can accumulate at intranuclear structures termed GLFG bodies
GO:0005829 cytosol
IEA
GO_REF:0000107
MARK AS OVER ANNOTATED
Summary: IEA (Ensembl Compara) transfer of cytosol from rat Nup98.
Reason: In interphase Nup98 is at the NPC and in the nucleoplasm; there is no evidence for a distinct functional cytosolic pool in healthy cells (cytoplasmic accumulation is reported only in pathological or viral conditions). Over-annotation.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-1176059
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-141409
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-141422
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-141431
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-141439
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-1638803
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-1638821
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-165043
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-165047
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-170796
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-180622
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-1855161
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-1855168
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-1855173
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-1855188
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-1855190
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-1855201
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-1855203
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-1855212
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-1855220
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-192627
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-192925
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-2467809
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-2467811
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-2468287
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-2484822
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-2990880
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-2990882
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-3000348
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-3000399
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-3000411
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-375302
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-4551649
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-4551679
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-4570493
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-4615872
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-4615987
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-5228508
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-5228523
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-5252041
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-5661474
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-5666129
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-5666160
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-5666169
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-6783483
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-75096
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-75097
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-75098
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-9614367
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-9614369
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0005829 cytosol
TAS
Reactome:R-HSA-9615901
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-9618378
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-9634169
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-9648114
MARK AS OVER ANNOTATED
Summary: Reactome mitotic reaction (kinetochore/spindle function or NPC disassembly/reassembly) in which the Nup107-160 complex (including Nup96) or NUP98 is placed in the cytosol.
Reason: After nuclear envelope breakdown the Nup107-160 complex (containing Nup96) localizes to kinetochores and Nup98 disperses into the mitotic cytoplasm, so a transient cytosolic location during mitosis is defensible, but it is not where NUP98 performs its core function; flagged as over-annotation consistently with the other cytosol rows.
Supporting Evidence:
PMID:15146057
a specific labeling of Nup96 at kinetochores was already observed during prophase, when Nup96 is mainly localized at the nuclear envelope
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0005829 cytosol
TAS
Reactome:R-HSA-9708889
MARK AS OVER ANNOTATED
Summary: Reactome transport/SUMOylation reaction modelled with the NPC complex spanning compartments; NUP98 is assigned to the cytosol by the reaction compartment.
Reason: NUP98 acts within the nuclear pore (nucleoplasmic side, NPC core) and nucleoplasm; the cytosol assignment is an artefact of Reactome compartment modelling of NPC-mediated reactions rather than evidence of a cytosolic pool.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0006405 RNA export from nucleus
IBA
GO_REF:0000033
MODIFY
Summary: IBA for RNA export from nucleus at the GLFG nucleoporin node (yeast Nup100/Nup116/Nup145, Drosophila, Arabidopsis members).
Reason: The GLFG-nucleoporin node placement is sound and well supported for human Nup98, which binds RAE1 and NXF1 and plays its primary role in RNA export. The specific, experimentally supported process is mRNA export: Nup98 FG repeats bind the NXF1 export receptor and the RAE1-Nup98 GLEBS complex contacts the mRNP (IDA, PMID:20498086), and viral proteins block host mRNA export by targeting Nup98-RAE1. Participation test: Nup98 does part of the work of export rather than merely being required. Comparator: other FG nucleoporins on the mRNA export path (NUP214, NUP153, NUP62) carry mRNA export from nucleus. Refining this row to the child term records that specificity without adding a separate annotation that would sit beneath it as a redundant descendant.
Propagation Review
Root cause: NO FAILURE CORE
Failure modes: GRANULARITY MISMATCH
Sources checked:
PANTHER:PTN000574450 SUPPORTS TRANSFER
GLFG-nucleoporin node; RNA export is correctly inherited, and human Nup98 has direct evidence for the more specific mRNA export child.
Proposed replacements: mRNA export from nucleus
Supporting Evidence:
PMID:12191480
Nup98 is a component of the nuclear pore that plays its primary role in the export of RNAs.
PMID:20498086
Rae1 and Nup98 are evolutionarily conserved mRNA export factors
PMID:28221134
Nup98 binds to the mRNA export factors Rae1 and NXF1 (TAP) and it has been shown to mediate mRNA export
PMID:33849972
ORF6's nuclear entrapment of host mRNA is associated with its ability to copurify with the mRNA export factors, Rae1 and Nup98.
GO:0006606 protein import into nucleus
IBA
GO_REF:0000033
ACCEPT
Summary: IBA for protein import into nucleus.
Reason: Nup98 FG repeats provide docking sites for importin-cargo complexes; SARS-CoV-2 Orf6 blocks STAT nuclear import specifically by targeting Nup98.
Supporting Evidence:
PMID:7736573
Nup98 functions as one of several docking site nucleoporins in a cytosolic docking activity-mediated binding of a model transport substrate.
PMID:33097660
strongly suggesting that Orf6 specifically targets Nup98 to block STAT nuclear import
PMID:28221134
Nup98 also participates in nuclear import and export of proteins though its interaction with importin-Ξ² family members
GO:0006606 protein import into nucleus
IEA
GO_REF:0000107
ACCEPT
Summary: IEA (Ensembl Compara) for protein import into nucleus.
Reason: Consistent with experimental and IBA evidence.
Supporting Evidence:
PMID:33097660
strongly suggesting that Orf6 specifically targets Nup98 to block STAT nuclear import
GO:0006913 nucleocytoplasmic transport
IEA
GO_REF:0000002
ACCEPT
Summary: InterPro2GO mapping for nucleocytoplasmic transport.
Reason: Core process of the FG nucleoporin Nup98.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
NUP98 and NUP96 are involved in the bidirectional
file:human/NUP98/NUP98-uniprot.txt
Contains G-L-F-G repeats. The FG repeat domains in Nup98 have a
GO:0006913 nucleocytoplasmic transport
TAS
PMID:9348540
Nup93, a vertebrate homologue of yeast Nic96p, forms a compl...
ACCEPT
Summary: TAS for nucleocytoplasmic transport from the Nup93 complex paper.
Reason: Nup98 is an established FG nucleoporin mediating bidirectional transport.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
NUP98 and NUP96 are involved in the bidirectional
PMID:25562883
All Nup98 FG phases rejected inert macromolecules and yet allowed far larger NTR cargo complexes to rapidly enter.
GO:0006999 nuclear pore organization
NAS
PMID:9348540
Nup93, a vertebrate homologue of yeast Nic96p, forms a compl...
ACCEPT
Summary: NAS for nuclear pore organization.
Reason: Nup96 (from the NUP98 precursor) is a core Nup107-160 subunit essential for NPC assembly, and Nup98 cleavage is required for correct NPC targeting.
Supporting Evidence:
PMID:15229283
We show that Nup96 and Nup107 are core elements of the NPC proper that are essential for NPC assembly and docking of Nup153 and Tpr to the NPC.
GO:0016604 nuclear body
IDA
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
KEEP AS NON CORE
Summary: Nup98 accumulates at intranuclear GLFG bodies and regulates DHX9 distribution to intranuclear foci.
Reason: Supported; GLFG bodies are an intranuclear location of the off-pore Nup98 pool.
Supporting Evidence:
PMID:28221134
Immunofluorescence analysis revealed that Nup98 is visible throughout the nucleoplasm, but can accumulate at intranuclear structures termed GLFG bodies
PMID:28221134
Cells depleted of Nup98 show partial relocation of DHX9 into intranuclear foci
GO:0017056 structural constituent of nuclear pore
IBA
GO_REF:0000033
ACCEPT
Summary: IBA at the GLFG nucleoporin node. NUP98 encodes two nucleoporins: the FG-repeat Nup98 that forms the permeability barrier and the scaffold nucleoporin Nup96.
Reason: Core molecular function of both NUP98 products: Nup98 FG domain constitutes the selective permeability barrier and transport-receptor binding sites; Nup96 is a structural scaffold subunit of the NPC outer rings.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Contains G-L-F-G repeats. The FG repeat domains in Nup98 have a
PMID:25562883
The NPC barrier in Xenopus relies primarily on the intrinsically disordered FG domain of Nup98.
GO:0017056 structural constituent of nuclear pore
IEA
GO_REF:0000002
ACCEPT
Summary: InterPro2GO mapping. NUP98 encodes two nucleoporins: the FG-repeat Nup98 that forms the permeability barrier and the scaffold nucleoporin Nup96.
Reason: Core molecular function of both NUP98 products: Nup98 FG domain constitutes the selective permeability barrier and transport-receptor binding sites; Nup96 is a structural scaffold subunit of the NPC outer rings.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Contains G-L-F-G repeats. The FG repeat domains in Nup98 have a
GO:0017056 structural constituent of nuclear pore
IMP
PMID:15229283
Nucleoporins as components of the nuclear pore complex core ...
ACCEPT
Summary: RNAi of Nup96 (C-terminal precursor product) disrupts NPC assembly and Nup153/Tpr docking. NUP98 encodes two nucleoporins: the FG-repeat Nup98 that forms the permeability barrier and the scaffold nucleoporin Nup96.
Reason: Core molecular function of both NUP98 products: Nup98 FG domain constitutes the selective permeability barrier and transport-receptor binding sites; Nup96 is a structural scaffold subunit of the NPC outer rings.
Supporting Evidence:
PMID:15229283
We show that Nup96 and Nup107 are core elements of the NPC proper that are essential for NPC assembly and docking of Nup153 and Tpr to the NPC.
GO:0017056 structural constituent of nuclear pore
NAS
PMID:9348540
Nup93, a vertebrate homologue of yeast Nic96p, forms a compl...
ACCEPT
Summary: NAS from the Nup93 complex paper. NUP98 encodes two nucleoporins: the FG-repeat Nup98 that forms the permeability barrier and the scaffold nucleoporin Nup96.
Reason: Core molecular function of both NUP98 products: Nup98 FG domain constitutes the selective permeability barrier and transport-receptor binding sites; Nup96 is a structural scaffold subunit of the NPC outer rings.
Supporting Evidence:
PMID:9348540
Two proteins have been localized to the nuclear side of the pore on or near the nuclear basket, Nup153 and Nup98.
GO:0031080 nuclear pore outer ring
IDA
PMID:17360435
Cell-cycle-dependent phosphorylation of the nuclear pore Nup...
ACCEPT
Summary: Nup96 identified as a phosphorylated subunit of the Nup107-160 subcomplex.
Reason: The Nup107-160 (Y) complex forms the NPC outer rings, and Nup96 (encoded by NUP98) is a stable subunit.
Supporting Evidence:
PMID:17360435
we found that Nup107, Nup96, and Nup133 are phosphorylated during mitosis
PMID:17360435
we examined the cell-cycle-dependent phosphorylation of the Nup107-160 subcomplex, a core building block of the NPC
GO:0031080 nuclear pore outer ring
NAS
PMID:15146057
The entire Nup107-160 complex, including three new members, ...
ACCEPT
Summary: NAS: Nup96 is a constituent of the Nup107-160 complex.
Reason: Correct for the Nup96 chain.
Supporting Evidence:
PMID:15146057
indicating that most, if not all, Nup96 is stably associated with the Nup107-160 complex during the entire cell cycle
GO:0031965 nuclear membrane
EXP
PMID:10087256
A conserved biogenesis pathway for nucleoporins: proteolytic...
ACCEPT
Summary: NUP98/Nup96 detected at the nuclear rim/nuclear membrane (UniProt: nucleus membrane, peripheral; nucleoplasmic side).
Reason: NPC-associated proteins at the nuclear rim; the more precise location is nuclear pore, but nuclear membrane is acceptable.
Supporting Evidence:
PMID:10087256
Using immunoelectron microscopy, Nup96 was localized to the nucleoplasmic side of the NPC, at or near the nucleoplasmic basket.
GO:0031965 nuclear membrane
EXP
PMID:11106761
Vesicular stomatitis virus matrix protein inhibits host cell...
ACCEPT
Summary: NUP98/Nup96 detected at the nuclear rim/nuclear membrane (UniProt: nucleus membrane, peripheral; nucleoplasmic side).
Reason: NPC-associated proteins at the nuclear rim; the more precise location is nuclear pore, but nuclear membrane is acceptable.
Supporting Evidence:
PMID:11106761
Additionally, the nucleoporin Nup98 specifically interacts with M but not with M(D).
GO:0031965 nuclear membrane
EXP
PMID:12191480
The three-dimensional structure of the autoproteolytic, nucl...
ACCEPT
Summary: NUP98/Nup96 detected at the nuclear rim/nuclear membrane (UniProt: nucleus membrane, peripheral; nucleoplasmic side).
Reason: NPC-associated proteins at the nuclear rim; the more precise location is nuclear pore, but nuclear membrane is acceptable.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus membrane
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0031965 nuclear membrane
EXP
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
ACCEPT
Summary: NUP98/Nup96 detected at the nuclear rim/nuclear membrane (UniProt: nucleus membrane, peripheral; nucleoplasmic side).
Reason: NPC-associated proteins at the nuclear rim; the more precise location is nuclear pore, but nuclear membrane is acceptable.
Supporting Evidence:
PMID:28221134
Immunofluorescence analysis revealed that Nup98 is visible throughout the nucleoplasm, but can accumulate at intranuclear structures termed GLFG bodies
GO:0031965 nuclear membrane
EXP
PMID:33360543
Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 an...
ACCEPT
Summary: NUP98/Nup96 detected at the nuclear rim/nuclear membrane (UniProt: nucleus membrane, peripheral; nucleoplasmic side).
Reason: NPC-associated proteins at the nuclear rim; the more precise location is nuclear pore, but nuclear membrane is acceptable.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus membrane
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0031965 nuclear membrane
IDA
PMID:11839768
Tpr is localized within the nuclear basket of the pore compl...
ACCEPT
Summary: NUP98/Nup96 detected at the nuclear rim/nuclear membrane (UniProt: nucleus membrane, peripheral; nucleoplasmic side).
Reason: NPC-associated proteins at the nuclear rim; the more precise location is nuclear pore, but nuclear membrane is acceptable.
Supporting Evidence:
PMID:11839768
The nuclear basket proteins Nup98 and Nup153 and the cytoplasmic fibril protein Nup358 also were localized at the NE and in intranuclear foci
GO:0031965 nuclear membrane
IDA
PMID:12802065
Direct interaction with nup153 mediates binding of Tpr to th...
ACCEPT
Summary: NUP98/Nup96 detected at the nuclear rim/nuclear membrane (UniProt: nucleus membrane, peripheral; nucleoplasmic side).
Reason: NPC-associated proteins at the nuclear rim; the more precise location is nuclear pore, but nuclear membrane is acceptable.
Supporting Evidence:
PMID:12802065
NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase.
GO:0031965 nuclear membrane
IDA
PMID:15229283
Nucleoporins as components of the nuclear pore complex core ...
ACCEPT
Summary: NUP98/Nup96 detected at the nuclear rim/nuclear membrane (UniProt: nucleus membrane, peripheral; nucleoplasmic side).
Reason: NPC-associated proteins at the nuclear rim; the more precise location is nuclear pore, but nuclear membrane is acceptable.
Supporting Evidence:
PMID:15229283
Immunogold-labeling for Nup98 also results in preferential labeling of NPC core regions
GO:0031965 nuclear membrane
IDA
PMID:20407419
Protein Tpr is required for establishing nuclear pore-associ...
ACCEPT
Summary: NUP98/Nup96 detected at the nuclear rim/nuclear membrane (UniProt: nucleus membrane, peripheral; nucleoplasmic side).
Reason: NPC-associated proteins at the nuclear rim; the more precise location is nuclear pore, but nuclear membrane is acceptable.
Supporting Evidence:
PMID:20407419
In human HeLa cells though, both the FG-repeat and the NPC-anchor domains of Nup98 were found at the NPC proper
GO:0031965 nuclear membrane
IEA
GO_REF:0000120
ACCEPT
Summary: NUP98/Nup96 detected at the nuclear rim/nuclear membrane (UniProt: nucleus membrane, peripheral; nucleoplasmic side).
Reason: NPC-associated proteins at the nuclear rim; the more precise location is nuclear pore, but nuclear membrane is acceptable.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Nucleus membrane
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0034398 telomere tethering at nuclear periphery
IBA
GO_REF:0000033
MARK AS OVER ANNOTATED
Summary: IBA for telomere tethering at nuclear periphery, inherited from yeast GLFG nucleoporin evidence.
Reason: No evidence in the reviewed literature for a role of human Nup98 or Nup96 in tethering telomeres to the nuclear periphery; peripheral telomere anchoring is a feature documented in budding yeast, and the cached human literature does not support transfer of this specific process. Retained only as an over-annotation flag rather than removal, given the phylogenetic basis.
Propagation Review
Root cause: UNRESOLVED
Sources checked:
PANTHER:PTN000574450 UNRESOLVED
GLFG nucleoporin ancestral node carrying the telomere-tethering IBD; placement appears driven by budding-yeast evidence and no human or other metazoan experimental support was found in the reviewed literature.
SGD:S000003060 UNRESOLVED
Yeast GLFG nucleoporin donor; experimental yeast evidence not re-examined here, and whether peripheral telomere tethering is conserved in the vertebrate Nup98/Nup96 lineage is unresolved.
GO:0034399 nuclear periphery
IDA
PMID:11839768
Tpr is localized within the nuclear basket of the pore compl...
ACCEPT
Summary: Nup98 localizes at the nuclear periphery (NPCs).
Reason: Correct; NPC localization.
Supporting Evidence:
PMID:11839768
The nuclear basket proteins Nup98 and Nup153 and the cytoplasmic fibril protein Nup358 also were localized at the NE and in intranuclear foci
GO:0034399 nuclear periphery
IDA
PMID:15229283
Nucleoporins as components of the nuclear pore complex core ...
ACCEPT
Summary: Nup98 localizes at the nuclear periphery (NPCs).
Reason: Correct; NPC localization.
Supporting Evidence:
PMID:15229283
Immunogold-labeling for Nup98 also results in preferential labeling of NPC core regions
GO:0034399 nuclear periphery
IEA
GO_REF:0000107
ACCEPT
Summary: Nup98 localizes at the nuclear periphery (NPCs).
Reason: Correct; NPC localization.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0042277 peptide binding
IEA
GO_REF:0000107
REMOVE
Summary: IEA transfer of peptide binding from rat Nup98 (P49793).
Reason: The Nup98 FG domain provides docking sites for transport receptors carrying cargo; it does not bind peptides as such. The rat-based term is uninformative and misleading for the FG nucleoporin function, which is captured by structural constituent of nuclear pore.
Supporting Evidence:
PMID:7736573
Nup98 functions as one of several docking site nucleoporins in a cytosolic docking activity-mediated binding of a model transport substrate.
GO:0042405 nuclear inclusion body
IDA
PMID:11839768
Tpr is localized within the nuclear basket of the pore compl...
MODIFY
Summary: Nup98 observed in intranuclear foci (GLFG bodies) in HeLa cells.
Reason: GO:0042405 nuclear inclusion body denotes foci of sequestered aggregated protein; GLFG bodies are dynamic intranuclear bodies, better captured by nuclear body (GO:0016604), which is already used for this location.
Proposed replacements: nuclear body
Supporting Evidence:
PMID:11839768
The nuclear basket proteins Nup98 and Nup153 and the cytoplasmic fibril protein Nup358 also were localized at the NE and in intranuclear foci
GO:0042405 nuclear inclusion body
IEA
GO_REF:0000107
MODIFY
Summary: IEA transfer of nuclear inclusion body from rat Nup98.
Reason: As above; intranuclear GLFG bodies are nuclear bodies, not aggregate inclusion bodies.
Proposed replacements: nuclear body
Supporting Evidence:
PMID:28221134
Immunofluorescence analysis revealed that Nup98 is visible throughout the nucleoplasm, but can accumulate at intranuclear structures termed GLFG bodies
GO:0044614 nuclear pore cytoplasmic filaments
IBA
GO_REF:0000033
KEEP AS NON CORE
Summary: IBA for nuclear pore cytoplasmic filaments, from yeast Nup100/Nup116-type members.
Reason: Vertebrate Nup98 interacts with the cytoplasmic filament nucleoporins NUP88 and NUP214 (UniProt, by similarity) and is mobile across the pore, but human Nup98 is concentrated on the nucleoplasmic side and in the NPC core. Non-core location.
Supporting Evidence:
file:human/NUP98/NUP98-uniprot.txt
Localized to the nucleoplasmic side of the nuclear pore complex
GO:0044615 nuclear pore nuclear basket
IDA
PMID:11839768
Tpr is localized within the nuclear basket of the pore compl...
ACCEPT
Summary: Immunogold EM: Nup98 is a nuclear basket component with Nup153.
Reason: Directly supported.
Supporting Evidence:
PMID:11839768
Since the distribution of Tpr is very similar to that of the well-recognized nuclear basket components Nup153 and Nup98, this strongly suggests that Tpr is an element of the nuclear basket.
GO:0044615 nuclear pore nuclear basket
IEA
GO_REF:0000107
ACCEPT
Summary: IEA (Ensembl Compara) nuclear basket.
Reason: Consistent with experimental data.
Supporting Evidence:
PMID:11839768
Since the distribution of Tpr is very similar to that of the well-recognized nuclear basket components Nup153 and Nup98, this strongly suggests that Tpr is an element of the nuclear basket.
GO:0045893 positive regulation of DNA-templated transcription
IEA
GO_REF:0000108
KEEP AS NON CORE
Summary: IEA inferred from the transcription coactivator activity annotation.
Reason: Nup98 supports DHX9-stimulated transcription and regulates gene expression off the pore; non-core.
Supporting Evidence:
PMID:28221134
Importantly, binding of Nup98 stimulates the ATPase activity of DHX9, and a transcriptional reporter assay suggests Nup98 supports DHX9-stimulated transcription.
GO:0048026 positive regulation of mRNA splicing, via spliceosome
IMP
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
KEEP AS NON CORE
Summary: Nup98 depletion alters DHX9-dependent alternative splicing.
Reason: Supported by IMP; an indirect, DHX9-mediated effect on splicing, non-core.
Supporting Evidence:
PMID:28221134
Their interactions ultimately influence gene expression at the level of DHX9-mediated transcription and splicing.
GO:0051292 nuclear pore complex assembly
IMP
PMID:15229283
Nucleoporins as components of the nuclear pore complex core ...
ACCEPT
Summary: Nup96 RNAi blocks NPC assembly in HeLa cells.
Reason: Nup96 (NUP98 precursor product) is essential for NPC assembly as a Nup107-160 complex scaffold subunit.
Supporting Evidence:
PMID:15229283
We show that Nup96 and Nup107 are core elements of the NPC proper that are essential for NPC assembly and docking of Nup153 and Tpr to the NPC.
GO:0140597 protein carrier activity
IEA
GO_REF:0000107
REMOVE
Summary: IEA transfer of protein carrier activity from rat Nup98.
Reason: FG nucleoporins provide a stationary selective phase and binding sites; it is the shuttling transport receptors (importins/exportins) that carry and deliver cargo. Nup98 is not a cargo carrier.
Supporting Evidence:
PMID:25562883
All Nup98 FG phases rejected inert macromolecules and yet allowed far larger NTR cargo complexes to rapidly enter.
PMID:7736573
Nup98 functions as one of several docking site nucleoporins in a cytosolic docking activity-mediated binding of a model transport substrate.
GO:0140693 molecular condensate scaffold activity
IDA
PMID:25562883
Nup98 FG domains from diverse species spontaneously phase-se...
ACCEPT
Summary: Human and other Nup98 FG domains spontaneously phase-separate into FG particles with NPC-like permselectivity.
Reason: Cohesive FG-repeat phase formation is the biophysical basis of the Nup98-dominated NPC permeability barrier; IDA for condensate scaffolding is well supported.
Supporting Evidence:
PMID:25562883
Nup98 FG domains of mammals, lancelets, insects, nematodes, fungi, plants, amoebas, ciliates, and excavates spontaneously and rapidly phase-separate
PMID:25562883
All Nup98 FG phases rejected inert macromolecules and yet allowed far larger NTR cargo complexes to rapidly enter.
PMID:25562883
The NPC barrier in Xenopus relies primarily on the intrinsically disordered FG domain of Nup98.
GO:1990841 promoter-specific chromatin binding
IMP
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
KEEP AS NON CORE
Summary: Nup98 binds promoter regions of target genes interdependently with DHX9 (ChIP).
Reason: Supported; off-pore gene regulatory role.
Supporting Evidence:
PMID:28221134
Nup98 and DHX9 bind interdependently to similar gene loci and their transcripts
PMID:28221134
One such nucleoporin, Nup98, binds chromatin and regulates gene expression.
GO:1990904 ribonucleoprotein complex
IMP
PMID:28221134
Human Nup98 regulates the localization and activity of DExH/...
KEEP AS NON CORE
Summary: Nup98 associates with DHX9-containing RNP complexes on transcripts.
Reason: Supported for the intranuclear pool; Nup98 is also part of the RAE1-Nup98 mRNA export complex.
Supporting Evidence:
PMID:28221134
Nup98 and DHX9 bind interdependently to similar gene loci and their transcripts
PMID:20498086
we demonstrate that the complex possesses single-stranded RNA-binding capability
GO:0016540 protein autoprocessing
IDA
PMID:12191480
The three-dimensional structure of the autoproteolytic, nucl...
NEW
Summary: The NUP98 precursor (Nup98-Nup96 and Nup98-only forms) is cleaved autoproteolytically by its own C-terminal domain, which adopts a novel autocatalytic protease fold.
Reason: The gene product itself performs the cleavage (autoprocessing is the case where the substrate does the work), and cleavage is required for correct NPC targeting of Nup98 and Nup96.
Supporting Evidence:
PMID:12191480
Both forms are processed into two peptides through autoproteolysis mediated by the C-terminal domain of hNup98.
PMID:10087256
Proteolytic cleavage of the precursor yields two nucleoporins: Nup98, a previously characterized GLFG-repeat containing nucleoporin, and Nup96.

Core Functions

FG-repeat nucleoporin forming the NPC selective permeability barrier. The intrinsically disordered FG/GLFG-repeat domain of Nup98 assembles into a cohesive, phase-separated FG meshwork in the NPC that excludes inert macromolecules while providing low-affinity binding sites that allow nuclear transport receptor-cargo complexes to translocate, thereby mediating bidirectional nucleocytoplasmic transport including importin-dependent protein import. Nup98 resides at the nucleoplasmic side/NPC core and nuclear basket region.

Supporting Evidence:
  • PMID:25562883
    The NPC barrier in Xenopus relies primarily on the intrinsically disordered FG domain of Nup98.
  • PMID:25562883
    All Nup98 FG phases rejected inert macromolecules and yet allowed far larger NTR cargo complexes to rapidly enter.
  • PMID:7736573
    Nup98 functions as one of several docking site nucleoporins in a cytosolic docking activity-mediated binding of a model transport substrate.
  • PMID:33097660
    strongly suggesting that Orf6 specifically targets Nup98 to block STAT nuclear import
  • file:human/NUP98/NUP98-uniprot.txt
    Contains G-L-F-G repeats. The FG repeat domains in Nup98 have a

mRNA export factor at the NPC. Through its GLEBS motif Nup98 binds RAE1, forming a RAE1-Nup98 complex that binds single-stranded RNA and mRNPs, and its FG repeats bind the mRNA export receptor NXF1; this complex is the target by which VSV M and SARS-CoV-2 ORF6 block host mRNA export.

Directly Involved In:
Cellular Locations:
In Complex:
nuclear pore
Supporting Evidence:
  • PMID:20498086
    Rae1 and Nup98 are evolutionarily conserved mRNA export factors
  • PMID:20498086
    we demonstrate that the complex possesses single-stranded RNA-binding capability
  • PMID:28221134
    Nup98 binds to the mRNA export factors Rae1 and NXF1 (TAP) and it has been shown to mediate mRNA export
  • PMID:33849972
    ORF6's nuclear entrapment of host mRNA is associated with its ability to copurify with the mRNA export factors, Rae1 and Nup98.

Scaffold nucleoporin Nup96 (C-terminal product of the autoproteolytically processed NUP98 precursor). Nup96 is a stable subunit of the Nup107-160 (Y) complex forming the NPC outer rings and is essential for NPC assembly and for docking Nup153 and Tpr to the pore.

Supporting Evidence:
  • PMID:15229283
    We show that Nup96 and Nup107 are core elements of the NPC proper that are essential for NPC assembly and docking of Nup153 and Tpr to the NPC.
  • PMID:15146057
    indicating that most, if not all, Nup96 is stably associated with the Nup107-160 complex during the entire cell cycle
  • PMID:10087256
    Proteolytic cleavage of the precursor yields two nucleoporins: Nup98, a previously characterized GLFG-repeat containing nucleoporin, and Nup96.

Off-pore cofactor of the RNA helicase DHX9. Intranuclear Nup98 (nucleoplasm and GLFG bodies) binds DHX9 in an RNA-facilitated manner, stimulates its ATPase activity, and co-occupies target gene loci and transcripts, supporting DHX9-dependent transcription and splicing.

Molecular Function:
ATPase activator activity
Cellular Locations:
Supporting Evidence:
  • PMID:28221134
    Importantly, binding of Nup98 stimulates the ATPase activity of DHX9, and a transcriptional reporter assay suggests Nup98 supports DHX9-stimulated transcription.
  • PMID:28221134
    We demonstrate that Nup98 binds DHX9 in the nucleoplasm, regulates the nuclear distribution of DHX9, and influences DHX9 RNA-binding and ATPase activity.
  • PMID:28221134
    Nup98 and DHX9 bind interdependently to similar gene loci and their transcripts

References

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Suggested Questions for Experts

Q: In human NPCs, what fraction of the permeability barrier is contributed by the Nup98 FG domain relative to NUP62-complex and other FG nucleoporins, and is the Nup98 FG phase in vivo a condensate-like cohesive meshwork as in vitro?

Q: Should GO annotations to P52948 be split by cleavage product (Nup98 chain PRO_0000019929 vs Nup96 chain PRO_0000019930), given that Nup107-160 complex, outer ring and kinetochore annotations apply only to Nup96 while FG-barrier and mRNA-export annotations apply only to Nup98?

Q: Does human Nup98 tether recently repressed or inducible genes to the nuclear periphery, as its yeast orthologs do, or does its transcriptional memory role occur entirely in the nucleoplasm?

Q: Is cytoplasmic mislocalization of Nup98 seen in degenerating neurons a cause or a consequence of nucleocytoplasmic transport failure, and does it reflect loss of Nup98 from the FG barrier of individual pores?

Suggested Experiments

Experiment: Acute degron-mediated depletion of Nup98 (or replacement with FG-domain-deleted Nup98) in human cells, followed by measurement of passive leakage of inert dextrans/GFP multimers and receptor-mediated import/export kinetics, and cryo-ET of the central channel.

Hypothesis: The Nup98 FG domain is the dominant constituent of the permeability barrier in human NPCs.

Type: genetic perturbation with transport assay

Experiment: Steady-state ATPase kinetics of purified DHX9 with titrated recombinant Nup98 FG/GLFG fragments, FG-to-SG mutants, and RNA substrates, to determine whether Nup98 alters kcat, Km or RNA affinity.

Hypothesis: Nup98 activates DHX9 ATPase by direct allosteric stimulation through its FG/GLFG region.

Type: biochemical assay

πŸ“š Additional Documentation

Notes

(NUP98-notes.md)

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