Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Automatic assignment of GO terms using logical inference, based on on inter-ontology links

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.

Vesicular stomatitis virus matrix protein inhibits host cell gene expression by targeting the nucleoporin Nup98.

Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export.

The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98.

Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex.

The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis.

Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket.

Rae1 interaction with NuMA is required for bipolar spindle formation.

Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 subcomplex.

Cohesin subunit SMC1 associates with mitotic microtubules at the spindle pole.

Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion.

Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1.

Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity.

Human Nup98 regulates the localization and activity of DExH/D-box helicase DHX9.

Biallelic mutations in nucleoporin NUP88 cause lethal fetal akinesia deformation sequence.

A SARS-CoV-2 protein interaction map reveals targets for drug repurposing.

Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.

SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling.

Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex.

Sarbecovirus ORF6 proteins hamper induction of interferon signaling.

SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98.

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1-Nup98 Complex to Compete With mRNA Nuclear Export.

The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex.

Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly.

Translocation of Influenza A virus nonstructural protein 1 (NS1A) into the nucleus

Mad1 binds kinetochore

MAD2 converted to an inhibitory state via interaction with Mad1

MAD2 associates with the Mad1 kinetochore complex

Release of activated MAD2 from kinetochores

Phosphorylation of cohesin by PLK1 at centromeres

PP2A-B56 dephosphorylates centromeric cohesin

Rev multimer-bound HIV mRNA:Crm1:Ran:GTP complex associates with the NPC

Translocation of nuclear RNA transport complex to cytoplasm

NPC transports GCK1:GCKR from cytosol to nucleoplasm

Vpr binds nucleoporins

I(1,3,4,5,6)P5 transports from the nucleus to the cytosol

I(1,3,4,5)P4 transports from the cytosol to the nucleus

5-PP-IP4 transports from the nucleus to the cytosol

IP6 transports from the cytosol to the nucleus

I(1,4,5)P3 transports from the cytosol to the nucleus

I(1,3,4,6)P4 transports from the cytosol to the nucleus

5-PP-IP5 transports from the nucleus to the cytosol

1/3-PP-IP5 transports from the cytosol to the nucleus

(PP)2-IP4 transports from the nucleus to the cytosol

Viral mRNA Export

Export of Spliced Viral mRNA

ESPL1 (Separase) cleaves centromeric cohesin

Separation of sister chromatids

CDK1 phosphorylates CDCA5 (Sororin) at centromeres

Kinetochore assembly

NEK6/NEK7 phosphorylates NUP98

CDK1 phosphorylates NUP98

RANBP2 SUMOylates SP100 with SUMO2

RANBP2 SUMOylates SP100 with SUMO1

RANBP2 SUMOylates PML with SUMO2

Kinetochore capture of astral microtubules

RANBP2 SUMOylates RANBP2 with SUMO1

RANBP2 SUMOylates RANBP2 with SUMO2

RANBP2 (NUP358) SUMOylates HNRNPC with SUMO1

RANBP2 SUMOylates HDAC4 with SUMO1

RANBP2 SUMOylates HDAC4 with SUMO2,3

RANBP2 SUMOylates CDCA8 (Borealin) and PIAS3 SUMOylates AURKB (Aurora-B)

RANBP2 SUMOylates PML with SUMO1

RANBP2 SUMOylates MDM2 with SUMO1

NPC transports Hikeshi:HSP70s:ATP from cytosol to nucleoplasm

Defective NPC does not transport GCK1:GKRP from cytosol to nucleoplasm

CDC42:GTP recruits DIAPH2-2 to kinetochores

AURKB phosphorylates DIAPH2-2 at kinetochores

Kinetochore capture of astral microtubules is positively regulated by CDC42:GTP:p-S196-DIAPH2-2

tRNA:XPOT:RAN:GTP translocates from the nucleus to the cytosol

Docking of the TAP:EJC Complex with the NPC

Transport of the export-competent mRNP complex through the NPC

mRNP complex dissociates from cytosolic face of NPC

HCMV Nuclear Pore Docking

Transport of HCMV DNA Into the Nucleus

AHCTF1 (ELYS) binds chromatin and Nup107-Nup160 complex

POM121 binds the Nup107-Nup160 complex

POM121 and NDC1 bind the Nup93 complex

EML4 recruits NUDC to mitotic spindle

SARS-CoV-2 6 binds NUP98:RAE1 within NPC