Function
Locations
Autoproteolytic precursor of the FG-repeat nucleoporin Nup98, which lines the pore's permeability barrier, and the Y-complex scaffold subunit Nup96.
Proteins and RNAs cross the nuclear envelope through nuclear pore complexes, built from nucleoporins that form a scaffold of stacked rings and a central channel lined with FG repeats. Karyopherins of the importin-beta superfamily carry cargo through the channel, and the small GTPase Ran sets the direction: Ran-GTP, made in the nucleus by RCC1, releases import cargo and loads export cargo, while Ran-GDP is returned to the nucleus by NTF2. This module is the eukaryote-wide part of that system that can be grounded locally, written so that it can be evaluated in any genome.
Eukaryote-wide scope: PAINT places the NTF2, Nup88, Cse1 (exportin-2) and Crm1-specific exportin-1 nodes at Eukaryota (taxon:2759); the Seh1/Sec13 outer-ring node and the exportin-1/5 receptor node carry no taxon in the source rows, and their seeds are listed on each node. The Ran and Nup98 families have no PAINT table locally and their selectors rest on family membership. Each cited node is shown to be an ancestor of the human protein by its IBA rows or its IBD seeds (for Cse1, which has no gene folder, by its IBA rows in QuickGO). Read as a satisfiability rule, every part is expected in any eukaryote. Molecular functions come from the human NUP98 review and from the F IBD of the exportin nodes (nuclear export signal receptor activity for both; the Cse1 node records the loss of the import-receptor activity it would otherwise inherit); Ran, NTF2, Nup88, Seh1 and Sec13 are untyped. This is a partial rule. Many required parts of the system have no local PANTHER entry for the human protein, so they cannot be family selectors in this rule: importin beta (KPNB1) and importin alpha, RCC1, RanGAP and RanBP1, and most scaffold and FG nucleoporins (NUP93, NUP205, NUP155, NUP160, NUP107, NUP85, NUP62 and others). The importins, RCC1, RanGAP1 and RanBP1 are modelled in karyopherin_nuclear_protein_import, grounded on UniProt accessions and literature rather than PANTHER families; that module also types human RAN as GTPase activity, while the Ran step here stays untyped because its family has no PAINT table or family review locally. A genome that passes this rule has therefore not been shown to have a complete pore. Selector caveats are on each family: Seh1 and Sec13 also work outside the pore, the NTF2 family takes in NXT1/NXT2, and no Dictyostelium member is listed for Nup88 or Seh1 and no Arabidopsis member for Sec13. The modules dmel_nuclear_pore_complex (Drosophila) and mrna_nuclear_export (human) describe the pore and mRNA export in one species, and karyopherin_nuclear_protein_import describes the import cycle.
All recommended fields populated.
✗ none found
No MODULE:nuclear_pore_transport_core deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
1 gene-function check(s) reflected in core functions · 0 conflict(s) · 5 evidence or coverage gap(s) (6 comparison(s))
Retained noncore functions are reported separately; they do not require promotion to core functions. Support from representative genes does not establish conservation across the whole family. Missing reviews or identifiers leave a claim unverified.
| Annoton | Participant | Function | Assessment |
|---|---|---|---|
| nup98_96 | NUP98 (human) UniProtKB:P52948 Family Representative |
structural constituent of nuclear pore GO:0017056 |
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass). |
| crm1_exportin | XPO1 (human) UniProtKB:O14980 Family Representative |
nuclear export signal receptor activity GO:0005049 |
Review Missing
No ai-review exists for this protein; its function and core-function coverage cannot yet be checked. |
| cse1_exportin | CSE1L (human) UniProtKB:P55060 Family Representative |
nuclear export signal receptor activity GO:0005049 |
Review Missing
No ai-review exists for this protein; its function and core-function coverage cannot yet be checked. |
| nup98_96 | Nup98-Nup96 subfamily PANTHER:PTHR23198:SF6 Family |
structural constituent of nuclear pore GO:0017056 |
Family Review Missing
No supported structured family review is available for PANTHER:PTHR23198:SF6. |
| crm1_exportin | Exportin-1 subfamily PANTHER:PTHR11223:SF2 Family |
nuclear export signal receptor activity GO:0005049 |
Family Function Unreviewed
The family review has no applicable adjudication supporting or excluding GO:0005049. |
| cse1_exportin | Exportin-2 subfamily PANTHER:PTHR10997:SF8 Family |
nuclear export signal receptor activity GO:0005049 |
Family Function Unreviewed
The family review has no applicable adjudication supporting or excluding GO:0005049. |
1 complete review(s) · 0 with deep research · 7 missing review · 1 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| NUP98 P52948 | ✓ | ✓ | ✗ |
| XPO1 (human) O14980 | ✗ | — | — |
| CSE1L (human) P55060 | ✗ | — | — |
| SEC13 (human) P55735 | ✗ | — | — |
| NUTF2 (human) P61970 | ✗ | — | — |
| RAN (human) P62826 | ✗ | — | — |
| SEH1L (human) Q96EE3 | ✗ | — | — |
| NUP88 (human) Q99567 | ✗ | — | — |
Autoproteolytic precursor of the FG-repeat nucleoporin Nup98, which lines the pore's permeability barrier, and the Y-complex scaffold subunit Nup96.
Beta-propeller nucleoporin of the cytoplasmic filaments that anchors the Nup214/Nup159 complex.
Beta-propeller subunit of the Y-complex (outer ring) scaffold.
Beta-propeller subunit of the Y-complex scaffold; it is also the inner subunit of the COPII outer coat.
Small GTPase whose GTP-bound form, kept nuclear by chromatin-bound RCC1, sets the direction of karyopherin transport.
Small dimeric carrier that returns Ran-GDP from the cytoplasm to the nucleus through the pore.
Exportin that binds leucine-rich nuclear export signals together with Ran-GTP and carries proteins and some RNAs out of the nucleus.
Exportin that returns importin alpha to the cytoplasm in complex with Ran-GTP, recycling the classical import receptor.