Q96P70: Importin-9 (IPO9)

Importin-9 (IPO9) is a 1041-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96P70.

Gene
IPO9
Organism
Homo sapiens
Length
1041 residues
Mean pLDDT
88.3
Model
AF-Q96P70-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate73%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

Nuclear transport receptor that mediates nuclear import of proteins, such as histones, proteasome and actin (PubMed:11823430, PubMed:30855230, PubMed:34711951). Serves as receptor for nuclear localization signals (NLS) in cargo substrates (PubMed:11823430). Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11823430). At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP…

Subunit structure

Interacts with histones H2A, H2B, H3 and H4 (PubMed:11823430, PubMed:30855230). The binding is coupled to RanGTP cycles (PubMed:11823430). Interacts with AKIRIN2; promoting association with pre-assembled proteasomes (PubMed:34711951). Associates with pre-assembled proteasomes; interaction is indirect and mediated via interaction with AKIRIN2 (PubMed:34711951). Interacts with PPP2R1A and PPP2R1B…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6N1ZX-ray2.7 ÅA/D=1-1041
9QONEM3.2 ÅA=1-1041
9QOOEM3.3 ÅA=1-1041
9QOPEM3.7 ÅA=1-1041
8F7AEM3.78 ÅA=1-1041
9QNOEM4.2 ÅA=1-1041

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