O14893: Gem-associated protein 2 (GEMIN2)

Gem-associated protein 2 (GEMIN2) is a 280-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14893.

Gene
GEMIN2
Organism
Homo sapiens
Length
280 residues
Mean pLDDT
80.8
Model
AF-O14893-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.8 (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 accurate42%
70 to 90Confident: backbone generally right37%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:18984161, PubMed:9323129). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (PubMed:18984161). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). To…

Subunit structure

Monomer (PubMed:26092730). Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:11714716, PubMed:16314521, PubMed:17178713, PubMed:9323129). Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2,…

Subcellular location

Nucleus, gem, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5XJLX-ray2.5 Å2=1-280
5XJUX-ray2.58 Å2=40-280
5XJTX-ray2.92 Å2=1-280
5XJRX-ray3.12 Å2=40-280
5XJQX-ray3.28 Å2=1-280
5XJSX-ray3.38 Å2=40-280
2LEHNMRA=95-280

More AlphaFold highlights

About this viewer

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