Q96Q15: Serine/threonine-protein kinase SMG1 (SMG1)

Serine/threonine-protein kinase SMG1 (SMG1) is a 2392-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96Q15.

Gene
SMG1
Organism
Homo sapiens
Length
2392 residues
Mean pLDDT
76.9
Model
AF-Q96Q15-4-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.9 (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 accurate16%
70 to 90Confident: backbone generally right62%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Also acts as a…

Subunit structure

Component of the SMG1C complex composed of SMG1, SMG8 and SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large conformational change in the SMG1 C-terminal head domain containing the catalytic domain (PubMed:33205750). Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Part of a complex composed of SMG1, DHX34 and UPF1; within the complex DHX34 acts as a scaffolding…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7PW8EM2.82 ÅA=311-3661
6Z3REM2.97 ÅA=259-3661
7PW6EM3.05 ÅA=766-3661
7PW9EM3.12 ÅA=311-3661
7PW4EM3.27 ÅA=311-3661
7PW5EM3.4 ÅA=311-3661
6L54EM3.43 ÅA=1-3661
6SYTEM3.45 ÅA=311-3661
7PW7EM3.59 ÅA=311-3661
6L53EM3.63 ÅA=1-3661

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