Q9UQ13: Leucine-rich repeat protein SHOC-2 (SHOC2)

Leucine-rich repeat protein SHOC-2 (SHOC2) is a 582-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UQ13.

Gene
SHOC2
Organism
Homo sapiens
Length
582 residues
Mean pLDDT
87.5
Model
AF-Q9UQ13-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.5 (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 accurate83%
70 to 90Confident: backbone generally right2%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates activation of the MAPK pathway (PubMed:10783161, PubMed:16630891, PubMed:25137548, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). Acts as a scaffolding protein in the SMP complex (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:10783161, PubMed:16630891, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex enhances the…

Subunit structure

Component of the SHOC2-MRAS-PP1c (SMP) complex consisting of SHOC2, GTP-bound M-Ras/MRAS and the catalytic subunit of protein phosphatase 1 (either PPP1CA, PPP1CB or PPP1CC) (PubMed:16630891, PubMed:25137548, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). SHOC2 and PP1c preferably bind M-Ras/MRAS, but they also bind K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS; these interactions…

Subcellular location

Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7T7AX-ray1.79 ÅA/B=88-581
7TYGX-ray1.9 ÅA/B=80-582
7TXHX-ray1.95 ÅB/E=80-582
9BTNX-ray2.04 ÅA=80-582
7TVFX-ray2.17 ÅA/D=2-582
9BTPX-ray2.37 ÅA=80-582
7TVGX-ray2.4 ÅD=59-564
9OVJX-ray2.68 ÅA=80-582
9BTMX-ray2.73 ÅB=80-582
7UPIEM2.89 ÅC=1-582
7SD0EM2.95 ÅA=2-582
9O65EM3.0 ÅA=1-582
7SD1X-ray3.19 ÅA/B/C/D=2-582

More AlphaFold highlights

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