Proteins / SOS2
SOS2
Son of sevenless homolog 2
GEF
UniProt Q07890
HSP90 client (literature): unknown
3D structure ↓
13 interaction partners · volcano ↗
Abundance under HSP90 inhibition (pimitespib). The HSP90 calls compare each variant's inhibited and untreated abundance. Scores are WT-relative: 1 = wild type.
8,572 variantsmissense decreased 27% · increased 5%HSP90-dependent 0% of missense & deletionsbuffered 13% · poorly buffered 17% · WT-like or increased 70%
Other cells fade; highlighted cells are outlined.
Annotation tracks
Structure
Function
Chaperone
Variant effect
Track legend & definitions
Secondary structure
alpha helix3-10 helixpi helixbeta strandbeta bridgeturnbendno_ss
DSSP assignment on the reference structure.
Relative SASA
0.000.250.500.751.00
Side-chain solvent accessibility (0 = buried, 1 = fully exposed). The pipeline calls a residue surface-exposed above 0.25.
pLDDT
50.062.575.087.5100.0
AlphaFold per-residue confidence. The analysis drops residues below 60.
Curated feature
Protein-protein interfaceCatalytic / active siteLigand / substrate pocketRegulatory elementOther annotation
UniProt / literature annotation, coloured by class. Red marks a curated protein-protein interface — the independent comparison for our predicted interfaces.
Annotated interface
yesno
Curated protein-interface residue, independent of any structure prediction in this study.
Active site
yesno
Curated catalytic / active-site residue.
Inter-domain contact
yesno
Residue contacting another domain of the same protein (all-atom), so a variant effect there may be intramolecular rather than at a PPI.
HSP90 contact
TrueFalseUnknown
Contacts HSP90 in the chaperone-client cryo-EM structures ('Unknown' where the protein was not mapped).
CDC37 contact
TrueFalseUnknown
Contacts CDC37. These positions report kinase foldability rather than a canonical binding surface.
Fraction buffered
0%25%50%75%100%
Fraction of variants at this position that are buffered: wild-type-like untreated but decreased under HSP90 inhibition (HSP90i condition only).
Fraction HSP90-dependent
0%25%50%75%100%
Fraction of variants at this position whose abundance falls under HSP90 inhibition by at least the wild-type-to-synonymous gap (the paper's dependence call; HSP90i condition only).
Fraction decreased
0%25%50%75%100%
Fraction of variants at this position classified decreased in this assay (2.5th-percentile rule).
Fraction increased
0%25%50%75%100%
Fraction of variants at this position classified increased in this assay.
Click a position for its interactions and annotations
— ■ the Interface strip marks
positions in ≥1 supported interface (darker = more partners)
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One row per interface: complexes of the same pair and source whose interfaces overlap (IoU ≥ 0.3) are merged, as in the Fig. 6c,d volcano plots (median Cohen's d; q from the geometric-mean p). Supported: at least one complex with q < 0.05 and |d| ≥ 0.2 in either basal assay.
| Partner | Source | Activity d | q | Abundance d | q | Interface positions | Supported | |
|---|---|---|---|---|---|---|---|---|
| RAP1B | AF-M | -1.80 | 4.8e-114 | +1.12 | 2.4e-46 | 20 | supported | Structure ↗ |
| ZNF410 | RF2-PPI | -1.67 | 1.7e-65 | +1.12 | 1.0e-25 | 10 | supported | Structure ↗ |
| NCK2 | RF2-PPI | -1.65 | 7.0e-61 | +1.05 | 5.0e-26 | 11 | supported | Structure ↗ |
| FOXO1 | RF2-PPI | -1.42 | 1.7e-51 | +0.94 | 1.1e-21 | 12 | supported | Structure ↗ |
| RASL11A | RF2-PPI | -1.48 | 3.2e-51 | +0.95 | 1.4e-21 | 11 | supported | Structure ↗ |
| BIN1 | RF2-PPI | -2.15 | 2.3e-37 | +1.40 | 2.0e-18 | 4 | supported | Structure ↗ |
| RASL11B | RF2-PPI | -1.31 | 4.9e-37 | +0.84 | 8.7e-17 | 10 | supported | Structure ↗ |
| EGFR | RF2-PPI | -1.17 | 2.2e-26 | +0.96 | 4.2e-14 | 7 | supported | Structure ↗ |
| RERG | RF2-PPI | -1.39 | 3.8e-24 | +0.75 | 6.1e-08 | 6 | supported | Structure ↗ |
| CD2AP | RF2-PPI | -1.10 | 4.1e-21 | +0.61 | 1.2e-08 | 8 | supported | Structure ↗ |
| SHC1 | RF2-PPI | -0.95 | 2.5e-17 | +0.64 | 1.2e-06 | 7 | supported | Structure ↗ |
| ABI1 | RF2-PPI | -0.96 | 3.7e-11 | +0.49 | 0.001 | 3 | supported | Structure ↗ |
| STARD13 | RF2-PPI | -0.93 | 8.7e-10 | +0.45 | 0.002 | 5 | supported | Structure ↗ |
| SOS1 | RF2-PPI | +0.01 | 0.135 | -0.17 | 0.229 | 4 | not supported | Structure ↗ |
| ARHGAP39 | RF2-PPI | -0.33 | 0.150 | +0.15 | 0.478 | 5 | not supported | Structure ↗ |