Proteins / MRAS
MRAS
Ras-related protein M-Ras
GTPase
UniProt O14807
HSP90 client (literature): unknown
3D structure ↓
12 interaction partners · volcano ↗
Protein abundance under basal conditions (untreated, or vehicle where a drug arm exists). Scores are WT-relative: 1 = wild type.
4,432 variantsmissense decreased 40% · increased 15%
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 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 | |
|---|---|---|---|---|---|---|---|---|
| PIK3CA | PDB | -1.39 | 2.8e-47 | +0.58 | 3.3e-13 | 10 | supported | Structure ↗ |
| RALGDS | AF-M | -0.81 | 4.3e-39 | +0.58 | 6.1e-15 | 21 | supported | Structure ↗ |
| RAPGEF2 | AF-M | -0.91 | 4.3e-39 | +0.64 | 1.2e-18 | 21 | supported | Structure ↗ |
| MRAS | PDB | -0.96 | 6.6e-39 | +0.54 | 6.4e-15 | 17 | supported | Structure ↗ |
| RAPGEF5 | AF-M | -0.82 | 3.3e-27 | +0.89 | 7.3e-28 | 15 | supported | Structure ↗ |
| CRAF | AF-M | -0.98 | 1.8e-24 | +0.46 | 3.2e-08 | 10 | supported | Structure ↗ |
| BRAF | AF-M | -0.94 | 3.7e-22 | +0.37 | 1.7e-06 | 9 | supported | Structure ↗ |
| RAPGEF6 | AF-M | -0.53 | 3.6e-21 | +0.63 | 1.1e-13 | 14 | supported | Structure ↗ |
| LZTR1 | PDB | -0.52 | 5.1e-16 | +0.63 | 8.2e-12 | 15 | supported | Structure ↗ |
| SHOC2 | PDB | -0.51 | 8.1e-04 | +1.43 | 6.1e-13 | 3 | supported | Structure ↗ |
| PPP1CA | PDB | -0.47 | 4.2e-07 | +0.19 | 0.006 | 10 | supported | Structure ↗ |
| PPP1CC | PDB | -0.37 | 6.8e-05 | +0.12 | 0.088 | 9 | supported | Structure ↗ |