O14807: Ras-related protein M-Ras (MRAS)

Ras-related protein M-Ras (MRAS) is a 208-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14807.

Gene
MRAS
Organism
Homo sapiens
Length
208 residues
Mean pLDDT
86.4
Model
AF-O14807-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.4 (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 accurate72%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

Signal transducer in the Ras-MAPK signaling pathway that regulates cell proliferation and survival (PubMed:16630891, PubMed:28289718, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:16630891, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The formation of the SMP complex only occurs when MRAS is GTP-bound (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670, PubMed:39809765). Unlike other Ras proteins, MRAS has low intrinsic GTPase activity and may require additional factors for activation (PubMed:39809765). The SMP…

Subunit structure

Component of the SHOC2-MRAS-PP1c (SMP) holophosphatase 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:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670, PubMed:39809765). Interacts (active GTP-bound form) with both SHOC2 and PP1c (all isoforms) to form a tertiary complex;…

Subcellular location

Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9O0PX-ray1.5 ÅA/B=1-178
9O0QX-ray1.9 ÅA/B/C=1-178
7TXHX-ray1.95 ÅA/D=1-178
9C1AX-ray1.96 ÅA=1-178
9B4RX-ray2.1 ÅA=11-178
7TVFX-ray2.17 ÅB/E=1-178
9C1BX-ray2.27 ÅA/B/C/D=1-204
9B4TX-ray2.75 ÅB=1-178
9MEZX-ray2.8 ÅA/C/E/G/I=1-181
7UPIEM2.89 ÅA=1-182
7SD0EM2.95 ÅB=1-208

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