O75807: Protein phosphatase 1 regulatory subunit 15A (PPP1R15A)

Protein phosphatase 1 regulatory subunit 15A (PPP1R15A) is a 674-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75807.

Gene
PPP1R15A
Organism
Homo sapiens
Length
674 residues
Mean pLDDT
49.5
Model
AF-O75807-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 49.5 (very low 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 accurate4%
70 to 90Confident: backbone generally right7%
50 to 70Low: treat with caution20%
Below 50Very low: often disordered regions69%

What pLDDT means and how to read it

Function

Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress (PubMed:26095357, PubMed:26742780). Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1 (PubMed:14718519). May promote apoptosis by inducing p53/TP53 phosphorylation on 'Ser-15' (PubMed:14635196). Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux (PubMed:32978159). Also acts a…

Subunit structure

Interacts with PPP1CA (PubMed:15705855, PubMed:26095357). Interacts with EIF2S1 (PubMed:26095357). Interacts with PCNA (By similarity). Interacts with LYN and KMT2A/MLL1 (PubMed:11517336). Interacts with PPP1R1A and SMARCB1 (PubMed:12016208). Interacts with SMAD7 (PubMed:14718519). Interacts with BAG1 (PubMed:12724406). Interacts with NOX4 (PubMed:26742780)

Subcellular location

Endoplasmic reticulum membrane, Mitochondrion outer membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4XPNX-ray2.29 ÅB/D=552-591
7NXVX-ray2.55 ÅC/E=582-621
8QZZX-ray3.35 ÅC=420-452
7NZMEM3.96 ÅC=553-624

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