CREB-regulated transcription coactivator 1 (CRTC1) is a 634-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6UUV9.
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The mean pLDDT of this model is 51.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 5% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 27% |
| Below 50 | Very low: often disordered regions | 59% |
What pLDDT means and how to read it
Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PGC1alpha and inducer of mitochondrial biogenesis in muscle cells. In the hippocampus, involved in late-phase long-term potentiation (L-LTP) maintenance at the Schaffer collateral-CA1 synapses. May be required for dendritic growth of developing…
Binds, as a tetramer, through its N-terminal region, with the bZIP domain of CREB1 (PubMed:14536081). 'Arg-314' in the bZIP domain of CREB1 is essential for this interaction (PubMed:14536081). Interaction, via its C-terminal, with TAF4, enhances recruitment of TAF4 to CREB1 (PubMed:14536081). Interacts with 14-3-3 proteins, including YWHAE/14-3-3 epsilon (PubMed:30611118). Interacts with…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7D8P | X-ray | 2.0 Å | C/D=146-156 |
| 7D9V | X-ray | 2.21 Å | C/D=240-250 |
| 7D8H | X-ray | 2.42 Å | B=59-69 |
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