RNA polymerase-associated protein RTF1 homolog (RTF1) is a 710-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92541.
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The mean pLDDT of this model is 67.0 (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 | 19% |
| 70 to 90 | Confident: backbone generally right | 31% |
| 50 to 70 | Low: treat with caution | 15% |
| Below 50 | Very low: often disordered regions | 34% |
What pLDDT means and how to read it
Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through…
Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and SKIC8; the association of RTF1 appears to be less stable than that of other subunits. At least in HeLa cells a N-terminal shorter form of RTF1 is also found in the complex (PubMed:20178742). The PAF1 complex interacts with PHF5A (By similarity)
Nucleus, nucleoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3U1U | X-ray | 1.8 Å | A/B=347-482 |
| 4L1P | X-ray | 2.12 Å | A/B=353-484 |
| 4L1U | X-ray | 2.42 Å | A/B/C/D/E/F=353-484 |
| 9EGX | EM | 2.9 Å | R=1-710 |
| 9EGY | EM | 2.9 Å | R=1-710 |
| 9EGZ | EM | 2.9 Å | R=1-710 |
| 7UNC | EM | 3.0 Å | R=1-710 |
| 7UND | EM | 3.0 Å | R=1-710 |
| 6TED | EM | 3.1 Å | R=1-710 |
| 9EH1 | EM | 3.1 Å | R=353-600 |
| 9EH2 | EM | 3.1 Å | R=1-710 |
| 8A3Y | EM | 3.3 Å | R=353-600 |
| 9EH0 | EM | 3.6 Å | R=1-710 |
| 9S3G | EM | 6.4 Å | R=1-710 |
| 9S0U | EM | 6.72 Å | R=1-710 |
| 9RZE | EM | 8.53 Å | R=1-710 |
| 2BZE | NMR | A=346-484 | |
| 2DB9 | NMR | A=347-482 |
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