Q5UIP0: Telomere-associated protein RIF1 (RIF1)

Telomere-associated protein RIF1 (RIF1) is a 2472-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5UIP0.

Gene
RIF1
Organism
Homo sapiens
Length
2472 residues
Mean pLDDT
53.8
Model
AF-Q5UIP0-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 53.8 (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 accurate18%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions58%

What pLDDT means and how to read it

Function

Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs (PubMed:15342490, PubMed:28241136). In response to DNA damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23333306, PubMed:28241136). Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs (PubMed:28241136). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs (PubMed:23333306). In the same time, RIF1 and TP53BP1…

Subunit structure

Interacts with TP53BP1 (when phosphorylated by ATM) (PubMed:23333306, PubMed:28241136). May interact with TRF2 (By similarity). Interacts with SHLD2 (PubMed:29789392). Interacts with ERCC6 (via WHD region) (PubMed:29203878). Interacts with ASTE1 (PubMed:34354233)

Subcellular location

Nucleus, Chromosome, Chromosome, telomere, Cytoplasm, cytoskeleton, spindle

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8RS8X-ray1.31 ÅE/F/G/H=2260-2270

More AlphaFold highlights

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